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Sequence
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35.2k
EC number
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118
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Cofactor
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1.77k
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Gene Ontology (biological process)
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11.3k
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Gene Ontology (cellular component)
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2.09k
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Pfam
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232
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Gene3D
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250
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Protein families
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237
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Post-translational modification
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8.52k
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Subcellular location [CC]
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6.18k
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Catalytic activity
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908
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pH dependence
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955
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Temperature dependence
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1.16k
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Function [CC]
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Organism
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196
O23629
H2B6_ARATH
MAPRAEKKPAEKKPAAEKPVEEKSKAEKAPAEKKPKAGKKLPKEAGAGGDKKKKMKKKSVETYKIYIFKVLKQVHPDIGISSKAMGIMNSFINDIFEKLASESSKLARYNKKPTITSREIQTAVRLVLPGELAKHAVSEGTKAVTKFTSS
null
null
null
chloroplast stroma [GO:0009570]; chloroplast thylakoid [GO:0009534]; cytosol [GO:0005829]; nucleolus [GO:0005730]; nucleosome [GO:0000786]
DNA binding [GO:0003677]; protein heterodimerization activity [GO:0046982]; structural constituent of chromatin [GO:0030527]
PF00125;
1.10.20.10;
Histone H2B family
PTM: Can be acetylated to form H2BK6ac, H2BK11ac, H2BK22ac, H2BK27ac H2BK33ac and H2BK34ac. {ECO:0000269|PubMed:17691833}.; PTM: Mono-, di- or trimethylated at the N-terminus to form H2BA1me1/2/3. H2BA1me2 may be acetylated to form H2BA1me2K6ac and H2BA1me2K6acK11ac. {ECO:0000269|PubMed:17691833}.; PTM: Monoubiquitinated by BRE1 to form H2BK143ub1 and deubiquitinated by UBP26. Required for heterochromatic histone H3 di- and trimethylation at H3K4me. May give a specific tag for epigenetic transcriptional activation.
SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome {ECO:0000250}.
null
null
null
null
null
FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
Arabidopsis thaliana (Mouse-ear cress)
O23647
GLGB1_ARATH
MVYTISGVRFPHLPSIKKKNSSLHSFNEDLRRSNAVSFSLRKDSRSSGKVFARKPSYDSDSSSLATTASEKLRGHQSDSSSSASDQVQSRDTVSDDTQVLGNVDVQKTEEAQETETLDQTSALSTSGSISYKEDFAKMSHSVDQEVGQRKIPPPGDGKRIYDIDPMLNSHRNHLDYRYGQYRKLREEIDKNEGGLEAFSRGYEIFGFTRSATGITYREWAPGAKAASLIGDFNNWNAKSDVMARNDFGVWEIFLPNNADGSPAIPHGSRVKIRMDTPSGIKDSIPAWIKYSVQPPGEIPYNGVYYDPPEEDKYAFKHPRPKKPTSLRIYESHVGMSSTEPKINTYANFRDDVLPRIKKLGYNAVQIMAIQEHAYYASFGYHVTNFFAPSSRFGTPDDLKSLIDKAHELGLVVLMDIVHSHASKNTLDGLDMFDGTDGQYFHSGSRGYHWMWDSRLFNYGSWEVLRYLLSNARWWLEEYKFDGFRFDGVTSMMYTHHGLQVEFTGNYNEYFGYSTDVDAVVYLMLVNDLIHGLYPEAIVVGEDVSGMPAFCVPVEDGGVGFDYRLHMAVADKWIELLKKRDEDWQVGDITFTLTNRRWGEKCVVYAESHDQALVGDKTIAFWLMDKDMYDFMAVDRQATPRVDRGIALHKMIRLITMGLGGEGYLNFMGNEFGHPEWIDFPRTDQHLPDGRVIAGNNGSYDKCRRRFDLGDAEYLRYHGLQEFDRAMQNLEETYGFMTSEHQYISRKDEGDRVIVFERGNLLFVFNFHWTNSYSDYRIGCSVPGKYKIVLDSDNSLFGGFNRLDDSAEFFTSDGRHDDRPCSFMVYAPCRTAVVYAAVDDDDDDERSSLVPIGLLPEDV
2.4.1.18
null
amylopectin biosynthetic process [GO:0010021]; cellular response to fructose stimulus [GO:0071332]; cellular response to glucose stimulus [GO:0071333]; cellular response to light stimulus [GO:0071482]; cellular response to sucrose stimulus [GO:0071329]; glycogen biosynthetic process [GO:0005978]; starch biosynthetic process [GO:0019252]; starch metabolic process [GO:0005982]
amyloplast [GO:0009501]; chloroplast [GO:0009507]; chloroplast stroma [GO:0009570]
1,4-alpha-glucan branching enzyme activity [GO:0003844]; 1,4-alpha-glucan branching enzyme activity (using a glucosylated glycogenin as primer for glycogen synthesis) [GO:0102752]; cation binding [GO:0043169]; hydrolase activity, hydrolyzing O-glycosyl compounds [GO:0004553]
PF00128;PF02806;PF02922;
3.20.20.80;2.60.40.1180;2.60.40.10;
Glycosyl hydrolase 13 family, GlgB subfamily
null
SUBCELLULAR LOCATION: Plastid, chloroplast stroma {ECO:0000269|PubMed:18431481}. Plastid, amyloplast {ECO:0000250}.
CATALYTIC ACTIVITY: Reaction=Transfers a segment of a (1->4)-alpha-D-glucan chain to a primary hydroxy group in a similar glucan chain.; EC=2.4.1.18;
null
PATHWAY: Glycan biosynthesis; starch biosynthesis.
null
null
FUNCTION: Catalyzes the formation of the alpha-1,6-glucosidic linkages in starch by scission of a 1,4-alpha-linked oligosaccharide from growing alpha-1,4-glucan chains and the subsequent attachment of the oligosaccharide to the alpha-1,6 position. {ECO:0000269|PubMed:17028209}.
Arabidopsis thaliana (Mouse-ear cress)
O23653
AK2_ARATH
MASLQLYGVKTPGLALSSKRLEFASKGACFSVTLPSSSAVFRDVEHSCRNIGLRVSCEALRVDLLQRKEPETCDSSGTGKELTCVMKFGGSSVESAERMKEVANLILSFPDERPVIVLSAMGKTTNKLLKAGEKAVTCGVTNVESIEELSFIKELHLRTAHELGVETTVIEKHLEGLHQLLKGISMMKELTLRTRDYLVSFGECMSTRLFSAYLNKIGHKARQYDAFEIGFITTDDFTNADILEATYPAVSKTLVGDWSKENAVPVVTGYLGKGWRSCAITTLGRGGSDLTATTIGKALGLREIQVWKDVDGVLTCDPNIYPGAQSVPYLTFDEAAELAYFGAQVLHPLSMRPARDGDIPVRVKNSYNPTAPGTVITRSRDMSKAVLTSIVLKRNVTMLDIASTRMLGQYGFLAKVFTTFEDLGISVDVVATSEVSISLTLDPAKLWGRELIQRVNELDNLVEELEKIAVVKLLQRRSIISLIGNVQKSSLILEKVFQVFRSNGVNVQMISQGASKVNISLIVNDEEAEQCVRALHSAFFETDP
2.7.2.4
null
homoserine biosynthetic process [GO:0009090]; lysine biosynthetic process via diaminopimelate [GO:0009089]; phosphorylation [GO:0016310]; threonine biosynthetic process [GO:0009088]
chloroplast stroma [GO:0009570]; cytosol [GO:0005829]
aspartate kinase activity [GO:0004072]; ATP binding [GO:0005524]
PF00696;
3.30.70.260;3.40.1160.10;1.20.120.1320;
Aspartokinase family
null
SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}.
CATALYTIC ACTIVITY: Reaction=ATP + L-aspartate = 4-phospho-L-aspartate + ADP; Xref=Rhea:RHEA:23776, ChEBI:CHEBI:29991, ChEBI:CHEBI:30616, ChEBI:CHEBI:57535, ChEBI:CHEBI:456216; EC=2.7.2.4;
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=980 uM for ATP {ECO:0000269|PubMed:17140415}; KM=1940 uM for aspartate {ECO:0000269|PubMed:17140415}; Note=K(cat) is 14.5/sec.;
PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 1/4.; PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-homoserine from L-aspartate: step 1/3.; PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine from L-aspartate: step 1/5.
null
null
FUNCTION: Involved in the first step of essential amino acids lysine, threonine, methionine and isoleucine synthesis via the aspartate-family pathway.
Arabidopsis thaliana (Mouse-ear cress)
O23654
VATA_ARATH
MPAFYGGKLTTFEDDEKESEYGYVRKVSGPVVVADGMAGAAMYELVRVGHDNLIGEIIRLEGDSATIQVYEETAGLTVNDPVLRTHKPLSVELGPGILGNIFDGIQRPLKTIARISGDVYIPRGVSVPALDKDCLWEFQPNKFVEGDTITGGDLYATVFENTLMNHLVALPPDAMGKITYIAPAGQYSLKDTVIELEFQGIKKSYTMLQSWPVRTPRPVASKLAADTPLLTGQRVLDALFPSVLGGTCAIPGAFGCGKTVISQALSKYSNSDAVVYVGCGERGNEMAEVLMDFPQLTMTLPDGREESVMKRTTLVANTSNMPVAAREASIYTGITIAEYFRDMGYNVSMMADSTSRWAEALREISGRLAEMPADSGYPAYLAARLASFYERAGKVKCLGGPERNGSVTIVGAVSPPGGDFSDPVTSATLSIVQVFWGLDKKLAQRKHFPSVNWLISYSKYSTALESFYEKFDPDFINIRTKAREVLQREDDLNEIVQLVGKDALAEGDKITLETAKLLREDYLAQNAFTPYDKFCPFYKSVWMMRNIIHFYNLANQAVERAAGMDGQKITYTLIKHRLGDLFYRLVSQKFEDPAEGEDTLVEKFKKLYDDLNAGFRALEDETR
7.1.2.2
null
Golgi organization [GO:0007030]; pollen development [GO:0009555]
chloroplast [GO:0009507]; chloroplast envelope [GO:0009941]; cytosol [GO:0005829]; Golgi apparatus [GO:0005794]; lysosomal membrane [GO:0005765]; mitochondrion [GO:0005739]; phagocytic vesicle [GO:0045335]; plant-type cell wall [GO:0009505]; plant-type vacuole [GO:0000325]; plasma membrane [GO:0005886]; plasmodesma [GO:0009506]; proton-transporting V-type ATPase, V1 domain [GO:0033180]; vacuolar membrane [GO:0005774]; vacuole [GO:0005773]
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; protease binding [GO:0002020]; proton-transporting ATP synthase activity, rotational mechanism [GO:0046933]; proton-transporting ATPase activity, rotational mechanism [GO:0046961]
PF00006;PF02874;PF16886;
2.40.30.20;2.40.50.100;3.40.50.300;
ATPase alpha/beta chains family
null
SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000269|PubMed:17151019}; Peripheral membrane protein {ECO:0000305}.
CATALYTIC ACTIVITY: Reaction=ATP + 4 H(+)(in) + H2O = ADP + 5 H(+)(out) + phosphate; Xref=Rhea:RHEA:57720, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.1.2.2;
null
null
null
null
FUNCTION: Catalytic subunit of the peripheral V1 complex of vacuolar ATPase. V-ATPase vacuolar ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells.
Arabidopsis thaliana (Mouse-ear cress)
O23661
ARFC_ARATH
MGGLIDLNVMETEEDETQTQTPSSASGSVSPTSSSSASVSVVSSNSAGGGVCLELWHACAGPLISLPKRGSLVLYFPQGHLEQAPDFSAAIYGLPPHVFCRILDVKLHAETTTDEVYAQVSLLPESEDIERKVREGIIDVDGGEEDYEVLKRSNTPHMFCKTLTASDTSTHGGFSVPRRAAEDCFPPLDYSQPRPSQELLARDLHGLEWRFRHIYRGQPRRHLLTTGWSAFVNKKKLVSGDAVLFLRGDDGKLRLGVRRASQIEGTAALSAQYNQNMNHNNFSEVAHAISTHSVFSISYNPKASWSNFIIPAPKFLKVVDYPFCIGMRFKARVESEDASERRSPGIISGISDLDPIRWPGSKWRCLLVRWDDIVANGHQQRVSPWEIEPSGSISNSGSFVTTGPKRSRIGFSSGKPDIPVSEGIRATDFEESLRFQRVLQGQEIFPGFINTCSDGGAGARRGRFKGTEFGDSYGFHKVLQGQETVPAYSITDHRQQHGLSQRNIWCGPFQNFSTRILPPSVSSSPSSVLLTNSNSPNGRLEDHHGGSGRCRLFGFPLTDETTAVASATAVPCVEGNSMKGASAVQSNHHHSQGRDIYAMRDMLLDIAL
null
null
abaxial cell fate specification [GO:0010158]; auxin metabolic process [GO:0009850]; auxin-activated signaling pathway [GO:0009734]; floral meristem determinacy [GO:0010582]; positive regulation of response to water deprivation [GO:1902584]; response to auxin [GO:0009733]; vegetative phase change [GO:0010050]
nucleus [GO:0005634]
chromatin DNA binding [GO:0031490]; DNA binding [GO:0003677]; DNA-binding transcription factor activity [GO:0003700]; molecular function activator activity [GO:0140677]; small molecule binding [GO:0036094]; transcription cis-regulatory region binding [GO:0000976]
PF06507;PF02362;
2.30.30.1040;2.40.330.10;
ARF family
null
SUBCELLULAR LOCATION: Nucleus.
null
null
null
null
null
FUNCTION: Auxin response factors (ARFs) are transcriptional factors that bind specifically to the DNA sequence 5'-TGTCTC-3' found in the auxin-responsive promoter elements (AuxREs). Could act as transcriptional activator or repressor. Formation of heterodimers with Aux/IAA proteins may alter their ability to modulate early auxin response genes expression. Involved in the establishment or elaboration of tissue patterning during gynoecial development. {ECO:0000269|PubMed:10952886, ECO:0000269|PubMed:12036261}.
Arabidopsis thaliana (Mouse-ear cress)
O23674
PKSA_ARATH
MSNSRMNGVEKLSSKSTRRVANAGKATLLALGKAFPSQVVPQENLVEGFLRDTKCDDAFIKEKLEHLCKTTTVKTRYTVLTREILAKYPELTTEGSPTIKQRLEIANEAVVEMALEASLGCIKEWGRPVEDITHIVYVSSSEIRLPGGDLYLSAKLGLRNDVNRVMLYFLGCYGGVTGLRVAKDIAENNPGSRVLLTTSETTILGFRPPNKARPYDLVGAALFGDGAAAVIIGADPRECEAPFMELHYAVQQFLPGTQNVIEGRLTEEGINFKLGRDLPQKIEENIEEFCKKLMGKAGDESMEFNDMFWAVHPGGPAILNRLETKLKLEKEKLESSRRALVDYGNVSSNTILYVMEYMRDELKKKGDAAQEWGLGLAFGPGITFEGLLIRSLTSS
2.3.1.-
null
flavonoid biosynthetic process [GO:0009813]; pollen exine formation [GO:0010584]; polyketide biosynthetic process [GO:0030639]; sporopollenin biosynthetic process [GO:0080110]
endoplasmic reticulum [GO:0005783]
tetraketide alpha-pyrone synthase activity [GO:0090439]
PF02797;PF00195;
3.40.47.10;
Thiolase-like superfamily, Chalcone/stilbene synthases family
null
SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000269|PubMed:21193570, ECO:0000269|PubMed:23632852}.
null
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=22.9 uM for n-dodecanoyl-CoA (at pH 7 and 30 degrees Celsius) {ECO:0000269|PubMed:19043200}; KM=25 uM for 16-OH-C16-CoA {ECO:0000269|PubMed:21193570}; KM=23 uM for 12-OH-C18-CoA {ECO:0000269|PubMed:21193570}; KM=48 uM for C16-CoA {ECO:0000269|PubMed:21193570}; Note=kcat is 0.11 min(-1) with n-dodecanoyl-CoA as substrate for the production of the triketide alpha-pyrone (at pH 7 and 30 degrees Celsius) (PubMed:19043200). kcat is 2.8 msec(-1) with 16-OH-C16-CoA as substrate, 5 msec(-1) with 12-OH-C18-CoA as substrate and 0.13 msec(-1) with C16-CoA as substrate (PubMed:21193570). {ECO:0000269|PubMed:19043200, ECO:0000269|PubMed:21193570};
PATHWAY: Secondary metabolite biosynthesis; flavonoid biosynthesis. {ECO:0000250|UniProtKB:Q9LKP7}.
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7 (at 30 degrees Celsius). {ECO:0000269|PubMed:19043200};
null
FUNCTION: Plant type III polyketide synthases (PKSs) that catalyzes the condensation of malonyl-CoA units with various CoA ester starter molecules to generate a diverse array of natural products including long-chain alkyl alpha-pyrones. Accepts up to C(20) chain-length fatty acyl CoAs as starter substrates, and carries out sequential condensations with malonyl-CoA to produce triketide and tetraketide alpha-pyrones, potential sporopollenin precursors (PubMed:19043200, PubMed:21193570). Favorite substrates for are midchain- and v-hydroxylated fatty acyl-CoAs (e.g. 12-hydroxyoctadecanoyl-CoA and 16-hydroxyhexadecanoyl-CoA). Required for pollen development and sporopollenin biosynthesis, the major constituent of exine in the outer pollen wall (PubMed:20442277, PubMed:21193570). In vitro, can use 4-coumaroyl-coenzyme A as substrate to produce bis-noryangonin and fatty acyl-coenzyme A as substrate to produce medium-chain alkyl pyrones. May play a role in both the synthesis of pollen fatty acids and phenolics found in exine (PubMed:20442277). {ECO:0000269|PubMed:19043200, ECO:0000269|PubMed:20442277, ECO:0000269|PubMed:21193570}.
Arabidopsis thaliana (Mouse-ear cress)
O23676
MGN_ARATH
MAAEEATEFYLRYYVGHKGKFGHEFLEFEFREDGKLRYANNSNYKNDTIIRKEVFLTPAVLKECKRIVSESEILKEDDNNWPEPDRVGKQELEIVLGNEHISFATSKIGSLVDCQSSNDPEGLRIFYYLVQDLKCLVFSLISLHFKIKPI
null
null
embryo development ending in seed dormancy [GO:0009793]; mRNA processing [GO:0006397]; mRNA transport [GO:0051028]; nuclear-transcribed mRNA catabolic process, nonsense-mediated decay [GO:0000184]; pollen tube guidance [GO:0010183]; positive regulation of gene expression [GO:0010628]; regulation of translation [GO:0006417]; RNA splicing [GO:0008380]
catalytic step 2 spliceosome [GO:0071013]; exon-exon junction complex [GO:0035145]; nuclear speck [GO:0016607]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; P-body [GO:0000932]
RNA binding [GO:0003723]
PF02792;
3.30.1560.10;
Mago nashi family
null
SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:19435936}. Nucleus speckle {ECO:0000269|PubMed:19435936}. Nucleus {ECO:0000269|PubMed:26867216}. Cytoplasm, P-body {ECO:0000269|PubMed:26867216}. Cytoplasm {ECO:0000250|UniProtKB:P61326}. Note=Nucleocytoplasmic shuttling protein. Travels to the cytoplasm as part of the exon junction complex (EJC) bound to mRNA. {ECO:0000250|UniProtKB:P61326}.
null
null
null
null
null
FUNCTION: Core component of the splicing-dependent multiprotein exon junction complex (EJC) deposited at splice junctions on mRNAs. The EJC is a dynamic structure consisting of core proteins and several peripheral nuclear and cytoplasmic associated factors that join the complex only transiently either during EJC assembly or during subsequent mRNA metabolism. The EJC marks the position of the exon-exon junction in the mature mRNA for the gene expression machinery and the core components remain bound to spliced mRNAs throughout all stages of mRNA metabolism thereby influencing downstream processes including nuclear mRNA export, subcellular mRNA localization, translation efficiency and nonsense-mediated mRNA decay (NMD). The MAGO-Y14 heterodimer inhibits the ATPase activity of EIF4A3, thereby trapping the ATP-bound EJC core onto spliced mRNA in a stable conformation. The MAGO-Y14 heterodimer interacts with the EJC key regulator PYM leading to EJC disassembly in the cytoplasm (By similarity). Can increase in vitro the expression from reporter constructs that contain leader introns required for the expression of different genes. In association with MAGO and PYM, participates in intron-mediated enhancement of gene expression (PubMed:21676911). The MAGO-Y14 heterodimer works synergistically with the NMD pathway to regulate male gametophyte development (PubMed:26867216). {ECO:0000250|UniProtKB:P61326, ECO:0000269|PubMed:21676911, ECO:0000269|PubMed:26867216}.
Arabidopsis thaliana (Mouse-ear cress)
O23680
TOC33_ARATH
MGSLVREWVGFQQFPAATQEKLIEFFGKLKQKDMNSMTVLVLGKGGVGKSSTVNSLIGEQVVRVSPFQAEGLRPVMVSRTMGGFTINIIDTPGLVEAGYVNHQALELIKGFLVNRTIDVLLYVDRLDVYRVDELDKQVVIAITQTFGKEIWCKTLLVLTHAQFSPPDELSYETFSSKRSDSLLKTIRAGSKMRKQEFEDSAIAVVYAENSGRCSKNDKDEKALPNGEAWIPNLVKAITDVATNQRKAIHVDKKMVDGSYSDDKGKKLIPLIIGAQYLIVKMIQGAIRNDIKTSGKPL
3.6.5.-
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:17337454, ECO:0000269|PubMed:18400179, ECO:0000269|PubMed:18541539}; Note=Binds 1 Mg(2+) ion by subunit. {ECO:0000269|PubMed:17337454, ECO:0000269|PubMed:18400179, ECO:0000269|PubMed:18541539};
intracellular protein transport [GO:0006886]; protein targeting to chloroplast [GO:0045036]
chloroplast [GO:0009507]; chloroplast envelope [GO:0009941]; chloroplast outer membrane [GO:0009707]; extracellular region [GO:0005576]
GTP binding [GO:0005525]; GTPase activity [GO:0003924]; identical protein binding [GO:0042802]; metal ion binding [GO:0046872]; protein homodimerization activity [GO:0042803]; protein-transporting ATPase activity [GO:0015450]
PF04548;
3.40.50.300;
TRAFAC class TrmE-Era-EngA-EngB-Septin-like GTPase superfamily, AIG1/Toc34/Toc159-like paraseptin GTPase family, TOC34 subfamily
PTM: Phosphorylated by a kinase present in the outer envelope of chloroplast. When Ser-181 is phosphorylated, the binding to preprotein, GTP and GDP is inhibited, and thus, GTPase activity is repressed. {ECO:0000269|PubMed:12741849, ECO:0000269|PubMed:16412428, ECO:0000269|PubMed:18054337}.
SUBCELLULAR LOCATION: Plastid, chloroplast outer membrane {ECO:0000269|PubMed:10998188, ECO:0000269|PubMed:12766230, ECO:0000269|PubMed:12951325}; Single-pass membrane protein {ECO:0000269|PubMed:10998188, ECO:0000269|PubMed:12766230, ECO:0000269|PubMed:12951325}. Note=May contain beta barrel transmembrane regions.
null
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=290 nM for GDP (at pH 7.4) {ECO:0000269|PubMed:12741849, ECO:0000269|PubMed:17261588}; KM=5.7 uM for GTP (at pH 7.6 and 25 degrees Celsius) {ECO:0000269|PubMed:12741849, ECO:0000269|PubMed:17261588}; Vmax=1040 nmol/min/ug enzyme with GTP as substrate (at pH 7.4) {ECO:0000269|PubMed:12741849, ECO:0000269|PubMed:17261588};
null
null
null
FUNCTION: GTPase involved in protein precursor import into chloroplasts. Seems to recognize chloroplast-destined precursor proteins and regulate their presentation to the translocation channel through GTP hydrolysis. Binds GTP, GDP, XTP, but not ATP. Probably specialized in the import of nuclear encoded photosynthetic preproteins from the cytoplasm to the chloroplast, especially during early development stages. {ECO:0000269|PubMed:11553737, ECO:0000269|PubMed:12741849, ECO:0000269|PubMed:12782294, ECO:0000269|PubMed:12869544, ECO:0000269|PubMed:12897258, ECO:0000269|PubMed:12951325, ECO:0000269|PubMed:15053763, ECO:0000269|PubMed:16412428, ECO:0000269|PubMed:16435266, ECO:0000269|PubMed:18054337}.
Arabidopsis thaliana (Mouse-ear cress)
O23702
CTBP_ARATH
MSKIRSSATMPHRDQPSPASPHVVTLNCIEDCALEQDSLAGVAGVEYVPLSRIADGKIESATAVLLHSLAYLPRAAQRRLRPHQLILCLGSADRAVDSTLAADLGLRLVHVDTSRAEEIADTVMALILGLLRRTHLLSRHALSASGWLGSLQPLCRGMRRCRGMVLGIVGRSVSARYLASRSLAFKMSVLYFDVPEGDEERIRPSRFPRAARRMDTLNDLLAASDVISLHCALTNDTVQILNAECLQHIKPGAFLVNTGSCQLLDDCAVKQLLIDGTIAGCALDGAEGPQWMEAWVKEMPNVLILPRSADYSEEVWMEIREKAISILHSFFLDGVIPSNTVSDEEVEESEASEEEEQSPSKHEKLAIVESTSRQQGESTLTSTEIVRREASELKESLSPGQQHVSQNTAVKPEGRRSRSGKKAKKRHSQQKYMQKTDGSSGLNEESTSRRDDIAMSDTEEVLSSSSRCASPEDSRSRKTPLEVMQESSPNQLVMSSKKFIGKSSELLKDGYVVALYAKDLSGLHVSRQRTKNGGWFLDTLSNVSKRDPAAQFIIAYRNKDTVGLRSFAAGGKLLQINRRMEFVFASHSFDVWESWSLEGSLDECRLVNCRNSSAVLDVRVEILAMVGDDGITRWID
null
COFACTOR: Name=NAD(+); Xref=ChEBI:CHEBI:57540; Evidence={ECO:0000250}; Note=Cofactor binding induces a conformational change. {ECO:0000250};
cotyledon morphogenesis [GO:0048826]; floral organ morphogenesis [GO:0048444]; fruit morphogenesis [GO:0048530]; inductive cell-cell signaling [GO:0031129]; leaf morphogenesis [GO:0009965]; microtubule cytoskeleton organization [GO:0000226]; monopolar cell growth [GO:0042814]; nuclear migration [GO:0007097]; regulation of cell shape [GO:0008360]; regulation of epidermal cell differentiation [GO:0045604]; regulation of epidermal cell division [GO:0010482]; regulation of trichome morphogenesis [GO:2000039]; response to osmotic stress [GO:0006970]; response to salt stress [GO:0009651]; stress granule assembly [GO:0034063]; trichome branching [GO:0010091]
cytoplasmic stress granule [GO:0010494]; cytosol [GO:0005829]; microtubule [GO:0005874]; trans-Golgi network [GO:0005802]
identical protein binding [GO:0042802]; kinase binding [GO:0019900]; NAD binding [GO:0051287]; oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor [GO:0016616]; protein homodimerization activity [GO:0042803]; protein self-association [GO:0043621]; transcription corepressor activity [GO:0003714]
PF02826;
3.40.50.720;
D-isomer specific 2-hydroxyacid dehydrogenase family, Plant AN subfamily
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11889033, ECO:0000269|PubMed:11889034, ECO:0000269|PubMed:32004461}. Golgi apparatus, trans-Golgi network {ECO:0000269|PubMed:21801251}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:35975703}. Note=Was thought initially to be located in nucleus (PubMed:11889033, PubMed:11889034) but the large dot-like structures are now believed to represent non-physiological aggregates (PubMed:11889033, PubMed:11889034). In root cells, cytoplasmic polarized localization near cell edges, at the vicinity of SOKs proteins (PubMed:32004461). Associates with membranes in puncta in embryos (PubMed:32004461). {ECO:0000269|PubMed:11889033, ECO:0000269|PubMed:11889034, ECO:0000269|PubMed:32004461}.
null
null
null
null
null
FUNCTION: Involved in controlling the equilibrium between tubular and stacked structures in the Golgi complex (By similarity). Required for cortical microtubules (MTs) arrangement that confers cell shape. Cooperatively with IPGA1, negatively regulates cortical microtubules (CMTs) organization in response to mechanical stress and modulates pavement cells morphogenesis leading to puzzle shape, probably in an AAA1/KTN1-dependent manner (PubMed:35975703). Regulates the width of leaves by controlling the polar elongation of leaf cells. Involved in the regulation of trichome branching. Seems to not be able to regulate gene transcription. Regulates epidermal cell divisions and elongation in a non-cell-autonomous manner (regulated by subepidermal cells), but regulates epidermal cell polarity, shape, trichome branching and elongation in a cell-autonomous manner. Negatively regulates growth in the petiole elongation. Prevents lipid peroxidation as a result of abiotic stress response. Is involved in the SUB-dependent signaling mechanism and may act in a membrane trafficking event around the trans-Golgi network. {ECO:0000250, ECO:0000269|PubMed:10572032, ECO:0000269|PubMed:11889033, ECO:0000269|PubMed:12079678, ECO:0000269|PubMed:17972097, ECO:0000269|PubMed:19843316, ECO:0000269|PubMed:23368817, ECO:0000269|PubMed:23672620, ECO:0000269|PubMed:35975703, ECO:0000269|PubMed:8625845, ECO:0000269|PubMed:9736998}.
Arabidopsis thaliana (Mouse-ear cress)
O23710
PSB7A_ARATH
MSQSTVDVPPKGGFSFDLCKRNDMLTQKGLKAPSFLKTGTTIVGLIFKDGVILGADTRATEGPIVADKNCEKIHYMAPNIYCCGAGTAADTEAVTDMVSSQLRLHRYQTGRDSRVITALTLLKKHLFSYQGHVSAALVLGGVDITGPHLHTIYPHGSTDTLPFATMGSGSLAAMSVFEAKYKEGLTRDEGIKLVAESICSGIFNDLGSGSNVDICVITKGNKEYLRNYMEPNPRTYVSSKGYSFTKKTEVLLTKITPLLERVEITEVGEAMEE
3.4.25.1
null
proteolysis involved in protein catabolic process [GO:0051603]
cytosol [GO:0005829]; nucleus [GO:0005634]; proteasome complex [GO:0000502]; proteasome core complex, beta-subunit complex [GO:0019774]
threonine-type endopeptidase activity [GO:0004298]
PF00227;
3.60.20.10;
Peptidase T1B family
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|PROSITE-ProRule:PRU00809}. Nucleus {ECO:0000250}.
CATALYTIC ACTIVITY: Reaction=Cleavage of peptide bonds with very broad specificity.; EC=3.4.25.1;
null
null
null
null
FUNCTION: The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity.
Arabidopsis thaliana (Mouse-ear cress)
O23712
PSA1B_ARATH
MFRNQYDTDVTTWSPTGRLFQVEYAMEAVKQGSAAIGLRSRSHVVLACVNKAQSELSSHQRKIFKVDDHIGVAIAGLTADGRVLSRYMRSESINHSFTYESPLPVGRLVVHLADKAQVCTQRSWKRPYGVGLLVGGLDESGAHLYYNCPSGNYFEYQAFAIGSRSQAAKTYLERKFESFQESSKEDLIKDAIMAIRETLQGETLKSSLCTVSVLGVDEPFHFLDQESIQKVIDTFEKVPEEEEDAGEGEAEPEAAPGAAGTGEQGGSGDQDVAPMEI
null
null
proteasomal protein catabolic process [GO:0010498]; ubiquitin-dependent protein catabolic process [GO:0006511]
cytosol [GO:0005829]; nucleus [GO:0005634]; plasmodesma [GO:0009506]; proteasome complex [GO:0000502]; proteasome core complex, alpha-subunit complex [GO:0019773]
null
PF00227;PF10584;
3.60.20.10;
Peptidase T1A family
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
null
null
null
null
null
FUNCTION: The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity. May play a role in thiol biosynthesis and arsenic tolerance in association with PAF1/ARS5. {ECO:0000269|PubMed:19453443}.
Arabidopsis thaliana (Mouse-ear cress)
O23715
PSA3_ARATH
MSSIGTGYDLSVTTFSPDGRVFQIEYAAKAVDNSGTVVGIKCKDGIVMGVEKLIASKMMLPGSNRRIHSVHRHAGMAVAGLAADGRQIVARAKSEARSYESVYGDAVPVKELSERVASYVHLCTLYWWLRPFGCGVILGGYDRDGPQLYMIEPSGISYRYFGAAIGKGKQAAKTEIEKLNLSEMTCKEGVIEVAKIIYKLHDEAKDKAFELEMSWICEESKREHQKVPDDLLEEAKTAAKTALEEMDAD
null
null
proteasomal protein catabolic process [GO:0010498]; ubiquitin-dependent protein catabolic process [GO:0006511]
apoplast [GO:0048046]; cytosol [GO:0005829]; nucleus [GO:0005634]; peroxisome [GO:0005777]; plant-type vacuole [GO:0000325]; proteasome complex [GO:0000502]; proteasome core complex, alpha-subunit complex [GO:0019773]; vacuole [GO:0005773]
null
PF00227;PF10584;
3.60.20.10;
Peptidase T1A family
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
null
null
null
null
null
FUNCTION: The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity.
Arabidopsis thaliana (Mouse-ear cress)
O23722
MVD1_ARATH
MAEEKWVVMVTAQTPTNIAVIKYWGKRDEVRILPINDSISVTLDPDHLCTLTTVAVSPSFDRDRMWLNGKEISLSGSRYQNCLREIRSRADDVEDKEKGIKIAKKDWEKLHLHIASHNNFPTAAGLASSAAGFACLVFALAKLMNVNEDPSQLSAIARQGSGSACRSLFGGFVKWNMGNKEDGSDSVAVQLVDDKHWDDLVIIIAVVSSRQKETSSTSGMRESVETSLLLQHRAKEVVPVRILQMEEAIKNRDFTSFTKLTCSDSNQFHAVCMDTSPPIFYMNDTSHRIISLVEKWNRSAGTPEIAYTFDAGPNAVMIARNRKVAVELLQGLLYCFPPKPDTDMKSYVLGDTSIVKEAGLEGELPQGIKDKIGSQDQKGEVSYFICSRPGRGPVVLQDQTQALLHPQTGLPK
4.1.1.33
null
isopentenyl diphosphate biosynthetic process, mevalonate pathway [GO:0019287]; sterol biosynthetic process [GO:0016126]
cytosol [GO:0005829]; peroxisome [GO:0005777]
ATP binding [GO:0005524]; diphosphomevalonate decarboxylase activity [GO:0004163]; identical protein binding [GO:0042802]
PF00288;PF18376;
3.30.230.10;3.30.70.890;
Diphosphomevalonate decarboxylase family
null
SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:21655959}.
CATALYTIC ACTIVITY: Reaction=(R)-5-diphosphomevalonate + ATP = ADP + CO2 + isopentenyl diphosphate + phosphate; Xref=Rhea:RHEA:23732, ChEBI:CHEBI:16526, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57557, ChEBI:CHEBI:128769, ChEBI:CHEBI:456216; EC=4.1.1.33; Evidence={ECO:0000269|PubMed:24327557, ECO:0000269|PubMed:26216978};
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=15.7 uM for (R)-5-diphosphomevalonate {ECO:0000269|PubMed:24327557}; KM=26 uM for (R)-5-diphosphomevalonate {ECO:0000269|PubMed:26216978}; KM=2800 uM for (R)-5-phosphomevalonate {ECO:0000269|PubMed:26216978}; Note=kcat is 2.0 sec(-1) with (R)-5-diphosphomevalonate as substrate (PubMed:24327557). kcat is 3.2 sec(-1) with (R)-5-diphosphomevalonate as substrate (PubMed:26216978). kcat is 0.033 sec(-1) with (R)-5-phosphomevalonate as substrate (PubMed:26216978). {ECO:0000269|PubMed:24327557, ECO:0000269|PubMed:26216978};
PATHWAY: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via mevalonate pathway; isopentenyl diphosphate from (R)-mevalonate: step 3/3. {ECO:0000305}.
null
null
FUNCTION: Performs the first committed step in the biosynthesis of isoprene-containing compounds such as sterols and terpenoids (PubMed:10344201, PubMed:26216978). Is specific for (R)-5-diphosphomevalonate (MVAPP). The catalytic efficiency with (R)-5-phosphomevalonate (MVAP) as substrate is 10000-fold lower than for MVAPP (PubMed:26216978). Can complement a yeast mutant defective in MVD activity (PubMed:10344201). {ECO:0000269|PubMed:10344201, ECO:0000269|PubMed:26216978}.
