Entry
stringlengths
6
10
Entry Name
stringlengths
5
11
Sequence
stringlengths
2
35.2k
EC number
stringlengths
7
118
Cofactor
stringlengths
38
1.77k
Gene Ontology (biological process)
stringlengths
18
11.3k
Gene Ontology (cellular component)
stringlengths
17
1.75k
Gene Ontology (molecular function)
stringlengths
24
2.09k
Pfam
stringlengths
8
232
Gene3D
stringlengths
10
250
Protein families
stringlengths
9
237
Post-translational modification
stringlengths
16
8.52k
Subcellular location [CC]
stringlengths
29
6.18k
Catalytic activity
stringlengths
64
35.7k
Kinetics
stringlengths
69
11.7k
Pathway
stringlengths
27
908
pH dependence
stringlengths
64
955
Temperature dependence
stringlengths
70
1.16k
Function [CC]
stringlengths
17
15.3k
Organism
stringlengths
8
196
O46600
GHR_BOVIN
MDLWQLLLTLAVAGSSDAFSGSEATPAFLVRASQSLQILYPVLETNSSGNPKFTKCRSPELETFSCHWTDGANHSLQSPGSVQMFYIRRDIQEWKECPDYVSAGENSCYFNSSYTSVWTPYCIKLTSNGGIVDHKCFSVEDIVQPDPPVGLNWTLLNISLTEIHADILVKWEPPPNTDVKMGWIILEYELHYKELNETQWKMMDPLMVTSVPMYSLRLDKEYEVRVRTRQRNTEKYGKFSEVLLITFPQMNPSACEEDFQFPWFLIIIFGILGLAVTLYLLIFSKQQRIKMLILPPVPVPKIKGIDPDLLKEGKLEEVNT...
null
null
cytokine-mediated signaling pathway [GO:0019221]; endocytosis [GO:0006897]; growth hormone receptor signaling pathway [GO:0060396]; positive regulation of peptidyl-tyrosine phosphorylation [GO:0050731]; positive regulation of receptor signaling pathway via JAK-STAT [GO:0046427]
cytosol [GO:0005829]; external side of plasma membrane [GO:0009897]; extracellular region [GO:0005576]; growth hormone receptor complex [GO:0070195]; membrane [GO:0016020]
cytokine binding [GO:0019955]; growth factor binding [GO:0019838]; growth hormone receptor activity [GO:0004903]; peptide hormone binding [GO:0017046]
PF09067;PF12772;
2.60.40.10;
Type I cytokine receptor family, Type 1 subfamily
PTM: On GH binding, phosphorylated on tyrosine residues in the cytoplasmic domain by JAK2. {ECO:0000250}.; PTM: On ligand binding, ubiquitinated on lysine residues in the cytoplasmic domain. This ubiquitination is not sufficient for GHR internalization (By similarity). {ECO:0000250}.
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Note=On growth hormone binding, GHR is ubiquitinated, internalized, down-regulated and transported into a degradative or non-degradative pathway. {ECO:0000250}.; SUBCELLULAR LOCATION: [Growth hormone-binding protein]: ...
null
null
null
null
null
FUNCTION: Receptor for pituitary gland growth hormone involved in regulating postnatal body growth. On ligand binding, couples to, and activates the JAK2/STAT5 pathway (By similarity). {ECO:0000250}.; FUNCTION: The soluble form (GHBP) acts as a reservoir of growth hormone in plasma and may be a modulator/inhibitor of G...
Bos taurus (Bovine)
O46606
DDHD1_BOVIN
MNYPGHGSPRSSERNGGRGGDGAAWELGSDTEPAFGGSVCRFDHLPVGEPGDDEVPLALLRGEPGLHLAPGAEDHNHHLALDPCLSDDNYDFSSAESGSSLRYYSEGESGGGGSSSSLHPPQQPLVPSNSGGGGAAGGGPGERKRTRPGGAAARHRYEVVTELGPEEVRWFYKEDKKTWKPFIGYDSLRIELAFRTLLQATGARARAQDPDGDHVCGPASPAGPASSSVEDEDEDRVCGFCPRIAGHGREMEELVNIERVCVRGGLYEVDVTQGECYPVYWNQSDKIPVMRGQWFIDGTWQPLEEEESNLIEQEHLSRFR...
3.1.1.111; 3.1.1.118; 3.1.1.32
null
phosphatidylinositol metabolic process [GO:0046488]
cytoplasm [GO:0005737]
metal ion binding [GO:0046872]; phospholipase A1 activity [GO:0008970]; phospholipase activity [GO:0004620]
PF02862;
null
PA-PLA1 family
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8NEL9}.
CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphate + H2O = a 2-acyl-sn-glycerol 3-phosphate + a fatty acid + H(+); Xref=Rhea:RHEA:44648, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:58608, ChEBI:CHEBI:64982; EC=3.1.1.118; Evidence={ECO:0000269|PubMed:10924127, ECO:0000305|PubMed:79...
null
PATHWAY: Phospholipid metabolism; phosphatidylinositol metabolism. {ECO:0000250|UniProtKB:Q8NEL9}.
null
null
FUNCTION: Phospholipase A1 (PLA1) that hydrolyzes ester bonds at the sn-1 position of glycerophospholipids producing a free fatty acid and a lysophospholipid (PubMed:10924127, PubMed:7937808, PubMed:9488669). Prefers phosphatidate (1,2-diacyl-sn-glycero-3-phosphate, PA) as substrate in vitro, but can efficiently hydrol...
Bos taurus (Bovine)
O46629
ECHB_BOVIN
MISLLTYTLKNLPNTSKWALRFCMRPLSSSSQLQAAAASQTKSKKTLAKPNIRNIVVVDGVRTPFLLSGTSYKDLMPHDLARAALSGLLHRTSVPKDVVDYIIFGTVIQEVKTSNVAREAALGAGFSDKTPAHTVTMACISSNQAMTTAVGLIASGQCDVVVAGGVELMSDIPIRHSRKMRKMMLDLNKAKTLAQRLSIISKFRLNFLSPELPAVSEFSTSETMGHSADRLAAAFAISREEQDEYALRSHSLAKKAQDEGLLSDVVPFKVPGRDTVTQDNGIRPSSLDQMAKLKPAFIKPYGTVTAANSSFLTDGASAVL...
2.3.1.155; 2.3.1.16
null
fatty acid beta-oxidation [GO:0006635]
cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; mitochondrial inner membrane [GO:0005743]; mitochondrial outer membrane [GO:0005741]; mitochondrion [GO:0005739]
acetyl-CoA C-acetyltransferase activity [GO:0003985]; acetyl-CoA C-myristoyltransferase activity [GO:0050633]
PF02803;PF00108;
3.40.47.10;
Thiolase-like superfamily, Thiolase family
null
SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:P55084}. Mitochondrion inner membrane {ECO:0000250|UniProtKB:P55084}. Mitochondrion outer membrane {ECO:0000250|UniProtKB:P55084}. Endoplasmic reticulum {ECO:0000250|UniProtKB:P55084}. Note=Protein stability and association with membranes require HADHA. {ECO:00...
CATALYTIC ACTIVITY: Reaction=acetyl-CoA + an acyl-CoA = a 3-oxoacyl-CoA + CoA; Xref=Rhea:RHEA:21564, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:58342, ChEBI:CHEBI:90726; EC=2.3.1.16; Evidence={ECO:0000250|UniProtKB:P55084}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:21566; Evidence={ECO:0000250|UniProt...
null
PATHWAY: Lipid metabolism; fatty acid beta-oxidation. {ECO:0000250|UniProtKB:P55084}.
null
null
FUNCTION: Mitochondrial trifunctional enzyme catalyzes the last three of the four reactions of the mitochondrial beta-oxidation pathway. The mitochondrial beta-oxidation pathway is the major energy-producing process in tissues and is performed through four consecutive reactions breaking down fatty acids into acetyl-CoA...
Bos taurus (Bovine)
O46631
SHPS1_BOVIN
MEPARPAPGRLRPLLCLLLAASNAWTGTAGDGELQVIQPERSVSVAAGETATLHCTVTSLSPVGPIKWFKGTGPGREFIYSQKEAPFPRVTNVSDATKRNNMDFSIRISNITPADAGVYYCVKFRKEERGDMEFKSGPGTHLTVSAKPSPPVLSGPTVRATPEQTVNFTCTSHGFSPRNISLKWFKNGNELSASQTSVDPEDNNVSYSINSTTKVLLATGDVHSQVICEVAHVTLQGGPPLRGTANLSETIRVPPTLEITGSPSAGNQVNVTCQVNKFYPRHLQLTWLENGNMSRTEAASVFVENKDGTFNQTSWFLVNS...
null
null
cellular response to stimulus [GO:0051716]; positive regulation of phagocytosis [GO:0050766]; positive regulation of T cell activation [GO:0050870]
plasma membrane [GO:0005886]
SH3 domain binding [GO:0017124]
PF07654;PF07686;
2.60.40.10;
null
PTM: Phosphorylated on tyrosine residues. {ECO:0000250}.
SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
null
null
null
null
null
FUNCTION: Immunoglobulin-like cell surface receptor for CD47. Acts as docking protein and induces translocation of PTPN6, PTPN11 and other binding partners from the cytosol to the plasma membrane. Supports adhesion of cerebellar neurons, neurite outgrowth and glial cell attachment. May play a key role in intracellular ...
Bos taurus (Bovine)
O46635
5HT2A_CANLF
MDVLFEDNAPLSPTTSSLMPSNGDPRLYGNDLNAGDANTSDAFNWTVDAENRTNLSCEGCLSPPCFSLLHLQEKNWSALLTAVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAVWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVSFFIPLTIMVITYFLTIKSLQKEATLCVSDPGTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYGRRTMQSISNEQKA...
null
null
behavior [GO:0007610]; chemical synaptic transmission [GO:0007268]; G protein-coupled receptor signaling pathway, coupled to cyclic nucleotide second messenger [GO:0007187]; intracellular calcium ion homeostasis [GO:0006874]; phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0043491]; phospholipase...
axon [GO:0030424]; caveola [GO:0005901]; cytoplasmic vesicle [GO:0031410]; dendrite [GO:0030425]; G protein-coupled serotonin receptor complex [GO:0098666]; plasma membrane [GO:0005886]; presynapse [GO:0098793]
1-(4-iodo-2,5-dimethoxyphenyl)propan-2-amine binding [GO:0071886]; G protein-coupled serotonin receptor activity [GO:0004993]; Gq/11-coupled serotonin receptor activity [GO:0001587]; identical protein binding [GO:0042802]; neurotransmitter receptor activity [GO:0030594]; serotonin binding [GO:0051378]
PF00001;
1.20.1070.10;
G-protein coupled receptor 1 family
null
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15862800}; Multi-pass membrane protein {ECO:0000269|PubMed:15862800}. Cell projection, dendrite {ECO:0000250|UniProtKB:P35363}. Cell projection, axon {ECO:0000250|UniProtKB:P14842}. Cytoplasmic vesicle {ECO:0000250|UniProtKB:P14842}. Membrane, caveola {ECO:0000250...
null
null
null
null
null
FUNCTION: G-protein coupled receptor for 5-hydroxytryptamine (serotonin). Also functions as a receptor for various drugs and psychoactive substances, including mescaline, psilocybin, 1-(2,5-dimethoxy-4-iodophenyl)-2-aminopropane (DOI) and lysergic acid diethylamide (LSD). Ligand binding causes a conformation change tha...
Canis lupus familiaris (Dog) (Canis familiaris)
O46647
LIPL_NEOVI
MESKALLLVALGMWFQSLTATRGGVAAADRGGDFIDIESKFALRTPEDTAEDTCHLIPGVTESVANCHFNHSSKTFVVIHGWTVTGMYESWVPKLVAALYKREPDSNVIVVDWLSRAQQHYPVSAGYTKLVGKDVAKFINWMAEEFHYPLDNVHLLGYSLGAHAAGIAGSLTNKKVNRITGLDPAGPNFEYAEAPSRLSPDDADFVDVLHTFTRGSPGRSIGIQKPVGHVDIYPNGGTFQPGCNIGEAIRVIAERGLGDVDQLVKCSHERSIHLFIDSLLNEENPSKAYRCNSKEAFEKGLCLSCRKNRCNNLGYEINKV...
3.1.1.34
null
chylomicron remodeling [GO:0034371]; fatty acid biosynthetic process [GO:0006633]; fatty acid metabolic process [GO:0006631]; response to glucose [GO:0009749]; triglyceride catabolic process [GO:0019433]; very-low-density lipoprotein particle remodeling [GO:0034372]
chylomicron [GO:0042627]; extracellular space [GO:0005615]; plasma membrane [GO:0005886]; very-low-density lipoprotein particle [GO:0034361]
apolipoprotein binding [GO:0034185]; heparan sulfate proteoglycan binding [GO:0043395]; heparin binding [GO:0008201]; lipoprotein lipase activity [GO:0004465]; lipoprotein particle binding [GO:0071813]; metal ion binding [GO:0046872]
PF00151;PF01477;
3.40.50.1820;2.60.60.20;
AB hydrolase superfamily, Lipase family
PTM: Tyrosine nitration after lipopolysaccharide (LPS) challenge down-regulates the lipase activity. {ECO:0000250|UniProtKB:Q06000}.
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P11151}; Peripheral membrane protein {ECO:0000250|UniProtKB:P11151}; Extracellular side {ECO:0000250|UniProtKB:P11151}. Secreted {ECO:0000250|UniProtKB:P11151}. Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:P11151}. Note=Newly synth...
CATALYTIC ACTIVITY: Reaction=a triacylglycerol + H2O = a diacylglycerol + a fatty acid + H(+); Xref=Rhea:RHEA:12044, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17855, ChEBI:CHEBI:18035, ChEBI:CHEBI:28868; EC=3.1.1.34; Evidence={ECO:0000250|UniProtKB:P11151};
null
null
null
null
FUNCTION: Key enzyme in triglyceride metabolism. Catalyzes the hydrolysis of triglycerides from circulating chylomicrons and very low density lipoproteins (VLDL), and thereby plays an important role in lipid clearance from the blood stream, lipid utilization and storage (PubMed:9852258). Mediates margination of triglyc...
Neovison vison (American mink) (Mustela vison)
O46658
CP2DP_PIG
MGLLTGDLLGILALAMVIFLLLVDLMHRRSRWAPRYPPGPMPLPGLGNLLQVNFQDPRLSFIQLRRRFGDVFSLQQIWRPVVVLNGLAAVREALVSHSHETSDRPPVFILEHLGYGPRSEGVILARYGKAWREQRRFSVSTLRNFGLGKKSLEEWVTQEASCLCAAFADQAGRPFSPNNLLNKAVSNVIASLTFARRFEYNDPRMLKLLDLVLEGLKEEVGLMRQVLEAMPVLRHIPGLCAKLFPRQKAFLVMIDELITEHKMTRDLAQPPRDLTDAFLDEMKEAKGNPESSFNDENLRLVVAHLFSAGMITTSTTLAWA...
1.14.14.24
COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
arachidonic acid metabolic process [GO:0019369]; xenobiotic metabolic process [GO:0006805]
cytoplasm [GO:0005737]; endoplasmic reticulum membrane [GO:0005789]; intracellular membrane-bounded organelle [GO:0043231]
3-alpha,7-alpha,12-alpha-trihydroxycholestan-26-al 26-oxidoreductase activity [GO:0047103]; cholestanetriol 26-monooxygenase activity [GO:0047749]; heme binding [GO:0020037]; iron ion binding [GO:0005506]; oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced fla...
PF00067;
1.10.630.10;
Cytochrome P450 family
null
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral membrane protein. Microsome membrane; Peripheral membrane protein.
CATALYTIC ACTIVITY: Reaction=calciol + O2 + reduced [NADPH--hemoprotein reductase] = calcidiol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:32903, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:17933, ChEBI:CHEBI:28940, ChEBI:CH...
null
null
null
null
FUNCTION: Catalyzes the 25-hydroxylation of vitamin D(3) (calciol), 1alpha-hydroxyvitamin D(3) (alphacalcidiol) and some C27 steroids. In addition the enzyme catalyzes the hydroxylation of positions 11 and 12 of dodecanoate. {ECO:0000269|PubMed:1445236, ECO:0000269|PubMed:2169238}.
Sus scrofa (Pig)
O46669
SCNAA_CANLF
MEFPFGSLETTNFRRFTPESLVEIEKRIAAKQAAKKAKGKHREQKDQEEKPRPQLDLKACNQPPKFYGELPAELVGEPLEDLDPFYSTHRTFMVLDKGRTISRFSATRALWLFSPFNLIRRTAIKVSVHSWFSLFITVTILVNCVGMTQTELPDRIEYVFTVIYTFEALIKILARGFCLNEFAYLRDPWDWLDFSVITLAYIGEATALRGISGLRTFRVLRALKTVSVIPGLKVIVGALIHSVRKLADVTILTVFCLSVFALVGLQLFKGNLKNKCVKNCAALNETGNYSSYGKQEWNFCHRDEDFYYNKPGTSDPLLCG...
null
null
membrane depolarization during action potential [GO:0086010]; neuronal action potential [GO:0019228]; regulation of atrial cardiac muscle cell membrane depolarization [GO:0060371]; regulation of heart rate [GO:0002027]; sodium ion transmembrane transport [GO:0035725]
axon [GO:0030424]; plasma membrane [GO:0005886]; voltage-gated sodium channel complex [GO:0001518]
voltage-gated sodium channel activity [GO:0005248]; voltage-gated sodium channel activity involved in cardiac muscle cell action potential [GO:0086006]
PF00520;PF06512;
1.10.287.70;1.10.238.10;1.20.5.1190;1.20.120.350;
Sodium channel (TC 1.A.1.10) family, Nav1.8/SCN10A subfamily
PTM: Ubiquitinated by NEDD4L; which promotes its endocytosis. {ECO:0000250}.; PTM: Phosphorylation at Ser-1458 by PKC in a highly conserved cytoplasmic loop slows inactivation of the sodium channel and reduces peak sodium currents. {ECO:0000250}.; PTM: Lacks the cysteine which covalently binds the conotoxin GVIIJ. This...
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:D0E0C2}; Multi-pass membrane protein {ECO:0000250|UniProtKB:D0E0C2}. Note=It can be translocated to the cell membrane through association with S100A10. {ECO:0000250}.
CATALYTIC ACTIVITY: Reaction=Na(+)(in) = Na(+)(out); Xref=Rhea:RHEA:34963, ChEBI:CHEBI:29101; Evidence={ECO:0000250|UniProtKB:Q9Y5Y9};
null
null
null
null
FUNCTION: Tetrodotoxin-resistant channel that mediates the voltage-dependent sodium ion permeability of excitable membranes. Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a sodium-selective channel through which sodium ions may pass in accordance wi...
Canis lupus familiaris (Dog) (Canis familiaris)
O46674
AT2A2_CANLF
MENAHTKTVEEVLGHFGVNESTGLSLEQVKKLKERWGSNELPAEEGKTLLELVIEQFEDLLVRILLLAACISFVLAWFEEGEETITAFVEPFVILLILVANAIVGVWQERNAENAIEALKEYEPEMGKVYRQDRKSVQRIKAKDIVPGDIVEIAVGDKVPADIRLTSIKSTTLRVDQSILTGESVSVIKHTDPVPDPRAVNQDKKNMLFSGTNIAAGKAMGVVVATGVNTEIGKIRDEMVATEQERTPLQQKLDEFGEQLSKVISLICIAVWIINIGHFNDPVHGGSWIRGAIYYFKIAVALAVAAIPEGLPAVITTCLA...
7.2.2.10
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P11607};
autophagosome assembly [GO:0000045]; autophagosome membrane docking [GO:0016240]; calcium ion transmembrane transport [GO:0070588]; intracellular calcium ion homeostasis [GO:0006874]; mitochondrion-endoplasmic reticulum membrane tethering [GO:1990456]; organelle localization by membrane tethering [GO:0140056]; regulati...
sarcoplasmic reticulum membrane [GO:0033017]
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; metal ion binding [GO:0046872]; P-type calcium transporter activity involved in regulation of cardiac muscle cell membrane potential [GO:0086039]
PF13246;PF00689;PF00690;PF00122;PF00702;
3.40.1110.10;2.70.150.10;1.20.1110.10;3.40.50.1000;
Cation transport ATPase (P-type) (TC 3.A.3) family, Type IIA subfamily
PTM: Nitrated under oxidative stress. Nitration on the two tyrosine residues inhibits catalytic activity. {ECO:0000250|UniProtKB:P16615}.; PTM: Serotonylated on Gln residues by TGM2 in response to hypoxia, leading to its inactivation. {ECO:0000250|UniProtKB:O55143}.