Arabidopsis thaliana (Mouse-ear cress)
O23736
GSH1_BRAJU
MALLSQAGGAYTVPSGHVSSRTGTKTVSGCVNVLRMKETYVSSYSRTLSTKSMLKRSKRGHQLIVAASPPTEEAVVATEPLTREDLIAYLASGCKSKEKWRIGTEHEKFGFEVNTLRPMKYDQIAELLNSIAERFEWEKVMEGDKIIGLKQGKQSISLEPGGQFELSGAPLETLHQTCAEVNSHLYQVKAVAEEMGIGFLGMGFQPKWRREDIPTMPKGRYDIMRNYMPKVGSLGLDMMLRTCTVQVNLDFSSEADMIRKFRAGLALQPIATALFANSPFTEGKPNGFLSMRSHIWTDTDKDRTGMLPFVFDDSFGFEQYVDYALDVPMYFAYRNGKYVDCTGMTFRQFLAGKLPCLPGELPTYNDWENHLTTIFPEVRLKRYMEMRGADGGPWRRLCALPAFWVGLLYDEDVLQSVLDLTADWTPAEREMLRNKVPVTGLKTPFRDGLLKHVAEDVLKLAKDGLERRGYKEVGFLNAVTEVVRTGVTPAENLLEMYNGEWGQSVDPVFQELLY
6.3.2.2
null
glutathione biosynthetic process [GO:0006750]; oxoacid metabolic process [GO:0043436]
chloroplast [GO:0009507]
ATP binding [GO:0005524]; glutamate-cysteine ligase activity [GO:0004357]
PF04107;
3.30.590.20;
Carboxylate-amine ligase family, Glutamate--cysteine ligase type 2 subfamily
PTM: The Cys-178-Cys-398 disulfide bridge is known to modulate the enzyme activity according to the redox status. The oxidized form constitutes the active enzyme.
SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000250}.
CATALYTIC ACTIVITY: Reaction=ATP + L-cysteine + L-glutamate = ADP + gamma-L-glutamyl-L-cysteine + H(+) + phosphate; Xref=Rhea:RHEA:13285, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:35235, ChEBI:CHEBI:43474, ChEBI:CHEBI:58173, ChEBI:CHEBI:456216; EC=6.3.2.2;
null
PATHWAY: Sulfur metabolism; glutathione biosynthesis; glutathione from L-cysteine and L-glutamate: step 1/2.
null
null
FUNCTION: Participates in the detoxification process. {ECO:0000269|PubMed:9119067, ECO:0000269|PubMed:9620267}.
Brassica juncea (Indian mustard) (Sinapis juncea)
O23813
SIR_MAIZE
MSGAIGGAEVHGFRGAAAQLPRSRVLGRPIRVAPPAAARPGGASAGSIRAVSAPAKKDASEVKRSKVEIIKEKSNFLRYPLNEELVSEAPNINESAVQLIKFHGSYQQTDRDVRGQKNYSFMLRTKNPCGKVPNQLYLAMDTLADEFGIGTLRLTTRQTFQLHGVLKKNLKTVLSTVIKNMGSTLGACGDLNRNVLAPAAPYVKKDILFAQQTAENIAALLTPQSGAYYDLWVDGEKIMSAEEPPEVTKARNDNSHGTNFPDSPEPIYGTQYLPRKFKVAVTAAGDNSVDILTNDIGVVVVSDDAGEPIGFNIYVGGGMGRTHRVETTFPRLADPLGYVPKEDILYAIKAIVVTQRENGRRDDRKYSRMKYMIDRWGIDRFRAEVEKYYGKKFESFRPLPEWQFNSYLGWQEQGDGKLFYGVHVDNGRVGGQAKKTLREIIEKYNLDVSITPNQNLILCGIDQAWREPITTALAQAGLLEPKDVDPLNLTAMACPALPLCPLAQTEAERGILPILKRIRAVFNKVGIKDSESVVVRITGCPNGCARPYMAELGFVGDGPKSYQIWLGGTPNQSTLAESFMDKVKLDDIEKVLEPLFTYWNGTRQEGESFGSFTNRTGFDKLKEVVNKWAESPSAA
1.8.7.1
COFACTOR: Name=siroheme; Xref=ChEBI:CHEBI:60052; Evidence={ECO:0000250}; Note=Binds 1 siroheme per subunit. {ECO:0000250}; COFACTOR: Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Note=Binds 1 [4Fe-4S] cluster per subunit.;
negative regulation of DNA-templated transcription [GO:0045892]; plastid chromosome packaging [GO:1900160]; response to cold [GO:0009409]; sulfate assimilation [GO:0000103]; sulfide oxidation [GO:0019418]
chloroplast nucleoid [GO:0042644]; chloroplast stroma [GO:0009570]; stromule [GO:0010319]; sulfite reductase complex (NADPH) [GO:0009337]
4 iron, 4 sulfur cluster binding [GO:0051539]; DNA binding [GO:0003677]; double-stranded DNA binding [GO:0003690]; heme binding [GO:0020037]; metal ion binding [GO:0046872]; sulfite reductase (ferredoxin) activity [GO:0050311]; sulfite reductase activity [GO:0016002]
PF01077;PF03460;
3.30.413.10;3.90.480.10;
Nitrite and sulfite reductase 4Fe-4S domain family
PTM: Phosphorylated; this phosphorylation reduces DNA-binding. {ECO:0000250}.
SUBCELLULAR LOCATION: Plastid, chloroplast stroma, chloroplast nucleoid. Plastid, chloroplast stroma. Plastid stroma.
CATALYTIC ACTIVITY: Reaction=3 H2O + hydrogen sulfide + 6 oxidized [2Fe-2S]-[ferredoxin] = 7 H(+) + 6 reduced [2Fe-2S]-[ferredoxin] + sulfite; Xref=Rhea:RHEA:23132, Rhea:RHEA-COMP:10000, Rhea:RHEA-COMP:10001, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17359, ChEBI:CHEBI:29919, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738; EC=1.8.7.1; Evidence={ECO:0000269|PubMed:10506201, ECO:0000269|PubMed:10712553};
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.7 uM for ferredoxin {ECO:0000269|PubMed:10506201, ECO:0000269|PubMed:11132635, ECO:0000269|PubMed:14871491, ECO:0000269|PubMed:16469743}; KM=1 mM for nitrite {ECO:0000269|PubMed:10506201, ECO:0000269|PubMed:11132635, ECO:0000269|PubMed:14871491, ECO:0000269|PubMed:16469743};
null
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5. {ECO:0000269|PubMed:10506201, ECO:0000269|PubMed:11132635, ECO:0000269|PubMed:14871491, ECO:0000269|PubMed:16469743};
null
FUNCTION: Essential protein with sulfite reductase activity required in assimilatory sulfate reduction pathway during both primary and secondary metabolism and thus involved in development and growth. {ECO:0000269|PubMed:10712553, ECO:0000269|PubMed:11163356, ECO:0000269|PubMed:14871491, ECO:0000269|PubMed:17371503}.; FUNCTION: DNA-binding protein that binds to both double-stranded and single-stranded DNA without significant sequence specificity to reversibly repress the transcriptional activity of chloroplast nucleoids by promoting DNA compaction and possibly regulate DNA replication. {ECO:0000269|PubMed:11163356}.
Zea mays (Maize)
O23887
ALDO1_MAIZE
MGKEAGAAESSTVVLAVNGKRYEAAGVAPSTSLLEFLRTQTPVRGPKLGCGEGGCGACVVLVSKYDPATDEVTEFSASSCLTLLHSVDRCSVTTSEGIGNTRDGYHPVQQRLSGFHASQCGFCTPGMCMSIFSALVKADNKSDRPDPPAGFSKITTSEAEKAVSGNLCRCTGYRPIVDTCKSFASDVDLEDLGLNCFWKKGEEPAEVSRLPGYNSGAVCTFPEFLKSEIKSTMKQVNDVPIAASGDGWYHPKSIEELHRLFDSSWFDDSSVKIVASNTGSGVYKDQDLYDKYIDIKGIPELSVINKNDKAIELGSVVSISKAIEVLSDGNLVFRKIADHLNKVASPFVRNTATIGGNIMMAQRLPFESDVATVLLAAGSTVTVQVASKRLCFTLEEFLEQPPCDSRTLLLSIFIPEWGSDYVTFETFRAAPRPFGNAVSYVNSAFLARTSGSLLIEDICLAFGAYGVDHAIRAKKVEDFLKGKSLSSFVILEAIKLLKDTVSPSEGTTHHEYRVSLAVSFLFSFLSSLANSSSAPSNIDTPNGSYTHETGSNVDSPERHIKVDSNDLPIRSRQEMVFSDEYKPVGKPIKKVGAEIQASGEAVYVDDIPAPKDCLYGAFIYSTHPHAHVRSINFKSSLASQKVITVITAKDIPSGGENIGSSFLMQGEALFADPIAEFAGQNIGVVIAETQRYANMAAKQAVVEYSTENLQPPILTIEDAIQRNSYIQIPPFLAPKPVGDYNKGMAEADHKILSAEVKLESQYYFYMETQAALAIPDEDNCITIYSSTQMPELTQNLIARCLGIPFHNVRVISRRVGGGFGGKAMKATHTACACALAAFKLRRPVRMYLDRKTDMIMAGGRHPMKAKYSVGFKSDGKITALHLDLGINAGISPDVSPLMPRAIIGALKKYNWGTLEFDTKVCKTNVSSKSAMRAPGDVQGSFIAEAIIEHVASALALDTNTVRRKNLHDFESLEVFYGESAGEASTYSLVSMFDKLALSPEYQHRAAMIEQFNSSNKWKKRGISCVPATYEVNLRPTPGKVSIMNDGSIAVEVGGIEIGQGLWTKVKQMTAFGLGQLCPDGGECLLDKVRVIQADTLSLIQGGMTAGSTTSETSCETVRQSCVALVEKLNPIKESLEAKSNTVEWSALIAQASMASVNLSAQPYWTPDPSFKSYLNYGAGTSEVEVDILTGATTILRSDLVYDCGQSLNPAVDLGQIEGCFVQGIGFFTNEDYKTNSDGLVIHDGTWTYKIPTVDNIPKEFNVEMFNSAPDKKRVLSSKASGEPPLVLATSVHCAMREAIRAARKEFSVSTSPAKSAVTFQMDVPATMPVVKELCGLDVVERYLENVSAASAGPNTAKA
1.2.3.7
COFACTOR: Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; Evidence={ECO:0000250}; Note=Binds 2 [2Fe-2S] clusters. {ECO:0000250}; COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|PubMed:12226218}; COFACTOR: Name=Mo-molybdopterin; Xref=ChEBI:CHEBI:71302; Evidence={ECO:0000305|PubMed:12226218}; Note=Binds 1 Mo-molybdopterin (Mo-MPT) cofactor per subunit. {ECO:0000305|PubMed:12226218};
abscisic acid biosynthetic process [GO:0009688]; auxin biosynthetic process [GO:0009851]
cytoplasm [GO:0005737]
2 iron, 2 sulfur cluster binding [GO:0051537]; FAD binding [GO:0071949]; indole-3-acetaldehyde oxidase activity [GO:0050302]; iron ion binding [GO:0005506]; molybdopterin cofactor binding [GO:0043546]; oxidoreductase activity [GO:0016491]
PF01315;PF03450;PF00941;PF00111;PF01799;PF02738;PF20256;
3.10.20.30;3.30.465.10;1.10.150.120;3.90.1170.50;3.30.365.10;3.30.390.50;
Xanthine dehydrogenase family
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CATALYTIC ACTIVITY: Reaction=H2O + indole-3-acetaldehyde + O2 = (indol-3-yl)acetate + H(+) + H2O2; Xref=Rhea:RHEA:16277, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:18086, ChEBI:CHEBI:30854; EC=1.2.3.7; Evidence={ECO:0000269|PubMed:12226218};
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=3.2 uM for (indol-3-yl)acetaldehyde (at pH 7.4 and 30 degrees Celsius, with O2 as electron acceptor) {ECO:0000269|PubMed:12226218}; KM=4.5 uM for indol-3-aldehyde (at pH 7.4 and 30 degrees Celsius, with O2 as electron acceptor) {ECO:0000269|PubMed:12226218}; KM=1.5 uM for benzaldehyde (at pH 7.4 and 30 degrees Celsius, with O2 as electron acceptor) {ECO:0000269|PubMed:12226218}; KM=2.9 uM for protocatechualdehyde (at pH 7.4 and 30 degrees Celsius, with O2 as electron acceptor) {ECO:0000269|PubMed:12226218}; KM=5 uM for (indol-3-yl)acetaldehyde (at pH 7.4 and 30 degrees Celsius, with DCIP as electron acceptor) {ECO:0000269|PubMed:12226218}; KM=14 uM for indol-3-aldehyde (at pH 7.4 and 30 degrees Celsius, with DCIP as electron acceptor) {ECO:0000269|PubMed:12226218}; KM=5 uM for benzaldehyde (at pH 7.4 and 30 degrees Celsius, with DCIP as electron acceptor) {ECO:0000269|PubMed:12226218}; KM=26 uM for protocatechualdehyde (at pH 7.4 and 30 degrees Celsius, with DCIP as electron acceptor) {ECO:0000269|PubMed:12226218}; KM=250 uM for phenylacetaldehyde (at pH 7.4 and 30 degrees Celsius, with DCIP as electron acceptor) {ECO:0000269|PubMed:12226218}; KM=26 uM for butyraldehyde (at pH 7.4 and 30 degrees Celsius, with DCIP as electron acceptor) {ECO:0000269|PubMed:12226218}; KM=74 uM for propionaldehyde (at pH 7.4 and 30 degrees Celsius, with DCIP as electron acceptor) {ECO:0000269|PubMed:12226218}; KM=345 uM for acetaldehyde (at pH 7.4 and 30 degrees Celsius, with DCIP as electron acceptor) {ECO:0000269|PubMed:12226218}; Vmax=76 nmol/min/mg enzyme with (indol-3-yl)acetaldehyde as substrate (at pH 7.4 and 30 degrees Celsius, with O2 as electron acceptor) {ECO:0000269|PubMed:12226218}; Vmax=69 nmol/min/mg enzyme with indol-3-aldehyde as substrate (at pH 7.4 and 30 degrees Celsius, with O2 as electron acceptor) {ECO:0000269|PubMed:12226218}; Vmax=453 nmol/min/mg enzyme with benzaldehyde as substrate (at pH 7.4 and 30 degrees Celsius, with O2 as electron acceptor) {ECO:0000269|PubMed:12226218}; Vmax=175 nmol/min/mg enzyme with protocatechualdehyde as substrate (at pH 7.4 and 30 degrees Celsius, with O2 as electron acceptor) {ECO:0000269|PubMed:12226218}; Vmax=28 nmol/min/mg enzyme with (indol-3-yl)acetaldehyde as substrate (at pH 7.4 and 30 degrees Celsius, with DCIP as electron acceptor) {ECO:0000269|PubMed:12226218}; Vmax=190 nmol/min/mg enzyme with indol-3-aldehyde as substrate (at pH 7.4 and 30 degrees Celsius, with DCIP as electron acceptor) {ECO:0000269|PubMed:12226218}; Vmax=247 nmol/min/mg enzyme with benzaldehyde as substrate (at pH 7.4 and 30 degrees Celsius, with DCIP as electron acceptor) {ECO:0000269|PubMed:12226218}; Vmax=316 nmol/min/mg enzyme with protocatechualdehyde as substrate (at pH 7.4 and 30 degrees Celsius, with DCIP as electron acceptor) {ECO:0000269|PubMed:12226218}; Vmax=120 nmol/min/mg enzyme with phenylacetaldehyde as substrate (at pH 7.4 and 30 degrees Celsius, with DCIP as electron acceptor) {ECO:0000269|PubMed:12226218}; Vmax=113 nmol/min/mg enzyme with butyraldehyde as substrate (at pH 7.4 and 30 degrees Celsius, with DCIP as electron acceptor) {ECO:0000269|PubMed:12226218}; Vmax=70 nmol/min/mg enzyme with propionaldehyde as substrate (at pH 7.4 and 30 degrees Celsius, with DCIP as electron acceptor) {ECO:0000269|PubMed:12226218}; Vmax=57 nmol/min/mg enzyme with acetaldehyde as substrate (at pH 7.4 and 30 degrees Celsius, with DCIP as electron acceptor) {ECO:0000269|PubMed:12226218};
null
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7-8. {ECO:0000269|PubMed:12226218};
null
FUNCTION: In higher plants aldehyde oxidases (AO) appear to be homo- and heterodimeric assemblies of AO subunits with probably different physiological functions. Involved in the biosynthesis of auxin from (indol-3-yl)acetaldehyde. Can also use indole-3-aldehyde and benzaldehyde as substrate. {ECO:0000269|PubMed:12226218}.
Zea mays (Maize)
O24006
AMP_IMPBA
MVQKGVVFGVLLILFICSTLTSADSKPNPTKEEEPAKKPDEVSVKSGGPEVSEDQYRHRCCAWGPGRKYCKRWCANAEEAAAAIPEASEELAQEEAPVYSEDQWGRRCCGWGPGRRYCVRWCQNAEEAAAAIPEATEKAQEAPVYSEDQWGRRCCGWGPGRRYCVRWCQNAEEAAAAVAIPEASEKAQEGPVYSEDQWGRRCCGWGPGRRYCVRWCSNAADEVATPEDVEPGQYGRRCCNWGPGRRYCKRWCHNAAEEATLKAFEEEAAREQPVYSEDQWGRRCCGWGPGRRYCRRWCQSAEEAAAFQAGEVTASLMLIMFKACPCMGPVPSV
null
null
defense response to bacterium [GO:0042742]; defense response to fungus [GO:0050832]; killing of cells of another organism [GO:0031640]
extracellular region [GO:0005576]
null
null
null
null
PTM: The N-terminal of all peptides are blocked.; PTM: The 4 cysteine residues of all peptides are involved in intrachain disulfide bonds.
SUBCELLULAR LOCATION: Secreted.
null
null
null
null
null
FUNCTION: Plays a role in the defense of the germinating seed against microorganisms, by inhibiting the growth of a range of filamentous fungi and bacteria, especially Gram-positive bacteria. Not cytotoxic for cultured human cells and are the smallest known plant-derived antimicrobial peptides. Peptide IB-AMP4 has a higher antifungal activity than IB-AMP1.
Impatiens balsamina (Balsam)
O24023
NCED1_SOLLC
MATTTSHATNTWIKTKLSMPSSKEFGFASNSISLLKNQHNRQSLNINSSLQAPPILHFPKQSSNYQTPKNNTISHPKQENNNSSSSSTSKWNLVQKAAAMALDAVESALTKHELEHPLPKTADPRVQISGNFAPVPENPVCQSLPVTGKIPKCVQGVYVRNGANPLFEPTAGHHFFDGDGMVHAVQFKNGSASYACRFTETERLVQEKALGRPVFPKAIGELHGHSGIARLMLFYARGLFGLVDHSKGTGVANAGLVYFNNRLLAMSEDDLPYHVKVTPTGDLKTEGRFDFDGQLKSTMIAHPKLDPVSGELFALSYDVIQKPYLKYFRFSKNGEKSNDVEIPVEDPTMMHDFAITENFVVIPDQQVVFKMSEMIRGGSPVVYDKNKVSRFGILDKYAKDGSDLKWVEVPDCFCFHLWNAWEEAETDEIVVIGSCMTPPDSIFNECDEGLKSVLSEIRLNLKTGKSTRKSIIENPDEQVNLEAGMVNRNKLGRKTEYAYLAIAEPWPKVSGFAKVNLFTGEVEKFIYGDNKYGGEPLFLPRDPNSKEEDDGYILAFVHDEKEWKSELQIVNAMSLKLEATVKLPSRVPYGFHGTFINANDLANQA
1.13.11.51
COFACTOR: Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000250|UniProtKB:O24592}; Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000250|UniProtKB:O24592};
abscisic acid biosynthetic process [GO:0009688]; abscisic acid-activated signaling pathway [GO:0009738]; anther development [GO:0048653]; beta-carotene biosynthetic process [GO:1901812]; carotene catabolic process [GO:0016121]; fruit ripening [GO:0009835]; lycopene biosynthetic process [GO:1901177]; pollen development [GO:0009555]; pollination [GO:0009856]; response to abscisic acid [GO:0009737]; response to auxin [GO:0009733]; response to gibberellin [GO:0009739]; response to salicylic acid [GO:0009751]; response to salt stress [GO:0009651]; response to water deprivation [GO:0009414]; xanthophyll biosynthetic process [GO:0016123]
chloroplast stroma [GO:0009570]
9-cis-epoxycarotenoid dioxygenase activity [GO:0045549]; carotenoid dioxygenase activity [GO:0010436]; metal ion binding [GO:0046872]
PF03055;
null
Carotenoid oxygenase family
null
SUBCELLULAR LOCATION: Plastid, chloroplast stroma {ECO:0000250|UniProtKB:Q9LRR7}. Note=Partially bound to the thylakoid. {ECO:0000250|UniProtKB:Q9LRR7}.
CATALYTIC ACTIVITY: Reaction=a 9-cis-epoxycarotenoid + O2 = 2-cis,4-trans-xanthoxin + a 12'-apo-carotenal; Xref=Rhea:RHEA:23328, ChEBI:CHEBI:15379, ChEBI:CHEBI:32304, ChEBI:CHEBI:51972, ChEBI:CHEBI:51973; EC=1.13.11.51; Evidence={ECO:0000250|UniProtKB:Q9LRR7}; CATALYTIC ACTIVITY: Reaction=9-cis-violaxanthin + O2 = (3S,5R,6S)-5,6-epoxy-3-hydroxy-5,6-dihydro-12'-apo-beta-caroten-12'-al + 2-cis,4-trans-xanthoxin; Xref=Rhea:RHEA:16541, ChEBI:CHEBI:15379, ChEBI:CHEBI:32304, ChEBI:CHEBI:34597, ChEBI:CHEBI:35305; EC=1.13.11.51; Evidence={ECO:0000250|UniProtKB:Q9LRR7}; CATALYTIC ACTIVITY: Reaction=9'-cis-neoxanthin + O2 = (3S,5R,6R)-3,5-dihydroxy-6,7-didehydro-5,6-dihydro-12'-apo-beta-caroten-12'-al + 2-cis,4-trans-xanthoxin; Xref=Rhea:RHEA:19677, ChEBI:CHEBI:15379, ChEBI:CHEBI:32304, ChEBI:CHEBI:34596, ChEBI:CHEBI:35306; EC=1.13.11.51; Evidence={ECO:0000250|UniProtKB:Q9LRR7};
null
PATHWAY: Plant hormone biosynthesis; abscisate biosynthesis. {ECO:0000269|Ref.2}.
null
null
FUNCTION: Has a 11,12(11',12') 9-cis epoxycarotenoid cleavage activity. Catalyzes the first step of abscisic-acid (ABA) biosynthesis from carotenoids. Required for ABA accumulation upon drought (Ref.2). Required for ABA-mediated regulation of anther/pollen development, including metabolism, cell wall modification and transcription level (PubMed:29632966). Positive regulator of fruit ripening involved in the biosynthesis of abscisic acid (ABA); initiates ABA biosynthesis at the onset of fruit ripening (PubMed:19246595, PubMed:22108525, PubMed:25039074). Modulates the degree of pigmentation and carotenoid composition as well as pectin catabolism during ripening and may regulate the ethylene production and action in climacteric tomato fruit (PubMed:22108525, PubMed:22345638). {ECO:0000269|PubMed:19246595, ECO:0000269|PubMed:22108525, ECO:0000269|PubMed:22345638, ECO:0000269|PubMed:25039074, ECO:0000269|PubMed:29632966, ECO:0000269|Ref.2}.
Solanum lycopersicum (Tomato) (Lycopersicon esculentum)
O24144
CAMT1_TOBAC
MATNGRHQEVGHKSLLQSDALYQYILETSVYPREPEPMKELREITAKHPWNLMTTSADEGQFLSMLIKLINAKNTMEIGVFTGYSLLATAMALPDDGKILAMDINRENYEIGLPVIEKAGLAHKIEFKEGPALPVLDQMIEDGKYHGSYDFIFVDADKDNYLNYHKRLIDLVKIGGLIGYDNTLWNGSVVAPPDAPLRKYVRYYRDFVLELNKALAADSRIEICQLPVGDGITLCRRIS
2.1.1.104
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Note=Binds 1 Mg(2+) ion per subunit.;
lignin biosynthetic process [GO:0009809]; methylation [GO:0032259]
null
caffeoyl-CoA O-methyltransferase activity [GO:0042409]; metal ion binding [GO:0046872]; S-adenosylmethionine-dependent methyltransferase activity [GO:0008757]
PF01596;
3.40.50.150;
Class I-like SAM-binding methyltransferase superfamily, Cation-dependent O-methyltransferase family, CCoAMT subfamily
null
null
CATALYTIC ACTIVITY: Reaction=(E)-caffeoyl-CoA + S-adenosyl-L-methionine = (E)-feruloyl-CoA + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:16925, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:87136, ChEBI:CHEBI:87305; EC=2.1.1.104;
null
PATHWAY: Aromatic compound metabolism; phenylpropanoid biosynthesis.
null
null
FUNCTION: Methylates caffeoyl-CoA to feruloyl-CoA and 5-hydroxyferuloyl-CoA to sinapoyl-CoA. Plays a role in the synthesis of feruloylated polysaccharides. Involved in the reinforcement of the plant cell wall. Also involved in the responding to wounding or pathogen challenge by the increased formation of cell wall-bound ferulic acid polymers.
Nicotiana tabacum (Common tobacco)
O24146
4CL2_TOBAC
MEKDTKQVDIIFRSKLPDIYIPNHLPLHSYCFENISEFSSRPCLINGANKQIYTYADVELNSRKVAAGLHKQGIQPKDTIMILLPNSPEFVFAFIGASYLGAISTMANPLFTPAEVVKQAKASSAKIIVTQACHVNKVKDYAFENDVKIICIDSAPEGCLHFSVLTQANEHDIPEVEIQPDDVVALPYSSGTTGLPKGVMLTHKGLVTSVAQQVDGENPNLYIHSEDVMLCVLPLFHIYSLNSVLLCGLRVGAAILIMQKFDIVSFLELIQRYKVTIGPFVPPIVLAIAKSPMVDDYDLSSVRTVMSGAAPLGKELEDTVRAKFPNAKLGQGYGMTEAGPVLAMCLAFAKEPFEIKSGACGTVVRNAEMKIVDPKTGNSLPRNQSGEICIRGDQIMKGYLNDPEATARTIDKEGWLYTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLLNHPNISDAAVVPMKDEQAGEVPVAFVVRSNGSTITEDEVKDFISKQVIFYKRIKRVFFVDAIPKSPSGKILRKDLRAKLAAGLPN
6.2.1.-; 6.2.1.12; 6.2.1.34
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:26412334};
phenylpropanoid metabolic process [GO:0009698]; response to jasmonic acid [GO:0009753]; response to wounding [GO:0009611]
null
(E)-caffeate-CoA ligase activity [GO:0106286]; 4-coumarate-CoA ligase activity [GO:0016207]; ATP binding [GO:0005524]; CoA-ligase activity [GO:0016405]; trans-cinnamate-CoA ligase activity [GO:0106290]; trans-feruloyl-CoA synthase activity [GO:0050563]
PF00501;PF13193;
3.30.300.30;3.40.50.12780;
ATP-dependent AMP-binding enzyme family
null
null
CATALYTIC ACTIVITY: Reaction=(E)-4-coumarate + ATP + CoA = (E)-4-coumaroyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:19641, ChEBI:CHEBI:12876, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:85008, ChEBI:CHEBI:456215; EC=6.2.1.12; Evidence={ECO:0000269|PubMed:26412334, ECO:0000269|PubMed:8819324}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19642; Evidence={ECO:0000269|PubMed:26412334, ECO:0000269|PubMed:8819324}; CATALYTIC ACTIVITY: Reaction=(E)-caffeate + ATP + CoA = (E)-caffeoyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:36299, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57770, ChEBI:CHEBI:87136, ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:26412334, ECO:0000269|PubMed:8819324}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36300; Evidence={ECO:0000269|PubMed:26412334, ECO:0000269|PubMed:8819324}; CATALYTIC ACTIVITY: Reaction=(E)-ferulate + ATP + CoA = (E)-feruloyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:36251, ChEBI:CHEBI:29749, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:87305, ChEBI:CHEBI:456215; EC=6.2.1.34; Evidence={ECO:0000269|PubMed:26412334, ECO:0000269|PubMed:8819324}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36252; Evidence={ECO:0000269|PubMed:26412334, ECO:0000269|PubMed:8819324}; CATALYTIC ACTIVITY: Reaction=(E)-cinnamate + ATP + CoA = (E)-cinnamoyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:64788, ChEBI:CHEBI:15669, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57252, ChEBI:CHEBI:57287, ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:8819324}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64789; Evidence={ECO:0000269|PubMed:8819324}; CATALYTIC ACTIVITY: Reaction=(E)-4-coumarate + ATP + H(+) = (E)-4-coumaroyl-AMP + diphosphate; Xref=Rhea:RHEA:72419, ChEBI:CHEBI:12876, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:192348; Evidence={ECO:0000269|PubMed:26412334}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:72420; Evidence={ECO:0000269|PubMed:26412334}; CATALYTIC ACTIVITY: Reaction=(E)-4-coumaroyl-AMP + CoA = (E)-4-coumaroyl-CoA + AMP + H(+); Xref=Rhea:RHEA:72423, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:85008, ChEBI:CHEBI:192348, ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:26412334}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:72424; Evidence={ECO:0000269|PubMed:26412334}; CATALYTIC ACTIVITY: Reaction=(E)-caffeate + ATP + H(+) = (E)-caffeoyl-AMP + diphosphate; Xref=Rhea:RHEA:72431, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57770, ChEBI:CHEBI:192349; Evidence={ECO:0000269|PubMed:26412334}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:72432; Evidence={ECO:0000269|PubMed:26412334}; CATALYTIC ACTIVITY: Reaction=(E)-caffeoyl-AMP + CoA = (E)-caffeoyl-CoA + AMP + H(+); Xref=Rhea:RHEA:72435, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:87136, ChEBI:CHEBI:192349, ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:26412334}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:72436; Evidence={ECO:0000269|PubMed:26412334}; CATALYTIC ACTIVITY: Reaction=(E)-ferulate + ATP + H(+) = (E)-feruloyl-AMP + diphosphate; Xref=Rhea:RHEA:72439, ChEBI:CHEBI:15378, ChEBI:CHEBI:29749, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:192350; Evidence={ECO:0000269|PubMed:26412334}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:72440; Evidence={ECO:0000269|PubMed:26412334}; CATALYTIC ACTIVITY: Reaction=(E)-feruloyl-AMP + CoA = (E)-feruloyl-CoA + AMP + H(+); Xref=Rhea:RHEA:72443, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:87305, ChEBI:CHEBI:192350, ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:26412334}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:72444; Evidence={ECO:0000269|PubMed:26412334};
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.5 uM for (E)-4-coumarate {ECO:0000269|PubMed:26412334}; KM=1 uM for (E)-caffeate {ECO:0000269|PubMed:26412334}; KM=2.9 uM for (E)-ferulate {ECO:0000269|PubMed:26412334}; KM=1321.9 uM for (E)-sinapate {ECO:0000269|PubMed:26412334}; Note=kcat is 3.978 sec(-1) with (E)-4-coumarate as substrate (PubMed:26412334). kcat is 2.652 sec(-1) with (E)-caffeate as substrate (PubMed:26412334). kcat is 3.576 sec(-1) with (E)-ferulate as substrate (PubMed:26412334). kcat is 0.018 sec(-1) with (E)-sinapate as substrate (PubMed:26412334). {ECO:0000269|PubMed:26412334};
PATHWAY: Phytoalexin biosynthesis; 3,4',5-trihydroxystilbene biosynthesis; 3,4',5-trihydroxystilbene from trans-4-coumarate: step 1/2. {ECO:0000305|PubMed:26412334}.
null
null
FUNCTION: Major enzyme of the phenylpropanoid pathway that mediates the production of several precursors for numerous metabolites and regulates carbon flow (PubMed:26412334). Catalyzes the formation of CoA thioesters using 4-coumarate, ferulate, caffeate, and cinnamate as substrates (PubMed:26412334, PubMed:8819324). Follows a two-step reaction mechanism, wherein a (hydroxy)cinnamate substrate first undergoes adenylation by ATP leading to an acyl-AMP, followed by a thioesterification in the presence of CoA to yield the final (hydroxy)cinnamoyl-CoA product (PubMed:26412334). Almost inactive toward sinapate (PubMed:26412334, PubMed:8819324). {ECO:0000269|PubMed:26412334, ECO:0000269|PubMed:8819324}.
Nicotiana tabacum (Common tobacco)
O24164
PPOM_TOBAC
MAPSAGEDKHSSAKRVAVIGAGVSGLAAAYKLKIHGLNVTVFEAEGKAGGKLRSVSQDGLIWDEGANTMTESEGDVTFLIDSLGLREKQQFPLSQNKRYIARNGTPVLLPSNPIDLIKSNFLSTGSKLQMLLEPILWKNKKLSQVSDSHESVSGFFQRHFGKEVVDYLIDPFVAGTCGGDPDSLSMHHSFPELWNLEKRFGSVILGAIRSKLSPKNEKKQGPPKTSANKKRQRGSFSFLGGMQTLTDAICKDLREDELRLNSRVLELSCSCTEDSAIDSWSIISASPHKRQSEEESFDAVIMTAPLCDVKSMKIAKRGNPFLLNFIPEVDYVPLSVVITTFKRENVKYPLEGFGVLVPSKEQQHGLKTLGTLFSSMMFPDRAPNNVYLYTTFVGGSRNRELAKASRTELKEIVTSDLKQLLGAEGEPTYVNHLYWSKAFPLYGHNYDSVLDAIDKMEKNLPGLFYAGNHRGGLSVGKALSSGCNAADLVISYLESVSTDSKRHC
1.3.3.4
COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|PubMed:15057273}; Note=Binds 1 FAD per subunit. {ECO:0000269|PubMed:15057273};
heme biosynthetic process [GO:0006783]; protoporphyrinogen IX biosynthetic process [GO:0006782]
chloroplast [GO:0009507]; mitochondrion [GO:0005739]
oxygen-dependent protoporphyrinogen oxidase activity [GO:0004729]
PF01593;
3.50.50.60;1.10.3110.10;
Protoporphyrinogen/coproporphyrinogen oxidase family, Protoporphyrinogen oxidase subfamily
null
SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:9238074}.
CATALYTIC ACTIVITY: Reaction=3 O2 + protoporphyrinogen IX = 3 H2O2 + protoporphyrin IX; Xref=Rhea:RHEA:25576, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:57306, ChEBI:CHEBI:57307; EC=1.3.3.4;
null
PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; protoporphyrin-IX from protoporphyrinogen-IX: step 1/1.
null
null
FUNCTION: Catalyzes the 6-electron oxidation of protoporphyrinogen-IX to form protoporphyrin-IX. {ECO:0000269|PubMed:9238074}.; FUNCTION: Provides precursor for the mitochondrial and plastidic heme synthesis and the predominant chlorophyll synthesis in plastids. {ECO:0000269|PubMed:9238074}.
Nicotiana tabacum (Common tobacco)
O24174
BADH1_ORYSJ
MAAPSAIPRRGLFIGGGWREPSLGRRLPVVNPATEATIGDIPAATAEDVELAVSAARDAFGRDGGRHWSRAPGAVRAKYLKAIAAKIKDKKSYLALLETLDSGKPLDEAAGDMEDVAACFEYYADLAEALDGKQRAPISLPMENFESYVLKEPIGVVGLITPWNYPLLMATWKVAPALAAGCTAVLKPSELASLTCLELGGICAEIGLPPGVLNIITGLGTEAGAPLASHPHVDKIAFTGSTETGKRIMITASQMVKPVSLELGGKSPLIVFDDVDIDKAVEWAMFGCFANAGQVCSATSRLLLHEKIAKRFLDRLVAWAKSIKISDPLEEGCRLGSVVSEGQYQKIMKFISTARCEGATILYGGARPQHLKRGFFIEPTIITNVSTSMQIWREEVFGPVICVKEFRTEREAVELANDTHYGLAGAVISNDLERCERISKAIQSGIVWINCSQPCFVQAPWGGNKRSGFGRELGQWGLDNYLSVKQVTKYCSDEPYGWYRPPSKL
1.2.1.8
null
cellular response to anoxia [GO:0071454]; glycine betaine biosynthetic process from choline [GO:0019285]
peroxisome [GO:0005777]
betaine-aldehyde dehydrogenase activity [GO:0008802]
PF00171;
null
Aldehyde dehydrogenase family
null
SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:19850038}.
CATALYTIC ACTIVITY: Reaction=betaine aldehyde + H2O + NAD(+) = glycine betaine + 2 H(+) + NADH; Xref=Rhea:RHEA:15305, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15710, ChEBI:CHEBI:17750, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.2.1.8; Evidence={ECO:0000269|PubMed:18704694};
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=420 uM for N-acetyl-gamma-aminobutyraldehyde (NAGABald) {ECO:0000269|PubMed:18704694}; KM=545 uM for gamma-guanidinobutyraldehyde (GGBald) {ECO:0000269|PubMed:18704694}; KM=3 mM for betaine aldehyde {ECO:0000269|PubMed:18704694}; KM=497 uM for gamma-aminobutyraldehyde {ECO:0000269|PubMed:18704694}; KM=1.29 mM for betaine aldehyde (at 30 degrees Celsius) {ECO:0000269|PubMed:22534193}; KM=432 uM for gamma-aminobutyraldehyde (at 30 degrees Celsius) {ECO:0000269|PubMed:22534193}; KM=99 uM for acetaldehyde (at 30 degrees Celsius) {ECO:0000269|PubMed:22534193}; KM=2.6 mM for betaine aldehyde {ECO:0000269|PubMed:19850038}; KM=4.5 uM for 4-aminobutyraldehyde (AB-ald) {ECO:0000269|PubMed:19850038}; KM=17 uM for 3-aminopropionaldehyde (AP-ald) {ECO:0000269|PubMed:19850038}; KM=7.8 uM for 4-N-trimethylaminobutyraldehyde (TMAB-ald) {ECO:0000269|PubMed:19850038}; KM=35 uM for 3-N-trimethylaminopropionaldehyde (TMAP-ald) {ECO:0000269|PubMed:19850038}; KM=130 uM for acetaldehyde {ECO:0000269|PubMed:19850038}; Vmax=0.71 umol/min/mg enzyme with acetaldehyde as substrate {ECO:0000269|PubMed:19850038};
PATHWAY: Amine and polyamine biosynthesis; betaine biosynthesis via choline pathway; betaine from betaine aldehyde: step 1/1.