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:O55143}; Multi-pass membrane protein {ECO:0000255}. Sarcoplasmic reticulum membrane {ECO:0000250|UniProtKB:O55143}; Multi-pass membrane protein {ECO:0000255}. Note=Colocalizes with FLVCR2 at the mitochondrial-ER contact junction. {ECO:0000250|U...
CATALYTIC ACTIVITY: Reaction=ATP + Ca(2+)(in) + H2O = ADP + Ca(2+)(out) + H(+) + phosphate; Xref=Rhea:RHEA:18105, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29108, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.2.2.10; Evidence={ECO:0000250|UniProtKB:P16615}; PhysiologicalDirection=left-to-right;...
null
null
null
null
FUNCTION: This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the translocation of calcium from the cytosol to the sarcoplasmic reticulum lumen. Involved in autophagy in response to starvation. Upon interaction with VMP1 and activation, controls ER-isolation membrane contacts for autophagosome ...
Canis lupus familiaris (Dog) (Canis familiaris)
O46680
TGFR1_BOVIN
MEAAAATPRPRLFLLMLAAAATLVPEATPLQCFCHLCTKDNFTCVTDGLCFVSVTETTDKVIHNSMCIAEIDLIPRDRPFVCAPSSKTGSITTTYCCNQDHCNKIELPTVGKPSSGLGPVELAAVIAGPVCFVCISLMLMVYICHNRTVIHHRVPNEEDPSLDRPFISEGTTLKDLIYDMTTSGSGSGLPLLVQRTIARTIVLQESIGKGRFGEVWRGKWRGEEVAVKIFSSREERSWFREAEIYQTVMLRHENILGFIAADNKDNGTWTQLWLVSDYHEHGSLFDYLNRYTVTVEGMIKLALSTASGLAHLHMEIVGTQ...
2.7.11.30
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
activin receptor signaling pathway [GO:0032924]; apoptotic process [GO:0006915]; cardiac epithelial to mesenchymal transition [GO:0060317]; cellular response to growth factor stimulus [GO:0071363]; cellular response to transforming growth factor beta stimulus [GO:0071560]; endothelial cell activation [GO:0042118]; hear...
activin receptor complex [GO:0048179]; bicellular tight junction [GO:0005923]; cell surface [GO:0009986]; endosome [GO:0005768]; membrane [GO:0016020]; membrane raft [GO:0045121]; nucleus [GO:0005634]; plasma membrane [GO:0005886]
activin binding [GO:0048185]; activin receptor activity, type I [GO:0016361]; ATP binding [GO:0005524]; metal ion binding [GO:0046872]; SMAD binding [GO:0046332]; transforming growth factor beta binding [GO:0050431]; transforming growth factor beta receptor activity, type I [GO:0005025]
PF01064;PF00069;PF08515;
2.10.60.10;1.10.510.10;
Protein kinase superfamily, TKL Ser/Thr protein kinase family, TGFB receptor subfamily
PTM: Phosphorylated at basal levels in the absence of ligand. Activated upon phosphorylation by TGFBR2, mainly in the GS domain. Phosphorylation in the GS domain abrogates FKBP1A-binding (By similarity). {ECO:0000250|UniProtKB:P36897}.; PTM: N-Glycosylated. {ECO:0000250|UniProtKB:P36897}.; PTM: Ubiquitinated; undergoes...
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P36897}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P36897}. Cell junction, tight junction {ECO:0000250|UniProtKB:P36897}. Membrane raft {ECO:0000250|UniProtKB:P36897}. Cell surface {ECO:0000250|UniProtKB:P36897}.
CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[receptor-protein] = ADP + H(+) + O-phospho-L-threonyl-[receptor-protein]; Xref=Rhea:RHEA:44880, Rhea:RHEA-COMP:11024, Rhea:RHEA-COMP:11025, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.30; CATALYTIC ACTIVITY: Rea...
null
null
null
null
FUNCTION: Transmembrane serine/threonine kinase forming with the TGF-beta type II serine/threonine kinase receptor, TGFBR2, the non-promiscuous receptor for the TGF-beta cytokines TGFB1, TGFB2 and TGFB3. Transduces the TGFB1, TGFB2 and TGFB3 signal from the cell surface to the cytoplasm and is thus regulating a plethor...
Bos taurus (Bovine)
O48528
OP163_ARATH
MDPAEMRYLEEEDGPLMKTIKGSITGFGAGTIYGTILATWKDVPRVERNVALPGLIRTLKMMGTHGLTFAAIGGVYIGVEQLVQNFRSKRDFYNGAIGGFVAGASVLGYRARSIPTAIAAGATLAVTSALIDSGGQTTRVDNGREYYPYTVEKRAEADS
null
null
monoatomic ion transport [GO:0006811]; protein insertion into mitochondrial inner membrane [GO:0045039]
chloroplast [GO:0009507]; chloroplast outer membrane [GO:0009707]; cytosol [GO:0005829]; mitochondrial outer membrane [GO:0005741]; mitochondrial respiratory chain complex I [GO:0005747]; mitochondrion [GO:0005739]; plastid outer membrane [GO:0009527]; pore complex [GO:0046930]; TIM22 mitochondrial import inner membran...
mitochondrion targeting sequence binding [GO:0030943]; porin activity [GO:0015288]; protein homodimerization activity [GO:0042803]; protein transmembrane transporter activity [GO:0008320]
PF02466;
null
Tim17/Tim22/Tim23 family, Plastid outer envelope porin OEP16 (TC 1.B.30) subfamily
null
SUBCELLULAR LOCATION: Plastid, chloroplast outer membrane {ECO:0000269|PubMed:18431481}; Multi-pass membrane protein. Mitochondrion outer membrane {ECO:0000269|PubMed:21841088}; Multi-pass membrane protein {ECO:0000255}. Mitochondrion inner membrane {ECO:0000269|PubMed:21841088}; Multi-pass membrane protein {ECO:000025...
null
null
null
null
null
FUNCTION: Voltage-dependent high-conductance channel with a slight cation-selectivity; selective for amino acids but excludes triosephosphates or uncharged sugars. Non-essential amino acid-selective channel protein and translocation pore for NADPH:protochlorophyllide oxidoreductase A (PORA) and possibly PORB (By simila...
Arabidopsis thaliana (Mouse-ear cress)
O48533
PYM_ARATH
MPEARDRIERQVDYPAAFLNRRSHGILLDEPATQHNLFGSPVQRVPSEATGGLGSIGQGSMTGRGGLVRGNFGIRRTGGGRRGQIQFRSPQGRENMSLGVTRRGRARASNSVLPSWYPRTPLRDISAVVRAIERRRARMGEGVGRDIETPTPQQLGVLDSLVPLSGAHLEHDYSMVTPGPSIGFKRPWPPSTAKVHQILLDITRENTGEEDALTPEKKLLNSIDKVEKVVMEEIQKMKSTPSAKRAEREKRVRTLMSMR
null
null
cell division [GO:0051301]; defense response [GO:0006952]; DNA endoreduplication [GO:0042023]; endosperm development [GO:0009960]; megagametogenesis [GO:0009561]; negative regulation of ubiquitin protein ligase activity [GO:1904667]; positive regulation of defense response to bacterium [GO:1900426]; regulation of nucle...
nucleus [GO:0005634]
null
null
null
null
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:22167059}. Note=Follows a patchy nuclear accumulation pattern.
null
null
null
null
null
FUNCTION: Negative regulator of the anaphase-promoting complex/cyclosome (APC/C) ubiquitin ligase required for proper mitotic progression and cell fate determination; inhibits premature cell differentiation. Prevents DNA endoreplication by promoting the maintenance of the mitotic state by preferentially inhibiting APC/...
Arabidopsis thaliana (Mouse-ear cress)
O48538
RBOHF_ARATH
MKPFSKNDRRRWSFDSVSAGKTAVGSASTSPGTEYSINGDQEFVEVTIDLQDDDTIVLRSVEPATAINVIGDISDDNTGIMTPVSISRSPTMKRTSSNRFRQFSQELKAEAVAKAKQLSQELKRFSWSRSFSGNLTTTSTAANQSGGAGGGLVNSALEARALRKQRAQLDRTRSSAQRALRGLRFISNKQKNVDGWNDVQSNFEKFEKNGYIYRSDFAQCIGMKDSKEFALELFDALSRRRRLKVEKINHDELYEYWSQINDESFDSRLQIFFDIVDKNEDGRITEEEVKEIIMLSASANKLSRLKEQAEEYAALIMEEL...
1.11.1.-; 1.6.3.-
null
abscisic acid-activated signaling pathway [GO:0009738]; carbohydrate homeostasis [GO:0033500]; defense response by callose deposition [GO:0052542]; ethylene-activated signaling pathway [GO:0009873]; hydrogen peroxide biosynthetic process [GO:0050665]; negative regulation of programmed cell death [GO:0043069]; osmosenso...
plasma membrane [GO:0005886]
calcium ion binding [GO:0005509]; NAD(P)H oxidase H2O2-forming activity [GO:0016174]; peroxidase activity [GO:0004601]
PF08022;PF01794;PF08030;PF08414;
1.10.238.10;3.40.50.80;2.40.30.10;
RBOH (TC 5.B.1.3) family
PTM: Not glycosylated. Phosphorylated by CIPK26. {ECO:0000269|PubMed:23335733}.
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23335733, ECO:0000269|PubMed:9490748}; Multi-pass membrane protein {ECO:0000269|PubMed:23335733, ECO:0000269|PubMed:9490748}.
null
null
null
null
null
FUNCTION: Calcium-dependent NADPH oxidase that generates superoxide. Generates reactive oxygen species (ROS) during incompatible interactions with pathogens and is important in the regulation of the hypersensitive response (HR). Involved in abscisic acid-induced stomatal closing and in UV-B and abscisic acid ROS-depend...
Arabidopsis thaliana (Mouse-ear cress)
O48573
LAZ5_ARATH
MAASSEILPESWQVFINFRGADLRNGFISHLAGALTSAGITYYIDTEEVPSEDLTVLFKRIEESEIALSIFSSNYAESKWCLDELVKIMEQVKKGKLRIMPVFFNVKPEEVREQNGEFGLKLYGEGKSKRPNIPNWENALRSVPSKIGLNLANFRNEKELLDKIIDSIKKVLARITRASRVAESLNGISKDSEAKNVDTFSPNSSDFPSTSIDDDLSINSPQYQATIPPASREGERLNTISTVSSTGSIEHPPPNYGIEPRLKEMEEKLDFDSLETKTVGIVGMPGIGKTTLAETLYRKWEHKFERSMFFPDASKMANEH...
3.2.2.6
null
defense response to virus [GO:0051607]; plant-type hypersensitive response [GO:0009626]; response to virus [GO:0009615]; signal transduction [GO:0007165]
null
ADP binding [GO:0043531]; ATP binding [GO:0005524]; NAD+ nucleosidase activity [GO:0003953]; NAD+ nucleotidase, cyclic ADP-ribose generating [GO:0061809]
PF20160;PF07725;PF00931;PF01582;
1.10.8.430;3.40.50.300;3.80.10.10;3.40.50.10140;
null
null
null
CATALYTIC ACTIVITY: Reaction=H2O + NAD(+) = ADP-D-ribose + H(+) + nicotinamide; Xref=Rhea:RHEA:16301, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17154, ChEBI:CHEBI:57540, ChEBI:CHEBI:57967; EC=3.2.2.6; Evidence={ECO:0000255|PROSITE-ProRule:PRU00204}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16302; Ev...
null
null
null
null
FUNCTION: TIR-NB-LRR receptor-like protein that may play a role in plant innate immunity. May trigger hypersensitive programmed cell death in response to pathogen attack (PubMed:20949080). Involved in tolerance to tobacco ringspot virus (TRSV) (PubMed:22057987). {ECO:0000269|PubMed:20949080, ECO:0000269|PubMed:22057987...
Arabidopsis thaliana (Mouse-ear cress)
O48593
SYNO_ARATH
MAATFLPATSLRLTQNSTLRFLSFFTISNPSYSLFRPLRRRVLPPFDAFPANSRRRCFCTAVSESLGSGDGNKVESYEKRFGSKVGEFRKKLRIAEVKGGADEGLSRVGQSLNIMGWVRTLRSQSSVTFIEINDGSCLSNLQCVMTSDAEGYDQVESGSILTGASVSVQGTIVASQGTKQKVELKVEKIIVVGECDSSYPIQKKRVSREFLRTKAHLRPRTNTFGAVARVRNTLAYATHKFFQESGFVWVASPIITASDCEGAGEQFCVTTLIPSSHENTDTSIDAIPKTKGGLIDWSQDFFGKPAFLTVSGQLNGETYA...
6.1.1.22
null
asparaginyl-tRNA aminoacylation [GO:0006421]; plant ovule development [GO:0048481]
chloroplast [GO:0009507]; chloroplast stroma [GO:0009570]; mitochondrion [GO:0005739]
asparagine-tRNA ligase activity [GO:0004816]; ATP binding [GO:0005524]; DNA binding [GO:0003677]
PF00152;PF01336;
2.40.50.140;
Class-II aminoacyl-tRNA synthetase family
null
SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000269|PubMed:10824085}. Mitochondrion {ECO:0000269|PubMed:10824085}.
CATALYTIC ACTIVITY: Reaction=ATP + L-asparagine + tRNA(Asn) = AMP + diphosphate + H(+) + L-asparaginyl-tRNA(Asn); Xref=Rhea:RHEA:11180, Rhea:RHEA-COMP:9659, Rhea:RHEA-COMP:9674, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:58048, ChEBI:CHEBI:78442, ChEBI:CHEBI:78515, ChEBI:CHEBI:456215; EC=6.1.1...
null
null
null
null
null
Arabidopsis thaliana (Mouse-ear cress)
O48626
ZW10_ARATH
MPEIDALFESINVRDLLAGHDLNDPTTPLSAPDLRLLINRLESHSLRIKSKVQSYLVAHHSDFSELFSLCQDTVSRTRLISDDVSDVLQLVSDRPIDVEIRSVVDEITEKTKEVKLKRESLDLVNAIVGICEALQETKEALKNGRFRFAAERIRELKVVLRIGEEEDGEPVAYALLRKEWSNCFDEIQEVLAKFMENAVRFELDSSRIRIKYQLSVGETAGIALSTVLEAMEVIGILDYGLAKAADSIFKHVITPAVTHASTFAAVEDLCKSAGEVTEATLRLEQSSDHKFEDVDGDAMYSGILKVVKFICSSLCFGNVT...
null
null
cell division [GO:0051301]; chromosome segregation [GO:0007059]; endoplasmic reticulum to Golgi vesicle-mediated transport [GO:0006888]; mitotic spindle assembly checkpoint signaling [GO:0007094]; protein exit from endoplasmic reticulum [GO:0032527]; protein transport [GO:0015031]
endoplasmic reticulum membrane [GO:0005789]; nucleus [GO:0005634]; RZZ complex [GO:1990423]; spindle [GO:0005819]
null
PF20666;PF20665;PF06248;
1.10.357.150;
ZW10 family
null
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, spindle. Cytoplasm. Chromosome, centromere. Chromosome, centromere, kinetochore. Endoplasmic reticulum membrane; Peripheral membrane protein {ECO:0000269|PubMed:24118572}. Note=In prometaphase, associated with the kinetochore. At metaphase, mostly associated with the spind...
null
null
null
null
null
FUNCTION: May be required for accurate chromosome segregation. Required for proper maturation of seed storage proteins. Forms a complex with MAG2, MIP2 and MIP3 on the endoplasmic reticulum that may be responsible for efficient transport of seed storage proteins. {ECO:0000269|PubMed:24118572, ECO:0000305}.
Arabidopsis thaliana (Mouse-ear cress)
O48651
SQE1_PANGI
MNSSSSTTTTDTLHSFMEASALLIDQYFLGWIFAFLFGFLLLLNFKRKREKNNSTEFGTDDSNGYYTPENIAGSTDVIIVGAGVAGSALAYTLANDGRRVHVIERDLTEQDRIVGELLQPGGYLKLIELGLEDCVNEIDAQRVFGYALYMDGKNTRLSYPLEKFHSDVAGRSFHNGRFVQRMREKAASLPNVRMEQGTVTSLVEKKGSVKGVQYKTKDGQELSAFAPLTIVCDGCFSNLRRSLCNPKVEVPSCFVGLILENIDLPHINHGHVILADPSPILFYKISSTEIRCLVDVPGQKVPCISNGELANYLKTVVAPQ...
1.14.14.17
COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250|UniProtKB:Q14534};
response to ethylene [GO:0009723]; response to hydrogen peroxide [GO:0042542]; response to jasmonic acid [GO:0009753]; response to metal ion [GO:0010038]; response to molecule of fungal origin [GO:0002238]; response to nitric oxide [GO:0071731]; response to salicylic acid [GO:0009751]; response to vanadate(3-) [GO:1902...
endoplasmic reticulum membrane [GO:0005789]
flavin adenine dinucleotide binding [GO:0050660]; squalene monooxygenase activity [GO:0004506]
PF01266;PF08491;
3.50.50.60;
Squalene monooxygenase family
null
SUBCELLULAR LOCATION: Microsome membrane {ECO:0000250|UniProtKB:P32476}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P32476}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P32476}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P32476}.
CATALYTIC ACTIVITY: Reaction=O2 + reduced [NADPH--hemoprotein reductase] + squalene = (S)-2,3-epoxysqualene + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:25282, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:15440, ChEBI:CHEBI:15...
null
PATHWAY: Terpene metabolism; lanosterol biosynthesis; lanosterol from farnesyl diphosphate: step 2/3.
null
null
FUNCTION: Component of the triterpene saponins (e.g. ginsenosides or panaxosides) and phytosterols biosynthetic pathways (PubMed:19857882, PubMed:27746309, PubMed:29378087). Catalyzes the first oxygenation step in sterol biosynthesis and is suggested to be one of the rate-limiting enzymes in this pathway (By similarity...
Panax ginseng (Korean ginseng)
O48652
UVR3_ARATH
MQRFCVCSPSSYRLNPITSMATGSGSLIWFRKGLRVHDNPALEYASKGSEFMYPVFVIDPHYMESDPSAFSPGSSRAGVNRIRFLLESLKDLDSSLKKLGSRLLVFKGEPGEVLVRCLQEWKVKRLCFEYDTDPYYQALDVKVKDYASSTGVEVFSPVSHTLFNPAHIIEKNGGKPPLSYQSFLKVAGEPSCAKSELVMSYSSLPPIGDIGNLGISEVPSLEELGYKDDEQADWTPFRGGESEALKRLTKSISDKAWVANFEKPKGDPSAFLKPATTVMSPYLKFGCLSSRYFYQCLQNIYKDVKKHTSPPVSLLGQLLW...
4.1.99.13
COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|PubMed:9421527}; Note=Binds 1 FAD per subunit. {ECO:0000269|PubMed:9421527};
circadian regulation of gene expression [GO:0032922]; entrainment of circadian clock by photoperiod [GO:0043153]; pyrimidine dimer repair [GO:0006290]; response to UV [GO:0009411]
cytoplasm [GO:0005737]; nucleus [GO:0005634]
deoxyribodipyrimidine photo-lyase activity [GO:0003904]; DNA (6-4) photolyase activity [GO:0003914]; DNA binding [GO:0003677]; FAD binding [GO:0071949]
PF00875;PF03441;
1.25.40.80;1.10.579.10;3.40.50.620;
DNA photolyase class-1 family
null
null
CATALYTIC ACTIVITY: Reaction=(6-4) photoproduct (in DNA) = 2 pyrimidine residues (in DNA).; EC=4.1.99.13;
null
null
null
null
FUNCTION: Involved in repair of UV radiation-induced DNA damage. Catalyzes the photoreactivation of pyrimidine [6-4] pyrimidone photoproduct (6-4 products). Binds specifically to DNA containing 6-4 products and repairs these lesions in a visible light-dependent manner. Not required for repair of cyclobutane pyrimidine ...
Arabidopsis thaliana (Mouse-ear cress)
O48653
DPOLA_ORYSJ
MDEGSADAGASGRRSRARGSEAVARSAALERLRAIRDGGARAAAAVQVRIEAPIYDTVAEEDYAALVARRRKDAGAFIVDDDGLGYADDGREEDWTHRTIHSSSDEGSDGEDGAPRKRKQPRPQSKRPPQQSAAAASLSAAAAMMGKQRLSSMFTSSVFRKPGSDRGRDSSLAADSIVDDVIAEFAPDDNDREERRRRVGRVCAPAPAPTTTAHIKAENVAVDTAMAFRSDNVFEAHEVSDHGNDMDMELKPDVEMEPKLDTPLGASAELANNSNSLEEPKQEANGEVKIEKVHRLNAKIKTEDSRNGDMASATAGWMKI...