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 9.5. {ECO:0000269|PubMed:18704694, ECO:0000269|PubMed:19850038, ECO:0000269|PubMed:22534193};
null
FUNCTION: Dehydrogenase that can use N-acetyl-gamma-aminobutyraldehyde (NAGABald), gamma-guanidinobutyraldehyde (GGBald), betaine aldehyde (Bet-ald), gamma-aminobutyraldehyde (GAB-ald), acetaldehyde, 4-aminobutylaldehyde (AB-ald), 3-aminopropionaldehyde (AP-ald), 4-N-trimethylaminobutyraldehyde (TMAB-ald) and 3-N-trimethylaminopropionaldehyde (TMAP-ald) as substrates. Catalyzes the oxidation of GAB-ald more efficiently than Bet-ald. May convert acetaldehyde into acetate, thus facilitating the production of acetyl-CoA in peroxisomes under anaerobic conditions. {ECO:0000269|PubMed:18704694, ECO:0000269|PubMed:19850038, ECO:0000269|PubMed:22534193}.
Oryza sativa subsp. japonica (Rice)
O24370
LOX21_SOLTU
MLKPQLQQSSQSTKALIPSWNTNPLFLASFPINILNKNFRLKKKNNFRVHHNYNGASTTKAVLSSTEKATGVKAVVTVQKQVNLNLSRGLDDIGDLLGKSLLLWIVAAELDHKTGIEKPGIRAYAHRGRDVDGDTHYEADFVIPQDFGEVGAILIENEHHKEMYVKNIVIDGFVHGKVEITCNSWVHSKFDNPDKRIFFTNKSYLPSQTPSGVSRLREEELVTLRGDGIGERKVFERIYDYDVYNDLGEADSNNDDAKRPVLGGKELPYPRRCKTGRPRSKKDPLSETRSTFVYVPRDEAFSEVKSVAFSGNTVYSVLHAVVPALESVVTDPNLGFPHFPAIDSLFNVGVDLPGLGDKKSGLFNVVPRLIKAISDTRKDVLLFESPQLVQRDKFSWFRDVEFARQTLAGLNPYSIRLVTEWPLRSKLDPKVYGPPESEITKELIEKEIGNYMTVEQAVQQKKLFILDYHDLLLPYVNKVNELKGSMLYGSRTIFFLTPQGTLKPLAIELTRPPVDDKPQWKEVYSPNDWNATGAWLWKLAKAHVLSHDSGYHQLVSHWLRTHCCTEPYIIASNRQLSAMHPIYRLLHPHFRYTMEINALAREALINANGVIESSFFPGKYAIELSSIAYGAEWRFDQEALPQNLISRGLAVEDPNEPHGLKLAIEDYPFANDGLVLWDILKQWVTNYVNHYYPQTNLIESDKELQAWWSEIKNVGHGDKRDEPWWPELKTPNDLIGIITTIVWVTSGHHAAVNFGQYSYAGYFPNRPTVARSKMPTEDPTAEEWEWFMNKPEEALLRCFPSQIQATKVMAILDVLSNHSPDEEYIGEKIEPYWAEDPVINAAFEVFSGKLKELEGIIDARNNDSKLSNRNGAGVMPYELLKPYSEPGVTGKGVPYSISI
1.13.11.12
COFACTOR: Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000255|PROSITE-ProRule:PRU00726}; Note=Binds 1 Fe cation per subunit. {ECO:0000255|PROSITE-ProRule:PRU00726};
fatty acid biosynthetic process [GO:0006633]; green leaf volatile biosynthetic process [GO:0010597]; lipid oxidation [GO:0034440]; oxylipin biosynthetic process [GO:0031408]
chloroplast stroma [GO:0009570]; chloroplast thylakoid [GO:0009534]
linoleate 13S-lipoxygenase activity [GO:0016165]; metal ion binding [GO:0046872]; oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen [GO:0016702]
PF00305;PF01477;
3.10.450.60;2.60.60.20;
Lipoxygenase family
null
SUBCELLULAR LOCATION: Plastid, chloroplast stroma {ECO:0000269|PubMed:11675388, ECO:0000269|PubMed:17210991}. Plastid, chloroplast thylakoid {ECO:0000269|PubMed:17210991}. Note=Associated with the non-appressed part of the thylakoid membrane. {ECO:0000269|PubMed:17210991}.
CATALYTIC ACTIVITY: Reaction=(9Z,12Z)-octadecadienoate + O2 = (13S)-hydroperoxy-(9Z,11E)-octadecadienoate; Xref=Rhea:RHEA:22780, ChEBI:CHEBI:15379, ChEBI:CHEBI:30245, ChEBI:CHEBI:57466; EC=1.13.11.12; Evidence={ECO:0000269|PubMed:11675388, ECO:0000269|PubMed:8702864}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22781; Evidence={ECO:0000269|PubMed:8702864}; CATALYTIC ACTIVITY: Reaction=(9Z,12Z,15Z)-octadecatrienoate + O2 = (13S)-hydroperoxy-(9Z,11E,15Z)-octadecatrienoate; Xref=Rhea:RHEA:34495, ChEBI:CHEBI:15379, ChEBI:CHEBI:32387, ChEBI:CHEBI:58757; EC=1.13.11.12; Evidence={ECO:0000269|PubMed:11675388, ECO:0000269|PubMed:8702864}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:34496; Evidence={ECO:0000269|PubMed:8702864};
null
PATHWAY: Lipid metabolism; oxylipin biosynthesis. {ECO:0000255|PROSITE-ProRule:PRU00726, ECO:0000269|PubMed:11675388, ECO:0000269|PubMed:8702864}.
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.0. {ECO:0000269|PubMed:8702864};
null
FUNCTION: Plant lipoxygenase involved in a number of diverse aspects of plant physiology including growth and development, pest resistance, and senescence. May not be involved in the bulk production of jasmonate upon wounding. Catalyzes the hydroperoxidation of lipids containing a cis,cis-1,4-pentadiene structure. Linolenic acid is the preferred substrate, before linoleic and arachidonic acids. Has also some activity with phosphatidylglycerol, but not with galactolipids. {ECO:0000269|PubMed:11675388, ECO:0000269|PubMed:8702864}.
Solanum tuberosum (Potato)
O24371
LOX31_SOLTU
MALAKEIMGISLLEKSSSFMNSSSMALFNPNNYHKENHLWFNQQFQGRRNLSRRKAFRQSTMAAISENLIKVVPEKAVRFKVRAVVTVRNKNKEDLKETIVKHLDAFTDKIGRNVTLELISTDMDPNTKGPKKSNQAVLKDWSKKSNLKTERVNYTAEFIVDSNFGNPGAITVTNKHQQEFFLESITIEGFACGPVHFPCNSWVQPKKDHPGKRIFFSNQPYLPDETPAGLKSLRERELRDLRGDGKGVRKLSDRIYDYDIYNDLGNPDKGIDFARPKLGGDDNVPYPRRCRSGRVPTDTDISAESRVEKPNPTYVPRDEQFEESKMNTFSTSRLKAVLHNLIPSLMASISSNNHDFKGFSDIDNLYSKGLLLKLGLQDEVLKKLPLPKVVSSIKEGDLLKYDTPKILSKDKFAWLRDDEFARQAIAGVNPVSIEKLQFFPPVSKLDPEIYGPQESALKEEHILGHLNGMTVQEALDANKLFIVDHHDVYLPFLDRINALDGRKAYATRTIFFLSDVGTLKPIAIELSLPQTGPSSRSKRVVTPPVCATGNWTWQIAKAHVCANDAGVHQLVNHWLRTHASLEPFILAAHRQLSAMHPIYKLLDPHMRYTLEINGLARQSLINADGVIEACFTPGRYCMEISAAAYKNWRFDLEGLPADLIRRGMAVPDSTQPHGLKLLIEDYPYAADGLMIWGAIESWVRDYVNHYYPSSAQVCSDRELQAWYAETINVGHVDLRNEEWWPTLATPEDLISILTTLIWLASAQHAALNFGQYPYGGYVPNRPPLMRRLIPDENDPEYAVFLADPQKYFFSALPSLLQATKFMAVVDTLSTHSPDEEYLGERHQPSTWTGDAEIVEAFYKFSAEIGRIEKEIDERNANTKLKNRCGAGVLPYELLAPSSGPGVTCRGVPNSVSI
1.13.11.12
COFACTOR: Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000255|PROSITE-ProRule:PRU00726}; Note=Binds 1 Fe cation per subunit. {ECO:0000255|PROSITE-ProRule:PRU00726};
fatty acid biosynthetic process [GO:0006633]; lipid oxidation [GO:0034440]; oxylipin biosynthetic process [GO:0031408]
chloroplast stroma [GO:0009570]; chloroplast thylakoid [GO:0009534]
linoleate 13S-lipoxygenase activity [GO:0016165]; metal ion binding [GO:0046872]; oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen [GO:0016702]
PF00305;PF01477;
3.10.450.60;2.60.60.20;
Lipoxygenase family
null
SUBCELLULAR LOCATION: Plastid, chloroplast stroma. Plastid, chloroplast thylakoid.
CATALYTIC ACTIVITY: Reaction=(9Z,12Z)-octadecadienoate + O2 = (13S)-hydroperoxy-(9Z,11E)-octadecadienoate; Xref=Rhea:RHEA:22780, ChEBI:CHEBI:15379, ChEBI:CHEBI:30245, ChEBI:CHEBI:57466; EC=1.13.11.12; Evidence={ECO:0000269|PubMed:8702864}; CATALYTIC ACTIVITY: Reaction=(9Z,12Z,15Z)-octadecatrienoate + O2 = (13S)-hydroperoxy-(9Z,11E,15Z)-octadecatrienoate; Xref=Rhea:RHEA:34495, ChEBI:CHEBI:15379, ChEBI:CHEBI:32387, ChEBI:CHEBI:58757; EC=1.13.11.12; Evidence={ECO:0000269|PubMed:8702864};
null
PATHWAY: Lipid metabolism; oxylipin biosynthesis. {ECO:0000255|PROSITE-ProRule:PRU00726}.
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.0. {ECO:0000269|PubMed:8702864};
null
FUNCTION: Plant lipoxygenases may be involved in a number of diverse aspects of plant physiology including growth and development, pest resistance, and senescence or responses to wounding. Required for the regulation of wound-induced gene expression, but is not involved in the bulk production of jasmonate upon wounding. Catalyzes the hydroperoxidation of lipids containing a cis,cis-1,4-pentadiene structure. Linolenic acid is the preferred substrate, before linoleic and arachidonic acids. {ECO:0000269|PubMed:8702864, ECO:0000269|PubMed:9927708}.
Solanum tuberosum (Potato)
O24379
LOX12_SOLTU
MIGQITSGLFGGPDDSKKLKGTVVMMNKNALDFTDLAGSLTDKAFEFLGQTVSFQLISSVQGDPTNGLQGKHSNPAYLENSLFTLTPLTAGSETAFGVTFDWNEEFGVPGAFIIKNTHINEFFLKSLTLEDVPNHGKVHFVCNSWVYPSFRYKSDRIFFVNQPYLPSKTPELLRKYRENELLTLRGDGTGKREAWDRIYDYDIYNDLGNPDEGKENVRTTLGGSAEYPYPRRGRTGRPPTRTDPKSESRIPLILSLDIYVPRDERFGHLKMSDFLTYALKSIVQFILPELHALFDGTPNEFDSFEDVLRLYEGGIKLPQGPLFKALTAAIPLEMIRELLRTDGEGILRFPTPLVIKDSKTAWRTDEEFAREMLAGVNPVIISRLQEFPPKSKLDPEAYGNQNSTITAEHIEDKLDGLTVDEAMNNNKLFILNHHDVLIPYLRRINTTTTKTYASRTLLFLQDNGSLKPLAIELSLPHPDGDQFGVTSKVYTPSDQGVESSIWQLAKAYVAVNDSGVHQLISHWLNTHAVIEPFVIATNRQLSVLHPIHKLLYPHFRDTMNINAMARQILINAGGVLESTVFQSKFAMEMSAVVYKDWVFPDQALPADLVKRGVAVEDSSSPHGVRLLIEDYPYAVDGLEIWSAIKSWVSDYCSFYYGSDEEILKDNELQAWWKELREVGHGDKKNEPWWPEMERPQELIDSCTTIIWIASALHAAVNFGQYPYAGYLPNRPTVSRRFMPEPGTPEYEELKKNPDKAFLKTITAQLQTLLGVSLIEILSRHTTDEIYLGQRESPEWTKDKEPLAAFDKFGKKLTDIEKQIIQRNGDNILTNRSGPVNAPYTLLFPTSEGGLTGKGIPNSVSI
1.13.11.58
COFACTOR: Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000255|PROSITE-ProRule:PRU00726}; Note=Binds 1 Fe cation per subunit. Iron is tightly bound. {ECO:0000255|PROSITE-ProRule:PRU00726};
fatty acid biosynthetic process [GO:0006633]; lipid oxidation [GO:0034440]; oxylipin biosynthetic process [GO:0031408]
cytoplasm [GO:0005737]
linoleate 13S-lipoxygenase activity [GO:0016165]; linoleate 9S-lipoxygenase activity [GO:1990136]; metal ion binding [GO:0046872]; oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen [GO:0016702]
PF00305;PF01477;
3.10.450.60;2.60.60.20;
Lipoxygenase family
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|PROSITE-ProRule:PRU00726}.
CATALYTIC ACTIVITY: Reaction=(9Z,12Z)-octadecadienoate + O2 = (9S)-hydroperoxy-(10E,12Z)-octadecadienoate; Xref=Rhea:RHEA:30291, ChEBI:CHEBI:15379, ChEBI:CHEBI:30245, ChEBI:CHEBI:60955; EC=1.13.11.58; Evidence={ECO:0000269|PubMed:8702864};
null
PATHWAY: Lipid metabolism; oxylipin biosynthesis. {ECO:0000255|PROSITE-ProRule:PRU00726}.
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.0. {ECO:0000269|PubMed:8702864};
null
FUNCTION: Plant lipoxygenases may be involved in a number of diverse aspects of plant physiology including growth and development, pest resistance, and senescence or responses to wounding. Catalyzes the hydroperoxidation of lipids containing a cis,cis-1,4-pentadiene structure. Linoleic acid is the preferred substrate, but is also active with linolenic and arachidonic acids. {ECO:0000255|PROSITE-ProRule:PRU00726, ECO:0000269|PubMed:8702864}.
Solanum tuberosum (Potato)
O24407
IAA16_ARATH
MINFEATELRLGLPGGNHGGEMAGKNNGKRGFSETVDLKLNLSSTAMDSVSKVDLENMKEKVVKPPAKAQVVGWPPVRSFRKNVMSGQKPTTGDATEGNDKTSGSSGATSSASACATVAYVKVSMDGAPYLRKIDLKLYKTYQDLSNALSKMFSSFTIGNYGPQGMKDFMNESKLIDLLNGSDYVPTYEDKDGDWMLVGDVPWEMFVDSCKRIRIMKGSEAIGLAPRALEKCKNRS
null
null
auxin-activated signaling pathway [GO:0009734]; response to auxin [GO:0009733]
nucleus [GO:0005634]
DNA-binding transcription factor activity [GO:0003700]; identical protein binding [GO:0042802]; transcription cis-regulatory region binding [GO:0000976]
PF02309;
null
Aux/IAA family
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
null
null
null
null
null
FUNCTION: Aux/IAA proteins are short-lived transcriptional factors that function as repressors of early auxin response genes at low auxin concentrations. Repression is thought to result from the interaction with auxin response factors (ARFs), proteins that bind to the auxin-responsive promoter element (AuxRE). Formation of heterodimers with ARF proteins may alter their ability to modulate early auxin response genes expression. {ECO:0000269|PubMed:12036262}.
Arabidopsis thaliana (Mouse-ear cress)
O24408
IAA18_ARATH
MEGYSRNGEISPKLLDLMIPQERRNWFHDEKNSVFKTEEKKLELKLGPPGEEDDDESMIRHMKKEPKDKSILSLAGKYFSPSSTKTTSHKRTAPGPVVGWPPVRSFRKNLASGSSSKLGNDSTTSNGVTLKNQKCDAAAKTTEPKRQGGMFVKINMYGVPIGRKVDLSAHNSYEQLSFTVDKLFRGLLAAQRDFPSSIEDEKPITGLLDGNGEYTLTYEDNEGDKMLVGDVPWQMFVSSVKRLRVIKTSEISSALTYGNGKQEKMRR
null
null
auxin-activated signaling pathway [GO:0009734]; response to auxin [GO:0009733]
nucleus [GO:0005634]
DNA-binding transcription factor activity [GO:0003700]
PF02309;
null
Aux/IAA family
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
null
null
null
null
null
FUNCTION: Aux/IAA proteins are short-lived transcriptional factors that function as repressors of early auxin response genes at low auxin concentrations. Repression is thought to result from the interaction with auxin response factors (ARFs), proteins that bind to the auxin-responsive promoter element (AuxRE). Formation of heterodimers with ARF proteins may alter their ability to modulate early auxin response genes expression. {ECO:0000269|PubMed:12036262}.
Arabidopsis thaliana (Mouse-ear cress)
O24409
IAA19_ARATH
MEKEGLGLEITELRLGLPGRDVAEKMMKKRAFTEMNMTSSGSNSDQCESGVVSSGGDAEKVNDSPAAKSQVVGWPPVCSYRKKNSCKEASTTKVGLGYVKVSMDGVPYLRKMDLGSSQGYDDLAFALDKLFGFRGIGVALKDGDNCEYVTIYEDKDGDWMLAGDVPWGMFLESCKRLRIMKRSDATGFGLQPRGVDE
null
null
auxin-activated signaling pathway [GO:0009734]; response to auxin [GO:0009733]; stamen filament development [GO:0080086]
nucleus [GO:0005634]
DNA-binding transcription factor activity [GO:0003700]; identical protein binding [GO:0042802]
PF02309;
null
Aux/IAA family
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
null
null
null
null
null
FUNCTION: Aux/IAA proteins are short-lived transcriptional factors that function as repressors of early auxin response genes at low auxin concentrations. Repression is thought to result from the interaction with auxin response factors (ARFs), proteins that bind to the auxin-responsive promoter element (AuxRE). Formation of heterodimers with ARF proteins may alter their ability to modulate early auxin response genes expression. {ECO:0000269|PubMed:12036262}.
Arabidopsis thaliana (Mouse-ear cress)
O24410
IAA20_ARATH
MGRGRSSSSSSIESSSKSNPFGASSSTRNLSTDLRLGLSFGTSSGTQYFNGGYGYSVAAPAVEDAEYVAAVEEEEENECNSVGSFYVKVNMEGVPIGRKIDLMSLNGYRDLIRTLDFMFNASILWAEEEDMCNEKSHVLTYADKEGDWMMVGDVPWEMFLSTVRRLKISRANYHY
null
null
auxin-activated signaling pathway [GO:0009734]; cotyledon vascular tissue pattern formation [GO:0010588]; gravitropism [GO:0009630]; response to auxin [GO:0009733]; root development [GO:0048364]; skotomorphogenesis [GO:0009647]
nucleus [GO:0005634]
DNA-binding transcription factor activity [GO:0003700]; identical protein binding [GO:0042802]
PF02309;
null
Aux/IAA family
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
null
null
null
null
null
FUNCTION: Aux/IAA proteins are short-lived transcriptional factors that function as repressors of early auxin response genes at low auxin concentrations. Repression is thought to result from the interaction with auxin response factors (ARFs), proteins that bind to the auxin-responsive promoter element (AuxRE). Formation of heterodimers with ARF proteins may alter their ability to modulate early auxin response genes expression. {ECO:0000269|PubMed:12036262}.
Arabidopsis thaliana (Mouse-ear cress)
O24412
PSD7A_ARATH
MDVIKTQQISARTIEKVVVHPLVLLSIVDHYNRVAKDSSKRVVGVLLGSSSRGVVDVTNSYAVPFEEDDKDPSIWFLDHNYHESMFHMFKRINAKEHVVGWYSTGPKLRENDLDVHALFNGYVPNPVLVIIDVQPKELGIPTKAYYAVEEVKENATQKSQKVFVHVSTEIAAHEVEEIGVEHLLRDVKDTTISTLATEVTAKLTALKGLDARLREIRSYLDLVIEGKLPLNHEILYHLQDVFNLLPNLNVNELVKAFSVKTNDMMLVIYLSSLIRSVIALHNLINNKLLNKEHEKAEDSKPVAIPATS
null
null
innate immune response [GO:0045087]; leaf morphogenesis [GO:0009965]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]
plasma membrane [GO:0005886]; proteasome complex [GO:0000502]; proteasome regulatory particle [GO:0005838]
metallopeptidase activity [GO:0008237]
PF01398;PF13012;
3.40.140.10;
Peptidase M67A family
null
null
null
null
null
null
null
FUNCTION: Acts as a regulatory subunit of the 26S proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins (By similarity). Required for innate immunity. {ECO:0000250, ECO:0000269|PubMed:22577987}.
Arabidopsis thaliana (Mouse-ear cress)
O24456
GBLPA_ARATH
MAEGLVLKGTMRAHTDMVTAIATPIDNADIIVSASRDKSIILWKLTKDDKAYGVAQRRLTGHSHFVEDVVLSSDGQFALSGSWDGELRLWDLAAGVSTRRFVGHTKDVLSVAFSLDNRQIVSASRDRTIKLWNTLGECKYTISEGGEGHRDWVSCVRFSPNTLQPTIVSASWDKTVKVWNLSNCKLRSTLAGHTGYVSTVAVSPDGSLCASGGKDGVVLLWDLAEGKKLYSLEANSVIHALCFSPNRYWLCAATEHGIKIWDLESKSIVEDLKVDLKAEAEKADNSGPAATKRKVIYCTSLNWSADGSTLFSGYTDGVIRVWGIGRY
null
null
cellular response to abscisic acid stimulus [GO:0071215]; gibberellin mediated signaling pathway [GO:0010476]; positive regulation of protein phosphorylation [GO:0001934]; positive regulation of signal transduction [GO:0009967]; regulation of translation [GO:0006417]; rescue of stalled ribosome [GO:0072344]; response to gibberellin [GO:0009739]; response to glucose [GO:0009749]; ribosome biogenesis [GO:0042254]; seed germination [GO:0009845]; vegetative to reproductive phase transition of meristem [GO:0010228]
chloroplast [GO:0009507]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; cytosolic ribosome [GO:0022626]; nucleus [GO:0005634]; ribonucleoprotein complex [GO:1990904]
MAP-kinase scaffold activity [GO:0005078]; molecular adaptor activity [GO:0060090]; mRNA binding [GO:0003729]; protein kinase C binding [GO:0005080]; ribosome binding [GO:0043022]; structural constituent of ribosome [GO:0003735]; translation regulator activity [GO:0045182]
PF00400;
2.130.10.10;
WD repeat G protein beta family, Ribosomal protein RACK1 subfamily
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22068106}. Nucleus {ECO:0000269|PubMed:22068106}. Note=Detected in the cytoplasm and nucleus when interacting with NUDT7.
null
null
null
null
null
FUNCTION: Major component of the RACK1 regulatory proteins that play a role in multiple signal transduction pathways. Involved in multiple hormone responses and developmental processes (PubMed:16829549, PubMed:18715992, PubMed:18947417). MAPK cascade scaffolding protein involved in the protease IV and ArgC signaling pathway but not the flg22 pathway (PubMed:25731164). {ECO:0000269|PubMed:16829549, ECO:0000269|PubMed:18715992, ECO:0000269|PubMed:18947417, ECO:0000269|PubMed:25731164}.
Arabidopsis thaliana (Mouse-ear cress)
O24495
GLO2M_ARATH
MPVISKASSTTTNSSIPSCSRIGGQLCVWPGLRQLCLRKSLLYGVMWLLSMPLKTLRGARKTLKITHFCSISNMPSSLKIELVPCSKDNYAYLLHDEDTGTVGVVDPSEAAPVIEALSRKNWNLTYILNTHHHDDHIGGNAELKERYGAKVIGSAVDKDRIPGIDILLKDSDKWMFAGHEVRILDTPGHTQGHISFYFPGSATIFTGDLIYSLSCGTLSEGTPEQMLSSLQKIVSLPDDTNIYCGRENTAGNLKFALSVEPKNETLQSYATRVAHLRSQGLPSIPTTVKVEKACNPFLRISSKDIRKSLSIPDSATEAEALRRIQRARDRF
3.1.2.6
COFACTOR: Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000250|UniProtKB:O24496}; Name=Fe(3+); Xref=ChEBI:CHEBI:29034; Evidence={ECO:0000250|UniProtKB:O24496}; Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:O24496}; Note=Binds 1 Fe(2+) or Fe(3+) and 1 Zn(2+) ion per subunit. Electron spin resonance indicates the presence of a mixture of protein molecules that contain either Fe(2+) or Zn(2+). {ECO:0000250|UniProtKB:O24496};
antibiotic catabolic process [GO:0017001]; methylglyoxal catabolic process to D-lactate via S-lactoyl-glutathione [GO:0019243]; response to amino acid [GO:0043200]; response to anoxia [GO:0034059]; response to salt stress [GO:0009651]
mitochondrion [GO:0005739]
beta-lactamase activity [GO:0008800]; hydroxyacylglutathione hydrolase activity [GO:0004416]; metal ion binding [GO:0046872]; zinc ion binding [GO:0008270]
PF16123;PF00753;
3.60.15.10;
Metallo-beta-lactamase superfamily, Glyoxalase II family
null
SUBCELLULAR LOCATION: Mitochondrion.
CATALYTIC ACTIVITY: Reaction=an S-(2-hydroxyacyl)glutathione + H2O = a 2-hydroxy carboxylate + glutathione + H(+); Xref=Rhea:RHEA:21864, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57925, ChEBI:CHEBI:58896, ChEBI:CHEBI:71261; EC=3.1.2.6;
null
PATHWAY: Secondary metabolite metabolism; methylglyoxal degradation; (R)-lactate from methylglyoxal: step 2/2.
null
null
FUNCTION: Thiolesterase that catalyzes the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid.
Arabidopsis thaliana (Mouse-ear cress)
O24496
GLO2C_ARATH
MKIFHVPCLQDNYSYLIIDESTGDAAVVDPVDPEKVIASAEKHQAKIKFVLTTHHHWDHAGGNEKIKQLVPDIKVYGGSLDKVKGCTDAVDNGDKLTLGQDINILALHTPCHTKGHISYYVNGKEGENPAVFTGDTLFVAGCGKFFEGTAEQMYQSLCVTLAALPKPTQVYCGHEYTVKNLEFALTVEPNNGKIQQKLAWARQQRQADLPTIPSTLEEELETNPFMRVDKPEIQEKLGCKSPIDTMREVRNKKDQWRG
3.1.2.6
COFACTOR: Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000269|PubMed:19834746}; Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:19834746}; Name=Fe(3+); Xref=ChEBI:CHEBI:29034; Evidence={ECO:0000269|PubMed:19834746}; Note=Binds 1 Fe(2+) or Fe(3+) and 1 Zn(2+) ion per subunit, catalysis is optimal with 1 Fe and 1 Zn. Electron spin resonance indicates the presence of a mixture of protein molecules that contain either Fe(2+) or Fe(3+) and Zn(2+). Mn(2+) is not a cofactor (PubMed:19834746). {ECO:0000269|PubMed:19834746};
methylglyoxal catabolic process to D-lactate via S-lactoyl-glutathione [GO:0019243]
cytosol [GO:0005829]; secretory vesicle [GO:0099503]
hydroxyacylglutathione hydrolase activity [GO:0004416]; metal ion binding [GO:0046872]
PF16123;PF00753;
3.60.15.10;
Metallo-beta-lactamase superfamily, Glyoxalase II family
null
SUBCELLULAR LOCATION: Cytoplasm.
CATALYTIC ACTIVITY: Reaction=an S-(2-hydroxyacyl)glutathione + H2O = a 2-hydroxy carboxylate + glutathione + H(+); Xref=Rhea:RHEA:21864, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57925, ChEBI:CHEBI:58896, ChEBI:CHEBI:71261; EC=3.1.2.6; Evidence={ECO:0000269|PubMed:11085979, ECO:0000269|PubMed:19834746};
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=220 uM for S-D-lactoylglutathion {ECO:0000269|PubMed:14529289};
PATHWAY: Secondary metabolite metabolism; methylglyoxal degradation; (R)-lactate from methylglyoxal: step 2/2.
null
null
FUNCTION: Thiolesterase that catalyzes the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid. {ECO:0000269|PubMed:11085979, ECO:0000269|PubMed:14529289, ECO:0000269|PubMed:19834746}.
Arabidopsis thaliana (Mouse-ear cress)
O24520
HBL1_ARATH
MESEGKIVFTEEQEALVVKSWSVMKKNSAELGLKLFIKIFEIAPTTKKMFSFLRDSPIPAEQNPKLKPHAMSVFVMCCESAVQLRKTGKVTVRETTLKRLGASHSKYGVVDEHFEVAKYALLETIKEAVPEMWSPEMKVAWGQAYDHLVAAIKAEMNLSN
1.7.2.-
COFACTOR: Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000269|PubMed:23485912}; Note=Binds 1 heme group per subunit. {ECO:0000269|PubMed:23485912};
cellular response to hypoxia [GO:0071456]; response to hypoxia [GO:0001666]
cytosol [GO:0005829]; plant-type cell wall [GO:0009505]; plasma membrane [GO:0005886]; plasmodesma [GO:0009506]
heme binding [GO:0020037]; metal ion binding [GO:0046872]; oxygen binding [GO:0019825]
PF00042;
1.10.490.10;
Plant globin family
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:A2XE98}. Nucleus {ECO:0000250|UniProtKB:A2XE98}.
CATALYTIC ACTIVITY: Reaction=Fe(III)-heme b-[protein] + H2O + nitric oxide = Fe(II)-heme b-[protein] + 2 H(+) + nitrite; Xref=Rhea:RHEA:77711, Rhea:RHEA-COMP:18975, Rhea:RHEA-COMP:18976, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16301, ChEBI:CHEBI:16480, ChEBI:CHEBI:55376, ChEBI:CHEBI:60344; Evidence={ECO:0000250|UniProtKB:O04986}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:77713; Evidence={ECO:0000250|UniProtKB:O04986};
null
null
null
null
FUNCTION: Phytoglobin that reduces nitrite to nitric oxide (NO) under anoxic conditions (e.g. during flooding or in waterlogged soil) (By similarity). May not function as an oxygen storage or transport protein (By similarity). Has an unusually high affinity for O(2) through an hexacoordinate heme iron because of a very low dissociation constant (By similarity). {ECO:0000250|UniProtKB:O04986, ECO:0000250|UniProtKB:Q42831}.
Arabidopsis thaliana (Mouse-ear cress)
O24527
SIK1_ARATH
MDHNSPKSRRSRKPEPKPDIYSTFVVHSDSDSDQGRDRDKRKAKPEEDENVDLYATMVYKGDSDGEGEEDDDDDSMLPPLLKRLPKDFGGGASLDYDDDDGDESGDFGTMIVKTDRSSHSKKNSPYSSKPRMGVSPRRRARGGDEESSDEEDEEEDDDDDDGDYGTFVVKSKDKKGKKKDKEIDMTTMGRAVASMQKSNFGGKTRKLDPSSSSSKLHGEDNRKMQQQNSKMSTTSLPDSITREDPTTKYEFLNELGKGSYGSVYKARDLKTSEIVAVKVISLTEGEEGYEEIRGEIEMLQQCNHPNVVRYLGSYQGEDYLWIVMEYCGGGSVADLMNVTEEALEEYQIAYICREALKGLAYLHSIYKVHRDIKGGNILLTEQGEVKLGDFGVAAQLTRTMSKRNTFIGTPHWMAPEVIQENRYDGKVDVWALGVSAIEMAEGLPPRSSVHPMRVLFMISIEPAPMLEDKEKWSLVFHDFVAKCLTKEPRLRPTAAEMLKHKFVERCKTGASAMSPKIEKSRQIRATMALQAQSVVAPSLEDTSTLGPKSSEELGITVPSKPPQNSTEAPLTSTLNRQHITGNTVLAGEGGDFGTMIVHGEDETEESDSRSQLVREKESSSSQFEGVPREFPGEELPDSWIHDKKKPPAIDLPVEASISQSMQASSSHEHRTKLHNIAGTQMEGGSDASGSTLKNETVGRKAFALQDKLWSIYAAGNTVPIPFLRATDISPIALLSENMIGGMQQDGNGTVAVEALQELFTSSDPQSKKGRRGQNEMPLPPSVYQRLTTSSSLMNLAQVLAYHRACYEEMPLQELQATQEQQTIQNLCDTLRTILRL
2.7.11.1
COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:P70218};
defense response to bacterium [GO:0042742]; intracellular signal transduction [GO:0035556]; MAPK cascade [GO:0000165]; neuron projection morphogenesis [GO:0048812]; protein autophosphorylation [GO:0046777]; protein phosphorylation [GO:0006468]; regulation of cell growth [GO:0001558]; regulation of cell population proliferation [GO:0042127]; regulation of MAPK cascade [GO:0043408]; regulation of reactive oxygen species biosynthetic process [GO:1903426]; response to molecule of bacterial origin [GO:0002237]
chromosome [GO:0005694]; chromosome, centromeric region [GO:0000775]; early endosome [GO:0005769]; mitochondrion [GO:0005739]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; trans-Golgi network [GO:0005802]
ATP binding [GO:0005524]; protein serine/threonine kinase activity [GO:0004674]
PF00069;
1.10.510.10;
Protein kinase superfamily, STE Ser/Thr protein kinase family, STE20 subfamily
PTM: Autophosphorylates. {ECO:0000269|PubMed:30212650}.
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:26685188}. Nucleus {ECO:0000269|PubMed:26685188}. Golgi apparatus, trans-Golgi network {ECO:0000269|PubMed:26685188}. Early endosome {ECO:0000269|PubMed:26685188}. Note=Observed at the plasma membrane and in the nucleus when associated with MOB1A. {ECO:0000269|PubMed:26685188}.
CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000269|PubMed:30212650}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000269|PubMed:30212650};
null
null
null
null
FUNCTION: Serine/threonine-protein kinase (PubMed:30212650). Regulates organ size in coordination with MOB1A by modulating cell proliferation and cell expansion, possibly by facilitating cell cycle exit (PubMed:26685188). Positive regulator of the pathogen-associated molecular pattern (PAMP, e.g. flg22)-triggered immunity (PTI) signaling by stabilizing BIK1 and activating RBOHD by phosphorylation to promote the extracellular reactive oxygen species (ROS) burst involved in defense responses to bacterial infection (PubMed:30212650). {ECO:0000269|PubMed:26685188, ECO:0000269|PubMed:30212650}.
Arabidopsis thaliana (Mouse-ear cress)
O24585
CRI4_MAIZE
MDHVPALVLAGCCFLALLPGWACGLGSMSSIAVSYGEDGPVFCGLNSDGSHLVACFGADASVLYGAPPNIPFLGLTAGDGFVCGLLLDTRQPYCWGSNSYVKSGVPQPMVEGARYSELSAGDNHLCALRAAQDGGRGSSAATSLIDCWGYNMTATHAVDEAVSTVSAGSVFNCGLFARNRTVFCWGDETVSGVVGLAPRDLHFQSIGAGGYHVCGVLENAQVFCWGRSLEMQQVVPSSAIGDGDVNIVPMDAMSTVVGGRFHACGIRSLDHQVACWGFTLHNSTSPPKGLKMYALVAGDYFTCGVPAETSLMPRCWGNSGPLALPMAVPPGICVPTACSHGYYEYVNHGEVGSIKVCKPANSRLCLPCSTGCPEGLYESSPCNATADRVCQFDCLKCVTDECLSFCLSQKRTKSRKLMAFQMRIFVAEIVFAVVLVLSVSVTTCLYVRHKLRHCQCSNRELRLAKSTAYSFRKDNMKIQPDMEDLKIRRAQEFSYEELEQATGGFSEDSQVGKGSFSCVFKGILRDGTVVAVKRAIKASDVKKSSKEFHNELDLLSRLNHAHLLNLLGYCEDGSERLLVYEFMAHGSLYQHLHGKDPNLKKRLNWARRVTIAVQAARGIEYLHGYACPPVIHRDIKSSNILIDEDHNARVADFGLSILGPADSGTPLSELPAGTLGYLDPEYYRLHYLTTKSDVYSFGVVLLEILSGRKAIDMQFEEGNIVEWAVPLIKAGDIFAILDPVLSPPSDLEALKKIASVACKCVRMRGKDRPSMDKVTTALEHALALLMGSPCIEQPILPTEVVLGSSRMHKVSQMSSNHSCSENELADGEDQGIGYRAPSWITFPSVTSSQRRKSSASEADIVGRRATDGRNVGSSIGDGLRSLEEEIAPASPQENLYLQHNF
2.7.11.1
null
embryo development ending in seed dormancy [GO:0009793]; flower morphogenesis [GO:0048439]; lateral root formation [GO:0010311]; phosphorylation [GO:0016310]; positive regulation of DNA endoreduplication [GO:0032877]; regulation of asymmetric cell division [GO:0009786]; root cap development [GO:0048829]; sepal giant cell differentiation [GO:0090392]
cell surface [GO:0009986]; endocytic vesicle [GO:0030139]; multivesicular body membrane [GO:0032585]; plasma membrane [GO:0005886]
ATP binding [GO:0005524]; protein homodimerization activity [GO:0042803]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]
PF07714;PF13540;PF00020;
2.130.10.30;1.10.510.10;
Protein kinase superfamily, Ser/Thr protein kinase family
null
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Endosome, multivesicular body membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Note=Also localized into protein export bodies. {ECO:0000250}.
CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1;
null
null
null
null
FUNCTION: Putative receptor protein kinase. Could play a role in a differentiation signal. The CRINKLY4 (CR4) mutation affects leaf epidermis differentiation such that cell size and morphology are altered, and surface functions are compromised, allowing graft-like fusions between organs.
Zea mays (Maize)
O24591
HDT1_MAIZE
MEFWGLEVKPGSTVKCEPGYGFVLHLSQAALGESKKSDNALMYVKIDDQKLAIGTLSVDKNPHIQFDLIFDKEFELSHTSKTTSVFFTGYKVEQPFEEDEMDLDSEDEDEELNVPVVKENGKADEKKQKSQEKAVAAPSKSSPDSKKSKDDDDSDEDETDDSDEDETDDSDEGLSSEEGDDDSSDEDDTSDDEEEDTPTPKKPEVGKKRPAESSVLKTPLSDKKAKVATPSSQKTGGKKGAAVHVATPHPAKGKTIVNNDKSVKSPKSAPKSGGSVPCKPCSKSFISETALQAHSRAKMGASESQVQ
null
null
chromatin organization [GO:0006325]
nucleolus [GO:0005730]
hydrolase activity [GO:0016787]; metal ion binding [GO:0046872]
PF17800;
2.60.120.340;
Histone deacetylase HD2 family
PTM: The N-terminus is blocked.; PTM: Phosphorylated. Required for enzyme activity. {ECO:0000269|PubMed:9204905}.
SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:9204905}.
null
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=55 uM for core histone {ECO:0000269|PubMed:8961957};
null
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5. {ECO:0000269|PubMed:8961957};
null
FUNCTION: Mediates the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Able to deacetylate all 4 core histones.
Zea mays (Maize)
O24592
NCED1_MAIZE
MQGLAPPTSVSIHRHLPARSRARASNSVRFSPRAVSSVPPAECLQAPFHKPVADLPAPSRKPAAIAVPGHAAAPRKAEGGKKQLNLFQRAAAAALDAFEEGFVANVLERPHGLPSTADPAVQIAGNFAPVGERPPVHELPVSGRIPPFIDGVYARNGANPCFDPVAGHHLFDGDGMVHALRIRNGAAESYACRFTETARLRQERAIGRPVFPKAIGELHGHSGIARLALFYARAACGLVDPSAGTGVANAGLVYFNGRLLAMSEDDLPYHVRVADDGDLETVGRYDFDGQLGCAMIAHPKLDPATGELHALSYDVIKRPYLKYFYFRPDGTKSDDVEIPLEQPTMIHDFAITENLVVVPDHQVVFKLQEMLRGGSPVVLDKEKTSRFGVLPKHAADASEMAWVDVPDCFCFHLWNAWEDEATGEVVVIGSCMTPADSIFNESDERLESVLTEIRLDARTGRSTRRAVLPPSQQVNLEVGMVNRNLLGRETRYAYLAVAEPWPKVSGFAKVDLSTGELTKFEYGEGRFGGEPCFVPMDPAAAHPRGEDDGYVLTFVHDERAGTSELLVVNAADMRLEATVQLPSRVPFGFHGTFITGQELEAQAA
1.13.11.51
COFACTOR: Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000269|PubMed:20884803}; Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000269|PubMed:20884803};
abscisic acid biosynthetic process [GO:0009688]; carotene catabolic process [GO:0016121]
chloroplast stroma [GO:0009570]
9-cis-epoxycarotenoid dioxygenase activity [GO:0045549]; carotenoid dioxygenase activity [GO:0010436]; metal ion binding [GO:0046872]
PF03055;
null
Carotenoid oxygenase family
null
SUBCELLULAR LOCATION: Plastid, chloroplast stroma {ECO:0000269|PubMed:11576422, ECO:0000269|PubMed:9342392}. Note=Partially bound to the thylakoid membranes.
CATALYTIC ACTIVITY: Reaction=a 9-cis-epoxycarotenoid + O2 = 2-cis,4-trans-xanthoxin + a 12'-apo-carotenal; Xref=Rhea:RHEA:23328, ChEBI:CHEBI:15379, ChEBI:CHEBI:32304, ChEBI:CHEBI:51972, ChEBI:CHEBI:51973; EC=1.13.11.51; Evidence={ECO:0000269|PubMed:12495810, ECO:0000269|PubMed:20884803}; CATALYTIC ACTIVITY: Reaction=9-cis-violaxanthin + O2 = (3S,5R,6S)-5,6-epoxy-3-hydroxy-5,6-dihydro-12'-apo-beta-caroten-12'-al + 2-cis,4-trans-xanthoxin; Xref=Rhea:RHEA:16541, ChEBI:CHEBI:15379, ChEBI:CHEBI:32304, ChEBI:CHEBI:34597, ChEBI:CHEBI:35305; EC=1.13.11.51; Evidence={ECO:0000269|PubMed:12495810, ECO:0000269|PubMed:20884803}; CATALYTIC ACTIVITY: Reaction=9'-cis-neoxanthin + O2 = (3S,5R,6R)-3,5-dihydroxy-6,7-didehydro-5,6-dihydro-12'-apo-beta-caroten-12'-al + 2-cis,4-trans-xanthoxin; Xref=Rhea:RHEA:19677, ChEBI:CHEBI:15379, ChEBI:CHEBI:32304, ChEBI:CHEBI:34596, ChEBI:CHEBI:35306; EC=1.13.11.51; Evidence={ECO:0000269|PubMed:12495810, ECO:0000269|PubMed:20884803};
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=20 uM for 9-cis antheraxanthin {ECO:0000269|PubMed:12495810}; KM=15 uM for 9-cis luteoxanthin 8'S {ECO:0000269|PubMed:12495810}; KM=8 uM for 9-cis luteoxanthin 8'R {ECO:0000269|PubMed:12495810}; KM=27 uM for 9-cis neoxanthin {ECO:0000269|PubMed:12495810}; KM=58 uM for 9-cis violaxanthin {ECO:0000269|PubMed:12495810}; Note=Vmax with 9-cis violaxanthin as substrate is more than twice the Vmax with 9-cis neoxanthin as substrate.;
null
null
null
FUNCTION: Has a 11,12(11',12') 9-cis epoxycarotenoid cleavage activity. Catalyzes the first step of abscisic-acid biosynthesis from carotenoids. Not active on the all-trans isomers of violaxanthin and neoxanthin. Contributes probably to abscisic acid synthesis for the induction of seed dormancy. {ECO:0000269|PubMed:20884803, ECO:0000269|PubMed:9188535, ECO:0000269|PubMed:9342392}.
Zea mays (Maize)
O24606
EIN3_ARATH
MMFNEMGMCGNMDFFSSGSLGEVDFCPVPQAEPDSIVEDDYTDDEIDVDELERRMWRDKMRLKRLKEQDKGKEGVDAAKQRQSQEQARRKKMSRAQDGILKYMLKMMEVCKAQGFVYGIIPENGKPVTGASDNLREWWKDKVRFDRNGPAAITKYQAENNIPGIHEGNNPIGPTPHTLQELQDTTLGSLLSALMQHCDPPQRRFPLEKGVPPPWWPNGKEDWWPQLGLPKDQGPAPYKKPHDLKKAWKVGVLTAVIKHMFPDIAKIRKLVRQSKCLQDKMTAKESATWLAIINQEESLARELYPESCPPLSLSGGSCSLLMNDCSQYDVEGFEKESHYEVEELKPEKVMNSSNFGMVAKMHDFPVKEEVPAGNSEFMRKRKPNRDLNTIMDRTVFTCENLGCAHSEISRGFLDRNSRDNHQLACPHRDSRLPYGAAPSRFHVNEVKPVVGFPQPRPVNSVAQPIDLTGIVPEDGQKMISELMSMYDRNVQSNQTSMVMENQSVSLLQPTVHNHQEHLQFPGNMVEGSFFEDLNIPNRANNNNSSNNQTFFQGNNNNNNVFKFDTADHNNFEAAHNNNNNSSGNRFQLVFDSTPFDMASFDYRDDMSMPGVVGTMDGMQQKQQDVSIWF
null
null
defense response to bacterium [GO:0042742]; epigenetic regulation of gene expression [GO:0040029]; ethylene-activated signaling pathway [GO:0009873]; regulation of DNA-templated transcription [GO:0006355]; regulation of L-ascorbic acid biosynthetic process [GO:2000082]; response to ethylene [GO:0009723]; response to hypoxia [GO:0001666]; sugar mediated signaling pathway [GO:0010182]
nucleus [GO:0005634]
chromatin binding [GO:0003682]; DNA binding [GO:0003677]; DNA-binding transcription factor activity [GO:0003700]; histone binding [GO:0042393]; kinase binding [GO:0019900]; transcription cis-regulatory region binding [GO:0000976]
PF04873;
1.10.3180.10;
EIN3 family
PTM: Phosphorylated by KIN10. {ECO:0000269|PubMed:28600557}.
SUBCELLULAR LOCATION: Nucleus.
null
null
null
null
null
FUNCTION: Transcription factor acting as a positive regulator in the ethylene response pathway, by promoting histone acetylation in an ENAP1-dependent manner, thus accelerating the expression of ethylene-responsive genes (PubMed:28874528). Binds DNA (PubMed:26352699). Is required for ethylene responsiveness in adult plant tissues. Binds a primary ethylene response element present in the ETHYLENE-RESPONSE-FACTOR1 promoter with consequence to activate the transcription of this gene. {ECO:0000269|PubMed:26352699, ECO:0000269|PubMed:28874528, ECO:0000269|PubMed:9215635, ECO:0000269|PubMed:9851977}.
Arabidopsis thaliana (Mouse-ear cress)
O24610
CNDD3_ARATH
MDEELLLTRILAGIEGGDDESDYHELVTDLKSLLDTDDDEILNRFYGSLSSMASSFLRCISAAMDSPVESGRLAILASDAYLSLLLSTNCPVFTFFSPIAFLSLLGSIRRYLKRRDDSAGQGSNSQREKGNKKKRGRGKRNLGYEDGEETEEGGFDAKLMFIVLEKLGSVLSFVHLDRFPDSLKSLVQTVSEIPLLALEHSGVLNYDRLMEMCGKILGGVLNSDHGDMALTAAEISKSLTPLLLMGKHQARSFALGFVSRKLMSLAKDNPELKKVVSNLPKFLVHKAPEKAEPRGFAVEAVLEIVKAMEVEGQSEFVDFVMKMCQGKSNFRVLAVDIIPLLISSLGNPLGDISSENGLKDSWGLGCIDALVQRCSDTSALIRARALSNLAQVVEFLSGDERSRSILKQALGFNGETSEGKGAVTDLLKKRCVDEKAAVRRAALLLVTKLTSLMGGCFDGSILKTMGTSCSDPLISIRKAAVSAISEAFRICTDEIVTTEWLHSVPRMIMDNETSIQEECENVFHELVLERILRAGNVLSPDSASLPNNRNTTSKDLDRDIEALFPEGVLVLLRELCNSEVSPWVTKICGSLGKKKRLKPRVALALQCIIKESESLWLSRSMPINRWTAPAGAWFLLSEVSVYLSKSVEWEFLHHHWQLLDKNDVQGLDEQGDEQGVECNSSTWAGDRVCLLQTISNVSLQLPAEPAADLADNLLKKIENFNLHSAEVDAHVKALKTLCKKKASTSEEADMLVKKWVEQVSLKASKVTEKYIEGVSSHNHSFVTPATLGSRRSKRLDTVSKKLSKAVTAVYTIGSCVIIYPSADTTKIVPFLHTVITSGNSDSKLKNKLPQANVCLKQKAPLLYSQSWLTMAKMCLADGKLAKRYLPLFAQELEKSDCAALRNNLVVAMTDFCVHYTAMIECYIPKITKRLRDPCEVVRRQTFILLSRLLQRDYVKWRGVLFLRFLLSLVDESEKIRRLADFLFGSILKVKAPLLAYNSFVEAIYVLNDCHAHTGHSNPDSKQSRTKDQVFSIRGNDERARSKRMQIYVTLLKQMAPEHLLATFAKLCAEILAAASDGMLNIEDVTGQSVLQDAFQILACKEIRLSVSRGASSETADIEEEGGDAATAKGRAITHAVRKGLIQNTIPIFIELKRLLESKNSPLTGSLMDCLRVLLKDYKNEIEEMLVADKQLQKELVYDMQKHEAAKARSMANQGVACGTSHRNGEPEASAASEENVRDSGLESRVVSAAADVVAAKAARSVLREVNGGAATPPLSAMSVPKLRSSRGVSQSGRPSADVLESLRRRPTFMSDDES
null
null
cell division [GO:0051301]; centromere clustering [GO:0098653]; chromatin organization [GO:0006325]; chromosome condensation [GO:0030261]; meiotic chromosome condensation [GO:0010032]; microsporogenesis [GO:0009556]; mitotic cell cycle [GO:0000278]; mitotic chromosome condensation [GO:0007076]; sister chromatid cohesion [GO:0007062]
condensed chromosome, centromeric region [GO:0000779]; condensin complex [GO:0000796]; euchromatin [GO:0000791]; nucleoplasm [GO:0005654]
histone binding [GO:0042393]
PF12717;
1.25.10.10;
null
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768, ECO:0000269|PubMed:23929493, ECO:0000269|PubMed:27385818}. Chromosome {ECO:0000269|PubMed:23929493, ECO:0000269|PubMed:25065716, ECO:0000269|PubMed:27385818}. Note=Observed throughout euchromatic nucleoplasm (PubMed:23929493, PubMed:27385818). Associates with the chromosomes throughout meiosis (PubMed:25065716). {ECO:0000269|PubMed:23929493, ECO:0000269|PubMed:25065716, ECO:0000269|PubMed:27385818}.
null
null
null
null
null
FUNCTION: Regulatory subunit of the condensin-2 complex, a complex which establishes mitotic chromosome architecture and is involved in physical rigidity of the chromatid axis (By similarity). May promote the resolution of double-strand DNA catenanes (intertwines) between sister chromatids (By similarity). Required for plant vigor, fertility, chromatin condensation and sister chromatid cohesion both during mitosis and meiosis (PubMed:23929493, PubMed:27385818). Necessary to maintain normal structural integrity of the meiotic chromosomes during the two nuclear divisions of gametogenesis, especially to prevent interchromosome connections at metaphase I (PubMed:25065716). Seems also involved in crossover formation during meiotic prophase I (PubMed:25065716). Prevents centromeric and pericentromeric heterochromatin repeats association (PubMed:23929493). {ECO:0000250|UniProtKB:P42695, ECO:0000269|PubMed:23929493, ECO:0000269|PubMed:25065716, ECO:0000269|PubMed:27385818}.
Arabidopsis thaliana (Mouse-ear cress)
O24617
MSH2_ARATH
MEGNFEEQNKLPELKLDAKQAQGFLSFYKTLPNDTRAVRFFDRKDYYTAHGENSVFIAKTYYHTTTALRQLGSGSNALSSVSISRNMFETIARDLLLERNDHTVELYEGSGSNWRLVKTGSPGNIGSFEDVLFANNEMQDTPVVVSIFPSFHDGRCVIGMAYVDLTRRVLGLAEFLDDSRFTNLESSLIALGAKECIFPAESGKSNECKSLYDSLERCAVMITERKKHEFKGRDLDSDLKRLVKGNIEPVRDLVSGFDLATPALGALLSFSELLSNEDNYGNFTIRRYDIGGFMRLDSAAMRALNVMESKTDANKNFSLFGLMNRTCTAGMGKRLLHMWLKQPLVDLNEIKTRLDIVQCFVEEAGLRQDLRQHLKRISDVERLLRSLERRRGGLQHIIKLYQSTIRLPFIKTAMQQYTGEFASLISERYLKKLEALSDQDHLGKFIDLVECSVDLDQLENGEYMISSSYDTKLASLKDQKELLEQQIHELHKKTAIELDLQVDKALKLDKAAQFGHVFRITKKEEPKIRKKLTTQFIVLETRKDGVKFTNTKLKKLGDQYQSVVDDYRSCQKELVDRVVETVTSFSEVFEDLAGLLSEMDVLLSFADLAASCPTPYCRPEITSSDAGDIVLEGSRHPCVEAQDWVNFIPNDCRLMRGKSWFQIVTGPNMGGKSTFIRQVGVIVLMAQVGSFVPCDKASISIRDCIFARVGAGDCQLRGVSTFMQEMLETASILKGASDKSLIIIDELGRGTSTYDGFGLAWAICEHLVQVKRAPTLFATHFHELTALAQANSEVSGNTVGVANFHVSAHIDTESRKLTMLYKVEPGACDQSFGIHVAEFANFPESVVALAREKAAELEDFSPSSMIINNEESGKRKSREDDPDEVSRGAERAHKFLKEFAAIPLDKMELKDSLQRVREMKDELEKDAADCHWLRQFL
null
null
mismatch repair [GO:0006298]; mitotic recombination [GO:0006312]; negative regulation of reciprocal meiotic recombination [GO:0045128]; pyrimidine dimer repair [GO:0006290]
MutSalpha complex [GO:0032301]; plasma membrane [GO:0005886]
ATP binding [GO:0005524]; ATP-dependent DNA damage sensor activity [GO:0140664]; damaged DNA binding [GO:0003684]; mismatched DNA binding [GO:0030983]
PF01624;PF05188;PF05192;PF05190;PF00488;
1.10.1420.10;3.40.1170.10;3.30.420.110;3.40.50.300;
DNA mismatch repair MutS family
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
null
null
null
null
null
FUNCTION: Component of the post-replicative DNA mismatch repair system (MMR). Forms three different heterodimers: MutS alpha (MSH2-MSH6 heterodimer), MutS beta (MSH2-MSH3 heterodimer) and MutS gamma (MSH2-MSH7 heterodimer) which binds to DNA mismatches thereby initiating DNA repair. MutS alpha and MutS beta recognize single base mismatches and trinucleotide insertion-deletion loops (IDL) in the DNA. MutS gamma recognizes specifically the T/G single base mismatch. Plays a role in DNA homologous recombination repair and has a broad range of anti-recombination effects. Can suppress recombination between divergent direct repeats in somatic cells and possesses an anti-recombination meiotic effect. Is involved in a UV-B-induced DNA damage response pathway. {ECO:0000269|PubMed:10852942, ECO:0000269|PubMed:11550901, ECO:0000269|PubMed:12970498, ECO:0000269|PubMed:14530450, ECO:0000269|PubMed:16311517, ECO:0000269|PubMed:16507082, ECO:0000269|PubMed:17294256, ECO:0000269|PubMed:21307385}.
Arabidopsis thaliana (Mouse-ear cress)
O24621
SIGC_ARATH
MASFNSFPIPKQIVGSSSSSSSSTSRPRILVRSSLTSSMTSTNSMLVFVHPHPLIKHWLSLLRSDQTSFPIFVRIPMTSVVATRWSFLSSVKEESRIYQNDSLKACGCASVSPYTAQNNVYVELKDPKENIGVGSAERSYSSRSMLQYNLLAKNLLALEETFVALDSVRMERDIMLQMGKLGAAELFKTCLSRYRGSSITSCLSDTTELVDTTPNQQVFVSSRRKVKKKARRSSVTAENGDQSSLPIGLRTTWNNIDVPRVRRPPKYRKKRERISRNETEMSTGVKIVADMERIRTQLEEESGKVASLSCWAAAAGMNEKLLMRNLHYGWYCRDELVKSTRSLVLFLARNYRGLGIAHEDLIQAGYVGVLQGAERFDHTRGYKFSTYVQYWIRKSMSTMVSRHARGVHIPSSIIRTINHIQKARKTLKTSHGIKYAADEEIAKLTGHSVKKIRAANQCLKVVGSIDKKVGDCFTTKFLEFTPDTTMESPEEAVMRQSARRDIHDLLEGLEPREKQVMVLRYGLQDYRPKSLEEIGKLLKVSKEWIRKIERRAMAKLRDQPNAEDLRYYLNQ
null
null
cellular response to light stimulus [GO:0071482]; DNA-templated transcription initiation [GO:0006352]; regulation of RNA biosynthetic process [GO:2001141]
chloroplast [GO:0009507]
DNA-directed 5'-3' RNA polymerase activity [GO:0003899]; sigma factor activity [GO:0016987]; transcription cis-regulatory region binding [GO:0000976]
PF04542;PF04539;PF04545;
1.20.120.1810;1.10.10.10;
Sigma-70 factor family
null
SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000269|PubMed:10555304, ECO:0000269|PubMed:12602869, ECO:0000269|PubMed:9405719}. Note=Seems attached to membranes. {ECO:0000269|PubMed:12602869}.
null
null
null
null
null
FUNCTION: Sigma factors are initiation factors that promote the attachment of plastid-encoded RNA polymerase (PEP) to specific initiation sites and are then released. {ECO:0000269|PubMed:10734058, ECO:0000269|PubMed:12602869}.
Arabidopsis thaliana (Mouse-ear cress)
O24629
SIGA_ARATH
MATAAVIGLNTGKRLLSSSFYHSDVTEKFLSVNDHCSSQYHIASTKSGITAKKASNYSPSFPSSNRHTQSAKALKESVDVASTEKPWLPNGTDKELEEECYDDDDLISHSVEAILLLQKSMLEKSWNLSFEKAVSSEYPGKGTIRKKKIPVITCSGISARQRRIGAKKKTNMTHVKAVSDVSSGKQVRGYVKGVISEDVLSHVEVVRLSKKIKSGLRLDDHKSRLKDRLGCEPSDEQLAVSLKISRAELQAWLMECHLAREKLAMSNVRLVMSIAQRYDNLGAEMSDLVQGGLIGLLRGIEKFDSSKGFRISTYVYWWIRQGVSRALVDNSRTLRLPTHLHERLGLIRNAKLRLQEKGITPSIDRIAESLNMSQKKVRNATEAVSKVFSLDRDAFPSLNGLPGETHHSYIADTRLENNPWHGYDDLALKEEVSKLISATLGEREKEIIRLYYGLDKECLTWEDISKRIGLSRERVRQVGLVALEKLKHAARKRKMEAMILKN
null
null
cellular response to light stimulus [GO:0071482]; cellular response to redox state [GO:0071461]; DNA-templated transcription initiation [GO:0006352]; photosystem stoichiometry adjustment [GO:0080005]; regulation of DNA-templated transcription [GO:0006355]; regulation of RNA biosynthetic process [GO:2001141]
chloroplast [GO:0009507]
DNA binding [GO:0003677]; sigma factor activity [GO:0016987]
PF04542;PF04539;PF04545;
1.10.601.10;1.10.10.10;
Sigma-70 factor family
PTM: The phosphorylation of Thr-170 mediated by oxidative conditions of plastoquinone (PQ) changes the promoter specificity, selectively inhibiting the transcription of the psaA gene, which encodes a PS-I protein. Phosphorylation of the holoenzyme occurs in the dark. This phosphorylation in response to plastoquinone redox state modification is mediated by CSK. {ECO:0000269|PubMed:20498041, ECO:0000269|PubMed:23754813}.
SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000269|PubMed:10555304, ECO:0000269|PubMed:9405719}.
null
null
null
null
null
FUNCTION: Essential protein. Sigma factors are initiation factors that promote the attachment of plastid-encoded RNA polymerase (PEP) to specific initiation sites and are then released. Controls the transcription of the psaA gene and thus modulates photosystem stoichiometry. Thereby maintains a harmonious electron flow and photosynthetic efficiency. {ECO:0000269|PubMed:10734058, ECO:0000269|PubMed:12602869}.
Arabidopsis thaliana (Mouse-ear cress)
O24646
HY5_ARATH
MQEQATSSLAASSLPSSSERSSSSAPHLEIKEGIESDEEIRRVPEFGGEAVGKETSGRESGSATGQERTQATVGESQRKRGRTPAEKENKRLKRLLRNRVSAQQARERKKAYLSELENRVKDLENKNSELEERLSTLQNENQMLRHILKNTTGNKRGGGGGSNADASL
null
null
abscisic acid-activated signaling pathway [GO:0009738]; gibberellic acid mediated signaling pathway [GO:0009740]; positive gravitropism [GO:0009958]; positive regulation of anthocyanin metabolic process [GO:0031539]; positive regulation of circadian rhythm [GO:0042753]; positive regulation of flavonoid biosynthetic process [GO:0009963]; positive regulation of transcription by RNA polymerase II [GO:0045944]; red or far-red light signaling pathway [GO:0010017]; red, far-red light phototransduction [GO:0009585]; regulation of abscisic acid-activated signaling pathway [GO:0009787]; regulation of photomorphogenesis [GO:0010099]; response to abscisic acid [GO:0009737]; response to cold [GO:0009409]; response to far red light [GO:0010218]; response to red light [GO:0010114]; response to UV-B [GO:0010224]
nucleus [GO:0005634]; protein-DNA complex [GO:0032993]
DNA binding [GO:0003677]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; double-stranded DNA binding [GO:0003690]; transcription cis-regulatory region binding [GO:0000976]
PF00170;
1.20.5.490;
BZIP family
PTM: Phosphorylated by CK2. Shows a stronger interaction with COP1 when unphosphorylated. However, phosphorylation does not affect its susceptibility to be ubiquitinated. {ECO:0000269|PubMed:10990463}.; PTM: Ubiquitinated by COP1 and/or CIP8. Ubiquitination takes place in darkness and leads to its subsequent degradation, thereby preventing activation of photomorphogenesis signals (PubMed:10839542, PubMed:12028569). Ubiquitination and subsequent COP1-mediated degradation is triggered by SHW1 in the darkness during seedling development (PubMed:26474641). Ubiquinated and degraded in response to cold when reaching an accumulation peak after 2 days; this proteasome-mediated decay is promoted by prefoldin co-chaperone complex (e.g. PFD4) (PubMed:28412546). {ECO:0000269|PubMed:10839542, ECO:0000269|PubMed:12028569, ECO:0000269|PubMed:26474641, ECO:0000269|PubMed:28412546}.
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:26474641, ECO:0000269|PubMed:28412546, ECO:0000269|PubMed:31061103, ECO:0000269|PubMed:9367981}.
null
null
null
null
null
FUNCTION: Transcription factor that promotes photomorphogenesis in light. Acts downstream of the light receptor network and directly affects transcription of light-induced genes. Specifically involved in the blue light specific pathway, suggesting that it participates in transmission of cryptochromes (CRY1 and CRY2) signals to downstream responses. In darkness, its degradation prevents the activation of light-induced genes (Probable). Involved in responses to cold conditions probably by modulating the expression of several genes and triggering anthocyanin biosynthesis (PubMed:28412546). Acts coordinately with SPL7 to regulate the microRNA miR408 and its target genes in response to changes in light and copper conditions (PubMed:25516599). Regulates the abscisic acid (ABA) signaling pathway. Also involved in root gravitropism (PubMed:26474641). Involved in the repression of hypocotyl cell elongation to promote photomorphogenesis (PubMed:31061103). Recruits the histone deacetylase HDA15 to the promoters of a subset of cell wall organization and auxin signaling-related genes (PubMed:31061103). HDA15 represses their transcription by decreasing the levels of histone H4 acetylation in a light-dependent manner (PubMed:31061103). {ECO:0000269|PubMed:25516599, ECO:0000269|PubMed:26474641, ECO:0000269|PubMed:28412546, ECO:0000269|PubMed:31061103, ECO:0000305}.
Arabidopsis thaliana (Mouse-ear cress)
O24648
G3OX_PEA
MPSLSEAYRAHPVHVNHKHPDFNSLQELPESYNWTHLDDHTLIDSNNIMKESTTTVPVIDLNDPNASKLIGLACKTWGVYQVMNHGIPLSLLEDIQWLGQTLFSLPSHQKHKATRSPDGVSGYGIARISSFFPKLMWYEGFTIVGSPLDHFRELWPQDYTRFCDIVVQYDETMKKLAGTLMCLMLDSLGITKEDIKWAGSKAQFEKACAALQLNSYPSCPDPDHAMGLAPHTDSTFLTILSQNDISGLQVNREGSGWITVPPLQGGLVVNVGDLFHILSNGLYPSVLHRVLVNRTRQRFSVAYLYGPPSNVEICPHAKLIGPTKPPLYRSVTWNEYLGTKAKHFNKALSSVRLCTPINGLFDVNDSNKNSVQVG
1.14.11.15
COFACTOR: Name=L-ascorbate; Xref=ChEBI:CHEBI:38290; Evidence={ECO:0000250}; COFACTOR: Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000255|PROSITE-ProRule:PRU00805}; Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000255|PROSITE-ProRule:PRU00805};
gibberellin biosynthetic process [GO:0009686]; response to light stimulus [GO:0009416]
null
gibberellin 3-beta-dioxygenase activity [GO:0016707]; metal ion binding [GO:0046872]
PF03171;PF14226;
null
Iron/ascorbate-dependent oxidoreductase family, GA3OX subfamily
null
null
CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + gibberellin A20 + O2 = CO2 + gibberellin A1 + succinate; Xref=Rhea:RHEA:10104, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031, ChEBI:CHEBI:58524, ChEBI:CHEBI:58526; EC=1.14.11.15; Evidence={ECO:0000269|PubMed:9238076, ECO:0000269|PubMed:9286112, ECO:0000269|Ref.3};
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.5 uM for GA9 {ECO:0000269|PubMed:9238076}; KM=13 uM for GA20 {ECO:0000269|PubMed:9238076}; Vmax=0.29 nmol/min/mg enzyme with GA9 as substrate {ECO:0000269|PubMed:9238076}; Vmax=0.1 nmol/min/mg enzyme with GA20 as substrate {ECO:0000269|PubMed:9238076};
PATHWAY: Plant hormone biosynthesis; gibberellin biosynthesis.
null
null
FUNCTION: Converts the inactive gibberellin (GA) precursors GA9 and GA20 in the bioactives gibberellins GA4 and GA1. Has a small activity on GA29, producing GA8. Unable to convert GA20 to GA5, GA5 to GA3 or GA12 to GA14. Involved in the production of bioactive GA for vegetative growth and development, but not for the 3-beta-hydroxylation of GA in developing seeds. {ECO:0000269|PubMed:9238076, ECO:0000269|PubMed:9286112, ECO:0000269|Ref.3}.
Pisum sativum (Garden pea) (Lathyrus oleraceus)
O24767
INGK_EXIAC
MNKIAVIGKVFVDIKGTSFAPLHKDAKNVGDITFSNGGTGRNVAQNLAVLGNEVRFISTVTNDQIGVGVLDELKSYGANVDHVEMLEDHGMGMWLAVMDNEGDLQTSISKQPDAKLLEEAILRQSIYALDGVDAVAIDLDLSVTVLERLIHLCRKMELPLFGVCGHLSVIERNRHLLQGFTGFICSREEAEILSDLSIVTVEDAIHVANELAKKGAPFTVVTMSELGAVYVDRRTATSGHVGTKKVKVVDSTGAGDSFFSAVLSELTQEKSAEEALKLGMKVAAEVIASTENGLVPEMLDALQ
2.7.1.73
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:9357959}; Note=Manganese or cobalt, but not calcium, nickel or zinc can replace Mg(2+) but results in reduced reaction rates. {ECO:0000269|PubMed:9357959};
GMP salvage [GO:0032263]; IMP salvage [GO:0032264]; phosphorylation [GO:0016310]; purine ribonucleoside salvage [GO:0006166]
cytosol [GO:0005829]
ATP binding [GO:0005524]; guanosine kinase activity [GO:0106366]; inosine kinase activity [GO:0008906]
PF00294;
3.40.1190.20;
Carbohydrate kinase PfkB family
null
null
CATALYTIC ACTIVITY: Reaction=ATP + guanosine = ADP + GMP + H(+); Xref=Rhea:RHEA:27710, ChEBI:CHEBI:15378, ChEBI:CHEBI:16750, ChEBI:CHEBI:30616, ChEBI:CHEBI:58115, ChEBI:CHEBI:456216; EC=2.7.1.73; Evidence={ECO:0000269|PubMed:11129609, ECO:0000269|PubMed:9357959}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27711; Evidence={ECO:0000269|PubMed:9357959}; CATALYTIC ACTIVITY: Reaction=ATP + inosine = ADP + H(+) + IMP; Xref=Rhea:RHEA:21140, ChEBI:CHEBI:15378, ChEBI:CHEBI:17596, ChEBI:CHEBI:30616, ChEBI:CHEBI:58053, ChEBI:CHEBI:456216; EC=2.7.1.73; Evidence={ECO:0000269|PubMed:11129609, ECO:0000269|PubMed:9357959}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21141; Evidence={ECO:0000269|PubMed:9357959};
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.022 mM for guanosine {ECO:0000269|PubMed:9357959}; KM=0.87 mM for inosine {ECO:0000269|PubMed:9357959}; KM=2.83 mM for deoxyguanosine {ECO:0000269|PubMed:9357959}; Vmax=217 umol/min/mg enzyme with guanosine as substrate {ECO:0000269|PubMed:9357959}; Vmax=35.9 umol/min/mg enzyme with inosine as substrate {ECO:0000269|PubMed:9357959}; Vmax=59.3 umol/min/mg enzyme with deoxyguanosine as substrate {ECO:0000269|PubMed:9357959};
PATHWAY: Purine metabolism; IMP biosynthesis via salvage pathway; IMP from inosine: step 1/1. {ECO:0000305|PubMed:9357959}.; PATHWAY: Purine metabolism; GMP biosynthesis via salvage pathway. {ECO:0000305|PubMed:9357959}.
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is around 8.3. {ECO:0000269|PubMed:9357959};
null
FUNCTION: Catalyzes the phosphorylation of guanosine and inosine to GMP and IMP, respectively (PubMed:11129609, PubMed:9357959). Can also use deoxyguanosine (PubMed:9357959). Shows a strong preference for guanosine (PubMed:9357959). dATP, GTP and dGTP can serve as phosphate donors (PubMed:9357959). {ECO:0000269|PubMed:11129609, ECO:0000269|PubMed:9357959}.
Exiguobacterium acetylicum (Brevibacterium acetylicum)
O24915
MQMTN_HELPY
MVQKIGILGAMREEITPILELFGVDFEEIPLGGNVFHKGVYHNKEIIVAYSKIGKVHSTLTTTSMILAFGVQKVLFSGVAGSLVKDLKINDLLVAIQLVQHDVDLSAFDHPLGFIPESAIFIETSESLNALAKEVANEQHIVLKEGVIASGDQFVHSKERKEFLVSEFKASAVEMEGASVAFVCQKFGVPCCVLRSISDNADEEANMSFDAFLEKSAQTSAKFLKSMVDEL
3.2.2.30; 3.2.2.9
null
L-methionine salvage from methylthioadenosine [GO:0019509]; L-methionine salvage from S-adenosylmethionine [GO:0019284]; menaquinone biosynthetic process [GO:0009234]; nucleoside catabolic process [GO:0009164]
cytosol [GO:0005829]
6-amino-6-deoxyfutalosine hydrolase activity [GO:0102246]; adenosylhomocysteine nucleosidase activity [GO:0008782]; methylthioadenosine nucleosidase activity [GO:0008930]
PF01048;
3.40.50.1580;
PNP/UDP phosphorylase family
null
null
CATALYTIC ACTIVITY: Reaction=6-amino-6-deoxyfutalosine + H2O = adenine + dehypoxanthine futalosine; Xref=Rhea:RHEA:33079, ChEBI:CHEBI:15377, ChEBI:CHEBI:16708, ChEBI:CHEBI:58864, ChEBI:CHEBI:64286; EC=3.2.2.30; Evidence={ECO:0000269|PubMed:21098241, ECO:0000269|PubMed:24083939}; CATALYTIC ACTIVITY: Reaction=H2O + S-adenosyl-L-homocysteine = adenine + S-(5-deoxy-D-ribos-5-yl)-L-homocysteine; Xref=Rhea:RHEA:17805, ChEBI:CHEBI:15377, ChEBI:CHEBI:16708, ChEBI:CHEBI:57856, ChEBI:CHEBI:58195; EC=3.2.2.9; Evidence={ECO:0000269|PubMed:21098241, ECO:0000269|PubMed:24083939}; CATALYTIC ACTIVITY: Reaction=H2O + S-methyl-5'-thioadenosine = 5-(methylsulfanyl)-D-ribose + adenine; Xref=Rhea:RHEA:13617, ChEBI:CHEBI:15377, ChEBI:CHEBI:16708, ChEBI:CHEBI:17509, ChEBI:CHEBI:78440; EC=3.2.2.9; Evidence={ECO:0000269|PubMed:21098241, ECO:0000269|PubMed:24083939}; CATALYTIC ACTIVITY: Reaction=5'-deoxyadenosine + H2O = 5-deoxy-D-ribose + adenine; Xref=Rhea:RHEA:29859, ChEBI:CHEBI:15377, ChEBI:CHEBI:16708, ChEBI:CHEBI:17319, ChEBI:CHEBI:149540; EC=3.2.2.9; Evidence={ECO:0000269|PubMed:21098241, ECO:0000269|PubMed:24083939};
null
PATHWAY: Quinol/quinone metabolism; menaquinone biosynthesis.; PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via salvage pathway; S-methyl-5-thio-alpha-D-ribose 1-phosphate from S-methyl-5'-thioadenosine (hydrolase route): step 1/2.
null
null
FUNCTION: Catalyzes the direct conversion of aminodeoxyfutalosine (AFL) into dehypoxanthine futalosine (DHFL) and adenine via the hydrolysis of the N-glycosidic bond; this reaction seems to represent an essential step in the menaquinone biosynthesis pathway in Helicobacter species. Can also probably catalyzes the hydrolysis of 5'-methylthioadenosine (MTA) and S-adenosylhomocysteine (SAH) to adenine and the corresponding thioribose, 5'-methylthioribose and S-ribosylhomocysteine, respectively. These other activities highlight the tremendous versatility of the enzyme, which also plays key roles in S-adenosylmethionine recycling and in the biosynthesis of the quorum-sensing molecule autoinducer-2. Does not act on futalosine (FL) as substrate. {ECO:0000269|PubMed:21098241, ECO:0000269|PubMed:24083939}.
Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori)
O25001
HCPA_HELPY
MLGNVKKTLFGVLCLGTLCLRGLMAEPDAKELVNLGIESAKKQDFAQAKTHFEKACELKNGFGCVFLGAFYEEGKGVGKDLKKAIQFYTKGCELNDGYGCNLLGNLYYNGQGVSKDAKKASQYYSKACDLNHAEGCMVLGSLHHYGVGTPKDLRKALDLYEKACDLKDSPGCINAGYIYSVTKNFKEAIVRYSKACELKDGRGCYNLGVMQYNAQGTAKDEKQAVENFKKGCKSSVKEACDALKELKIEL
3.5.2.6
null
response to antibiotic [GO:0046677]
extracellular region [GO:0005576]
beta-lactamase activity [GO:0008800]
PF08238;PF13181;
1.25.40.10;
Hcp beta-lactamase family
null
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:9596777}.
CATALYTIC ACTIVITY: Reaction=a beta-lactam + H2O = a substituted beta-amino acid; Xref=Rhea:RHEA:20401, ChEBI:CHEBI:15377, ChEBI:CHEBI:35627, ChEBI:CHEBI:140347; EC=3.5.2.6; Evidence={ECO:0000269|PubMed:10748053};
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=145 uM for ampicillin {ECO:0000269|PubMed:10748053}; KM=48 uM for benzylpenicillin {ECO:0000269|PubMed:10748053}; KM=155 uM for amoxicillin {ECO:0000269|PubMed:10748053}; KM=406 uM for cephaloridine {ECO:0000269|PubMed:10748053}; KM=47 uM for nitrocefine {ECO:0000269|PubMed:10748053}; Note=kcat is 1.06 min(-1) with ampicillin as substrate. kcat is 0.74 min(-1) with benzylpenicillin as substrate. kcat is 0.55 min(-1) with amoxicillin as substrate. kcat is 0.30 min(-1) with cephaloridine as substrate. kcat is 0.28 min(-1) with nitrocefine as substrate. {ECO:0000269|PubMed:10748053};
null
null
null
FUNCTION: Slowly hydrolyzes 6-aminopenicillinic acid and 7-aminocephalosporanic acid (ACA) derivatives. May be involved in the synthesis of the cell wall peptidoglycan. {ECO:0000269|PubMed:10748053}.
Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori)
O25067
AMIE_HELPY
MRHGDISSSPDTVGVAVVNYKMPRLHTKNEVLENCRNIAKVIGGVKQGLPGLDLIIFPEYSTHGIMYDRQEMFDTAASVPGEETAIFAEACKKNKVWGVFSLTGEKHEQAKKNPYNTLILVNDKGEIVQKYRKILPWCPIECWYPGDKTYVVDGPKGLKVSLIICDDGNYPEIWRDCAMRGAELIVRCQGYMYPAKEQQIAIVKAMAWANQCYVAVANATGFDGVYSYFGHSSIIGFDGHTLGECGEEENGLQYAQLSVQQIRDARKYDQSQNQLFKLLHRGYSGVFASGDGDKGVAECPFEFYKTWVNDPKKAQENVEKITRPSVGVAACPVGDLPTK
3.5.1.4
null
beta-alanine biosynthetic process via 3-ureidopropionate [GO:0033396]; nitrogen compound metabolic process [GO:0006807]
null
amidase activity [GO:0004040]; beta-ureidopropionase activity [GO:0003837]; hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides [GO:0016811]; indoleacetamide hydrolase activity [GO:0043864]
PF00795;
3.60.110.10;
Carbon-nitrogen hydrolase superfamily, Aliphatic amidase family
null
null
CATALYTIC ACTIVITY: Reaction=a monocarboxylic acid amide + H2O = a monocarboxylate + NH4(+); Xref=Rhea:RHEA:12020, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938, ChEBI:CHEBI:35757, ChEBI:CHEBI:83628; EC=3.5.1.4; Evidence={ECO:0000269|PubMed:11359566, ECO:0000269|PubMed:9364923};
null
null
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7. {ECO:0000269|PubMed:11359566};
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 55 degrees Celsius. {ECO:0000269|PubMed:11359566};
FUNCTION: Catalyzes the hydrolysis of short-chain aliphatic amides to their corresponding organic acids with release of ammonia. Hydrolyzes propionamide, acetamide and acrylamide, but has no activity with formamide or urea. The natural substrates of AmiE in its gastric environment are not known. Probably functions to ensure nitrogen supply to the bacteria.; FUNCTION: Also exhibits in vitro acyl transferase activity, transferring the acyl moiety of short-chain amides to hydroxylamine to form hydroxamates. The highest level of acyl transfer activity is observed with acetamide.
Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori)
O25080
PGDAE_HELPY
MAKEILVAYGVDIDAVAGWLGSYGGEDSPDDISRGLFAGEVGIPRLLKLFKKYHLPATWFSPGHSIETFSEQMKMIVDAGHEVGAHGYSHENPIAMTAKQEEDVLLKSVELIKDLTGKAPTGYVAPWWEFSNITNELLLKHGFKYDHSLMHNDFTPYYVRVGDSWSKIDYSLEAKDWMKPLIRGVETDLVEIPANWYLDDLPPMMFIKKSPNSFGFVSPHDIGQMWIDQFDWVYREMDYAVFSMTIHPDVSARPQVLLMHEKIIEHINKHEGVRWVTFNEIADDFLKRNPRKK
3.1.1.72; 3.5.1.-
null
cell wall organization [GO:0071555]; xylan catabolic process [GO:0045493]
null
acetylxylan esterase activity [GO:0046555]; hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds [GO:0016810]; metal ion binding [GO:0046872]
PF01522;
3.20.20.370;
Polysaccharide deacetylase family
null
null
CATALYTIC ACTIVITY: Reaction=Deacetylation of xylans and xylo-oligosaccharides.; EC=3.1.1.72; Evidence={ECO:0000269|PubMed:23825549};
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.85 mM for chitin {ECO:0000269|PubMed:23825549}; KM=0.85 mM for chitosan {ECO:0000269|PubMed:23825549}; KM=0.42 mM for acetylated xylan {ECO:0000269|PubMed:23825549}; KM=0.18 mM for pNP-acetate {ECO:0000269|PubMed:23825549}; Note=kcat is 775 min(-1), 968 min(-1), 2549 min(-1) and 1029 min(-1) with chitin, chitosan, acetylated xylan, and pNP-acetate as substrate, respectively.;
null
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.0 with acetylated xylan as substrate. Is active at acidic pH ranging from 5.0 to 6.0. {ECO:0000269|PubMed:23825549};
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 50 degrees Celsius with acetylated xylan as substrate. Retains about 80% of the activity at 30-55 degrees Celsius. {ECO:0000269|PubMed:23825549};
FUNCTION: Catalyzes the N-deacetylation of peptidoglycan (PG), an important mechanism that appears to confer lysozyme resistance and to mitigate host immune detection; this likely contributes to pathogen persistence in the host. The exact nature of the residue in PG that is deacetylated has not been determined. Is also able to catalyze the deacetylation of acetylated xylan, and, to a lesser extent, that of chitin and chitosan. Therefore, this enzyme might play a role during infection, considering that xylan-containing carbohydrate structures are among those commonly consumed by humans. {ECO:0000269|PubMed:19147492, ECO:0000269|PubMed:20805339, ECO:0000269|PubMed:23221800, ECO:0000269|PubMed:23825549}.
Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori)
O25119
FLIG_HELPY
MATKLTPKQKAQLDELSMSEKIAILLIQVGEDTTGEILRHLDIDSITEISKQIVQLNGTDKQIGAAVLEEFFAIFQSNQYINTGGLEYARELLTRTLGSEEAKKVMDKLTKSLQTQKNFAYLGKIKPQQLADFIINEHPQTIALILAHMEAPNAAETLSYFPDEMKAEISIRMANLGEISPQVVKRVSTVLENKLESLTSYKIEVGGLRAVAEIFNRLGQKSAKTTLARIESVDNKLAGAIKEMMFTFEDIVKLDNFAIREILKVADKKDLSLALKTSTKDLTDKFLNNMSSRAAEQFVEEMQYLGAVKIKDVDVAQRKIIEIVQSLQEKGVIQTGEEEDVIE
null
null
bacterial-type flagellum-dependent cell motility [GO:0071973]; bacterial-type flagellum-dependent swarming motility [GO:0071978]; chemotaxis [GO:0006935]
bacterial-type flagellum [GO:0009288]; bacterial-type flagellum basal body [GO:0009425]; plasma membrane [GO:0005886]
cytoskeletal motor activity [GO:0003774]
PF01706;PF14841;PF14842;
1.10.220.30;1.20.5.2020;
FliG family
null
SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250|UniProtKB:P0ABZ1}; Peripheral membrane protein {ECO:0000250|UniProtKB:P0ABZ1}; Cytoplasmic side {ECO:0000250|UniProtKB:P0ABZ1}. Bacterial flagellum basal body {ECO:0000250|UniProtKB:P0ABZ1}.
null
null
null
null
null
FUNCTION: One of the proteins that forms a switch complex that is proposed to be located at the base of the basal body. This complex interacts with chemotaxis proteins (such as CheY) in addition to contacting components of the motor that determine the direction of flagellar rotation. Required for flagellum synthesis and motility. In H.pylori four flagellar switch proteins are encoded, FliG, FliM, FliN and FliY. {ECO:0000250|UniProtKB:P0ABZ1, ECO:0000269|PubMed:10960117, ECO:0000269|PubMed:22325779, ECO:0000269|PubMed:9252185}.
Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori)
O25503
SPEE_HELPY
MWITQEITPYLRKEYTIEAKLLDVRSEHNILEIFKSKDFGEIAMLNRQLLFKNFLHIESELLAHMGGCTKKELKEVLIVDGFDLELAHQLFKYDTHIDFVQADEKILDSFISFFPHFHEVKNNKNFTHAKQLLDLDIKKYDLIFCLQEPDIHRIDGLKRMLKEDGVFISVAKHPLLEHVSMQNALKNMGGVFSVAMPFVAPLRILSNKGYIYASFKTHPLKDLMTPKIEALTSVRYYNEDIHRAAFALPKNLQEVFKDNIKS
2.5.1.16
null
polyamine biosynthetic process [GO:0006596]; spermidine biosynthetic process [GO:0008295]
cytosol [GO:0005829]
spermidine synthase activity [GO:0004766]
PF17284;PF01564;
2.30.140.10;3.40.50.150;
Spermidine/spermine synthase family
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00198}.
CATALYTIC ACTIVITY: Reaction=putrescine + S-adenosyl 3-(methylsulfanyl)propylamine = H(+) + S-methyl-5'-thioadenosine + spermidine; Xref=Rhea:RHEA:12721, ChEBI:CHEBI:15378, ChEBI:CHEBI:17509, ChEBI:CHEBI:57443, ChEBI:CHEBI:57834, ChEBI:CHEBI:326268; EC=2.5.1.16; Evidence={ECO:0000255|HAMAP-Rule:MF_00198, ECO:0000269|PubMed:16009566};
null
PATHWAY: Amine and polyamine biosynthesis; spermidine biosynthesis; spermidine from putrescine: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00198}.
null
null
FUNCTION: Involved in the cell growth and proliferation. Catalyzes the irreversible transfer of a propylamine group from the amino donor S-adenosylmethioninamine (decarboxy-AdoMet) to putrescine (1,4-diaminobutane) to yield spermidine. Spermidine cannot be used as an aminopropyl acceptor. {ECO:0000269|PubMed:16009566}.
Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori)
O25533
COAX_HELPY
MPARQSFTDLKNLVLCDIGNTRIHFAQNYQLFSSAKEDLKRLGIQKEIFYISVNEENEKALLNCYPNAKNIAGFFHLETDYVGLGIDRQMACLAVNNGVVVDAGSAITIDLIKEGKHLGGCILPGLAQYIHAYKKSAKILEQPFKALDSLEVLPKSTRDAVNYGMVLSVIACIQHLAKNQKIYLCGGDAKYLSAFLPHSVCKERLVFDGMEIALKKAGILECK
2.7.1.33
COFACTOR: Name=NH4(+); Xref=ChEBI:CHEBI:28938; Evidence={ECO:0000269|PubMed:16905099}; Name=K(+); Xref=ChEBI:CHEBI:29103; Evidence={ECO:0000269|PubMed:16905099}; Note=Monovalent cations. Ammonium or potassium. {ECO:0000269|PubMed:16905099};
coenzyme A biosynthetic process [GO:0015937]; phosphorylation [GO:0016310]
cytoplasm [GO:0005737]
ATP binding [GO:0005524]; metal ion binding [GO:0046872]; pantothenate kinase activity [GO:0004594]
PF03309;
3.30.420.40;
Type III pantothenate kinase family
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CATALYTIC ACTIVITY: Reaction=(R)-pantothenate + ATP = (R)-4'-phosphopantothenate + ADP + H(+); Xref=Rhea:RHEA:16373, ChEBI:CHEBI:10986, ChEBI:CHEBI:15378, ChEBI:CHEBI:29032, ChEBI:CHEBI:30616, ChEBI:CHEBI:456216; EC=2.7.1.33;
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=101 uM for pantothenate {ECO:0000269|PubMed:15795230}; KM=9.6 mM for ATP {ECO:0000269|PubMed:15795230};
PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 1/5.
null
null
FUNCTION: Catalyzes the phosphorylation of pantothenate (Pan), the first step in CoA biosynthesis. Can also utilize CTP or GTP instead of ATP as a phosphoryl donor, albeit to a lesser extent. {ECO:0000269|PubMed:15795230, ECO:0000269|PubMed:16905099}.
Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori)
O25560
HYPB_HELPY
MSEQRQESLQNNPNLSKKDVKIVEKILSKNDIKAAEMKERYLKEGLYVLNFMSSPGSGKTTMLENLADFKDFKFCVVEGDLQTNRDADRLRKKGVSAHQITTGEACHLEASMIEGAFDLLKDEGALEKSDFLIIENVGNLVCPSSYNLGAAMNIVLLSVPEGDDKVLKYPTMFMCADAVIISKADMVEVFNFRVSQVKEDMQKLKPEAPIFLMSSKDPKSLEDFKNFLLEKKRENYQSTHSF
null
null
protein maturation [GO:0051604]
null
GTP binding [GO:0005525]; GTPase activity [GO:0003924]; nickel cation binding [GO:0016151]; zinc ion binding [GO:0008270]
PF02492;
3.40.50.300;
SIMIBI class G3E GTPase family, HypB/HupM subfamily
null
null
null
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.05 mM for GTP (apo form) {ECO:0000269|PubMed:21239585}; KM=0.16 mM for GTP (in the presence of 20 uM Ni(II)) {ECO:0000269|PubMed:21239585}; Note=kcat is 0.0006 sec(-1) for the apo form. kcat is 0.0016 sec(-1) in the presence of 20 uM Ni(II). {ECO:0000269|PubMed:21239585};
null
null
null
FUNCTION: Involved in the maturation of [NiFe] hydrogenases. Required for nickel insertion into the metal center of the hydrogenase. Is also required for maturation of urease (PubMed:11123699, PubMed:12533448). Exhibits a low intrinsic GTPase activity, which is essential for nickel insertion (PubMed:12533448, PubMed:21239585, PubMed:22179820, PubMed:24338018). {ECO:0000269|PubMed:12533448, ECO:0000269|PubMed:21239585, ECO:0000269|PubMed:22179820, ECO:0000269|PubMed:24338018, ECO:0000305|PubMed:11123699, ECO:0000305|PubMed:12533448}.
Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori)
O25830
DHPRS_HELPY
MIVKRLNPDALKNALQKIGPEKIAQDRMHQKGVSFVFEIQHLPLSATLILKQEAISVGGDFATPRDCILAKEPFYDGVLIASAKQLERLIVKCHSQPFGLKHLAQELKSHLKAPKPNTPQIMAVLNLTPDSFYEKSRFDSKKALEEIYQWLEKGITLIDIGAASSRPESEIIDPKIEQDRLKEILLEIKSQKLYQCAKFSIDTYHATTAQMALEHYFSILNDVSGFNSAEMLEVAKDYKPTCILMHTQKTPKDMQENVFYHNLFDEMDRFFKEKLEVLEKYVLQDIILDIGFGFAKLKEHNLALIKHLSHFLKFKKPLLVGASRKNTIGLITGREVQDRLAGTLSLHLMALQNGASVLRVHDIDEHIDLIKVFKSLEETD
1.5.8.-; 2.5.1.15
COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|PubMed:17416665}; Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000269|PubMed:17416665}; Note=Binds 1 FAD or 1 FMN per subunit. {ECO:0000269|PubMed:17416665}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P0AC13};
folic acid biosynthetic process [GO:0046656]; tetrahydrofolate biosynthetic process [GO:0046654]
cytosol [GO:0005829]
dihydropteroate synthase activity [GO:0004156]; metal ion binding [GO:0046872]; oxidoreductase activity [GO:0016491]
PF00809;
3.20.20.20;
DHPS family
null
null
CATALYTIC ACTIVITY: Reaction=(7,8-dihydropterin-6-yl)methyl diphosphate + 4-aminobenzoate = 7,8-dihydropteroate + diphosphate; Xref=Rhea:RHEA:19949, ChEBI:CHEBI:17836, ChEBI:CHEBI:17839, ChEBI:CHEBI:33019, ChEBI:CHEBI:72950; EC=2.5.1.15; Evidence={ECO:0000269|PubMed:17416665}; CATALYTIC ACTIVITY: Reaction=(6S)-5,6,7,8-tetrahydropteroate + NAD(+) = 7,8-dihydropteroate + H(+) + NADH; Xref=Rhea:RHEA:45744, ChEBI:CHEBI:15378, ChEBI:CHEBI:17839, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:85414; Evidence={ECO:0000269|PubMed:17416665};
null
PATHWAY: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 7,8-dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate and 4-aminobenzoate: step 1/2.
null
null
FUNCTION: Bifunctional enzyme that catalyzes the formation of dihydropteroate, the immediate precursor of folic acid and the reduction of dihydropteroate to tetrahydropteroate. {ECO:0000269|PubMed:15554970, ECO:0000269|PubMed:17416665}.
Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori)
O26061
THYX_HELPY
MEVICKHYTPLDIASQAIRTCWQSFEYSDDGGCKDKELIHRVGNIFRHSSTLEHLYYNFEIKGLSRGALQELSRHRIASLSVKSSRYTLRELKEVESFLPLNETNLERAKEFLVFVDNEKVNAMSVLALENLRILLSEHNIKNDLAKYAMPESYKTHLAYSINARSLQNFLTLRSSNKALKEMQDLAKALFDALPGEHQYLFEDCLKH
2.1.1.148
COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|PubMed:22512654, ECO:0000305|PubMed:12029065}; Note=Binds 4 FAD per tetramer. Each FAD binding site is formed by three monomers. {ECO:0000269|PubMed:22512654};
dTMP biosynthetic process [GO:0006231]; dTTP biosynthetic process [GO:0006235]; methylation [GO:0032259]
null
flavin adenine dinucleotide binding [GO:0050660]; NADPH binding [GO:0070402]; thymidylate synthase (FAD) activity [GO:0050797]; thymidylate synthase activity [GO:0004799]
PF02511;
3.30.1360.170;
Thymidylate synthase ThyX family
null
null
CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP + H(+) + NADPH = (6S)-5,6,7,8-tetrahydrofolate + dTMP + NADP(+); Xref=Rhea:RHEA:29043, ChEBI:CHEBI:15378, ChEBI:CHEBI:15636, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.148; Evidence={ECO:0000269|PubMed:12029065};
null
PATHWAY: Pyrimidine metabolism; dTTP biosynthesis. {ECO:0000255|HAMAP-Rule:MF_01408}.
null
null
FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor, and NAD(P)H and FADH(2) as the reductant. {ECO:0000269|PubMed:12029065}.
Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori)
O26314
UREND_METTH
MTVLKIISWNVNGLRAVHRKGFLKWFMEEKPDILCLQEIKAAPEQLPRKLRHVEGYRSFFTPAERKGYSGVAMYTKVPPSSLREGFGVERFDTEGRIQIADFDDFLLYNIYFPNGKMSEERLKYKLEFYDAFLEDVNRERDSGRNVIICGDFNTAHREIDLARPKENSNVSGFLPVERAWIDKFIENGYVDTFRMFNSDPGQYTWWSYRTRARERNVGWRLDYFFVNEEFKGKVKRSWILSDVMGSDHCPIGLEIEL
3.1.11.2; 4.2.99.18
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:15725624, ECO:0000269|PubMed:17012282}; Note=Can also use Mn(2+), Co(2+) and Ni(2+). {ECO:0000269|PubMed:15725624};
base-excision repair [GO:0006284]
null
class I DNA-(apurinic or apyrimidinic site) endonuclease activity [GO:0140078]; DNA binding [GO:0003677]; double-stranded DNA 3'-5' DNA exonuclease activity [GO:0008311]; endonuclease activity [GO:0004519]; metal ion binding [GO:0046872]; phosphoric diester hydrolase activity [GO:0008081]
PF03372;
3.60.10.10;
DNA repair enzymes AP/exoA family
null
null
CATALYTIC ACTIVITY: Reaction=2'-deoxyribonucleotide-(2'-deoxyribose 5'-phosphate)-2'-deoxyribonucleotide-DNA = a 3'-end 2'-deoxyribonucleotide-(2,3-dehydro-2,3-deoxyribose 5'-phosphate)-DNA + a 5'-end 5'-phospho-2'-deoxyribonucleoside-DNA + H(+); Xref=Rhea:RHEA:66592, Rhea:RHEA-COMP:13180, Rhea:RHEA-COMP:16897, Rhea:RHEA-COMP:17067, ChEBI:CHEBI:15378, ChEBI:CHEBI:136412, ChEBI:CHEBI:157695, ChEBI:CHEBI:167181; EC=4.2.99.18; Evidence={ECO:0000269|PubMed:15725624, ECO:0000269|PubMed:17012282}; CATALYTIC ACTIVITY: Reaction=Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleoside 5'-phosphates.; EC=3.1.11.2; Evidence={ECO:0000269|PubMed:15725624, ECO:0000269|PubMed:17012282};
null
null
null
null
FUNCTION: Involved in DNA uracil repair (PubMed:17012282, PubMed:19240141, PubMed:20129830). Recognizes DNA uracil residues within double-stranded DNA and initiates DNA-U repair by endonucleotic incision on the 5'-side of the 2'-d-uridine residue, irrespective of the nature of the opposing nucleotide (PubMed:17012282, PubMed:19240141, PubMed:20129830). In addition, acts as an apurinic/apyrimidinic (AP) endonuclease hydrolyzing the DNA phosphodiester backbone immediately at the 5'-side of AP sites, and as a 3'-5' exonuclease (PubMed:15725624, PubMed:17012282). Strongly binds to double-stranded DNA (PubMed:15725624). {ECO:0000269|PubMed:15725624, ECO:0000269|PubMed:17012282, ECO:0000269|PubMed:19240141, ECO:0000269|PubMed:20129830}.
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum)
O26901
HELS_METTH
MKSLPPEMRQILGDCYPHIRELNPAQRSAIEAGYLESEDNYIIAIPTASGKTLLGIIAALKTVMEGGRVIYTVPLLSIQNEKIKEFRKLEEHGIRVGKDPRTSDIAVMVFESFDSLTRFSWNILREVDLLIVDEFHMIGEYTRGPVIESAITRARTLNPSVRIVALSATLSNMDEIAGWLDARVVEHDYRPVPLHREVLDTEMFGVREKNDVVLKVLERSLEDGSQTLAFVSTRRFTESLASHLADKISGKIPDDMVESFREVAGKVLEVPKSRGSPPTSTCLKLAECLEAGIAFHHAGLFNRQREIIEDEFRDGNILMITATPSLMYGVNLPSRTVVIRDYTRWTSQGPRRIPVFDYEQMSGRAGRPQYDDAGYSYLIARSHDEAMDLEEYYIRGEVERTTSRIIENRDALYRQIIAQVASGLSGTTEELADFFRNTFYGYQMVEGPFSDSFGMDSIQYEVENATEYLMRNRILYPGPEGFSATEFGLLIAKSNYSVETAIKLHQFASEMDEMDIYRLIYEITRTPDMPLISFKGRKSRDPVRDKLMEHGLFLMDVGNEEATAAALIEWINERTEYEIENAFHVYAASTRRSAYEASKIVKFFGKICEIMGVYRHSSQLEILSARLYYGVKEDAIPLVVGVRGLGRVRARKIIKTFGEDLRHVREDELKRIDGIGPKMAGAIRRYCERF
5.6.2.4
null
DNA repair [GO:0006281]
null
3'-5' DNA helicase activity [GO:0043138]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; DNA binding [GO:0003677]; isomerase activity [GO:0016853]
PF00270;PF00271;PF21280;PF12826;
1.10.3380.30;1.10.150.20;3.40.50.300;
Helicase family, Hel308 subfamily
null
null
CATALYTIC ACTIVITY: Reaction=Couples ATP hydrolysis with the unwinding of duplex DNA by translocating in the 3'-5' direction.; EC=5.6.2.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00442, ECO:0000269|PubMed:15994460, ECO:0000269|PubMed:17991488, ECO:0000269|PubMed:28738244}; CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=5.6.2.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00442, ECO:0000269|PubMed:15994460, ECO:0000269|PubMed:17991488, ECO:0000269|PubMed:28738244};
null
null
null
null
FUNCTION: DNA-dependent ATPase and 3'-5' DNA helicase that may be involved in repair of stalled replication forks. Helicase with 3'-to 5'- polarity; able to unwind over 100 bp of DNA at 50 degrees Celsius. Unwinds forked DNA, preferentially on lagging strand forks; has weaker activity on Holliday junctions. Displaces the invading strand in DNA D-loops. Unwinds short oligonucleotides from dsDNA with 3'- but not blunt ends or 5'-ssDNA tails in an ATP-dependent manner. ATPase activity is stimulated by ssDNA but not dsDNA, protein binds ssDNA, dsDNA with 5'- or 3'-overhangs but not blunt ended dsDNA and replication forks. Replication forks bind both this protein and RPA. RPA does not stimulate the helicase activity of this protein. {ECO:0000255|HAMAP-Rule:MF_00442, ECO:0000269|PubMed:15994460, ECO:0000269|PubMed:17991488, ECO:0000269|PubMed:19143605, ECO:0000269|PubMed:28738244}.
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum)
O27026
CAPPA_METTH
MKVPRCMSTQHPDNVNPPFFAEEPELGGEDEIREAYYVFSHLGCDEQMWDCEGKEVDNYVVKKLLTKYQAFFRDHVLGEDLRLTLRVPNPTVERAEAKILLETLESIPRSYDTASLFYGMDAAPVFEVILPMTSSSSCLNRIHSYYLDFVKGKERLQLADGVTVKEWIGEFRPDEINVIPLFEDHEGMLNAAKITGEYLDGKDIQEQRVFLARSDPAMNYGMISATLLNRIALSDFRDLEEESGVKLYPIIGMGSAPFRGNLRPDNVEDVTWEYRGAYTFTVQSSFKYDHEPSDVIRGIKKLRSVKPGRAAEIERESVLEIISAYCREYRRQVMDLVDIINRVARYVPGRRKRKLHIGLFGYSRSMGNVSLPRAITFTAALYSLGVPPELLGFNALSSGDLEFIEEVYPGLGRDLHDAARYANPESPFLSPEVKSSFEEYLEPEYDEGHMKTTEEIIRALRINRTANLQELILEAASQRKFLG
4.1.1.31
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:15262949};
carbon fixation [GO:0015977]; oxaloacetate metabolic process [GO:0006107]; tricarboxylic acid cycle [GO:0006099]
null
magnesium ion binding [GO:0000287]; phosphoenolpyruvate carboxylase activity [GO:0008964]
PF14010;
null
PEPCase type 2 family
null
null
CATALYTIC ACTIVITY: Reaction=oxaloacetate + phosphate = hydrogencarbonate + phosphoenolpyruvate; Xref=Rhea:RHEA:28370, ChEBI:CHEBI:16452, ChEBI:CHEBI:17544, ChEBI:CHEBI:43474, ChEBI:CHEBI:58702; EC=4.1.1.31; Evidence={ECO:0000269|PubMed:15262949};
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.8 mM for KHCO(3) {ECO:0000269|PubMed:15262949}; KM=0.46 mM for phosphoenolpyruvate {ECO:0000269|PubMed:15262949};
null
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.8. {ECO:0000269|PubMed:15262949};
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 62 degrees Celsius. {ECO:0000269|PubMed:15262949};
FUNCTION: Catalyzes the irreversible beta-carboxylation of phosphoenolpyruvate (PEP) to form oxaloacetate (OAA), a four-carbon dicarboxylic acid source for the tricarboxylic acid cycle. {ECO:0000269|PubMed:15262949}.
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum)
O27271
FTTA_METTH
MVSEMLEEIKRTIMQRLPERVQVAKVEFEGPEVVIYTKNPEIITENGNLIRDIAKDIRKRIIIRSDRSVLMDPEKAIRKIHEIVPEEAKITNISFDDVTCEVIIEARKPGLVIGKYGSTSREIVKNTGWAPKILRTPPISSEIIERIRRTLRKNSKERKKILQQLGNRIHQKPKYDNDWARLTAMGGFREVGRSCLYLQTPNSRVLLDCGVNVAGGDDKNSYPYLNVPEFTLDSLDAVIITHAHLDHSGFLPYLYHYGYDGPVYCTAPTRDLMTLLQLDHIDIAHREDEPLPFNVKHVKKSVKHTITLDYGEVTDIAPDIRLTLHNAGHILGSAMAHLHIGDGQHNMVYTGDFKYEQSRLLEAAANRFPRIETLVMESTYGGHEDVQPSRNRAEKELVKTIYSTLRRGGKILIPVFAVGRAQELMIVLEEYIRTGIIDEVPVYIDGMIWEANAIHTARPEYLSKDLRDQIFHMGHNPFISDIFHKVNGMDERREIVEGEPSIILSTSGMLTGGNSLEYFKWLCEDPDNSLVFVGYQAEGSLGRRIQKGWKEIPLKDEDDKMRVYNVRMNIKTIEGFSGHSDRRQLMEYVKRISPKPEKILLCHGDNYKTLDLASSIYRTYRIETKTPLNLETVRIQ
3.1.-.-
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|HAMAP-Rule:MF_00870, ECO:0000269|PubMed:21565697}; Note=Binds 2 Zn(2+) ions, which are required for nuclease activity (PubMed:21565697). {ECO:0000255|HAMAP-Rule:MF_00870, ECO:0000269|PubMed:21565697, ECO:0007744|PDB:2YCB};
snRNA processing [GO:0016180]
null
identical protein binding [GO:0042802]; metal ion binding [GO:0046872]; RNA binding [GO:0003723]; RNA endonuclease activity [GO:0004521]
PF10996;PF17214;PF16661;PF07521;
3.30.300.20;3.30.300.230;3.40.50.10890;3.60.15.10;
Metallo-beta-lactamase superfamily, RNA-metabolizing metallo-beta-lactamase-like family, FttA subfamily
null
null
null
null
null
null
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 22-37 degrees Celsius, less active at 55 degrees Celsius (PubMed:21565697). {ECO:0000269|PubMed:21565697};
FUNCTION: Terminates transcription on the whole genome. Termination is linked to FttA-mediated RNA cleavage and does not require NTP hydrolysis. Cleaves endonucleolytically at the RNA exit channel of RNA polymerase (RNAP); the 5'-3' exonuclease activity of this protein degrades the nascent RNA released from RNAP. {ECO:0000255|HAMAP-Rule:MF_00870}.; FUNCTION: An RNA nuclease, it bind single-stranded RNA (ssRNA) with a preference for U-rich sequences (PubMed:21565697). {ECO:0000269|PubMed:21565697}.
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum)
O27433
GLYA_METTH
MVSNQDYTEKIRQLMKDHNSWMESSINLIASENITSSRVKEALLSDLSHRYAEGLPGERLYEGCRYIDEIEELTIELSKRLFRAEHANVQPTSGVVANLACFFATAEVGDPIMAMEVPYGGHISHARVSAAGVRGFQIYTHPFDFENMNIDADAMKKKILEVKPRIILFGGSLFLFPHPVEEALEAAEEVGARIMYDGAHVLGLIAGGYFQDPLREGADMLVGSTHKTFPGPQGGIILCREELAADIDEAVFPGLVSNHHLHHVAGLGIATAEMLEFGAEYAAQTINNARKLAENLHELGFNVLCEHLDFTESHQVVMDVSDIGRAAEISKRLEANNIILNKNLLPWDDVNRSDDPSGIRIGTQEITRRGMKESEMSEVAEYIKRVVMDGKDVRDEVAEFMSSYTRVHYAFEDSEAYKYMEIQ
2.1.2.-
COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000255|HAMAP-Rule:MF_00051, ECO:0000269|Ref.2};
folic acid metabolic process [GO:0046655]; glycine biosynthetic process from serine [GO:0019264]; L-serine catabolic process [GO:0006565]; tetrahydrofolate interconversion [GO:0035999]
cytosol [GO:0005829]
cobalt ion binding [GO:0050897]; glycine hydroxymethyltransferase activity [GO:0004372]; pyridoxal phosphate binding [GO:0030170]; serine binding [GO:0070905]; zinc ion binding [GO:0008270]
PF00464;
3.90.1150.10;3.40.640.10;
SHMT family
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00051}.
CATALYTIC ACTIVITY: Reaction=5,10-methylenetetrahydromethanopterin + glycine + H2O = 5,6,7,8-tetrahydromethanopterin + L-serine; Xref=Rhea:RHEA:47104, ChEBI:CHEBI:15377, ChEBI:CHEBI:33384, ChEBI:CHEBI:57305, ChEBI:CHEBI:57818, ChEBI:CHEBI:58103; Evidence={ECO:0000255|HAMAP-Rule:MF_00051, ECO:0000269|Ref.2};
null
PATHWAY: Amino-acid biosynthesis; glycine biosynthesis; glycine from L-serine: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00051}.
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.1. {ECO:0000269|Ref.2};
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 60 degrees Celsius. {ECO:0000269|Ref.2};
FUNCTION: Catalyzes the reversible interconversion of serine and glycine with tetrahydromethanopterin (H4MPT) serving as the one-carbon carrier. Cannot use tetrahydrofolate (THF or H4PteGlu) instead of H4MPT as the pteridine substrate. Also probably exhibits a pteridine-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism. {ECO:0000269|Ref.2}.
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum)
O27564
MTHK_METTH
MVLVIEIIRKHLPRVLKVPATRILLLVLAVIIYGTAGFHFIEGESWTVSLYWTFVTIATVGYGDYSPSTPLGMYFTVTLIVLGIGTFAVAVERLLEFLINREQMKLMGLIDVAKSRHVVICGWSESTLECLRELRGSEVFVLAEDENVRKKVLRSGANFVHGDPTRVSDLEKANVRGARAVIVDLESDSETIHCILGIRKIDESVRIIAEAERYENIEQLRMAGADQVISPFVISGRLMSRSIDDGYEAMFVQDVLAEESTRRMVEVPIPEGSKLEGVSVLDADIHDVTGVIIIGVGRGDELIIDPPRDYSFRAGDIILGIGKPEEIERLKNYISA
null
null
potassium ion transport [GO:0006813]
plasma membrane [GO:0005886]
identical protein binding [GO:0042802]; metal ion binding [GO:0046872]; monoatomic cation transmembrane transporter activity [GO:0008324]
PF07885;PF02080;PF02254;
1.10.287.70;3.40.50.720;3.30.70.1450;1.20.5.870;
null
null
SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
null
null
null
null
null
FUNCTION: Calcium-gated potassium channel.
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum)
O27939
PYCA_METTH
MFSKILVANRGEIAIRVMRACRELGIKSVAVYSEADKNALFTRYADEAYEIGKPAPSQSYLRIDRILEVAEKAGAEAIHPGYGFLAENPRLGEECEKQGIKLIGPKGSVIEAMGDKITSKKLMKKAGVPVIPGTDQGVSDPDEAARIADSIGYPVIIKASAGGGGIGMRAVYEEDELIRAMESTQSVAASAFGDPTVYIEKYLERPRHIEFQVMADESGNVIHLADRECSIQRRHQKLIEEAPSPIMTPELRERMGSAAVKAAEYIGYENAGTVEFLYSNGDFYFLEMNTRIQVEHPITEVITGVDLVKEQIRVASGEELRFTQKDINIRGHAIECRINAENPLADFAPNPGKITGYRSPGGIGVRVDSGVYMNYEIPPFYDSMISKLIVWGMDRQEAINRMKRALSEYIILGVKTTIPFHKAIMRNEAFRRGELHTHFVDEYRRGIDAEMRKIVKEDQEMVERLQSTFLPSKKVAAISAAIGTYMHSRRG
6.4.1.1
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Name=Co(2+); Xref=ChEBI:CHEBI:48828;
gluconeogenesis [GO:0006094]
null
ATP binding [GO:0005524]; metal ion binding [GO:0046872]; methylcrotonoyl-CoA carboxylase activity [GO:0004485]; propionyl-CoA carboxylase activity [GO:0004658]; pyruvate carboxylase activity [GO:0004736]; urea carboxylase activity [GO:0004847]
PF02785;PF00289;PF02786;
3.30.470.20;
null
null
null
CATALYTIC ACTIVITY: Reaction=ATP + hydrogencarbonate + pyruvate = ADP + H(+) + oxaloacetate + phosphate; Xref=Rhea:RHEA:20844, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378, ChEBI:CHEBI:16452, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=6.4.1.1;
null
PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.;
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 60 degrees Celsius.;
FUNCTION: Pyruvate carboxylase catalyzes a 2-step reaction, involving the ATP-dependent carboxylation of the covalently attached biotin in the first step and the transfer of the carboxyl group to pyruvate in the second.