2.7.7.7
null
DNA replication initiation [GO:0006270]; lagging strand elongation [GO:0006273]; leading strand elongation [GO:0006272]; leaf morphogenesis [GO:0009965]; mitotic DNA replication initiation [GO:1902975]
alpha DNA polymerase:primase complex [GO:0005658]; nucleus [GO:0005634]
chromatin binding [GO:0003682]; DNA primase activity [GO:0003896]; DNA replication origin binding [GO:0003688]; DNA-directed DNA polymerase activity [GO:0003887]; metal ion binding [GO:0046872]; nucleotide binding [GO:0000166]; single-stranded DNA binding [GO:0003697]
PF12254;PF00136;PF03104;PF08996;
2.40.50.730;3.30.70.2820;1.10.3200.20;1.10.132.60;1.10.287.690;3.90.1600.10;3.30.420.10;
DNA polymerase type-B family
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CATALYTIC ACTIVITY: Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339, Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:173112; EC=2.7.7.7;
null
null
null
null
FUNCTION: Polymerase alpha in a complex with DNA primase is a replicative polymerase.
Oryza sativa subsp. japonica (Rice)
O48666
SQS1_PANGI
MGSLGAILKHPEDFYPLLKLKFAARHAEKQIPPEPHWAFCYSMLHKVSRSFGLVIQQLGPQLRDAVCIFYLVLRALDTVEDDTSIPTEVKVPILMAFHRHIYDKDWHFSCGTKEYKVLMDEFHHVSNAFLELGSGYQEAIEDITMRMGAGMAKFICKEVETINDYDEYCHYVAGLVGLGLSKLFHASGAEDLATDSLSNSMGLFLQKTNIIRDYLEDINEIPKSRMFWPRQIWSKYVDKLEDLKYEENSAKAVQCLNDMVTDALVHAEDCLKYMSDLRGPAIFRFCAIPQIMAIGTLALCFNNTQVFRGVVKMRRGLTAK...
2.5.1.21
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P53799}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:P53799};
cholesterol biosynthetic process [GO:0006695]; ergosterol biosynthetic process [GO:0006696]; farnesyl diphosphate metabolic process [GO:0045338]; response to ethylene [GO:0009723]; response to hydrogen peroxide [GO:0042542]; response to jasmonic acid [GO:0009753]; response to molecule of fungal origin [GO:0002238]; res...
endoplasmic reticulum membrane [GO:0005789]
farnesyl-diphosphate farnesyltransferase activity [GO:0004310]; farnesyltranstransferase activity [GO:0004311]; squalene synthase activity [GO:0051996]
PF00494;
1.10.600.10;
Phytoene/squalene synthase family
null
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P53799}; Multi-pass membrane protein {ECO:0000255}.
CATALYTIC ACTIVITY: Reaction=2 (2E,6E)-farnesyl diphosphate + H(+) + NADH = 2 diphosphate + NAD(+) + squalene; Xref=Rhea:RHEA:32299, ChEBI:CHEBI:15378, ChEBI:CHEBI:15440, ChEBI:CHEBI:33019, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:175763; EC=2.5.1.21; Evidence={ECO:0000250|UniProtKB:P53799}; PhysiologicalDirec...
null
PATHWAY: Terpene metabolism; lanosterol biosynthesis; lanosterol from farnesyl diphosphate: step 1/3. {ECO:0000250|UniProtKB:P53799}.
null
null
FUNCTION: Component of the triterpene saponins (e.g. ginsenosides or panaxosides) and phytosterols biosynthetic pathways (PubMed:15356323, PubMed:27746309, PubMed:29378087). Catalyzes the biosynthesis of squalene (PubMed:15356323). {ECO:0000269|PubMed:15356323, ECO:0000269|PubMed:27746309, ECO:0000303|PubMed:29378087}.
Panax ginseng (Korean ginseng)
O48676
U74B1_ARATH
MAETTPKVKGHVVILPYPVQGHLNPMVQFAKRLVSKNVKVTIATTTYTASSITTPSLSVEPISDGFDFIPIGIPGFSVDTYSESFKLNGSETLTLLIEKFKSTDSPIDCLIYDSFLPWGLEVARSMELSAASFFTNNLTVCSVLRKFSNGDFPLPADPNSAPFRIRGLPSLSYDELPSFVGRHWLTHPEHGRVLLNQFPNHENADWLFVNGFEGLEETQDCENGESDAMKATLIGPMIPSAYLDDRMEDDKDYGASLLKPISKECMEWLETKQAQSVAFVSFGSFGILFEKQLAEVAIALQESDLNFLWVIKEAHIAKLP...
2.4.1.195
null
defense response by callose deposition in cell wall [GO:0052544]; defense response to bacterium [GO:0042742]; glucosinolate biosynthetic process [GO:0019761]
cytosol [GO:0005829]; nucleus [GO:0005634]
quercetin 3-O-glucosyltransferase activity [GO:0080043]; quercetin 7-O-glucosyltransferase activity [GO:0080044]; thiohydroximate beta-D-glucosyltransferase activity [GO:0047251]; UDP-glucose: 4-methylthiobutylhydroximate S-glucosyltransferase activity [GO:0102659]; UDP-glucose: 6-methylthiohexylhydroximate S-glucosylt...
PF00201;
3.40.50.2000;
UDP-glycosyltransferase family
null
null
CATALYTIC ACTIVITY: Reaction=(Z)-2-phenyl-1-thioacetohydroximate + UDP-alpha-D-glucose = (Z)-desulfoglucotropeolin + UDP; Xref=Rhea:RHEA:13757, ChEBI:CHEBI:58176, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885, ChEBI:CHEBI:136422; EC=2.4.1.195; Evidence={ECO:0000269|PubMed:15584955}; CATALYTIC ACTIVITY: Reaction=a (Z)-omega-(met...
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=5.8 uM for PATH {ECO:0000269|PubMed:15584955}; KM=48 uM for UDP-glucose {ECO:0000269|PubMed:15584955};
null
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6. Stable between pH 5-9. {ECO:0000269|PubMed:15584955};
null
FUNCTION: Involved in the biosynthesis of glucosinolate. In in vitro assay, may use phenylacetothiohydroximate (PATH), but not phenylacetic acid (PAA), indole-3-acetic acid (IAA) or salicylic acid (SA) as substrate. Specific for the thiohydroximate functional group and does not glucosylate the carboxylate group or a hy...
Arabidopsis thaliana (Mouse-ear cress)
O48709
PI5K3_ARATH
MQETVFLFTEENLNKEQSLGVKYKQSSRRVVPMTSCEVSDTAAEIRIVEKVLKNGDLYNGGLSAGVPHGTGKYLWSDGCMYEGEWTRGKASGKGRFSWPSGATYEGQFKDGRMDGEGTFIGIDGDTYRGHWLWGRKHGYGEKRYANGDGYQGNWKANLQDGNGRYVWSDGNEYVGEWKNGVISGKGKMTWANGNRYDGLWENGAPVGKGVLSWGEEKTSYNGWGRKSKKKDEEIVQNHKLSSVETLSANTNFPRICISELEDTGVCDHVEASPYTSESDTSGCGEQEWARSPLLLESGGAMSVQQSPRWLDEGDVKKPGH...
2.7.1.68
null
phosphatidylinositol phosphate biosynthetic process [GO:0046854]; phosphorylation [GO:0016310]; regulation of establishment of cell polarity [GO:2000114]; root hair cell tip growth [GO:0048768]; root hair elongation [GO:0048767]; root hair initiation [GO:0048766]
apical plasma membrane [GO:0016324]; cytoplasm [GO:0005737]; plasma membrane [GO:0005886]
1-phosphatidylinositol-4-phosphate 5-kinase activity [GO:0016308]; ATP binding [GO:0005524]
PF02493;PF01504;
3.30.810.10;2.20.110.10;3.30.800.10;
null
null
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:27251533}. Note=Accumulates in a sterol-enriched, polar membrane domain during root hair initiation. {ECO:0000269|PubMed:27251533}.
CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol 4-phosphate) + ATP = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-bisphosphate) + ADP + H(+); Xref=Rhea:RHEA:14425, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:58178, ChEBI:CHEBI:58456, ChEBI:CHEBI:456216; EC=2.7.1.68; Evide...
null
null
null
null
FUNCTION: With DRP1A and DRP2B, required for the precise coordination of polar ARAC3/ROP6 and ARAC4/ROP2 placement and subsequent root hair positioning during planar polarity formation in root hair-forming cells, probably by mediating the correct basal-to-planar polarity switching of D6PK into the polar, lipid-enriched...
Arabidopsis thaliana (Mouse-ear cress)
O48711
PME12_ARATH
MALSSFNLSSLLFLLFFTPSVFSYSYQPSLNPHETSATSFCKNTPYPDACFTSLKLSISINISPNILSFLLQTLQTALSEAGKLTDLLSGAGVSNNLVEGQRGSLQDCKDLHHITSSFLKRSISKIQDGVNDSRKLADARAYLSAALTNKITCLEGLESASGPLKPKLVTSFTTTYKHISNSLSALPKQRRTTNPKTGGNTKNRRLLGLFPDWVYKKDHRFLEDSSDGYDEYDPSESLVVAADGTGNFSTINEAISFAPNMSNDRVLIYVKEGVYDENIDIPIYKTNIVLIGDGSDVTFITGNRSVGDGWTTFRSATLAV...
3.1.1.11
null
cell wall modification [GO:0042545]; pectin catabolic process [GO:0045490]; response to bacterium [GO:0009617]
extracellular region [GO:0005576]
aspartyl esterase activity [GO:0045330]; pectinesterase activity [GO:0030599]; pectinesterase inhibitor activity [GO:0046910]
PF01095;PF04043;
1.20.140.40;2.160.20.10;
PMEI family; Pectinesterase family
null
SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000250}.
CATALYTIC ACTIVITY: Reaction=[(1->4)-alpha-D-galacturonosyl methyl ester](n) + n H2O = [(1->4)-alpha-D-galacturonosyl](n) + n H(+) + n methanol; Xref=Rhea:RHEA:22380, Rhea:RHEA-COMP:14570, Rhea:RHEA-COMP:14573, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17790, ChEBI:CHEBI:140522, ChEBI:CHEBI:140523; EC=3.1.1.11;
null
PATHWAY: Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-gluconate from pectin: step 1/5.
null
null
FUNCTION: Acts in the modification of cell walls via demethylesterification of cell wall pectin. {ECO:0000250}.
Arabidopsis thaliana (Mouse-ear cress)
O48723
PLP2_ARATH
MQMDSPKSPLQPPTYGNLVTILSIDGGGIRGLIPAVILGFLESELQKLDGEEARLADYFDVIAGTSTGGLVTAMLTAPNKEGRPLFAASEIKDFYLEQCPKIFPQDHFPFSAAKKLVKSLTGPKYDGKYLHQLIHAKLGDTKLSQTLTNVVIPTFDIKHLQPTIFSSYEVKNHPLKDATLADIAISTSAAPTYLPAHFFKVEDLNGNAKEYNLIDGGVAANNPALLAIGEVTNEISGGSSDFFPIRPNDYGRFLVLSLGTGNHKAEEKFNAKEVAGWGLLNWLTHDNSTPIIDAFSQASSDMVDFHLSAVFRALHSEANY...
3.1.1.-
null
cellular response to hypoxia [GO:0071456]; D-xylose catabolic process [GO:0042843]; defense response to virus [GO:0051607]; lipid catabolic process [GO:0016042]; lipid metabolic process [GO:0006629]; oxylipin biosynthetic process [GO:0031408]; plant-type hypersensitive response [GO:0009626]; response to cadmium ion [GO...
cytoplasm [GO:0005737]; membrane [GO:0016020]; peroxisome [GO:0005777]
acylglycerol lipase activity [GO:0047372]; identical protein binding [GO:0042802]; lipase activity [GO:0016298]; phospholipase activity [GO:0004620]; xylose isomerase activity [GO:0009045]
PF01734;
3.40.1090.10;
Patatin family
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12226489, ECO:0000269|PubMed:16297072}.
null
null
null
null
null
FUNCTION: Possesses non-specific lipolytic acyl hydrolase (LAH) activity. Catalyzes the hydrolysis of the galactolipids monogalactosyldiacylglycerol (MGDG) and digalactosyldiacylglycerol (DGDG), and less efficiently the phoshpolipids phosphatidylcholine (PC), phosphatidylethanolamine (PE), phosphatidylglycerol (PG), ph...
Arabidopsis thaliana (Mouse-ear cress)
O48726
RPN13_ARATH
MSSSEAFPVMQEIMLEFRAGKMSLQGTRVVPDARKGLVRIARGDEGLIHFQWLDRNQNTVEDDQIVFPDEALFEKVNQSSDRVYILKFNSDDRKLFFWMQEPRAEGDAELCSSVNQYLNQPLEFPGEEGLAAAITEELEDMAEDNTSSRAGNLVVPNLSSEVSDVTSSSGPVKLADLQRILNNLSGGPVGIAGDQDEGLALGDILKPELIMPLLEALPVQERLSSHLPEGHSRAEDILELLQSPPFRQQVDAFTYVLRTGQIDLTQFGIDPSKYKFTVDSFLEALEDSVSTQSRDAMDES
null
null
null
cytoplasm [GO:0005737]; nucleus [GO:0005634]; proteasome regulatory particle, lid subcomplex [GO:0008541]
endopeptidase activator activity [GO:0061133]; proteasome binding [GO:0070628]
PF04683;PF16550;
1.10.2020.20;2.30.29.70;
RPN13 family
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|PROSITE-ProRule:PRU01265}. Nucleus {ECO:0000255|PROSITE-ProRule:PRU01265}.
null
null
null
null
null
FUNCTION: Functions as a proteasomal ubiquitin receptor. Binds and presumably selects ubiquitin-conjugates for destruction. Prefers multiubiquitin chains rather than single ubiquitins, with a binding affinity for 'Lys-63'-linked ubiquitin chains. {ECO:0000269|PubMed:21764993, ECO:0000269|PubMed:22751321}.
Arabidopsis thaliana (Mouse-ear cress)
O48737
TRXM1_ARATH
MAAYTCTSRPPISIRSEMRIASSPTGSFSTRQMFSVLPESSGLRTRVSLSSLSKNSRVSRLRRGVICEAQDTATGIPVVNDSTWDSLVLKADEPVFVDFWAPWCGPCKMIDPIVNELAQKYAGQFKFYKLNTDESPATPGQYGVRSIPTIMIFVNGEKKDTIIGAVSKDTLATSINKFL
null
null
negative regulation of catalytic activity [GO:0043086]; positive regulation of catalytic activity [GO:0043085]; regulation of carbohydrate metabolic process [GO:0006109]; response to cold [GO:0009409]
apoplast [GO:0048046]; chloroplast [GO:0009507]; chloroplast envelope [GO:0009941]; chloroplast stroma [GO:0009570]; extracellular region [GO:0005576]; stromule [GO:0010319]; thylakoid [GO:0009579]
enzyme activator activity [GO:0008047]; enzyme inhibitor activity [GO:0004857]; protein-disulfide reductase activity [GO:0015035]; salicylic acid binding [GO:1901149]
PF00085;
3.40.30.10;
Thioredoxin family, Plant M-type subfamily
null
SUBCELLULAR LOCATION: Plastid, chloroplast stroma {ECO:0000269|PubMed:19259774}.
null
null
null
null
null
FUNCTION: Thiol-disulfide oxidoreductase involved in the redox regulation of enzymes of both reductive pentose phosphate pathway (Calvin-Benson cycle) and oxidative pentose phosphate pathway. Under reducing conditions, activates the glyceraldehyde-3-phosphate dehydrogenase and the phosphoribulokinase, and inhibits. the...
Arabidopsis thaliana (Mouse-ear cress)
O48741
PORC_ARATH
MALQAAYSLLPSTISIQKEGKFNASLKETTFTGSSFSNHLRAEKISTLLTIKEQRRQKPRFSTGIRAQTVTATPPANEASPEQKKTERKGTAVITGASSGLGLATAKALADTGKWHVIMACRNFLKAEKAARSVGMSKEDYTVMHLDLASLESVKQFVENFRRTEQPLDVLVCNAAVYQPTAKEPSFTAEGFEISVGTNHLGHFLLSRLLLDDLKKSDYPSKRMIIVGSITGNTNTLAGNVPPKANLGDLRGLASGLNGQNSSMIDGGEFDGAKAYKDSKVCNMLTMQELHRRYHEETGVTFASLYPGCIATTGLFREHI...
1.3.1.33
null
chlorophyll biosynthetic process [GO:0015995]; photosynthesis [GO:0015979]
chloroplast [GO:0009507]; chloroplast envelope [GO:0009941]; chloroplast membrane [GO:0031969]; chloroplast thylakoid [GO:0009534]; chloroplast thylakoid membrane [GO:0009535]; extracellular region [GO:0005576]
NADPH dehydrogenase activity [GO:0003959]; protochlorophyllide reductase activity [GO:0016630]
PF00106;
3.40.50.720;
Short-chain dehydrogenases/reductases (SDR) family, POR subfamily
null
SUBCELLULAR LOCATION: Plastid, chloroplast membrane {ECO:0000269|PubMed:22212719}. Note=Prolamellar body of etiolated seedling.
CATALYTIC ACTIVITY: Reaction=chlorophyllide a + NADP(+) = H(+) + NADPH + protochlorophyllide a; Xref=Rhea:RHEA:11132, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:83348, ChEBI:CHEBI:83350; EC=1.3.1.33;
null
PATHWAY: Porphyrin-containing compound metabolism; chlorophyll biosynthesis.
null
null
FUNCTION: Phototransformation of protochlorophyllide (Pchlide) to chlorophyllide (Chlide). {ECO:0000269|PubMed:11785941, ECO:0000269|PubMed:12848821}.
Arabidopsis thaliana (Mouse-ear cress)
O48773
PDI23_ARATH
MYKSPLTLLTLLTICFGFFDLSSALYGSSSPVVQLTASNFKSKVLNSNGVVLVEFFAPWCGHCKALTPTWEKVANILKGVATVAAIDADAHQSAAQDYGIKGFPTIKVFVPGKAPIDYQGARDAKSIANFAYKQIKGLLSDRLEGKSKPTGGGSKEKKSEPSASVELNASNFDDLVIESNELWIVEFFAPWCGHCKKLAPEWKRAAKNLQGKVKLGHVNCDVEQSIMSRFKVQGFPTILVFGPDKSSPYPYEGARSASAIESFASELVESSAGPVEVTELTGPDVMEKKCGSAAICFISFLPDILDSKAEGRNKYLEMLL...
5.3.4.1
null
response to endoplasmic reticulum stress [GO:0034976]
endoplasmic reticulum [GO:0005783]; endoplasmic reticulum lumen [GO:0005788]; Golgi apparatus [GO:0005794]; plant-type vacuole [GO:0000325]
protein disulfide isomerase activity [GO:0003756]; protein-disulfide reductase activity [GO:0015035]
PF00085;
3.40.30.10;
Protein disulfide isomerase family
null
SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000305}.
CATALYTIC ACTIVITY: Reaction=Catalyzes the rearrangement of -S-S- bonds in proteins.; EC=5.3.4.1;
null
null
null
null
FUNCTION: Acts as a protein-folding catalyst that interacts with nascent polypeptides to catalyze the formation, isomerization, and reduction or oxidation of disulfide bonds. {ECO:0000250}.
Arabidopsis thaliana (Mouse-ear cress)
O48782
HMOX1_ARATH
MAYLAPISSSLSIFKNPQLSRFQFSSSSPNPLFLRPRIQILSMTMNKSPSLVVVAATTAAEKQKKRYPGESKGFVEEMRFVAMRLHTKDQAKEGEKETKSIEERPVAKWEPTVEGYLRFLVDSKLVYDTLELIIQDSNFPTYAEFKNTGLERAEKLSTDLEWFKEQGYEIPEPTAPGKTYSQYLKELAEKDPQAFICHFYNIYFAHSAGGRMIGRKVAERILDNKELEFYKWDGELSQLLQNVREKLNKVAEEWTREEKNHCLEETEKSFKYSGEILRLILS
1.14.14.18
null
carotenoid biosynthetic process [GO:0016117]; cellular response to UV-C [GO:0071494]; chloroplast-nucleus signaling pathway [GO:0010019]; flavonoid biosynthetic process [GO:0009813]; heme oxidation [GO:0006788]; photosynthesis [GO:0015979]; phytochromobilin biosynthetic process [GO:0010024]; regulation of meristem grow...
chloroplast [GO:0009507]
heme binding [GO:0020037]; heme oxygenase (decyclizing) activity [GO:0004392]; metal ion binding [GO:0046872]
PF01126;
1.20.910.10;
Heme oxygenase family
null
SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000269|PubMed:10072395, ECO:0000269|PubMed:19860740}.