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum)
O28007
UDGA_ARCFU
MESLDDIVREIMSCRKCDLHKTKTNYVPGVGNEKAEIVFVGEAPGRDEDLKGEPFVGAAGKLLTEMLASIGLRREDVYITNVLKCRPPNNRDPTPEEVEKCGDYLVRQLEAIRPNVIVCLGRFAAQFIFNLFDLEFTTISRVKGKVYEVERWGKKVKVIAIYHPAAVLYRPQLREEYESDFKKIGELCGKKQPTLFDYL
3.2.2.27
null
DNA repair [GO:0006281]
null
4 iron, 4 sulfur cluster binding [GO:0051539]; metal ion binding [GO:0046872]; uracil DNA N-glycosylase activity [GO:0004844]
PF03167;
3.40.470.10;
Uracil-DNA glycosylase (UDG) superfamily, Type 4 (UDGa) family
null
null
CATALYTIC ACTIVITY: Reaction=Hydrolyzes single-stranded DNA or mismatched double-stranded DNA and polynucleotides, releasing free uracil.; EC=3.2.2.27; Evidence={ECO:0000269|PubMed:10777501, ECO:0000269|PubMed:20453094, ECO:0000269|PubMed:22646210};
null
null
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is around 6.2. {ECO:0000269|PubMed:24936520};
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Extremely thermostable, maintaining full activity after heating for 1.5 hour at 95 degrees Celsius (PubMed:10777501). Exhibits a broad temperature optimum for activity around 80 degrees Celsius (PubMed:24936520). {ECO:0000269|PubMed:10777501, ECO:0000269|PubMed:24936520};
FUNCTION: Removes uracil bases that are present in DNA as a result of either deamination of cytosine or misincorporation of dUMP instead of dTMP. Can remove uracil from double-stranded DNA containing either a U/G or U/A base pair as well as from single-stranded DNA. {ECO:0000269|PubMed:10777501, ECO:0000269|PubMed:20453094, ECO:0000269|PubMed:22646210}.
Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)
O28025
TIAS_ARCFU
MRVWVGIDDTDSSRGMCTTYLAVLAMERVERELGKVIGFPRLIRLNPTIPYKTRGNGAVSFLVEVDDVGELVDVVNEVIIEHAMLDDEKTNPGAVFVDEELAVKLKPFADKAIKDVLQIDEALFVIGKYFIPHLRHKKGRGLIGALAAVGAELEDFTLELIAYRYPERFGTEREYDEESFFDMDYELYPQTFDNVDWCNDVVVCIPNTPCPVLYGIRGESVEALYKAMESVKTEPVDRRMIFVTNHATDMHLIGEEEVHRLENYRSYRLRGRVTLEPYDIEGGHVFFEIDTKFGSVKCAAFEPTKQFRNVIRLLRKGDVVEVYGSMKKDTINLEKIQIVELAEIWVEKNPICPSCGRRMESAGRGQGFRCKKCRTKADEKLREKVERELQPGFYEVPPSARRHLSKPLIRMNVEGRHIFR
6.3.4.22
null
tRNA wobble cytosine modification [GO:0002101]
cytoplasm [GO:0005737]
ATP binding [GO:0005524]; ligase activity, forming carbon-nitrogen bonds [GO:0016879]; nucleic acid binding [GO:0003676]
PF08489;PF01336;
2.40.50.1010;3.30.70.2200;3.90.600.20;
TiaS family
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CATALYTIC ACTIVITY: Reaction=agmatine + ATP + cytidine(34) in tRNA(Ile2) + H2O = 2-agmatinylcytidine(34) in tRNA(Ile2) + AMP + 2 H(+) + 2 phosphate; Xref=Rhea:RHEA:43608, Rhea:RHEA-COMP:10625, Rhea:RHEA-COMP:10626, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58145, ChEBI:CHEBI:82748, ChEBI:CHEBI:83545, ChEBI:CHEBI:456215; EC=6.3.4.22; Evidence={ECO:0000269|PubMed:20139989};
null
null
null
null
FUNCTION: ATP-dependent agmatine transferase that catalyzes the formation of 2-agmatinylcytidine (agm2C) at the wobble position (C34) of tRNA(Ile2), converting the codon specificity from AUG to AUA. {ECO:0000269|PubMed:20139989}.
Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)
O28029
SYA_ARCFU
MTLDEEYLDITFLTENGFVRKRCPKCGKHFWTADPEREICGDPPCESYSFIGNPVFKKPFELDEMREYYLNFFERRGHGRIERYPVVARWRTDIYLTIASIADFQPFVTSGVAPPPANPLTISQPCIRLDDLDSVGRTGRHLTLFEMMAHHAFNYPGKEIYWKNETVAYCTELLNELGVKKEDIVYKEEPWAGGGNAGPCLEAIVGGLEVATLVFMNLEEHPEGDIEIKGARYRKMDNYIVDTGYGLERFVWASKGTPTVYDAIFPEVVDTIIDNSNVSFNREDERVRRIVAESSKLAGIMGELRGERLNQLRKSVADTVGVSVEELEGIVVPLEKVYSLADHTRCILFMLGDGLVPSNAGAGYLARLMIRRSLRLAEELELGLDLYDLVEMHKKILGFEFDVPLSTVQEILELEKERYRTTVSKGTRLVERLVERKKKLEKDDLIELYDSHGIPVELAVGIAAEKGAEVEMPKDIYAELAKRHSKAEKVQEKKITLQNEYPATEKLYYDDPTLLEFEAEVIGVEGDFVILNRSAFYPESGGQDNDVGYLIANGGKFEVVDVLEADGVVLHVVKGAKPEVGTKVKGVIDSDVRWRHMRHHSATHVLLYSLQKVLGNHVWQAGARKEFSKARLDVTHFRRPSEEEIKEIEMLANREILANKPIKWEWMDRIEAERKFGFRLYQGGVPPGRKIRVVQVGDDVQACGGTHCRSTGEIGMLKILKVESIQDGVIRFEFAAGEAAIEAVEEMERLLREASSILRVEPAKLPKTVERFFEEWKDQRKEIERLKSVIADLWADILMERAEEFDSMKVVAEVVDADMQALQKLAERLAEKGAVGCLMAKGEGKVFVVTFSGQKYDARELLREIGRVAKGSGGGRKDVAQGAVQQLLDREEMLDVIFRFLSEHEG
6.1.1.7
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:19423669}; Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:19423669};
alanyl-tRNA aminoacylation [GO:0006419]; negative regulation of DNA-templated transcription [GO:0045892]
cytosol [GO:0005829]
alanine-tRNA ligase activity [GO:0004813]; aminoacyl-tRNA editing activity [GO:0002161]; ATP binding [GO:0005524]; identical protein binding [GO:0042802]; tRNA binding [GO:0000049]; zinc ion binding [GO:0008270]
PF02272;PF01411;PF07973;
2.40.30.130;3.10.310.40;3.30.54.20;6.10.250.550;
Class-II aminoacyl-tRNA synthetase family
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CATALYTIC ACTIVITY: Reaction=ATP + L-alanine + tRNA(Ala) = AMP + diphosphate + L-alanyl-tRNA(Ala); Xref=Rhea:RHEA:12540, Rhea:RHEA-COMP:9657, Rhea:RHEA-COMP:9923, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57972, ChEBI:CHEBI:78442, ChEBI:CHEBI:78497, ChEBI:CHEBI:456215; EC=6.1.1.7;
null
null
null
null
FUNCTION: Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Incorrectly charged aminoacyl-tRNA(Ala) is also edited in situ by the editing domain. {ECO:0000269|PubMed:19423669}.
Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)
O28050
KATG_ARCFU
MMRQGGVMVGARKRWITDWWPNRLNLKILRQNLQNPYGEDYDYVEEVENLDIDAVIRDLKELMRSSQDWWPADFGHYGPLFIRLAWHSAGSYRIFDGRGGARDGSIRFPPRINWPDNINLDKAIRLLWPIKKKYGRKLSWADLIILAGTVAMEDMGVKLFGFALGREDIFEPDESPDWGPEEEMLTAKRGEKEELERPFAATEMGLIYVNPEGPGGNPDPLGSAQEIRVAFRRMGMNDEETVALIAGGHAFGKCHGAGPADYLGPDPSSSPIEMQGLGWKYNYGKGKGSDTFTSGLEVTWSPTPTKFGINYLRILFTYEWELEKSPAGKNQWVAKDAPEIIPDAHDPNKKHRPRMLTADLALRFDPEFSKIARRFLENPEEFEKAFAIAWYKLTHRDMGPKDCYIGKYVPEETFVWQDPLPRRDYELVDEKDVEELKRRILASGLSLSQLVYFAWASASTYRNSDRRGGANGARIRLKPMSVWEVNHPEELKKVIAAYEKIQQEFNEGAKGSEKRISIADLIVLGGIAAVEEAARRAGFSVKVPFIPGRVDAQQEHVDEEFYRVIEPFADGFRNYFRYPERINERDVYTTPEYFLVDKANLLTLTVPEMVVLIGGMRALGANYSHSDYGVLTERPGVLSNDFFVNLLDMSVEWRAADDYRYTFEGYDRKSGELRWRATRVDLILGHHDELRAVAEVYGCDDAKEKFVKDFAAVCAKVMHLDRFDLWRSNRKLYKEITAGLR
1.11.1.21
COFACTOR: Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000255|HAMAP-Rule:MF_01961}; Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per dimer. {ECO:0000255|HAMAP-Rule:MF_01961};
cellular response to hydrogen peroxide [GO:0070301]; hydrogen peroxide catabolic process [GO:0042744]
cytosol [GO:0005829]
catalase activity [GO:0004096]; heme binding [GO:0020037]; metal ion binding [GO:0046872]
PF00141;
1.10.520.10;1.10.420.10;
Peroxidase family, Peroxidase/catalase subfamily
PTM: Formation of the three residue Trp-Tyr-Met cross-link is important for the catalase, but not the peroxidase activity of the enzyme. {ECO:0000255|HAMAP-Rule:MF_01961}.
null
CATALYTIC ACTIVITY: Reaction=AH2 + H2O2 = A + 2 H2O; Xref=Rhea:RHEA:30275, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240, ChEBI:CHEBI:17499; EC=1.11.1.21; Evidence={ECO:0000255|HAMAP-Rule:MF_01961}; CATALYTIC ACTIVITY: Reaction=2 H2O2 = 2 H2O + O2; Xref=Rhea:RHEA:20309, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240; EC=1.11.1.21; Evidence={ECO:0000255|HAMAP-Rule:MF_01961};
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=32 mM for H(2)O(2) for the catalase reaction (at pH 5.5-6.0) {ECO:0000269|PubMed:18178143}; KM=3.8 mM for H(2)O(2) for the catalase reaction (at pH 7.0) {ECO:0000269|PubMed:18178143}; KM=95 mM for H(2)O(2) for the peroxidase reaction {ECO:0000269|PubMed:18178143}; KM=16 mM for ABTS for the peroxidase reaction {ECO:0000269|PubMed:18178143}; Vmax=11760 umol/min/mg enzyme for H(2)O(2) for the catalase reaction (at pH 5.5-6.0) {ECO:0000269|PubMed:18178143}; Vmax=5500 umol/min/mg enzyme for H(2)O(2) for the catalase reaction (at pH 7.0) {ECO:0000269|PubMed:18178143}; Vmax=12 umol/min/mg enzyme for ABTS for the peroxidase reaction {ECO:0000269|PubMed:18178143};
null
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 4.5 for the peroxidase reaction. {ECO:0000269|PubMed:18178143};
null
FUNCTION: Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity. Also displays NADH oxidase, INH lyase and isonicotinoyl-NAD synthase activities.
Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)
O28126
CCA_ARCFU
MKVEEILEKALELVIPDEEEVRKGREAEEELRRRLDELGVEYVFVGSYARNTWLKGSLEIDVFLLFPEEFSKEELRERGLEIGKAVLDSYEIRYAEHPYVHGVVKGVEVDVVPCYKLKEPKNIKSAVDRTPFHHKWLEGRIKGKENEVRLLKGFLKANGIYGAEYKVRGFSGYLCELLIVFYGSFLETVKNARRWTRRTVIDVAKGEVRKGEEFFVVDPVDEKRNVAANLSLDNLARFVHLCREFMEAPSLGFFKPKHPLEIEPERLRKIVEERGTAVFAVKFRKPDIVDDNLYPQLERASRKIFEFLERENFMPLRSAFKASEEFCYLLFECQIKEISRVFRRMGPQFEDERNVKKFLSRNRAFRPFIENGRWWAFEMRKFTTPEEGVRSYASTHWHTLGKNVGESIREYFEIISGEKLFKEPVTAELCEMMGVKD
2.7.7.72
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000305|PubMed:14592988};
RNA repair [GO:0042245]; tRNA 3'-terminal CCA addition [GO:0001680]; tRNA surveillance [GO:0106354]
null
ATP binding [GO:0005524]; CCACCA tRNA nucleotidyltransferase activity [GO:0160016]; magnesium ion binding [GO:0000287]; tRNA binding [GO:0000049]
PF21133;PF01909;PF09249;
3.30.70.1550;3.30.460.10;1.10.1410.30;3.30.70.590;
TRNA nucleotidyltransferase/poly(A) polymerase family, Archaeal CCA-adding enzyme subfamily
null
null
CATALYTIC ACTIVITY: Reaction=a tRNA precursor + ATP + 2 CTP = a tRNA with a 3' CCA end + 3 diphosphate; Xref=Rhea:RHEA:14433, Rhea:RHEA-COMP:10465, Rhea:RHEA-COMP:10468, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:37563, ChEBI:CHEBI:74896, ChEBI:CHEBI:83071; EC=2.7.7.72; Evidence={ECO:0000269|PubMed:14592988, ECO:0000269|PubMed:25640237}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14434; Evidence={ECO:0000269|PubMed:14592988, ECO:0000269|PubMed:25640237}; CATALYTIC ACTIVITY: Reaction=a tRNA with a 3' CCA end + ATP + 2 CTP = a tRNA with a 3' CCACCA end + 3 diphosphate; Xref=Rhea:RHEA:76235, Rhea:RHEA-COMP:10468, Rhea:RHEA-COMP:18655, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:37563, ChEBI:CHEBI:83071, ChEBI:CHEBI:195187; Evidence={ECO:0000269|PubMed:25640237}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:76236; Evidence={ECO:0000269|PubMed:25640237};
null
null
null
null
FUNCTION: Catalyzes the addition and repair of the essential 3'-terminal CCA sequence in tRNAs without using a nucleic acid template (PubMed:14592988, PubMed:25640237). Adds these three nucleotides in the order of C, C, and A to the tRNA nucleotide-73, using CTP and ATP as substrates and producing inorganic pyrophosphate (PubMed:14592988, PubMed:25640237). tRNA 3'-terminal CCA addition is required both for tRNA processing and repair (PubMed:25640237). Also involved in tRNA surveillance by mediating tandem CCA addition to generate a CCACCA at the 3' terminus of unstable tRNAs (PubMed:25640237). While stable tRNAs receive only 3'-terminal CCA, unstable tRNAs are marked with CCACCA and rapidly degraded (PubMed:25640237). The structural flexibility of RNA controls the choice between CCA versus CCACCA addition: following the first CCA addition cycle, nucleotide-binding to the active site triggers a clockwise screw motion, producing torque on the RNA (PubMed:25640237). This ejects stable RNAs, whereas unstable RNAs are refolded while bound to the enzyme and subjected to a second CCA catalytic cycle (PubMed:25640237). {ECO:0000269|PubMed:14592988, ECO:0000269|PubMed:25640237}.
Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)
O28440
ASPD_ARCFU
MLVGLIGYGAIGKFLAEWLERNGFEIAAILDVRGEHEKMVRGIDEFLQREMDVAVEAASQQAVKDYAEKILKAGIDLIVLSTGAFADRDFLSRVREVCRKTGRRVYIASGAIGGLDAIFSASELIEEIVLTTRKNWRQFGRKGVIFEGSASEAAQKFPKNLNVAATLSIASGKDVKVRLVADEVEENIHEILVRGEFGEMEIRVRNRPMRENPKTSYLAALSVTRILRNLKEGLVV
1.4.1.21
null
NAD biosynthetic process [GO:0009435]
null
aspartate dehydrogenase activity [GO:0033735]; NAD binding [GO:0051287]; NADP binding [GO:0050661]; oxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor [GO:0016639]
PF01958;PF03447;
3.40.50.720;
L-aspartate dehydrogenase family
null
null
CATALYTIC ACTIVITY: Reaction=H2O + L-aspartate + NADP(+) = H(+) + NADPH + NH4(+) + oxaloacetate; Xref=Rhea:RHEA:11784, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16452, ChEBI:CHEBI:28938, ChEBI:CHEBI:29991, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.4.1.21; Evidence={ECO:0000255|HAMAP-Rule:MF_01265, ECO:0000269|PubMed:16731057}; CATALYTIC ACTIVITY: Reaction=H2O + L-aspartate + NAD(+) = H(+) + NADH + NH4(+) + oxaloacetate; Xref=Rhea:RHEA:11788, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16452, ChEBI:CHEBI:28938, ChEBI:CHEBI:29991, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.4.1.21; Evidence={ECO:0000255|HAMAP-Rule:MF_01265, ECO:0000269|PubMed:16731057};
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.19 mM for L-aspartate (in the presence of NAD) {ECO:0000269|PubMed:16731057}; KM=4.3 mM for L-aspartate (in the presence of NADP) {ECO:0000269|PubMed:16731057}; KM=0.11 mM for NAD {ECO:0000269|PubMed:16731057}; KM=0.32 mM for NADP {ECO:0000269|PubMed:16731057}; KM=1.2 mM for oxaloacetate (in the presence of NADH and NH(3)) {ECO:0000269|PubMed:16731057}; KM=0.014 mM for NADH (in the presence of oxaloacetate and NH(3)) {ECO:0000269|PubMed:16731057}; KM=167 mM for NH(3) (in the presence of oxaloacetate and NADH) {ECO:0000269|PubMed:16731057};
PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; iminoaspartate from L-aspartate (dehydrogenase route): step 1/1. {ECO:0000255|HAMAP-Rule:MF_01265, ECO:0000305|PubMed:16731057}.
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is around 11.6. {ECO:0000269|PubMed:16731057};
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 80 degrees Celsius. {ECO:0000269|PubMed:16731057};
FUNCTION: Specifically catalyzes the NAD or NADP-dependent dehydrogenation of L-aspartate to iminoaspartate. {ECO:0000255|HAMAP-Rule:MF_01265, ECO:0000269|PubMed:16731057}.
Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)
O28471
RIO1_ARCFU
MKDLKKIESYLDKLRIKEKDGEERKIYAEVLDGRTLKTLYKLSAKGYITAMGGVISTGKEANVFYADGVFDGKPVAMAVKIYRIETSEFDKMDEYLYGDERFDMRRISPKEKVFIWTEKEFRNLERAKEAGVSVPQPYTYMKNVLLMEFIGEDELPAPTLVELGRELKELDVEGIFNDVVENVKRLYQEAELVHADLSEYNIMYIDKVYFIDMGQAVTLRHPMAESYLERDVRNIIRFFSKYGVKADFEEMLKEVKGE
2.7.11.1
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000305|PubMed:16008568};
maturation of SSU-rRNA [GO:0030490]; phosphorylation [GO:0016310]
cytosol [GO:0005829]; preribosome, small subunit precursor [GO:0030688]
ATP binding [GO:0005524]; hydrolase activity [GO:0016787]; metal ion binding [GO:0046872]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]
PF01163;
1.10.510.10;
Protein kinase superfamily, RIO-type Ser/Thr kinase family
null
null
CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1;
null
null
null
null
FUNCTION: Autophosphorylation of the rio1 protein is not necessary for maintenance of kinase activity. Prefers ATP over GTP (PubMed:16008568). The yeast ortholog is involved in ribosome biogenesis. Despite the protein kinase domain is proposed to act predominantly as an ATPase (By similarity). {ECO:0000250|UniProtKB:G0S3J5, ECO:0000269|PubMed:16008568}.
Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)
O28597
NPD1_ARCFU
MDEKLLKTIAESKYLVALTGAGVSAESGIPTFRGKDGLWNRYRPEELANPQAFAKDPEKVWKWYAWRMEKVFNAQPNKAHQAFAELERLGVLKCLITQNVDDLHERAGSRNVIHLHGSLRVVRCTSCNNSFEVESAPKIPPLPKCDKCGSLLRPGVVWFGEMLPPDVLDRAMREVERADVIIVAGTSAVVQPAASLPLIVKQRGGAIIEINPDETPLTPIADYSLRGKAGEVMDELVRHVRKALS
2.3.1.286
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|HAMAP-Rule:MF_01121, ECO:0000269|PubMed:11336676, ECO:0000269|PubMed:12091395}; Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01121, ECO:0000269|PubMed:11336676, ECO:0000269|PubMed:12091395};
null
cytoplasm [GO:0005737]
NAD+ binding [GO:0070403]; NAD-dependent histone deacetylase activity [GO:0017136]; protein-malonyllysine demalonylase activity [GO:0036054]; protein-succinyllysine desuccinylase activity [GO:0036055]; transferase activity [GO:0016740]; zinc ion binding [GO:0008270]
PF02146;
3.30.1600.10;3.40.50.1220;
Sirtuin family, Class III subfamily
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01121}.
CATALYTIC ACTIVITY: Reaction=H2O + N(6)-acetyl-L-lysyl-[protein] + NAD(+) = 2''-O-acetyl-ADP-D-ribose + L-lysyl-[protein] + nicotinamide; Xref=Rhea:RHEA:43636, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:10731, ChEBI:CHEBI:15377, ChEBI:CHEBI:17154, ChEBI:CHEBI:29969, ChEBI:CHEBI:57540, ChEBI:CHEBI:61930, ChEBI:CHEBI:83767; EC=2.3.1.286; Evidence={ECO:0000255|HAMAP-Rule:MF_01121}; CATALYTIC ACTIVITY: Reaction=H2O + N(6)-succinyl-L-lysyl-[protein] + NAD(+) = 2''-O-succinyl-ADP-D-ribose + L-lysyl-[protein] + nicotinamide; Xref=Rhea:RHEA:47668, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:11877, ChEBI:CHEBI:15377, ChEBI:CHEBI:17154, ChEBI:CHEBI:29969, ChEBI:CHEBI:57540, ChEBI:CHEBI:87830, ChEBI:CHEBI:87832; Evidence={ECO:0000255|HAMAP-Rule:MF_01121};
null
null
null
null
FUNCTION: NAD-dependent lysine deacetylase and desuccinylase that specifically removes acetyl and succinyl groups on target proteins. Modulates the activities of several proteins which are inactive in their acylated form. Deacetylates the N-terminal lysine residue of Alba, the major archaeal chromatin protein and that, in turn, increases Alba's DNA binding affinity, thereby repressing transcription. {ECO:0000255|HAMAP-Rule:MF_01121, ECO:0000269|PubMed:10841563}.
Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)
O28608
ALADH_ARCFU
METLILTQEEVESLISMDEAMNAVEEAFRLYALGKAQMPPKVYLEFEKGDLRAMPAHLMGYAGLKWVNSHPGNPDKGLPTVMALMILNSPETGFPLAVMDATYTTSLRTGAAGGIAAKYLARKNSSVFGFIGCGTQAYFQLEALRRVFDIGEVKAYDVREKAAKKFVSYCEDRGISASVQPAEEASRCDVLVTTTPSRKPVVKAEWVEEGTHINAIGADGPGKQELDVEILKKAKIVVDDLEQAKHGGEINVAVSKGVIGVEDVHATIGEVIAGLKDGRESDEEITIFDSTGLAIQDVAVAKVVYENALSKNVGSKIKFFRI
1.4.1.1
null
alanine metabolic process [GO:0006522]; thyroid hormone metabolic process [GO:0042403]
cytoplasm [GO:0005737]
alanine dehydrogenase activity [GO:0000286]; NAD binding [GO:0051287]; protein homodimerization activity [GO:0042803]; thyroid hormone binding [GO:0070324]
PF02423;
3.40.50.720;3.30.1780.10;
Ornithine cyclodeaminase/mu-crystallin family, Archaeal alanine dehydrogenase subfamily
null
null
CATALYTIC ACTIVITY: Reaction=H2O + L-alanine + NAD(+) = H(+) + NADH + NH4(+) + pyruvate; Xref=Rhea:RHEA:18405, ChEBI:CHEBI:15361, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28938, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:57972; EC=1.4.1.1; Evidence={ECO:0000255|HAMAP-Rule:MF_00935, ECO:0000269|PubMed:15516582};
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.71 mM for L-alanine (at pH 8.5 and 82 degrees Celsius) {ECO:0000269|PubMed:15516582}; KM=0.085 mM for L-2-aminobutyrate (at pH 8.5 and 82 degrees Celsius) {ECO:0000269|PubMed:15516582}; KM=0.6 mM for NAD(+) (at pH 8.5 and 82 degrees Celsius) {ECO:0000269|PubMed:15516582}; KM=0.16 mM for pyruvate (at pH 8.5 and 82 degrees Celsius) {ECO:0000269|PubMed:15516582}; KM=0.48 mM for 2-oxobutyrate (at pH 8.5 and 82 degrees Celsius) {ECO:0000269|PubMed:15516582}; KM=0.97 mM for oxaloacetate (at pH 8.5 and 82 degrees Celsius) {ECO:0000269|PubMed:15516582}; KM=0.02 mM for NADH (at pH 8.5 and 82 degrees Celsius) {ECO:0000269|PubMed:15516582}; KM=17.3 mM for NH4(+) (at pH 8.5 and 82 degrees Celsius) {ECO:0000269|PubMed:15516582}; Note=kcat is 6.1 sec(-1) and 9.6 sec(-1) for the oxidative deamination of L-alanine and L-2-aminobutyrate, respectively (at pH 8.5 and 82 degrees Celsius). kcat is 118 sec(-1), 143 sec(-1) and 113 sec(-1) for the reductive amination of pyruvate, 2-oxobutyrate and oxaloacetate, respectively (at pH 8.5 and 82 degrees Celsius).;
null
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is about 7.0 for both the deamination and amination reactions. {ECO:0000269|PubMed:15516582};
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 82 degrees Celsius for the reductive amination of pyruvate. Retains 30% of its maximum activity at 25 degrees Celsius. Completely loses its activity when incubated at 90 degrees Celsius for 2 hours. The thermostability of the enzyme is increased by more than 10-fold by 1.5 M KCl to a half-life of 55 hours at 90 degrees Celsius. {ECO:0000269|PubMed:15516582};
FUNCTION: Catalyzes the NAD(+)-dependent oxidative deamination of L-alanine to pyruvate, and the reverse reaction, the reductive amination of pyruvate. Its physiological role is not known. Cannot use NADP(+) instead of NAD(+) as a cosubstrate. In the deamination direction, can also efficiently use L-2-aminobutyrate as substrate. In the reductive amination direction, also exhibits high activity with 2-oxobutyrate and oxaloacetate as substrate. In contrast to bacterial homologs, does not exhibit any ornithine cyclodeaminase activity. {ECO:0000255|HAMAP-Rule:MF_00935, ECO:0000269|PubMed:15516582}.
Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)
O29238
RGYR_ARCFU
MIPVVYSNLCPVCGGDLESKEIEKHVCFRKKRSLCLFPEDFLLKEFVEFFRKCVGEPRAIQKMWAKRILRKESFAATAPTGVGKTSFGLAMSLFLALKGKRCYVIFPTSLLVIQAAETIRKYAEKAGVGTENLIGYYHGRIPKREKENFMQNLRNFKIVITTTQFLSKHYRELGHFDFIFVDDVDAILKASKNVDKLLHLLGFHYDLKTKSWVGEARGCLMVSTATAKKGKKAELFRQLLNFDIGSSRITVRNVEDVAVNDESISTLSSILEKLGTGGIIYARTGEEAEEIYESLKNKFRIGIVTATKKGDYEKFVEGEIDHLIGTAHYYGTLVRGLDLPERIRFAVFVGCPSFRVTIEDIDSLSPQMVKLLAYLYRNVDEIERLLPAVERHIDEVREILKKVMGKERPQAKDVVVREGEVIFPDLRTYIQGSGRTSRLFAGGLTKGASFLLEDDSELLSAFIERAKLYDIEFKSIDEVDFEKLSRELDESRDRYRRRQEFDLIKPALFIVESPTKARQISRFFGKPSVKVLDGAVVYEIPMQKYVLMVTASIGHVVDLITNRGFHGVLVNGRFVPVYASIKRCRDCGYQFTEDRESCPKCGSENVDNSRSRIEALRKLAHDAEFVIVGTDPDTEGEKIAWDLKNLLSGCGAVKRAEFHEVTRRAILEALESLRDVDENLVKAQVVRRIEDRWIGFVLSQKLWERFNNRNLSAGRAQTPVLGWIIDRFQESRERRKIAIVRDFDLVLEHDEEEFDLTIKLVEEREELRTPLPPYTTETMLSDANRILKFSVKQTMQIAQELFENGLITYHRTDSTRVSDVGQRIAKEYLGDDFVGREWGESGAHECIRPTRPLTRDDVQRLIQEGVLVVEGLRWEHFALYDLIFRRFMASQCRPFKVVVKKYSIEFDGKTAEEERIVRAEGRAYELYRAVWVKNELPTGTFRVKAEVKSVPKVLPFTQSEIIQMMKERGIGRPSTYATIVDRLFMRNYVVEKYGRMIPTKLGIDVFRFLVRRYAKFVSEDRTRDLESRMDAIERGELDYLKALEDLYAEIKSID
5.6.2.-
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|HAMAP-Rule:MF_01125}; Note=Binds 2 zinc ions per subunit. {ECO:0000255|HAMAP-Rule:MF_01125}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_01125};
DNA topological change [GO:0006265]; DNA unwinding involved in DNA replication [GO:0006268]
cytoplasm [GO:0005737]
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; DNA binding [GO:0003677]; DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity [GO:0003918]; reverse gyrase activity [GO:0160097]; zinc ion binding [GO:0008270]
PF00270;PF01131;PF01751;
2.60.510.20;3.30.56.120;3.40.50.140;3.40.50.300;2.20.20.30;1.10.460.10;1.10.290.10;
DEAD box helicase family, DDVD subfamily; Type IA topoisomerase family
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01125}.
CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; Evidence={ECO:0000255|HAMAP-Rule:MF_01125};
null
null
null
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 80 degrees Celsius for positive supercoiling (PubMed:12048189, PubMed:16407212). Optimum temperature is 80 degrees Celsius for relaxation of negative supercoils (PubMed:16407212). {ECO:0000269|PubMed:12048189, ECO:0000269|PubMed:16407212};
FUNCTION: Modifies the topological state of DNA by introducing positive supercoils in an ATP-dependent process, increasing the linking number in steps of +1 (PubMed:12048189, PubMed:12755601, PubMed:16407212). Very efficient supercoiling occurs on relaxed DNA with a single-stranded bubble; the minimal bubble is 20 nucleotides (nt) and up to 10 positive supercoils can be introduced into a 3.1 kb plasmid with a 50 nt bubble (PubMed:16407212). Positively supercoils DNA with all (d)NTPS, although it requires about 10-fold more of non-(d)ATP (PubMed:12048189). In the absence of ATP (or at low levels of enzyme), or in the presence of ADP, relaxes negative supercoils (PubMed:12048189, PubMed:12755601, PubMed:16407212). Only relaxes positive supercoils when the substrate contains a bubble (PubMed:16407212). Also promotes strand annealing of complementary ssDNA circles (PubMed:16407212). Binds to single-stranded DNA, transiently cleaves and then rejoins the ends, introducing a positive supercoil in the process. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(5'-phosphotyrosyl)-enzyme intermediate. Probably involved in rewinding DNA strands in regions of the chromosome that have opened up to allow replication, transcription, DNA repair and/or for DNA protection (Probable) (PubMed:16407212). {ECO:0000269|PubMed:12048189, ECO:0000269|PubMed:12755601, ECO:0000269|PubMed:16407212, ECO:0000305|PubMed:16407212}.; FUNCTION: In vitro protects DNA against degradation at 90 degrees Celsius, reducing dsDNA breakage about 8-fold; ATP hydrolysis is not necessary, while ADP decreases the protection somewhat (PubMed:15247343). Coats all forms of dsDNA; the DNA is protected against cleavage and transcription (PubMed:15247343). Recognizes nicked DNA and forms a coat at the nicking site, which may help hold DNA in a structure amenable to repair (PubMed:15247343). {ECO:0000269|PubMed:15247343}.
Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)
O29370
FNO_ARCFU
MRVALLGGTGNLGKGLALRLATLGHEIVVGSRREEKAEAKAAEYRRIAGDASITGMKNEDAAEACDIAVLTIPWEHAIDTARDLKNILREKIVVSPLVPVSRGAKGFTYSSERSAAEIVAEVLESEKVVSALHTIPAARFANLDEKFDWDVPVCGDDDESKKVVMSLISEIDGLRPLDAGPLSNSRLVESLTPLILNIMRFNGMGELGIKFL
1.5.1.40
null
copper ion import [GO:0015677]; NADPH regeneration [GO:0006740]
plasma membrane [GO:0005886]
8-hydroxy-5-deazaflavin:NADPH oxidoreductase activity [GO:0102261]; coenzyme F420 binding [GO:0070967]; cupric reductase activity [GO:0008823]; ferric-chelate reductase (NADPH) activity [GO:0052851]; NADP binding [GO:0050661]; reduced coenzyme F420:NADP+ oxidoreductase activity [GO:0052808]
PF03807;
3.40.50.720;
F420-dependent NADP reductase family
null
null
CATALYTIC ACTIVITY: Reaction=NADP(+) + reduced coenzyme F420-(gamma-L-Glu)(n) = 2 H(+) + NADPH + oxidized coenzyme F420-(gamma-L-Glu)(n); Xref=Rhea:RHEA:31363, Rhea:RHEA-COMP:12939, Rhea:RHEA-COMP:14378, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:133980, ChEBI:CHEBI:139511; EC=1.5.1.40; Evidence={ECO:0000269|Ref.2};
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=20 uM for reduced coenzyme F420 (at pH 8.0 and 65 degrees Celsius) {ECO:0000269|Ref.2}; KM=40 uM for NADP(+) (at pH 8.0 and 65 degrees Celsius) {ECO:0000269|Ref.2}; KM=10 uM for oxidized coenzyme F420 (at pH 5.5 and 65 degrees Celsius) {ECO:0000269|Ref.2}; KM=40 uM for NADPH (at pH 5.5 and 65 degrees Celsius) {ECO:0000269|Ref.2}; Vmax=660 umol/min/mg enzyme for NADP reduction with F420H(2) (at pH 5.5 and 80 degrees Celsius) {ECO:0000269|Ref.2};
null
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.0 for NADP reduction with F420H(2). Optimum pH is 5.5 for F420 reduction with NADPH. {ECO:0000269|Ref.2};
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 80 degrees Celsius. Is highly thermostable. {ECO:0000269|Ref.2};
FUNCTION: Catalyzes the reversible reduction of NADP(+) by F420H(2). In this reaction the proS hydrogen at C5 of F420 is transferred into the proS position at C4 of NADPH. {ECO:0000269|PubMed:11726492, ECO:0000269|Ref.2}.
Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)
O29390
GPDA_ARCFU
MIVSILGAGAMGSALSVPLVDNGNEVRIWGTEFDTEILKSISAGREHPRLGVKLNGVEIFWPEQLEKCLENAEVVLLGVSTDGVLPVMSRILPYLKDQYIVLISKGLIDFDNSVLTVPEAVWRLKHDLRERTVAITGPAIAREVAKRMPTTVVFSSPSESSANKMKEIFETEYFGVEVTTDIIGTEITSALKNVYSIAIAWIRGYESRKNVEMSNAKGVIATRAINEMAELIEILGGDRETAFGLSGFGDLIATFRGGRNGMLGELLGKGLSIDEAMEELERRGVGVVEGYKTAEKAYRLSSKINADTKLLDSIYRVLYEGLKVEEVLFELATFK
1.1.1.-
null
carbohydrate metabolic process [GO:0005975]; glycerol-3-phosphate biosynthetic process [GO:0046167]; glycerol-3-phosphate catabolic process [GO:0046168]; glycerophospholipid biosynthetic process [GO:0046474]; NADH oxidation [GO:0006116]
cytosol [GO:0005829]; glycerol-3-phosphate dehydrogenase complex [GO:0009331]
glycerol-3-phosphate dehydrogenase [NAD(P)+] activity [GO:0047952]; NAD binding [GO:0051287]
PF07479;PF01210;
3.40.50.720;
NAD-dependent glycerol-3-phosphate dehydrogenase family
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CATALYTIC ACTIVITY: Reaction=NADP(+) + sn-glycerol 3-phosphate = dihydroxyacetone phosphate + H(+) + NADPH; Xref=Rhea:RHEA:11096, ChEBI:CHEBI:15378, ChEBI:CHEBI:57597, ChEBI:CHEBI:57642, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; Evidence={ECO:0000269|PubMed:15557260}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:11098; Evidence={ECO:0000305|PubMed:15557260};
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=40 uM for NADPH {ECO:0000269|PubMed:15557260}; KM=1 mM for dihydroxyacetone phosphate {ECO:0000269|PubMed:15557260}; KM=0.8 mM for NADP(+) {ECO:0000269|PubMed:15557260}; KM=0.1 mM for sn-glycerol 3-phosphate {ECO:0000269|PubMed:15557260}; Vmax=44 umol/min/mg enzyme for the NADPH-dependent dihydroxyacetone phosphate reduction {ECO:0000269|PubMed:15557260}; Vmax=4 umol/min/mg enzyme for the NADP(+)-dependent sn-glycerol 3-phosphate oxidation {ECO:0000269|PubMed:15557260};
null
null
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 70 degrees Celsius. Is thermostable up to 85 degrees Celsius. {ECO:0000269|PubMed:15557260};
FUNCTION: Catalyzes the reduction of the glycolytic intermediate dihydroxyacetone phosphate (DHAP) to sn-glycerol 3-phosphate (G3P). Shows a 15-fold preference for NADPH over NADH in the reduction process. Can also catalyze the reverse reaction in vitro. Shows no activity with dihydroxyacetone, glycerol, glycerol-2-phosphate, D-glyceraldehyde-3-phosphate, DL-glyceraldehyde, D-erythrose-4-phosphate, D-fructose-6-phosphate, beta-D-glucose-6-phosphate, or alpha-D-galactose-1-phosphate. {ECO:0000269|PubMed:15557260}.
Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)
O29428
FERCR_ARCFU
MDVEAFYKISYGLYIVTSESNGRKCGQIANTVFQLTSKPVQIAVCLNKENDTHNAVKESGAFGVSVLELETPMEFIGRFGFRKSSEFEKFDGVEYKTGKTGVPLVTQHAVAVIEAKVVKECDVGTHTLFVGEAVDAEVLKDAEVLTYADYHLMKKGKTPRTATVYFESK
1.16.1.10
COFACTOR: Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000269|PubMed:10593977}; Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|PubMed:10593977};
pyrimidine nucleobase catabolic process [GO:0006208]
null
ferric-chelate reductase (NADH) activity [GO:0140618]; ferric-chelate reductase (NADPH) activity [GO:0052851]; FMN binding [GO:0010181]; oxidoreductase activity, acting on metal ions, NAD or NADP as acceptor [GO:0016723]; protein homodimerization activity [GO:0042803]; riboflavin reductase (NADPH) activity [GO:0042602]
PF01613;
null
Non-flavoprotein flavin reductase family
null
null
CATALYTIC ACTIVITY: Reaction=2 a Fe(II)-siderophore + H(+) + NAD(+) = 2 a Fe(III)-siderophore + NADH; Xref=Rhea:RHEA:15061, Rhea:RHEA-COMP:11342, Rhea:RHEA-COMP:11344, ChEBI:CHEBI:15378, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.16.1.10; Evidence={ECO:0000269|PubMed:10593977}; CATALYTIC ACTIVITY: Reaction=2 a Fe(II)-siderophore + H(+) + NADP(+) = 2 a Fe(III)-siderophore + NADPH; Xref=Rhea:RHEA:28795, Rhea:RHEA-COMP:11342, Rhea:RHEA-COMP:11344, ChEBI:CHEBI:15378, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.16.1.10; Evidence={ECO:0000269|PubMed:10593977};
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=61 uM for NADH (with Fe(+3) as acceptor) {ECO:0000269|PubMed:10593977}; KM=80 uM for NAD(P)H (with Fe(+3) as acceptor) {ECO:0000269|PubMed:10593977}; KM=66 uM for Fe(+3) (with NAD(P)H as donor) {ECO:0000269|PubMed:10593977}; KM=0.3 uM for FMN (with NAD(P)H as donor) {ECO:0000269|PubMed:10593977}; Vmax=4935 umol/min/mg enzyme with NADH as donor and Fe(3+) as acceptor {ECO:0000269|PubMed:10593977}; Vmax=3505 umol/min/mg enzyme with NAD(P)H as donor and Fe(3+) as acceptor {ECO:0000269|PubMed:10593977}; Vmax=280 umol/min/mg enzyme with NAD(P)H as donor and FMN as acceptor {ECO:0000269|PubMed:10593977}; Vmax=350 umol/min/mg enzyme with NAD(P)H as donor and FAD as acceptor {ECO:0000269|PubMed:10593977};
null
null
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 88 degrees Celsius. {ECO:0000269|PubMed:10593977};
FUNCTION: Catalyzes the reduction of bound ferric iron (Fe(3+)) in a variety of iron chelators (siderophores) using NAD(P)H as the electron donor, resulting in the release of Fe(2+). Not active with uncomplexed Fe(3+). Also reduces FMN and FAD, but not riboflavin. {ECO:0000269|PubMed:10593977}.
Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)
O29634
RNH2_ARCFU
MKAGIDEAGKGCVIGPLVVAGVACSDEDRLRKLGVKDSKKLSQGRREELAEEIRKICRTEVLKVSPENLDERMAAKTINEILKECYAEIILRLKPEIAYVDSPDVIPERLSRELEEITGLRVVAEHKADEKYPLVAAASIIAKVEREREIERLKEKFGDFGSGYASDPRTREVLKEWIASGRIPSCVRMRWKTVSNLRQKTLDDF
3.1.26.4
COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:11527410}; Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:11527410}; Note=Manganese or magnesium. Binds 1 divalent metal ion per monomer in the absence of substrate. May bind a second metal ion after substrate binding. {ECO:0000269|PubMed:11527410};
DNA replication, removal of RNA primer [GO:0043137]; mismatch repair [GO:0006298]
cytoplasm [GO:0005737]; ribonuclease H2 complex [GO:0032299]
manganese ion binding [GO:0030145]; RNA binding [GO:0003723]; RNA-DNA hybrid ribonuclease activity [GO:0004523]
PF01351;
3.30.420.10;1.10.10.460;
RNase HII family
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CATALYTIC ACTIVITY: Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.; EC=3.1.26.4;
null
null
null
null
FUNCTION: Endonuclease that specifically degrades the RNA of RNA-DNA hybrids. {ECO:0000250}.
Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)
O29777
COPA_ARCFU
MVKDTYISSASKTPPMERTVRVTGMTCAMCVKSIETAVGSLEGVEEVRVNLATETAFIRFDEKRIDFETIKRVIEDLGYGVVDEQAAVSAEVEHLSRMKRKLYVAAFAGVLLLFLAHFISLPYEDFVQLLIALPAIFYSGSSIFKAAFSALRRRTLNMDVMYSMGVGAAFLASVLSTAGVLPREYSFYETSVLLLAFLLLGRTLEARAKSRTGEAIKKLVGLQAKTAVVIRDGKEIAVPVEEVAVGDIVIVRPGEKIPVDGVVVEGESYVDESMISGEPVPVLKSKGDEVFGATINNTGVLKIRATRVGGETLLAQIVKLVEDAMGSKPPIQRLADKVVAYFIPTVLLVAISAFIYWYFIAHAPLLFAFTTLIAVLVVACPCAFGLATPTALTVGMGKGAELGILIKNADALEVAEKVTAVIFDKTGTLTKGKPEVTDLVPLNGDERELLRLAAIAERRSEHPIAEAIVKKALEHGIELGEPEKVEVIAGEGVVADGILVGNKRLMEDFGVAVSNEVELALEKLEREAKTAVIVARNGRVEGIIAVSDTLKESAKPAVQELKRMGIKVGMITGDNWRSAEAISRELNLDLVIAEVLPHQKSEEVKKLQAKEVVAFVGDGINDAPALAQADLGIAVGSGSDVAVESGDIVLIRDDLRDVVAAIQLSRKTMSKIKQNIFWALIYNVILIPAAAGLLYPIFGVVFRPEFAGLAMAMSSVSVVANSLLLRNYVPPIRRGGDSVEKIVLELSGLSCHHCVARVKKALEEAGAKVEKVDLNEAVVAGNKEDVDKYIKAVEAAGYQAKLRS
7.2.2.8
null
copper ion export [GO:0060003]; copper ion import [GO:0015677]; intracellular copper ion homeostasis [GO:0006878]
plasma membrane [GO:0005886]
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; copper ion binding [GO:0005507]; identical protein binding [GO:0042802]; P-type divalent copper transporter activity [GO:0043682]; P-type monovalent copper transporter activity [GO:0140581]
PF00122;PF00403;PF00702;
3.30.70.100;3.40.1110.10;2.70.150.10;3.40.50.1000;
Cation transport ATPase (P-type) (TC 3.A.3) family, Type IB subfamily
null
SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CATALYTIC ACTIVITY: Reaction=ATP + Cu(+)(in) + H2O = ADP + Cu(+)(out) + H(+) + phosphate; Xref=Rhea:RHEA:25792, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:49552, ChEBI:CHEBI:456216; EC=7.2.2.8; Evidence={ECO:0000269|PubMed:16495228};
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.25 mM for ATP {ECO:0000269|PubMed:11756450, ECO:0000269|PubMed:12763798}; Vmax=14.9 umol/h/mg enzyme with Ag(+) as substrate {ECO:0000269|PubMed:11756450, ECO:0000269|PubMed:12763798}; Vmax=3.7 umol/h/mg enzyme with Cu(+) as substrate {ECO:0000269|PubMed:11756450, ECO:0000269|PubMed:12763798}; Note=Shows higher affinity for Cu(+) compared with Ag(+).;
null
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.1-6.5. {ECO:0000269|PubMed:11756450, ECO:0000269|PubMed:12763798};
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 75 degrees Celsius. {ECO:0000269|PubMed:11756450, ECO:0000269|PubMed:12763798};
FUNCTION: Probably involved in copper and silver export. {ECO:0000269|PubMed:11756450}.
Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)
O29867
AGLB3_ARCFU
MQNAESWFKKYWHLSVLVIAALISVKLRILNPWNSVFTWTVRLGGNDPWYYYRLIENTIHNFPHRIWFDPFTYYPYGSYTHFGPFLVYLGSIAGIIFSATSGESLRAVLAFIPAIGGVLAILPVYLLTREVFDKRAAVIAAFLIAIVPGQFLQRSILGFNDHHIWEAFWQVSALGTFLLAYNRWKGHDLSHNLTARQMAYPVIAGITIGLYVLSWGAGFIIAPIILAFMFFAFVLAGFVNADRKNLSLVAVVTFAVSALIYLPFAFNYPGFSTIFYSPFQLLVLLGSAVIAAAFYQIEKWNDVGFFERVGLGRKGMPLAVIVLTALIMGLFFVISPDFARNLLSVVRVVQPKGGALTIAEVYPFFFTHNGEFTLTNAVLHFGALFFFGMAGILYSAYRFLKRRSFPEMALLIWAIAMFIALWGQNRFAYYFAAVSAVYSALALSVVFDKLHLYRALENAIGARNKLSYFRVAFALLIALAAIYPTYILADAQSSYAGGPNKQWYDALTWMRENTPDGEKYDEYYLQLYPTPQSNKEPFSYPFETYGVISWWDYGHWIEAVAHRMPIANPFQAGIGNKYNNVPGASSFFTAENESYAEFVAEKLNVKYVVSDIEMETGKYYAMAVWAEGDLPLAEKYYGGYFYYSPTGTFGYANSQWDIPLNSIIIPLRIPSELYYSTMEAKLHLFDGSGLSHYRMIYESDYPAEWKSYSSQVNLNNESQVLQTALYEAVMRARYGVSPTMGTQEVLYKYAYTQLYEKKMGIPVKIAPSGYVKIFERVKGAVVTGKVSANVTEVSVNATIKTNQNRTFEYWQTVEVKNGTYTVVLPYSHNSDYPVKPITPYHIKAGNVVKEITIYESQVQNGEIIQLDL
2.4.99.21
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:24127570}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:24127570}; Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:24127570};
post-translational protein modification [GO:0043687]; protein N-linked glycosylation via asparagine [GO:0018279]
plasma membrane [GO:0005886]
dolichyl-diphosphooligosaccharide-protein glycotransferase activity [GO:0004579]; metal ion binding [GO:0046872]
PF18079;PF02516;
1.20.58.1650;2.60.40.3390;3.40.50.12610;
STT3 family
null
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q2EMT4}; Multi-pass membrane protein {ECO:0000269|PubMed:24127570}.
CATALYTIC ACTIVITY: Reaction=an archaeal dolichyl phosphooligosaccharide + [protein]-L-asparagine = an archaeal dolichyl phosphate + a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to a protein L-asparagine.; EC=2.4.99.21; Evidence={ECO:0000269|PubMed:24127570, ECO:0000269|PubMed:27997792};
null
PATHWAY: Protein modification; protein glycosylation. {ECO:0000305|PubMed:24127570}.
null
null
FUNCTION: Oligosaccharyl transferase (OST) that catalyzes the initial transfer of a defined glycan (a glucose-linked heptasaccharide composed of 3 Glc, 2 Man, 2 Gal and a sulfate for A.fulgidus AglB-L) from the lipid carrier dolichol-monophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation. {ECO:0000269|PubMed:24127570, ECO:0000269|PubMed:27015803, ECO:0000269|PubMed:27997792}.
Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)
O29889
XPB_ARCFU
MQMIAEIYYERGTIVVKGDAHVPHAKFDSRSGTYRALAFRYRDIIEYFESNGIEFVDNAADPIPTPYFDAEISLRDYQEKALERWLVDKRGCIVLPTGSGKTHVAMAAINELSTPTLIVVPTLALAEQWKERLGIFGEEYVGEFSGRIKELKPLTVSTYDSAYVNAEKLGNRFMLLIFDEVHHLPAESYVQIAQMSIAPFRLGLTATFEREDGRHEILKEVVGGKVFELFPDSLAGKHLAKYTIKRIFVPLAEDERVEYEKREKVYKQFLRARGITLRRAEDFNKIVMASGYDERAYEALRAWEEARRIAFNSKNKIRKLREILERHRKDKIIIFTRHNELVYRISKVFLIPAITHRTSREEREEILEGFRTGRFRAIVSSQVLDEGIDVPDANVGVIMSGSGSAREYIQRLGRILRPSKGKKEAVLYELISRGTGEVNTARRRKNAAKGAA
5.6.2.4
null
transcription initiation at RNA polymerase II promoter [GO:0006367]
transcription preinitiation complex [GO:0097550]
3'-5' DNA helicase activity [GO:0043138]; ATP binding [GO:0005524]; DNA binding [GO:0003677]; hydrolase activity [GO:0016787]
PF00271;PF04851;PF18458;
3.40.1170.30;3.40.50.300;
Helicase family, RAD25/XPB subfamily
null
null
CATALYTIC ACTIVITY: Reaction=Couples ATP hydrolysis with the unwinding of duplex DNA by translocating in the 3'-5' direction.; EC=5.6.2.4; Evidence={ECO:0000269|PubMed:16600867, ECO:0000269|PubMed:29285929}; CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=5.6.2.4; Evidence={ECO:0000269|PubMed:16600867};
null
null
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.2 for ATPase activity. {ECO:0000269|PubMed:16600867};
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 50 degrees Celsius for 3'-5' helicase activity, still active at 65, inactive at 37 degrees Celsius. {ECO:0000269|PubMed:16600867};
FUNCTION: ATP-dependent DNA translocase which moves along double-stranded DNA (dsDNA) in a 3'-5' direction, unwinding the DNA (PubMed:16600867, PubMed:29285929, PubMed:37874269). Unwinds DNA with a 3'-overhang but not a 5'-overhang or blunt-ended undamaged DNA; does unwind damaged blunt-ended DNA (cyclobutane pyrimidine dimer or thymine (6-4) thymine photoproduct) (PubMed:16600867). Binds single-stranded (ss) and dsDNA, as well as damaged DNA (PubMed:16600867). Has very low ATPase activity that is repressed by Bax1; Y-form DNA and a DNA substrate with a 6 base pair bubble in the center stimulate the XPB-Bax1 ATPase activity about 6- to 10-fold (PubMed:32374860). {ECO:0000269|PubMed:16600867, ECO:0000269|PubMed:29285929, ECO:0000269|PubMed:32374860, ECO:0000269|PubMed:37874269}.
Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)
O29976
DIPPS_ARCFU
MILPCESFNGVPSGCLIIEMNWYSVLKASTAIFFPEKYSSSTSSLSKRSPISAPMINVDGEYLKIFAGRIKLMKAVILAAGLGTRLGGVPKPLVRVGGCEIILRTMKLLSPHVSEFIIVASRYADDIDAFLKDKGFNYKIVRHDRPEKGNGYSLLVAKNHVEDRFILTMGDHVYSQQFIEKAVRGEGVIADREPRFVDIGEATKIRVEDGRVAKIGKDLREFDCVDTGFFVLDDSIFEHAEKLRDREEIPLSEIVKLARLPVTYVDGELWMDVDTKEDVRRANRALVSAAVKGSGDGFISRKINRKISTRISAAIVNKVNPNQMTLISFLVGAFSALASFFSIPLAGLLYQFSSILDGCDGEIARASLKMSKKGGYVDSILDRFVDFLFLAIIALLYPKTATVAMFAIFGSVMVSYTSEKYKAEFGESIFGKFRVLNYIPGKRDERIFLIMIFCLLSAISLQWIFWMFLFVAAISLTRVVVTLLAVLVSK
2.7.7.74; 2.7.8.34
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
phospholipid biosynthetic process [GO:0008654]
membrane [GO:0016020]
metal ion binding [GO:0046872]; nucleotidyltransferase activity [GO:0016779]; phosphotransferase activity, for other substituted phosphate groups [GO:0016780]
PF01066;PF12804;
1.20.120.1760;
MobA family; CDP-alcohol phosphatidyltransferase class-I family
null
SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
CATALYTIC ACTIVITY: Reaction=1D-myo-inositol 3-phosphate + CTP + H(+) = CDP-1L-myo-inositol + diphosphate; Xref=Rhea:RHEA:30647, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37563, ChEBI:CHEBI:58401, ChEBI:CHEBI:62573; EC=2.7.7.74; Evidence={ECO:0000269|PubMed:17526717}; CATALYTIC ACTIVITY: Reaction=1D-myo-inositol 3-phosphate + CDP-1L-myo-inositol = bis(1L-myo-inositol) 3,1'-phosphate 1-phosphate + CMP + H(+); Xref=Rhea:RHEA:31327, ChEBI:CHEBI:15378, ChEBI:CHEBI:58401, ChEBI:CHEBI:60377, ChEBI:CHEBI:62573, ChEBI:CHEBI:62576; EC=2.7.8.34; Evidence={ECO:0000269|PubMed:17526717};
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.58 mM for CTP (at pH 7 and 90 degrees Celsius) {ECO:0000269|PubMed:21378188}; KM=0.87 mM for Inositol-1-phosphate (at pH 7 and 90 degrees Celsius) {ECO:0000269|PubMed:21378188}; Vmax=62.9 umol/min/mg enzyme (at pH 7 and 90 degrees Celsius) {ECO:0000269|PubMed:21378188};
null
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is between 6.5 and 7.5. {ECO:0000269|PubMed:21378188};
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is between 90 and 95 degrees Celsius. The activity is undetectable at temperatures below 60 degrees Celsius. {ECO:0000269|PubMed:21378188};
FUNCTION: Involved in biosynthesis of di-myo-inositol phosphate (DIP), a widespread organic solute in microorganisms adapted to hot environments. Catalyzes the condensation of CTP and L-myo-inositol-1-phosphate into CDP-L-myo-inositol, as well as the biosynthesis of di-myo-inositol-1,3'-phosphate-1'-phosphate (DIPP) from CDP-L-myo-inositol and L-myo-inositol-1-phosphate. The cytidylyltransferase is absolutely specific for CTP and L-myo-inositol-1-P. The DIPP synthase uses only L-myoinositol-1-phosphate as an alcohol acceptor, but CDP-glycerol, as well as CDP-L-myo-inositol and CDP-D-myoinositol, are recognized as alcohol donors. {ECO:0000269|PubMed:17028285, ECO:0000269|PubMed:17526717, ECO:0000269|PubMed:21378188}.
Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)
O30085
COPB_ARCFU
MHEHDSHGEAAHSNSEDMQMIHQHHEHHGHEEEHSAHHEKMKHSADHGDHHRMMMEDFKKRFYVSTLLTIPILILSPAIQTFLGFRVEFAGSLYILFLLSSAVYFYGGYPFLKGIFDELRRRQPGMMTLIAVAISVAYFYSSAVVFGLKGKFFFWELATLIDIMLLGHYIEMRSVLGASRALEELVKIMPSEAHLLKDGEIVEVKVENLKPGDKVLVKPGEKIPVDGIVVEGESFVNEAMLTGESKPVAKKPGDTVIGGAINGEGSLVVEVEKTGKDTYLNQVIELVRQAQESKSRTQDLANRAALLLTVIALTVGSVTLAIWLAYIADFAFAIERAVTVMVITCPHALGLAIPLVVAVSTSLAAKSGLLIRDRQAFERAKDLQAVIFDKTGTLTEGRFGVTDIVGFNHSEDELLQIAASLEARSEHPIAAAIVEEAEKRGFGLTEVEEFRAIPGKGVEGIVNGRRYMVVSPGYIRELGIKTDESVEKLKQQGKTVVFILKNGEVSGVIALADRIRPESREAISKLKAIGIKCMMLTGDNRFVAKWVAEELGLDDYFAEVLPHEKAEKVKEVQQKYVTAMVGDGVNDAPALAQADVGIAIGAGTDVAVETADIVLVRNDPRDVAAIVELSRKTYSKMKQNLLWATGYNAFAIPLAAGVLYSAGILLSPAVGAILMSLSTVIVAINARLLR
7.2.2.9
null
copper ion export [GO:0060003]; copper ion import [GO:0015677]; intracellular copper ion homeostasis [GO:0006878]
plasma membrane [GO:0005886]
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; copper ion binding [GO:0005507]; P-type divalent copper transporter activity [GO:0043682]
PF00122;PF00702;
3.40.1110.10;2.70.150.10;3.40.50.1000;
Cation transport ATPase (P-type) (TC 3.A.3) family, Type IB subfamily
null
SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
CATALYTIC ACTIVITY: Reaction=ATP + Cu(2+)(in) + H2O = ADP + Cu(2+)(out) + H(+) + phosphate; Xref=Rhea:RHEA:10376, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29036, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.2.2.9;
null
null
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5.7. {ECO:0000269|PubMed:12763798, ECO:0000269|PubMed:12876283};
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 85 degrees Celsius. {ECO:0000269|PubMed:12763798, ECO:0000269|PubMed:12876283};
FUNCTION: Involved in copper export. {ECO:0000269|PubMed:12876283, ECO:0000269|PubMed:22663904}.
Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)
O30245
RIO2_ARCFU
MNIAELYGKMGKHSWRIMDAIFKNLWDYEYVPLQLISSHARIGEEKARNILKYLSDLRVVQNRQKDYEGSTFTFIGLSLYSLHRLVRSGKVDAIGKLMGEGKESAVFNCYSEKFGECVVKFHKVGHTSFKKVKEKRDYGDLHFSVLAIRSARNEFRALQKLQGLAVPKVYAWEGNAVLMELIDAKELYRVRVENPDEVLDMILEEVAKFYHRGIVHGDLSQYNVLVSEEGIWIIDFPQSVEVGEEGWREILERDVRNIITYFSRTYRTEKDINSAIDRILQE
2.7.11.1
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Note=Mg(2+). Mn(2+) is seen in the crystal structure; there are 2 Mn(2+) ions in the ATP-bound crystal and 1 Mn(2+) in the ADP-bound crystal.;
maturation of SSU-rRNA [GO:0030490]; phosphorylation [GO:0016310]
cytosol [GO:0005829]; preribosome, small subunit precursor [GO:0030688]
ATP binding [GO:0005524]; metal ion binding [GO:0046872]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]
PF01163;PF09202;
1.10.510.10;1.10.10.10;
Protein kinase superfamily, RIO-type Ser/Thr kinase family
PTM: Autophosphorylated. {ECO:0000269|PubMed:15943813}.
null
CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1;
null
null
null
null
null
Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)
O30298
BSUHB_ARCFU
MDERDALRISREIAGEVRKAIASMPLRERVKDVGMGKDGTPTKAADRVAEDAALEILRKERVTVVTEESGVLGEGDVFVALDPLDGTFNATRGIPVYSVSLCFSYSDKLKDAFFGYVYNLATGDEYYADSSGAYRNGERIEVSDAEELYCNAIIYYPDRKFPFKRMRIFGSAATELCFFADGSFDCFLDIRPGKMLRIYDAAAGVFIAEKAGGKVTELDGESLGNKKFDMQERLNIVAANEKLHPKLLELIK
3.1.3.11; 3.1.3.25
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:11940584}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:11940584}; Note=Magnesium. Can also use manganese. {ECO:0000269|PubMed:11940584};
inositol metabolic process [GO:0006020]; phosphatidylinositol phosphate biosynthetic process [GO:0046854]; signal transduction [GO:0007165]
null
fructose 1,6-bisphosphate 1-phosphatase activity [GO:0042132]; inositol monophosphate 1-phosphatase activity [GO:0008934]; inositol monophosphate 3-phosphatase activity [GO:0052832]; inositol monophosphate 4-phosphatase activity [GO:0052833]; metal ion binding [GO:0046872]
PF00459;
3.40.190.80;3.30.540.10;
Inositol monophosphatase superfamily, FBPase class 4 family
null
null
CATALYTIC ACTIVITY: Reaction=beta-D-fructose 1,6-bisphosphate + H2O = beta-D-fructose 6-phosphate + phosphate; Xref=Rhea:RHEA:11064, ChEBI:CHEBI:15377, ChEBI:CHEBI:32966, ChEBI:CHEBI:43474, ChEBI:CHEBI:57634; EC=3.1.3.11; Evidence={ECO:0000269|PubMed:11062561, ECO:0000269|PubMed:11940584}; CATALYTIC ACTIVITY: Reaction=a myo-inositol phosphate + H2O = myo-inositol + phosphate; Xref=Rhea:RHEA:24056, ChEBI:CHEBI:15377, ChEBI:CHEBI:17268, ChEBI:CHEBI:43474, ChEBI:CHEBI:84139; EC=3.1.3.25; Evidence={ECO:0000269|PubMed:10747806, ECO:0000269|PubMed:11062561, ECO:0000269|PubMed:11940584};
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.11 mM for inositol-1-phosphate (at 85 degrees Celsius) {ECO:0000269|PubMed:11062561, ECO:0000269|PubMed:11940584}; KM=0.08 mM for D-fructose 1,6-bisphosphate (at 85 degrees Celsius) {ECO:0000269|PubMed:11062561, ECO:0000269|PubMed:11940584}; Vmax=3.27 umol/min/mg enzyme with L-inositol-1-phosphate as substrate (at 80 degrees Celsius, pH 8, in the presence of Mg(2+)) {ECO:0000269|PubMed:11062561, ECO:0000269|PubMed:11940584}; Vmax=2.2 umol/min/mg enzyme with L-inositol-1-phosphate as substrate (at 80 degrees Celsius, pH 8, in the presence of Mn(2+)) {ECO:0000269|PubMed:11062561, ECO:0000269|PubMed:11940584}; Vmax=1.52 umol/min/mg enzyme with D-fructose 1,6-bisphosphate as substrate (at 80 degrees Celsius, pH 8, in the presence of Mg(2+)) {ECO:0000269|PubMed:11062561, ECO:0000269|PubMed:11940584}; Vmax=1.92 umol/min/mg enzyme with D-fructose 1,6-bisphosphate as substrate (at 80 degrees Celsius, pH 8, in the presence of Mn(2+)) {ECO:0000269|PubMed:11062561, ECO:0000269|PubMed:11940584}; Note=kcat is 2.5 sec(-1) for IMPase activity (at 85 degrees Celsius) and 2.7 sec(-1) for FBPase activity (at 85 degrees Celsius). {ECO:0000269|PubMed:11062561};
null
null
null
FUNCTION: Phosphatase with broad specificity; it can dephosphorylate fructose 1,6-bisphosphate, both D and L isomers of inositol-1-phosphate (I-1-P), 2'-AMP, pNPP, inositol-2-phosphate, beta-glycerol phosphate, and alpha-D-glucose-1-phosphate. Cannot hydrolyze glucose-6-phosphate and fructose-6-phosphate. May be involved in the biosynthesis of a unique osmolyte, di-myo-inositol 1,1-phosphate. {ECO:0000269|PubMed:10747806, ECO:0000269|PubMed:11062561, ECO:0000269|PubMed:11940584}.
Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)
O30508
ARUC_PSEAE
MSAPHAQVERADFDRYMVPNYAPAAFIPVRGEGSRVWDQSGRELIDFAGGIAVTSLGHAHPALVKALTEQAQRIWHVSNVFTNEPALRLARKLVDATFAERVFLANSGAEANEAAFKLARRYANDVYGPQKYEIIAASNSFHGRTLFTVNVGGQPKYSDGFGPKFEGITHVPYNDLEALKAAISDKTCAVVLEPIQGEGGVLPAQQAYLEGARKLCDEHNALLVFDEVQSGMGRVGELFAYMHYGVVPDILSSAKSLGGGFPIGAMLTTGEIAKHLSVGTHGTTYGGNPLASAVAEAALDVINTPEVLDGVKAKHERFKSRLQKIGQEYGIFDEIRGMGLLIGAALTDEWKGKARDVLNAAEKEAVMVLQASPDVVRFAPSLVIDDAEIDEGLERFERAVAKLVRG
2.6.1.11; 2.6.1.81
COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000250}; Note=Binds 1 pyridoxal phosphate per subunit. {ECO:0000250};
arginine biosynthetic process [GO:0006526]; arginine catabolic process [GO:0006527]; arginine catabolic process to succinate [GO:0019545]
cytoplasm [GO:0005737]
identical protein binding [GO:0042802]; N2-acetyl-L-ornithine:2-oxoglutarate 5-aminotransferase activity [GO:0003992]; pyridoxal phosphate binding [GO:0030170]; succinylornithine transaminase activity [GO:0043825]
PF00202;
3.90.1150.10;3.40.640.10;
Class-III pyridoxal-phosphate-dependent aminotransferase family, ArgD subfamily
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + N(2)-succinyl-L-ornithine = L-glutamate + N-succinyl-L-glutamate 5-semialdehyde; Xref=Rhea:RHEA:16953, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:58514, ChEBI:CHEBI:58520; EC=2.6.1.81; Evidence={ECO:0000269|PubMed:9393691}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + N(2)-acetyl-L-ornithine = L-glutamate + N-acetyl-L-glutamate 5-semialdehyde; Xref=Rhea:RHEA:18049, ChEBI:CHEBI:16810, ChEBI:CHEBI:29123, ChEBI:CHEBI:29985, ChEBI:CHEBI:57805; EC=2.6.1.11; Evidence={ECO:0000269|PubMed:9393691};
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.4 mM for N(2)-succinyl-L-ornithine (at 15 mM 2-ketoglutarate and pH 9.0) {ECO:0000269|PubMed:9393691}; KM=1.1 mM for N(2)-acetyl-L-ornithine (at pH 9.0) {ECO:0000269|PubMed:9393691};
PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 4/4.; PATHWAY: Amino-acid degradation; L-arginine degradation via AST pathway; L-glutamate and succinate from L-arginine: step 3/5.
null
null
FUNCTION: Transaminates both N(2)-acetylornithine and N(2)-succinylornithine.
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
O30511
FUCT_HELPX
MFQPLLDAYVESASIEKMASKSPPPLKIAVANWWGDEEIKEFKNSVLYFILSQRYTITLHQNPNEFSDLVFGNPLGSARKILSYQNAKRVFYTGENESPNFNLFDYAIGFDELDFNDRYLRMPLYYDRLHHKAESVNDTTAPYKLKDNSLYALKKPSHCFKEKHPNLCAVVNDESDPLKRGFASFVASNPNAPIRNAFYDALNSIEPVTGGGSVRNTLGYNVKNKNEFLSQYKFNLCFENTQGYGYVTEKIIDAYFSHTIPIYWGSPSVAKDFNPKSFVNVHDFKNFDEAIDYIKYLHTHKNAYLDMLYENPLNTLDGKAYFYQNLSFKKILAFFKTILENDTIYHDNPFIFCRDLNEPLVTIDDLRVNYDDLRVNYDDLRINYDDLRVNYDDLRINYDDLRVNYDDLRVNYDDLRINYDDLRVNYDDLRVNYERLLSKATPLLELSQNTTSKIYRKAYQKSLPLLRAIRRWVKKLGL
2.4.1.152
null
fucosylation [GO:0036065]; lipopolysaccharide biosynthetic process [GO:0009103]; protein glycosylation [GO:0006486]
cytoplasm [GO:0005737]; membrane [GO:0016020]
4-galactosyl-N-acetylglucosaminide 3-alpha-L-fucosyltransferase activity [GO:0017083]; fucose binding [GO:0042806]; identical protein binding [GO:0042802]
PF18025;PF00852;
1.20.5.400;3.40.50.11660;
Glycosyltransferase 10 family
null
SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:9261149}; Peripheral membrane protein {ECO:0000269|PubMed:9261149}. Cytoplasm {ECO:0000269|PubMed:9261149}. Note=Predominantly localizes at the membrane. {ECO:0000269|PubMed:9261149}.
CATALYTIC ACTIVITY: Reaction=a beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl derivative + GDP-beta-L-fucose = a beta-D-galactosyl-(1->4)-[alpha-L-fucosyl-(1->3)]-N-acetyl-beta-D-glucosaminyl derivative + GDP + H(+); Xref=Rhea:RHEA:14257, ChEBI:CHEBI:15378, ChEBI:CHEBI:57273, ChEBI:CHEBI:58189, ChEBI:CHEBI:133507, ChEBI:CHEBI:137941; EC=2.4.1.152; Evidence={ECO:0000269|PubMed:12676935, ECO:0000269|PubMed:16150700, ECO:0000269|PubMed:16800635, ECO:0000269|PubMed:17251184, ECO:0000269|PubMed:9261149};
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.31 mM for Gal-beta-1-4-GlcNAc-beta-O-R {ECO:0000269|PubMed:12676935}; KM=48 uM for GDP-fucose {ECO:0000269|PubMed:12676935}; Vmax=11.8 umol/min/mg enzyme toward Gal-beta-1-4-GlcNAc-beta-O-R {ECO:0000269|PubMed:12676935};
PATHWAY: Lipopolysaccharide biosynthesis; LPS oligosaccharide biosynthesis. {ECO:0000303|PubMed:12676935, ECO:0000303|PubMed:16150700, ECO:0000303|PubMed:16800635, ECO:0000303|PubMed:17251184}.
null
null
FUNCTION: Involved in the biosynthesis of the Lewis X (LeX) trisaccharide of the lipopolysaccharide (LPS) O-antigen. Catalyzes the addition of fucose in alpha 1-3 linkage to Gal-beta-1-4-GlcNAc-beta-O-R (LacNAc-R) type II acceptor. {ECO:0000269|PubMed:12676935, ECO:0000269|PubMed:16150700, ECO:0000269|PubMed:16800635, ECO:0000269|PubMed:17251184, ECO:0000269|PubMed:9261149}.
Helicobacter pylori (Campylobacter pylori)
O30640
MTBA_METBA
MAEYTPKERLYRALRKQQVDRMPAVCFTQTATVEQMEACGAYWPEAHSDAEKMATLAEAAHTVVGFEAVRVPFDITAEAEFFGCGIKAGDLKQQPSVIKPSVKNLEDLEKLKNYNLKEGRIAVVLEAVKILSEKYGKELPIIGSMIGPFSLAQHINGDAWFGNLFTGEEVVPALLDFCSDFNVAYAKAMVENGADTIAIIDPTASYELIGGEFYEKYALPYQKKIVDAMKELDVATVLHICGNTTNGLGIMDKTGVNGISVDQKVDIKTATGSVKNAIIVGNLDPVAVLWNGTPEEIAEASKKALDAGVGLLTVGCGTVSMTPTVNLQKMIECAKSHTY
2.1.1.247
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
methane biosynthetic process from dimethylamine [GO:2001129]; methylation [GO:0032259]; one-carbon metabolic process [GO:0006730]; porphyrin-containing compound biosynthetic process [GO:0006779]
null
[methyl-Co(III) methylamine-specific corrinoid protein]:coenzyme M methyltransferase activity [GO:0043833]; dimethylamine methyltransferase activity [GO:0043791]; metal ion binding [GO:0046872]; uroporphyrinogen decarboxylase activity [GO:0004853]
PF01208;
3.20.20.210;
Uroporphyrinogen decarboxylase family, MtbA/MtaA subfamily
null
null
CATALYTIC ACTIVITY: Reaction=coenzyme M + methyl-Co(III)-[methylamine-specific corrinoid protein] = Co(I)-[methylamine-specific corrinoid protein] + H(+) + methyl-coenzyme M; Xref=Rhea:RHEA:18773, Rhea:RHEA-COMP:11120, Rhea:RHEA-COMP:11121, ChEBI:CHEBI:15378, ChEBI:CHEBI:58286, ChEBI:CHEBI:58319, ChEBI:CHEBI:85033, ChEBI:CHEBI:85035; EC=2.1.1.247; Evidence={ECO:0000269|PubMed:10852929, ECO:0000269|PubMed:7635826, ECO:0000269|PubMed:8702528, ECO:0000269|PubMed:9195968};
null
PATHWAY: One-carbon metabolism; methanogenesis from methylated amine.
null
null
FUNCTION: Methyltransferase involved in methanogenesis from methylamines methanol pathway. Catalyzes the transfer of the methyl group from the methylated corrinoid protein MtmC (MtmC1 or MtmC2) or MtbC to coenzyme M, forming the substrate for coenzyme-B sulfoethylthiotransferase. {ECO:0000269|PubMed:10852929, ECO:0000269|PubMed:7635826, ECO:0000269|PubMed:8702528, ECO:0000269|PubMed:9195968}.