CATALYTIC ACTIVITY: Reaction=heme b + 3 O2 + 3 reduced [NADPH--hemoprotein reductase] = biliverdin IXalpha + CO + Fe(2+) + H(+) + 3 H2O + 3 oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:21764, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:1724...
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.3 uM for hemin {ECO:0000269|PubMed:12481078, ECO:0000269|PubMed:19860740}; KM=1.9 uM for ferredoxin {ECO:0000269|PubMed:12481078, ECO:0000269|PubMed:19860740}; KM=420 uM for ascorbate {ECO:0000269|PubMed:12481078, ECO:0000269|PubMed:19860740};
null
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.2. {ECO:0000269|PubMed:12481078, ECO:0000269|PubMed:19860740};
null
FUNCTION: Key enzyme in the synthesis of the chromophore of the phytochrome family of plant photoreceptors. Catalyzes the opening of the heme ring to form the open-chain tetrapyrrole biliverdin IX with the release of iron and carbon monoxide (CO). Produces specifically the biliverdin IX-alpha isomer. Can form complex w...
Arabidopsis thaliana (Mouse-ear cress)
O48791
SCAB1_ARATH
MTRVTRDFRDSLQRDGVPAVSADVKFASSRFPNYRIGANDQIFDVKDDPKVMSMKEVVARETAQLMDQQKRLSVRDLAHKFEKGLAAAAKLSEEAKLKEATSLEKHVLLKKLRDALESLRGRVAGRNKDDVEEAIAMVEALAVQLTQREGELFIEKAEVKKLASFLKQASEDAKKLVDEERAFARAEIESARAAVQRVEEALREHEQMSRASGKQDMEDLMKEVQEARRIKMLHQPSRVMDMEYELRALRNQLAEKSKHFLQLQKKLAMCRKSEENISLVYEIDGTEALGSCLRVRPCSNDAPDLSKCTIQWYRSSSDGS...
null
null
actin filament organization [GO:0007015]; regulation of stomatal movement [GO:0010119]
cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]
actin binding [GO:0003779]
PF16711;PF16709;PF17684;PF16712;
2.30.29.140;2.60.40.2700;1.20.5.440;
SCAB family
null
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:21719691}.
null
null
null
null
null
FUNCTION: Plant-specific actin binding protein that bundles and stabilizes microfilaments (MFs). Has no nucleation or capping activity. Regulates MF reorganization during stomatal closure. The binding to F-actin is insensitive to Ca(2+) and pH. Binds weakly to inositol phosphates (PubMed:22356912). {ECO:0000269|PubMed:...
Arabidopsis thaliana (Mouse-ear cress)
O48802
PHOX2_ARATH
MGKSGGRKKKSGGSNSNSSQVNSSETSGLSKPSTIVNGGVDFDASIFLKRAHELKEEGNKKFQARDYVGALEQYENGIKLIPKSHPDRAVFHSNRAACLMQMKPIDYESVISECSMALKSQPGFTRALLRRARAFEAVGKFDLAVQDVNVLLGSDPNHKDAGEISKRLKTALGPHQDLQSRPSPAALGASAALGGPIAGLGPCLPSRNVHKKGVTSPVGSVSLPNASNGKVERPQVVNPVTENGGSVSKGQASRVVLKPVSHSPKGSKVEELGSSSVAVVGKVQEKRIRWRPLKFVYDHDIRLGQMPVNCRFKELREIVS...
null
null
null
cytoplasm [GO:0005737]; nucleus [GO:0005634]
mRNA binding [GO:0003729]
PF00564;
1.25.40.10;
null
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22025705}. Note=Localized to distinct foci in the cytoplasm, which frequently colocalize with the cell periphery and with chloroplasts. {ECO:0000269|PubMed:22025705}.
null
null
null
null
null
FUNCTION: Required for plastid separation and partitioning during cell division (PubMed:22025705). Not involved in plastid constriction or in the organization of cytoplasmic actin cables (PubMed:22025705). Contributes to polar growth of root hairs (PubMed:28096376). {ECO:0000269|PubMed:22025705, ECO:0000269|PubMed:2809...
Arabidopsis thaliana (Mouse-ear cress)
O48814
BIK1_ARATH
MGSCFSSRVKADIFHNGKSSDLYGLSLSSRKSSSTVAAAQKTEGEILSSTPVKSFTFNELKLATRNFRPDSVIGEGGFGCVFKGWLDESTLTPTKPGTGLVIAVKKLNQEGFQGHREWLTEINYLGQLSHPNLVKLIGYCLEDEHRLLVYEFMQKGSLENHLFRRGAYFKPLPWFLRVNVALDAAKGLAFLHSDPVKVIYRDIKASNILLDADYNAKLSDFGLARDGPMGDLSYVSTRVMGTYGYAAPEYMSSGHLNARSDVYSFGVLLLEILSGKRALDHNRPAKEENLVDWARPYLTSKRKVLLIVDNRLDTQYLPEE...
2.7.11.1
null
defense response to bacterium [GO:0042742]; defense response to fungus [GO:0050832]; innate immune response [GO:0045087]; pattern recognition receptor signaling pathway [GO:0002221]; protein autophosphorylation [GO:0046777]; protein phosphorylation [GO:0006468]; regulation of defense response to bacterium [GO:1900424];...
cytoplasm [GO:0005737]; endomembrane system [GO:0012505]; endosome [GO:0005768]; endosome membrane [GO:0010008]; Golgi apparatus [GO:0005794]; nucleolus [GO:0005730]; nucleus [GO:0005634]; plasma membrane [GO:0005886]
ATP binding [GO:0005524]; kinase activity [GO:0016301]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]
PF07714;
1.10.510.10;
Protein kinase superfamily, Ser/Thr protein kinase family
PTM: Phosphorylated by SIK1 to be stabilized (PubMed:30212650). Phosphorylated by FLS2 and BAK1 (PubMed:20404519, Ref.20). Autophosphorylated (PubMed:22504181, PubMed:23431184, PubMed:24104392, PubMed:26021844). Autophosphorylation is reduced in presence of the Xanthomonas campestris effector XopAC/AvrAC (PubMed:225041...
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16339855, ECO:0000269|PubMed:26021844, ECO:0000269|PubMed:29649442, ECO:0000269|Ref.20}; Lipid-anchor {ECO:0000269|PubMed:16339855, ECO:0000269|PubMed:26021844}. Endosome membrane {ECO:0000269|Ref.20}; Lipid-anchor {ECO:0000269|PubMed:16339855, ECO:0000269|PubMed:...
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:24104392}; CATALYTIC...
null
null
null
null
FUNCTION: Plays a central role in immune responses (PubMed:20413097, PubMed:29649442). Required to activate the resistance responses to necrotrophic pathogens, including the regulation of defense hormone expression (e.g. jasmonic acid (JA) and salicylic acid (SA)) (PubMed:16339855, PubMed:29649442). Phosphorylates FLS2...
Arabidopsis thaliana (Mouse-ear cress)
O48847
LUH_ARATH
MAQSNWEADKMLDVYIYDYLVKKKLHNTAKSFMTEGKVSPDPVAIDAPGGFLFEWWSVFWDIFIARTNEKHSEAAAAYIEAQQGKAKEQQMQIQQLQMMRQAQMQRRDPNHPSLGGPMNAIGSEGMIGQSNASALAAKMYEERMKQPNPMNSETSQPHLDARMALLKSATNHHGQIVQGNHQGGVSAALQQIQSRTQQPTEIKTEVNLGTSPRQLPVDPSTVYGQGILQSKPGMGSAGLNPGVSGLPLKGWPLTGIEQMRPGLGGPQVQKSFLQNQSQFQLSPQQQQHQMLAQVQAQGNMTNSPMYGGDMDPRRFTGLPR...
null
null
cell differentiation [GO:0030154]; cellular response to external biotic stimulus [GO:0071217]; DNA damage response [GO:0006974]; embryo development ending in seed dormancy [GO:0009793]; flower development [GO:0009908]; galacturonan metabolic process [GO:0010393]; meristem maintenance [GO:0010073]; mucilage biosynthetic...
nucleus [GO:0005634]
transcription coactivator activity [GO:0003713]; transcription corepressor activity [GO:0003714]
PF08513;PF00400;
2.130.10.10;
null
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21518777}.
null
null
null
null
null
FUNCTION: Transcription repressor subunit of the SEU-SLK1 and SEU-SLK2 transcriptional corepressor of abiotic stress (e.g. salt and osmotic stress) response genes, by means of an epigenetic process involving histone modification (e.g. H3K9 and H3K14 acetylation), probably by recruiting HDAC, to facilitate the condensat...
Arabidopsis thaliana (Mouse-ear cress)
O48849
RLP23_ARATH
MSKALLHLHFLSLFLLCCVCHSSIFTLNFHFTGIVACRPHQIQAFTKFTNEFDTRGCNNSDTFNGVWCDNSTGAVAVLQLRKCLSGTLKSNSSLFGFHQLRYVDLQNNNLTSSSLPSGFGNLKRLEGLFLSSNGFLGQVPSSFSNLTMLAQLDLSYNKLTGSFPLVRGLRKLIVLDLSYNHFSGTLNPNSSLFELHQLRYLNLAFNNFSSSLPSKFGNLHRLENLILSSNGFSGQVPSTISNLTRLTKLYLDQNKLTSSFPLVQNLTNLYELDLSYNKFFGVIPSSLLTLPFLAHLALRENNLAGSVEVSNSSTSSRLEI...
null
null
defense response to bacterium [GO:0042742]; defense response to fungus [GO:0050832]; defense response to oomycetes [GO:0002229]; detection of molecule of fungal origin [GO:0032491]; innate immune response-activating signaling pathway [GO:0002758]; pathogen-associated molecular pattern receptor signaling pathway [GO:014...
endoplasmic reticulum [GO:0005783]; plasma membrane [GO:0005886]
protein kinase binding [GO:0019901]
PF00560;PF13516;PF13855;
3.80.10.10;
RLP family
null
SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
null
null
null
null
null
FUNCTION: Involved in the perception of necrosis and ethylene-inducing peptide 1-like proteins (NLPs), that act as extracellular signals mediating immune activation. Component of the RLP23-SOBIR1-BAK1 complex that mediates NLP-triggered immunity. {ECO:0000269|PubMed:27251392}.