Methanosarcina barkeri
O30916
SOPB_SALTY
MQIQSFYHSASLKTQEAFKSLQKTLYNGMQILSGQGKAPAKAPDARPEIIVLREPGATWGNYLQHQKASNHSLHNLYNLQRDLLTVAATVLGKQDPVLTSMANQMELAKVKADRPATKQEEAAAKALKKNLIELIAARTQQQDGLPAKEAHRFAAVAFRDAQVKQLNNQPWQTIKNTLTHNGHHYTNTQLPAAEMKIGAKDIFPSAYEGKGVCSWDTKNIHHANNLWMSTVSVHEDGKDKTLFCGIRHGVLSPYHEKDPLLRHVGAENKAKEVLTAALFSKPELLNKALAGEAVSLKLVSVGLLTASNIFGKEGTMVEDQMRAWQSLTQPGKMIHLKIRNKDGDLQTVKIKPDVAAFNVGVNELALKLGFGLKASDSYNAEALHQLLGNDLRPEARPGGWVGEWLAQYPDNYEVVNTLARQIKDIWKNNQHHKDGGEPYKLAQRLAMLAHEIDAVPAWNCKSGKDRTGMMDSEIKREIISLHQTHMLSAPGSLPDSGGQKIFQKVLLNSGNLEIQKQNTGGAGNKVMKNLSPEVLNLSYQKRVGDENIWQSVKGISSLITS
3.1.3.-
null
negative regulation of cell growth [GO:0030308]; negative regulation of signaling [GO:0023057]; positive regulation of DNA replication [GO:0045740]; regulation of protein kinase activity [GO:0045859]
cell periphery [GO:0071944]; symbiont-containing vacuole [GO:0020003]
lipid phosphatase activity [GO:0042577]; molecular function activator activity [GO:0140677]
PF05925;
1.20.58.450;
Phosphatase IpgD/SopB family
null
SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Note=Secreted via the type III secretion system 1 (SPI-1 T3SS). {ECO:0000250}.
null
null
null
null
null
FUNCTION: Converts phosphatidylinositol 3,4,5-trisphosphate (PtdIns 3,4,5-P3) to PtdIns 3-P and prevents the transition of PtdIns 3-P to PtdIns 3,5-P2. It is one of the known effectors injected by Salmonella into the host cell and is required for invasion and for an efficient generation and maintenance of Salmonella-containing vacuole (SVC). Alteration of the phosphoinositide composition of the plasma membrane causes membrane ruffling and actin cytoskeleton rearrangements. The persistence of PtdIns 3-P diverts the SCV from the endocytic pathway resulting in enlarged vesicles, which are essential to create a favorable environment where Salmonella can replicate and avoid immune defenses of the host cell. {ECO:0000269|PubMed:11136447, ECO:0000269|PubMed:11244077, ECO:0000269|PubMed:12360287, ECO:0000269|PubMed:15205533}.
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
O31041
PDUD_SALTY
MEINEKLLRQIIEDVLRDMKGSDKPVSFNAPAASTAPQTAAPAGDGFLTEVGEARQGTQQDEVIIAVGPAFGLAQTVNIVGLPHKSILREVIAGIEEEGIKARVIRCFKSSDVAFVAVEGNRLSGSGISIGIQSKGTTVIHQQGLPPLSNLELFPQAPLLTLETYRQIGKNAARYAKRESPQPVPTLNDQMARPKYQAKSAILHIKETKYVVTGKNPQELRVAL
4.2.1.28
COFACTOR: Name=adenosylcob(III)alamin; Xref=ChEBI:CHEBI:18408; Evidence={ECO:0000269|PubMed:2166132};
propanediol catabolic process [GO:0051144]
propanediol degradation polyhedral organelle [GO:0031472]
cobalamin binding [GO:0031419]; propanediol dehydratase activity [GO:0050215]
PF02288;
3.40.50.10150;
Diol/glycerol dehydratase medium subunit family
null
SUBCELLULAR LOCATION: Bacterial microcompartment {ECO:0000269|PubMed:10498708, ECO:0000269|PubMed:11844753, ECO:0000269|PubMed:12923081, ECO:0000269|PubMed:21821773, ECO:0000269|PubMed:26283792}. Note=Probably located inside the BMC shell. {ECO:0000305|PubMed:10498708, ECO:0000305|PubMed:21821773}.
CATALYTIC ACTIVITY: Reaction=propane-1,2-diol = H2O + propanal; Xref=Rhea:RHEA:14569, ChEBI:CHEBI:15377, ChEBI:CHEBI:16997, ChEBI:CHEBI:17153; EC=4.2.1.28; Evidence={ECO:0000269|PubMed:9352910};
null
PATHWAY: Polyol metabolism; 1,2-propanediol degradation. {ECO:0000305|PubMed:10498708}.
null
null
FUNCTION: Part of the PduCDE complex that catalyzes the dehydration of 1,2-propanediol (1,2-PD) to propionaldehyde. Required for S.typhimurium growth on 1,2-PD as the sole carbon and energy source (Probable) (PubMed:9023178). This subunit is directly targeted to the bacterial microcompartment (BMC) dedicated to 1,2-PD degradation, and is also responsible for targeting the other 2 subunits (pduC and pduE) (PubMed:21821773, PubMed:26283792). {ECO:0000269|PubMed:21821773, ECO:0000269|PubMed:26283792, ECO:0000269|PubMed:9023178, ECO:0000305|PubMed:9352910}.; FUNCTION: The 1,2-PD-specific bacterial microcompartment (BMC) concentrates low levels of 1,2-PD catabolic enzymes, concentrates volatile reaction intermediates thus enhancing pathway flux and keeps the level of toxic, mutagenic propionaldehyde low. {ECO:0000269|PubMed:25713376, ECO:0000305|PubMed:28475631}.
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
O31042
PDUE_SALTY
MNTDAIESMVRDVLSRMNSLQGDAPAAAPAAGGTSRSAKVSDYPLANKHPEWVKTATNKTLDDFTLENVLSNKVTAQDMRITPETLRLQASIAKDAGRDRLAMNFERAAELTAVPDDRILEIYNALRPYRSTKEELLAIADDLENRYQAKICAAFVREAAGLYVERKKLKGDD
4.2.1.28
COFACTOR: Name=adenosylcob(III)alamin; Xref=ChEBI:CHEBI:18408; Evidence={ECO:0000269|PubMed:2166132};
propanediol catabolic process [GO:0051144]
propanediol degradation polyhedral organelle [GO:0031472]
cobalamin binding [GO:0031419]; propanediol dehydratase activity [GO:0050215]
PF02287;
1.10.1510.20;
Diol/glycerol dehydratase small subunit family
null
SUBCELLULAR LOCATION: Bacterial microcompartment {ECO:0000269|PubMed:10498708, ECO:0000269|PubMed:11844753, ECO:0000269|PubMed:12923081, ECO:0000269|PubMed:21821773}. Note=Probably located inside the BMC shell. {ECO:0000269|PubMed:10498708}.
CATALYTIC ACTIVITY: Reaction=propane-1,2-diol = H2O + propanal; Xref=Rhea:RHEA:14569, ChEBI:CHEBI:15377, ChEBI:CHEBI:16997, ChEBI:CHEBI:17153; EC=4.2.1.28; Evidence={ECO:0000269|PubMed:9352910};
null
PATHWAY: Polyol metabolism; 1,2-propanediol degradation. {ECO:0000305|PubMed:10498708}.
null
null
FUNCTION: Part of the PduCDE complex that catalyzes the dehydration of 1,2-propanediol (1,2-PD) to propionaldehyde. Required for S.typhimurium growth on 1,2-PD as the sole carbon and energy source. Localized in the bacterial microcompartment (BMC) dedicated to 1,2-PD degradation. {ECO:0000305|PubMed:9352910}.; FUNCTION: The 1,2-PD-specific bacterial microcompartment (BMC) concentrates low levels of 1,2-PD catabolic enzymes, concentrates volatile reaction intermediates thus enhancing pathway flux and keeps the level of toxic, mutagenic propionaldehyde low. {ECO:0000269|PubMed:25713376, ECO:0000305|PubMed:28475631}.
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
O31147
LON_MYCSM
MAEAKTVPVLFLNDSIVLPGMVVPIELDDAARAAVDAARASESGELLIAPRLEDRYPAYGVLASIVQIGRLPNGDAAAVVRGERRAHIGSGTSGPGAALWVQVEEVTDPEPTDETKKLAGEYKKLLLAMLQRRDAWQIVDMVNKITDPSALADTAGYASYLTGTQKRELLETTDVDRRLSLLIGWTGDHLAETEVNDKIAEDVRTGMEKQQKEFLLRQQLAAIRKELGELDDNGDGSSDDYRARIEQADLPEKVREAALREVGKLERASDQSPEGGWIRTWLDTVLDLPWNVRTEDSTDLARAREILDTDHHGLSDVKDRIVEYLAVRGAAPQRGMAVVGGRGSGAVMVLAGPPGVGKTSLGESVARALDRKFVRVALGGVRDEAEIRGHRRTYVGALPGRIVRAIGEAGSMNPVVLLDEIDKVGSDYRGDPAAALLEVLDPAQNHTFRDHYLDLDLDLSDVVFLVTANVIENIPSALLDRMELVEIDGYTADDKLAIAQGFLLPRQRERGGLTSDEVTVTEAALRKIAADYTREPGVRQFERLLAKAMRKAATKLADHPQAAPITIDEPDLVEYLGRPRFLPESAERTAVPGVATGLAVTGLGGDVLYIEANSTEGEPGLQLTGQLGDVMKESAQIAMSYVRAHAKQLGVDPEALNRRIHIHVPAGAVPKDGPSAGVTMVTALVSMATGRKVRGDVGMTGEVTLNGRVLPIGGVKQKLLAAQRAGLSTVFIPQRNQPDLDDVPADVLDALDVRPMTDVADIIAAALEPAHEASTAAAA
3.4.21.53
null
cellular response to heat [GO:0034605]; protein quality control for misfolded or incompletely synthesized proteins [GO:0006515]
cytoplasm [GO:0005737]
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATP-dependent peptidase activity [GO:0004176]; sequence-specific DNA binding [GO:0043565]; serine-type endopeptidase activity [GO:0004252]
PF00004;PF05362;PF02190;
1.10.8.60;1.20.5.5270;1.20.58.1480;3.30.230.10;2.30.130.40;3.40.50.300;
Peptidase S16 family
null
SUBCELLULAR LOCATION: Cytoplasm.
CATALYTIC ACTIVITY: Reaction=Hydrolysis of proteins in presence of ATP.; EC=3.4.21.53; Evidence={ECO:0000255|HAMAP-Rule:MF_01973};
null
null
null
null
FUNCTION: ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short-lived regulatory proteins. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypeptides processively to yield small peptide fragments that are 5 to 10 amino acids long. Binds to DNA in a double-stranded, site-specific manner. {ECO:0000255|HAMAP-Rule:MF_01973, ECO:0000269|PubMed:9425059}.
Mycolicibacterium smegmatis (Mycobacterium smegmatis)
O31156
PHNX_BACCE
MKIEAVIFDWAGTTVDYGCFAPLEVFMEIFHKRGVAITAEEARKPMGLLKIDHVRALTEMPRIASEWNRVFRQLPTEADIQEMYEEFEEILFAILPRYASPINGVKEVIASLRERGIKIGSTTGYTREMMDIVAKEAALQGYKPDFLVTPDDVPAGRPYPWMCYKNAMELGVYPMNHMIKVGDTVSDMKEGRNAGMWTVGVILGSSELGLTEEEVENMDSVELREKIEVVRNRFVENGAHFTIETMQELESVMEHIEKQELIIS
3.11.1.1
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Note=Binds 1 Mg(2+) ion per subunit.;
organic phosphonate catabolic process [GO:0019700]
null
magnesium ion binding [GO:0000287]; phosphonoacetaldehyde hydrolase activity [GO:0050194]
PF00702;
3.40.50.1000;
HAD-like hydrolase superfamily, PhnX family
null
null
CATALYTIC ACTIVITY: Reaction=H2O + phosphonoacetaldehyde = acetaldehyde + H(+) + phosphate; Xref=Rhea:RHEA:18905, ChEBI:CHEBI:15343, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:58383; EC=3.11.1.1;
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=33 uM for phosphonoacetaldehyde (at pH 7.0, 25 degrees Celsius);
null
null
null
FUNCTION: Involved in phosphonate degradation.
Bacillus cereus
O31266
HOD_PAENT
MTDTYLHETLVFDNKLSYIDNQRDTDGPAILLLPGWCHDHRVYKYLIQELDADFRVIVPNWRGHGLSPCEVPDFGYQEQVKDALEILDQLGVETFLPVSHSHGGWVLVELLEQAGPERAPRGIIMDWLMWAPKPDFAKSLTLLKDPERWREGTHGLFDVWLDGHDEKRVRHHLLEEMADYGYDCWGRSGRVIEDAYGRNGSPMQMMANLTKTRPIRHIFSQPTEPEYEKINSDFAEQHPWFSYAKLGGPTHFPAIDVPDRAAVHIREFATAIRQGQ
1.13.11.48
COFACTOR: Note=None. Contrary to most other dioxygenases, this enzyme does not require a cofactor for catalysis.;
aromatic compound catabolic process [GO:0019439]
null
3-hydroxy-2-methylquinolin-4-one 2,4-dioxygenase activity [GO:0050586]; oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen [GO:0016702]
PF00561;
1.10.210.20;3.40.50.1820;
AB hydrolase superfamily
null
null
CATALYTIC ACTIVITY: Reaction=3-hydroxy-2-methyl-1H-quinolin-4-one + O2 = CO + H(+) + N-acetylanthranilate; Xref=Rhea:RHEA:21572, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16803, ChEBI:CHEBI:17245, ChEBI:CHEBI:29216; EC=1.13.11.48; Evidence={ECO:0000269|PubMed:10746195, ECO:0000269|PubMed:15533053, ECO:0000269|PubMed:16187153, ECO:0000269|PubMed:20080731};
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.5 uM for 1H-3-hydroxy-4-oxoquinaldine {ECO:0000269|PubMed:15533053, ECO:0000269|PubMed:16187153, ECO:0000269|PubMed:20080731}; KM=180 uM for 1H-3-hydroxy-4-oxoquinoline {ECO:0000269|PubMed:15533053, ECO:0000269|PubMed:16187153, ECO:0000269|PubMed:20080731};
null
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8-11. {ECO:0000269|PubMed:15533053, ECO:0000269|PubMed:16187153, ECO:0000269|PubMed:20080731};
null
FUNCTION: Ring-cleaving dioxygenase involved in quinaldine degradation and utilization. {ECO:0000269|PubMed:10746195}.
Paenarthrobacter nitroguajacolicus (Arthrobacter nitroguajacolicus)
O31269
ISCS_AZOVI
MKLPIYLDYSATTPVDPRVAQKMCECLTMEGNFGNPASRSHVFGWKAEEAVENARRQVAELVNADPREIVWTSGATESDNLAIKGVAHFNASKGKHIITSKIEHKAVLDTTRQLEREGFEVTYLEPGEDGLITPAMVAAALREDTILVSVMHVNNEIGTVNDIAAIGELTRSRGVLYHVDAAQSTGKVAIDLERMKVDLMSFSAHKTYGPKGIGALYVRRKPRVRLEAQMHGGGHERGMRSGTLATHQIVGMGEAFRIAREEMAAESRRIAGLSHRFHEQVSTLEEVYLNGSATARVPHNLNLSFNYVEGESLIMSLRDLAVSSGSACTSASLEPSYVLRALGRNDELAHSSIRFTFGRFTTEEEVDYAARKVCEAVGKLRELSPLWDMYKDGVDLSKIEWQAH
2.8.1.7
COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000255|HAMAP-Rule:MF_00331, ECO:0000269|PubMed:9582371};
[2Fe-2S] cluster assembly [GO:0044571]; tRNA processing [GO:0008033]
cytosol [GO:0005829]
2 iron, 2 sulfur cluster binding [GO:0051537]; cysteine desulfurase activity [GO:0031071]; metal ion binding [GO:0046872]; pyridoxal phosphate binding [GO:0030170]
PF00266;
3.90.1150.10;3.40.640.10;
Class-V pyridoxal-phosphate-dependent aminotransferase family, NifS/IscS subfamily
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00331}.
CATALYTIC ACTIVITY: Reaction=[sulfur carrier]-H + L-cysteine = [sulfur carrier]-SH + L-alanine; Xref=Rhea:RHEA:43892, Rhea:RHEA-COMP:14737, Rhea:RHEA-COMP:14739, ChEBI:CHEBI:29917, ChEBI:CHEBI:35235, ChEBI:CHEBI:57972, ChEBI:CHEBI:64428; EC=2.8.1.7; Evidence={ECO:0000255|HAMAP-Rule:MF_00331, ECO:0000269|PubMed:9582371};
null
PATHWAY: Cofactor biosynthesis; iron-sulfur cluster biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00331, ECO:0000305|Ref.2}.
null
null
FUNCTION: Master enzyme that delivers sulfur to a number of partners involved in Fe-S cluster assembly, tRNA modification or cofactor biosynthesis. Catalyzes the removal of elemental sulfur from cysteine to produce alanine via an enzyme-bound persulfide intermediate. Functions as a sulfur delivery protein for Fe-S cluster synthesis. Cluster assembly on IscU homodimers proceeds sequentially from 1 2Fe-2S per dimer, to 2 2Fe-2S per dimer and finally 1 4Fe-4S per dimer. {ECO:0000269|PubMed:10891064, ECO:0000269|PubMed:9582371, ECO:0000269|Ref.2}.
Azotobacter vinelandii
O31422
SKFA_BACSU
MKRNQKEWESVSKKGLMKPGGTSIVKAAGCMGCWASKSIAMTRVCALPHPAMRAI
null
null
defense response to bacterium [GO:0042742]; killing of cells of another organism [GO:0031640]
extracellular region [GO:0005576]
null
null
null
null
PTM: This is a cyclic peptide (PubMed:20805502, PubMed:23282011). The first step in SKF maturation is probably thioether bond formation (PubMed:23282011). {ECO:0000269|PubMed:20805502, ECO:0000269|PubMed:23282011}.
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:20805502}. Note=Probably secreted by the ABC transporter SkfEF. {ECO:0000305}.
null
null
null
null
null
FUNCTION: Produces a 26-residue extracellular sporulation filling factor (SKF) that induces the lysis of other B.subtilis cells that have not entered the sporulation pathway, providing a source of nutrients to support sporulation, and at the same time delaying commitment to the energetically expensive and irreversible onset of sporulation (PubMed:12817086, PubMed:20805502). Can also inhibit growth of other bacteria at high concentrations (PubMed:11851812). Addition of SKF to solid cultures induces killing, but it is much less effective than SDP (AC O34344) (PubMed:20805502). Has a role in protecting the secreted lipase LipA against proteolysis, either by modulating its folding or by acting as a protease inhibitor (PubMed:15812018). {ECO:0000269|PubMed:11851812, ECO:0000269|PubMed:12817086, ECO:0000269|PubMed:15812018, ECO:0000269|PubMed:20805502}.
Bacillus subtilis (strain 168)
O31461
ILVE1_BACSU
MNKLIEREKTVYYKEKPDPSSLGFGQYFTDYMFVMDYEEGIGWHHPRIAPYAPLTLDPSSSVFHYGQAVFEGLKAYRTDDGRVLLFRPDQNIKRLNRSCERMSMPPLDEELVLEALTQLVELEKDWVPKEKGTSLYIRPFVIATEPSLGVKASRSYTFMIVLSPVGSYYGDDQLKPVRIYVEDEYVRAVNGGVGFAKTAGNYAASLQAQRKANELGYDQVLWLDAIEKKYVEEVGSMNIFFVINGEAVTPALSGSILSGVTRASAIELIRSWGIPVREERISIDEVYAASARGELTEVFGTGTAAVVTPVGELNIHGKTVIVGDGQIGDLSKKLYETITDIQLGKVKGPFNWTVEV
2.6.1.42
COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
amino acid biosynthetic process [GO:0008652]; isoleucine biosynthetic process [GO:0009097]; leucine biosynthetic process [GO:0009098]; valine biosynthetic process [GO:0009099]
null
L-isoleucine transaminase activity [GO:0052656]; L-leucine transaminase activity [GO:0052654]; L-leucine:2-oxoglutarate aminotransferase activity [GO:0050048]; L-valine transaminase activity [GO:0052655]
PF01063;
3.30.470.10;3.20.10.10;
Class-IV pyridoxal-phosphate-dependent aminotransferase family
null
null
CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-leucine = 4-methyl-2-oxopentanoate + L-glutamate; Xref=Rhea:RHEA:18321, ChEBI:CHEBI:16810, ChEBI:CHEBI:17865, ChEBI:CHEBI:29985, ChEBI:CHEBI:57427; EC=2.6.1.42; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-isoleucine = (S)-3-methyl-2-oxopentanoate + L-glutamate; Xref=Rhea:RHEA:24801, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:35146, ChEBI:CHEBI:58045; EC=2.6.1.42; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-valine = 3-methyl-2-oxobutanoate + L-glutamate; Xref=Rhea:RHEA:24813, ChEBI:CHEBI:11851, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:57762; EC=2.6.1.42;
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=2.36 mM for isoleucine (with 10 mM ketomethiobutyrate) {ECO:0000269|PubMed:12670965}; KM=2.78 mM for leucine (with 10 mM ketomethiobutyrate) {ECO:0000269|PubMed:12670965}; KM=2.82 mM for valine (with 10 mM alpha-ketoglutarate) {ECO:0000269|PubMed:12670965}; KM=3.15 mM for isoleucine (with 10 mM alpha-ketoglutarate) {ECO:0000269|PubMed:12670965}; KM=3.2 mM for valine (with 10 mM ketomethiobutyrate) {ECO:0000269|PubMed:12670965}; KM=3.99 mM for leucine (with 10 mM alpha-ketoglutarate) {ECO:0000269|PubMed:12670965}; Vmax=1.84 umol/min/mg enzyme toward isoleucine (with 10 mM ketomethiobutyrate) {ECO:0000269|PubMed:12670965}; Vmax=1.87 umol/min/mg enzyme toward leucine (with 10 mM ketomethiobutyrate) {ECO:0000269|PubMed:12670965}; Vmax=2.03 umol/min/mg enzyme toward valine (with 10 mM ketomethiobutyrate) {ECO:0000269|PubMed:12670965}; Vmax=13.93 umol/min/mg enzyme toward valine (with 10 mM alpha-ketoglutarate) {ECO:0000269|PubMed:12670965}; Vmax=14.58 umol/min/mg enzyme toward leucine (with 10 mM alpha-ketoglutarate) {ECO:0000269|PubMed:12670965}; Vmax=16.61 umol/min/mg enzyme toward isoleucine (with 10 mM alpha-ketoglutarate) {ECO:0000269|PubMed:12670965};
PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 4/4.; PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 4/4.; PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine from pyruvate: step 4/4.
null
null
FUNCTION: Transaminates branched-chain amino acids and ketoglutarate. Involved in the final step of the methionine regeneration pathway, where ketomethiobutyrate (KMTB) is converted to methionine via a transamination. The amino donor preference is isoleucine, leucine, valine, phenylalanine, and tyrosine. {ECO:0000269|PubMed:12670965}.
Bacillus subtilis (strain 168)
O31523
RHGT1_BACSU
MMKKPIQVFLAGDSTVSDCPPHEAPMAGWGQVFGQLFSEGVLVRNHAKGGASTNSFVEEGRLQAIAEHITQGDYLLIQFGHNDQKPRGTKPYSTFQQFLTLFADTAREKGAHPVFVTSVQRRRFDENGRIEHTLGEYPDAMKALAKELDVPVIDLLAKTKVLYEAYGPEESKRLFVWFQPNEHPNYPDGIEDNTHFSEKGAMEVAKLVAEGIEELGLPLKDHLVSREGKEHV
3.1.1.-
null
null
null
hydrolase activity [GO:0016787]
PF13472;
3.40.50.1110;
'GDSL' lipolytic enzyme family
null
null
null
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1 mM for alpha-naphthyl acetate (at 37 degrees Celsius and pH 7.3) {ECO:0000269|PubMed:17957779}; KM=1.1 mM for beta-naphthyl acetate (at 37 degrees Celsius and pH 7.3) {ECO:0000269|PubMed:17957779}; KM=2.8 mM for p-nitrophenyl acetate (at 37 degrees Celsius and pH 7.3) {ECO:0000269|PubMed:17957779}; KM=7.1 mM for cephalosporin C (at 37 degrees Celsius and pH 7.3) {ECO:0000269|PubMed:17957779}; KM=9.1 mM for glucose pentaacetate (at 37 degrees Celsius and pH 7.3) {ECO:0000269|PubMed:17957779}; KM=124.3 mM for 7-aminocephalosporanic acid (at 37 degrees Celsius and pH 7.3) {ECO:0000269|PubMed:17957779}; Vmax=709 umol/min/mg enzyme with alpha-naphthyl acetate (at 37 degrees Celsius and pH 7.3) {ECO:0000269|PubMed:17957779}; Vmax=1163 umol/min/mg enzyme with cephalosporin C (at 37 degrees Celsius and pH 7.3) {ECO:0000269|PubMed:17957779}; Vmax=3917 umol/min/mg enzyme with beta-naphthyl acetate (at 37 degrees Celsius and pH 7.3) {ECO:0000269|PubMed:17957779}; Vmax=4360 umol/min/mg enzyme with 7-aminocephalosporanic acid (at 37 degrees Celsius and pH 7.3) {ECO:0000269|PubMed:17957779}; Vmax=5160 umol/min/mg enzyme with p-nitrophenyl acetate (at 37 degrees Celsius and pH 7.3) {ECO:0000269|PubMed:17957779}; Vmax=13726 umol/min/mg enzyme with glucose pentaacetate (at 37 degrees Celsius and pH 7.3) {ECO:0000269|PubMed:17957779};
null
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.5. The enzyme is more active in the 7.5-9.0 range, achieving a sharp decrease in the activity below pH 7.0. {ECO:0000269|PubMed:17957779};
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 35 degrees Celsius. The enzyme is quite thermostable in the range of 35 to 40 degrees Celsius, and suffering a decrease in thermostability above 45 degrees Celsius. {ECO:0000269|PubMed:17957779};
FUNCTION: May play a role in the degradation of type I rhamnogalacturonan derived from plant cell walls. This enzyme has a broad substrate specificity, and shows strong preference for glucose pentaacetate, beta-naphthylacetate, and p-nitrophenyl acetate (pNPA). Also active toward acetylated xylan. {ECO:0000269|PubMed:17449691}.
Bacillus subtilis (strain 168)
O31526
YESW_BACSU
MRRSCLMIRRRKRMFTAVTLLVLLVMGTSVCPVKAEGAARQMEALNRGLVAVKTDGGIFVSWRFLGTENASVLFNVYRDGQKLNAAPVKTTNYVDKNGSAGSTYTVRAVVNGTEQPASEKASVWAQPYHSVPLDKPAGGTTPKGESYTYSANDASVGDVDGDGQYELILKWDPSNSKDNSQDGYTGDVLIDAYKLDGTKLWRINLGKNIRAGAHYTQFMVYDLDGDGKAEVAMKTADGTKDGTGKVIGNANADYRNEQGRVLSGPEYLTVFQGSTGKELVTANFEPARGNVSDWGDSYGNRVDRFLAGIAYLDGQRPSLIMTRGYYAKTMLVAYNFRDGKLSKLWTLDSSKSGNEAFAGQGNHNLSIADVDGDGKDEIIFGSMAVDHDGKGMYSTGLGHGDALHTGDLDPGRPGLEVFQVHEDKNAKYGLSFRDAATGKILWGVYAGKDVGRGMAADIDPRYPGQEVWANGSLYSAKGVKIGSGVPSSTNFGIWWDGDLLREQLDSNRIDKWDYQNGVSKNMLTASGAAANNGTKATPTLQADLLGDWREEVVWRTEDSSALRIYTTTIPTEHRLYTLMHDPVYRLGIAWQNIAYNQPPHTSFFLGDGMAEQPKPNMYTP
4.2.2.23
COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:16682770, ECO:0000269|PubMed:17449691, ECO:0000269|PubMed:17947240, ECO:0000269|PubMed:19193638}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:16682770, ECO:0000269|PubMed:17449691}; Note=Binds 10 calcium ions (PubMed:16682770, PubMed:17449691, PubMed:19193638). The calcium may have a structural role. Requires calcium or manganese for activity (PubMed:16682770, PubMed:17449691). {ECO:0000269|PubMed:16682770, ECO:0000269|PubMed:17449691, ECO:0000269|PubMed:19193638};
cell wall organization [GO:0071555]
extracellular region [GO:0005576]
metal ion binding [GO:0046872]; rhamnogalacturonan endolyase activity [GO:0102210]
PF18370;PF21348;
2.60.40.10;
Polysaccharide lyase 11 family
null
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17449691}.
CATALYTIC ACTIVITY: Reaction=Endotype eliminative cleavage of L-alpha-rhamnopyranosyl-(1->4)-alpha-D-galactopyranosyluronic acid bonds of rhamnogalacturonan I domains in ramified hairy regions of pectin leaving L-rhamnopyranose at the reducing end and 4-deoxy-4,5-unsaturated D-galactopyranosyluronic acid at the non-reducing end.; EC=4.2.2.23; Evidence={ECO:0000269|PubMed:17449691, ECO:0000269|PubMed:19193638};
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.181 mg/ml for rhamnogalacturonan (RG) type I region of plant cell wall pectin {ECO:0000269|PubMed:19193638};
null
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8. {ECO:0000269|PubMed:17449691};
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 60 degrees Celsius. {ECO:0000269|PubMed:17449691};
FUNCTION: Pectinolytic enzyme that degrades type I rhamnogalacturonan from plant cell walls and releases oligosaccharide products (PubMed:16682770, PubMed:17449691, PubMed:19193638). Degrades rhamnogalacturonan, polygalacturonic acid, pectic acid and pectin (PubMed:16682770, PubMed:17449691). {ECO:0000269|PubMed:16682770, ECO:0000269|PubMed:17449691, ECO:0000269|PubMed:19193638}.
Bacillus subtilis (strain 168)
O31527
YESX_BACSU
MKPKKRQMEYLTRGLIAVQTEQGVFVSWRFLGTDHETTAFHLYRDGKRITRDPIAESTNFLDQNGTADSVYQVAAVNKGREEKLSKKARVWQENVLEVPLAKPEGGVTPDGKPYTYSANDASVGDIDGDGEYEMILKWDPSNSKDNAHDGYTGEVLIDAYKLDGTFLWRINLGRNIRAGAHYTQFMVYDLDGDGKAEIAMKTADGTTDGKGHIIGDEQADFRNEQGRILSGPEYLTVFKGETGEALTTVEYEPPRGKLEDWGDGYGNRMDRFLAGTAYLDGERPSLVMARGYYTRTVLVAYDFRNGRLKKRWVFDSNQPGHEAYAGQGNHSLSVADVDGDGKDEIIYGAMAVDHDGTGLYSTGLGHGDAMHVGDLDPSRKGLEVFQVHEDATKPYGLSLRDAGTGEILWGVHAGTDVGRGMAAHIDPSYKGSLVWGIDPPGNDGMSYGLFTSKGEKISDKAPSSANFAIWWDGDLVRELLDHDWDGTIGRPKIEKWDAENGCLKTIFQPAGVLSNNGTKGNPVLQANLFGDWREEVIWRTEDSSALRIYTTTHLTRHCFYTLMHDPVYRLGIAWQNTAYNQPPHTSFYLGTGMKKPPKPALYIAGSKAEAPL
4.2.2.24
COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:17449691}; Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:17449691}; Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000269|PubMed:17449691}; Note=Divalent metal cations. Has highest activity with Mn(2+), followed by Zn(2+) and Co(2+). {ECO:0000269|PubMed:17449691}; COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:17449691, ECO:0000269|PubMed:19193638}; Note=Binds 10 calcium ions. The calcium may have a structural role. {ECO:0000269|PubMed:17449691};
cell wall organization [GO:0071555]
extracellular region [GO:0005576]
lyase activity [GO:0016829]; metal ion binding [GO:0046872]
PF18370;PF21348;
2.60.40.10;
Polysaccharide lyase 11 family
null
SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:17449691}.
CATALYTIC ACTIVITY: Reaction=Exotype eliminative cleavage of alpha-L-rhamnopyranosyl-(1->4)-alpha-D-galactopyranosyluronic acid bonds of rhamnogalacturonan I oligosaccharides containing alpha-L-rhamnopyranose at the reducing end and 4-deoxy-4,5-unsaturated D-galactopyranosyluronic acid at the non-reducing end. The products are the disaccharide 2-O-(4-deoxy-beta-L-threo-hex-4-enopyranuronosyl)-alpha-L-rhamnopyranose and the shortened rhamnogalacturonan oligosaccharide containing one 4-deoxy-4,5-unsaturated D-galactopyranosyluronic acid at the non-reducing end.; EC=4.2.2.24; Evidence={ECO:0000269|PubMed:17449691, ECO:0000269|PubMed:19193638};
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.78 mg/ml for rhamnogalacturonan (RG) type I region of plant cell wall pectin {ECO:0000269|PubMed:19193638};
null
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.5. {ECO:0000269|PubMed:17449691};
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 60 degrees Celsius. {ECO:0000269|PubMed:17449691};
FUNCTION: Pectinolytic enzyme that degrades type I rhamnogalacturonan from plant cell walls and releases disaccharide products (PubMed:17449691, PubMed:19193638). Degrades rhamnogalacturonan, polygalacturonic acid and pectic acid. Has very low activity on pectin (PubMed:17449691). {ECO:0000269|PubMed:17449691, ECO:0000269|PubMed:19193638}.
Bacillus subtilis (strain 168)
O31602
SPX_BACSU
MVTLYTSPSCTSCRKARAWLEEHEIPFVERNIFSEPLSIDEIKQILRMTEDGTDEIISTRSKVFQKLNVNVESMPLQDLYRLINEHPGLLRRPIIIDEKRLQVGYNEDEIRRFLPRKVRSFQLREAQRLAN
null
null
negative regulation of DNA-templated transcription [GO:0045892]
cytoplasm [GO:0005737]
null
PF03960;
3.40.30.10;
ArsC family, Spx subfamily
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
null
null
null
null
null
FUNCTION: Global transcriptional regulator that plays a key role in stress response and exerts either positive or negative regulation of genes (PubMed:12642660, PubMed:15659166, PubMed:16885442, PubMed:18662407, PubMed:18687074, PubMed:29271514). Acts by interacting with the C-terminal domain of the alpha subunit of the RNA polymerase (RNAP) (PubMed:12642660, PubMed:15659166, PubMed:18687074, PubMed:20084284). This interaction can enhance binding of RNAP to the promoter region of target genes and stimulate their transcription, or block interaction of RNAP with activator proteins and repress transcription (PubMed:12642660, PubMed:15659166, PubMed:18687074, PubMed:20084284). Exhibits no DNA-binding activity (PubMed:15659166, PubMed:18687074). {ECO:0000269|PubMed:12642660, ECO:0000269|PubMed:15659166, ECO:0000269|PubMed:16885442, ECO:0000269|PubMed:18662407, ECO:0000269|PubMed:18687074, ECO:0000269|PubMed:20084284, ECO:0000269|PubMed:29271514}.; FUNCTION: Induces the expression of a large number of genes in response to a variety of stress conditions, such as disulfide, heat and cell wall stress, while concurrently repressing transcription of genes involved in various developmental and growth-related pathways during periods of extreme stress (PubMed:12642660, PubMed:14597697). Functions in the oxidative stress response via induction of the transcription of thioredoxin (trxA) and thioredoxin reductase (trxB) during thiol-specific oxidative (disulfide) stress (PubMed:14597697, PubMed:15659166, PubMed:18687074). Mediates response to oxidative stress caused by paraquat (PQ) via induction of the methionine sulfoxide reductase genes, msrA and msrB (PubMed:18662407). Also acts as a transcriptional activator of the bacillithiol (BSH) biosynthesis genes in response to oxidizing conditions and thio-reactive compounds (PubMed:23894131). Involved in heat stress response and thermotolerance development, which results in diminished cellular protein aggregates (PubMed:24417481). Plays an important adaptive role in the cell wall stress response (PubMed:29271514). Participates in sulfate-dependent control of organosulfur metabolism. Negatively controls, via CymR, the expression of the organosulfur utilization operons ytmI, yxeI and ssu, and directly activates yrrT operon expression during growth in medium containing methionine as sole sulfur source (PubMed:16885442). Negatively affects competence and sporulation (PubMed:11703662, PubMed:12028382). Inhibits biofilm formation in response to disulfide stress by repressing biofilm matrix genes (PubMed:30718304). {ECO:0000269|PubMed:11703662, ECO:0000269|PubMed:12028382, ECO:0000269|PubMed:12642660, ECO:0000269|PubMed:14597697, ECO:0000269|PubMed:15659166, ECO:0000269|PubMed:16885442, ECO:0000269|PubMed:18662407, ECO:0000269|PubMed:18687074, ECO:0000269|PubMed:23894131, ECO:0000269|PubMed:24417481, ECO:0000269|PubMed:29271514, ECO:0000269|PubMed:30718304}.
Bacillus subtilis (strain 168)