Arabidopsis thaliana (Mouse-ear cress)
O48881
TPS1_BRANA
MQSLGGIRSWPATWRTTTASMTTTTTESVRKVAQVLTVAGSDSGAGAGIQADIKVCAARGVYCASVKTAVKAKNTRAVQSVHLLPPDSVSEQLKSVLSDFEVDVVKTGMLPSPEIVEVLLQNLSEYPVRALVVDPVMVSTSGHVLAGSSILSIFRERLLPLADIITPNVKEASALLGGVRIQTVAEMRSAAKSLHQMGPRFVLVKGGDLPDSSDSVDVYFDGNEFHELHSPRIATRNTHGTGCTLASCIAAELAKGSNMLSAVKVAKRFVDSALNYSKDIVIGSGMQGPFDHFLSLKDPQSYRQSTFKPDDLFLYAVTDS...
2.5.1.3; 2.7.1.49
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250};
phosphorylation [GO:0016310]; thiamine biosynthetic process [GO:0009228]; thiamine diphosphate biosynthetic process [GO:0009229]
chloroplast [GO:0009507]; cytosol [GO:0005829]
ATP binding [GO:0005524]; hydroxymethylpyrimidine kinase activity [GO:0008902]; metal ion binding [GO:0046872]; phosphomethylpyrimidine kinase activity [GO:0008972]; thiamine-phosphate diphosphorylase activity [GO:0004789]
PF08543;PF02581;
3.40.1190.20;3.20.20.70;
Thiamine-phosphate synthase family
null
SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000250}.
CATALYTIC ACTIVITY: Reaction=2-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-ylidene]ethyl phosphate + 4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine + 2 H(+) = CO2 + diphosphate + thiamine phosphate; Xref=Rhea:RHEA:47844, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:33019, ChEBI:CHEBI:37575, ChEBI:CHEBI:57841, ChEB...
null
PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; thiamine phosphate from 4-amino-2-methyl-5-diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)-thiazole: step 1/1.; PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; 4-amino-2-methyl-5-diphosphomethylpyrimidine from 5-amino-1-(5-p...
null
null
FUNCTION: Essential for thiamine biosynthesis. Bifunctional enzyme that catalyzes the phosphorylation of hydroxymethylpyrimidine phosphate (HMP-P) to HMP-PP and condenses 4-methyl-5-(beta-hydroxyethyl)thiazole monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl pyrimidine pyrophosphate (HMP-PP) to form thiamine ...
Brassica napus (Rape)
O48915
NDR1_ARATH
MNNQNEDTEGGRNCCTCCLSFIFTAGLTSLFLWLSLRADKPKCSIQNFFIPALGKDPNSRDNTTLNFMVRCDNPNKDKGIYYDDVHLNFSTINTTKINSSALVLVGNYTVPKFYQGHKKKAKKWGQVKPLNNQTVLRAVLPNGSAVFRLDLKTQVRFKIVFWKTKRYGVEVGADVEVNGDGVKAQKKGIKMKKSDSSFPLRSSFPISVLMNLLVFFAIR
null
null
defense response to bacterium [GO:0042742]; defense response to fungus [GO:0050832]; defense response to other organism [GO:0098542]; plant-type hypersensitive response [GO:0009626]
membrane [GO:0016020]; plasma membrane [GO:0005886]; plasmodesma [GO:0009506]; side of membrane [GO:0098552]
null
null
null
null
PTM: N-glycosylated. {ECO:0000269|PubMed:15447649}.
SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:15447649}; Lipid-anchor, GPI-anchor {ECO:0000305|PubMed:15447649}.
null
null
null
null
null
FUNCTION: Involved in disease resistance. Required for resistance conferred by multiple R genes recognizing different bacterial and oomycete pathogen isolates like avirulent P.syringae or H.parasitica (downy mildew). Required for the establishment of hypersensitive response (HR) and systemic acquired resistance (SAR) a...
Arabidopsis thaliana (Mouse-ear cress)
O48917
SQD1_ARATH
MAHLLSASCPSVISLSSSSSKNSVKPFVSGQTFFNAQLLSRSSLKGLLFQEKKPRKSCVFRATAVPITQQAPPETSTNNSSSKPKRVMVIGGDGYCGWATALHLSKKNYEVCIVDNLVRRLFDHQLGLESLTPIASIHDRISRWKALTGKSIELYVGDICDFEFLAESFKSFEPDSVVHFGEQRSAPYSMIDRSRAVYTQHNNVIGTLNVLFAIKEFGEECHLVKLGTMGEYGTPNIDIEEGYITITHNGRTDTLPYPKQASSFYHLSKVHDSHNIAFTCKAWGIRATDLNQGVVYGVKTDETEMHEELRNRLDYDAVFG...
3.13.1.1
COFACTOR: Name=NAD(+); Xref=ChEBI:CHEBI:57540;
cellular response to phosphate starvation [GO:0016036]; glycolipid biosynthetic process [GO:0009247]; sulfolipid biosynthetic process [GO:0046506]
chloroplast [GO:0009507]; plasma membrane [GO:0005886]
sulfotransferase activity [GO:0008146]; UDPsulfoquinovose synthase activity [GO:0046507]; zinc ion binding [GO:0008270]
PF01370;
3.40.50.720;3.90.25.10;
NAD(P)-dependent epimerase/dehydratase family
null
SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000269|PubMed:9465123}.
CATALYTIC ACTIVITY: Reaction=H(+) + sulfite + UDP-alpha-D-glucose = H2O + UDP-alpha-D-6-sulfoquinovose; Xref=Rhea:RHEA:13197, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17359, ChEBI:CHEBI:58885, ChEBI:CHEBI:60009; EC=3.13.1.1;
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=150 uM for UDP-glucose; KM=10 uM for sulfite;
null
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5-9.5.;
null
FUNCTION: Involved in the biosynthesis of sulfolipids found in thylakoid membranes. Converts UDP-glucose and sulfite to the sulfolipid head group precursor UDP-sulfoquinovose. {ECO:0000269|PubMed:11073956}.
Arabidopsis thaliana (Mouse-ear cress)
O48946
CESA1_ARATH
MEASAGLVAGSYRRNELVRIRHESDGGTKPLKNMNGQICQICGDDVGLAETGDVFVACNECAFPVCRPCYEYERKDGTQCCPQCKTRFRRHRGSPRVEGDEDEDDVDDIENEFNYAQGANKARHQRHGEEFSSSSRHESQPIPLLTHGHTVSGEIRTPDTQSVRTTSGPLGPSDRNAISSPYIDPRQPVPVRIVDPSKDLNSYGLGNVDWKERVEGWKLKQEKNMLQMTGKYHEGKGGEIEGTGSNGEELQMADDTRLPMSRVVPIPSSRLTPYRVVIILRLIILCFFLQYRTTHPVKNAYPLWLTSVICEIWFAFSWLL...
2.4.1.12
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:Q9SWW6}; Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:Q9SWW6}; COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:Q941L0};
cell wall organization [GO:0071555]; cellulose biosynthetic process [GO:0030244]; hyperosmotic salinity response [GO:0042538]; plant-type primary cell wall biogenesis [GO:0009833]
endosome [GO:0005768]; Golgi apparatus [GO:0005794]; plasma membrane [GO:0005886]; trans-Golgi network [GO:0005802]
cellulose synthase (UDP-forming) activity [GO:0016760]; metal ion binding [GO:0046872]
PF03552;PF14569;
3.30.40.10;
Glycosyltransferase 2 family, Plant cellulose synthase subfamily
PTM: S-acylated. {ECO:0000269|PubMed:27387950}.
SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
CATALYTIC ACTIVITY: Reaction=[(1->4)-beta-D-glucosyl](n) + UDP-alpha-D-glucose = [(1->4)-beta-D-glucosyl](n+1) + H(+) + UDP; Xref=Rhea:RHEA:19929, Rhea:RHEA-COMP:10033, Rhea:RHEA-COMP:10034, ChEBI:CHEBI:15378, ChEBI:CHEBI:18246, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885; EC=2.4.1.12; Evidence={ECO:0000305|PubMed:11901167, E...
null
PATHWAY: Glycan metabolism; plant cellulose biosynthesis.
null
null
FUNCTION: Catalytic subunit of cellulose synthase terminal complexes ('rosettes'), required for beta-1,4-glucan microfibril crystallization, a major mechanism of the cell wall formation. Involved in the primary cell wall formation. Required during embryogenesis for cell elongation, orientation of cell expansion and com...
Arabidopsis thaliana (Mouse-ear cress)
O48947
CESA2_ARATH
MNTGGRLIAGSHNRNEFVLINADESARIRSVQELSGQTCQICGDEIELTVSSELFVACNECAFPVCRPCYEYERREGNQACPQCKTRYKRIKGSPRVDGDDEEEEDIDDLEYEFDHGMDPEHAAEAALSSRLNTGRGGLDSAPPGSQIPLLTYCDEDADMYSDRHALIVPPSTGYGNRVYPAPFTDSSAPPQARSMVPQKDIAEYGYGSVAWKDRMEVWKRRQGEKLQVIKHEGGNNGRGSNDDDELDDPDMPMMDEGRQPLSRKLPIRSSRINPYRMLILCRLAILGLFFHYRILHPVNDAYGLWLTSVICEIWFAVSW...
2.4.1.12
COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:Q941L0}; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:Q9SWW6}; Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:Q9SWW6};
cell wall organization [GO:0071555]; cellulose biosynthetic process [GO:0030244]; plant-type primary cell wall biogenesis [GO:0009833]
plasma membrane [GO:0005886]; trans-Golgi network [GO:0005802]
cellulose synthase (UDP-forming) activity [GO:0016760]; metal ion binding [GO:0046872]
PF03552;PF14569;
3.30.40.10;
Glycosyltransferase 2 family, Plant cellulose synthase subfamily
null
SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
CATALYTIC ACTIVITY: Reaction=[(1->4)-beta-D-glucosyl](n) + UDP-alpha-D-glucose = [(1->4)-beta-D-glucosyl](n+1) + H(+) + UDP; Xref=Rhea:RHEA:19929, Rhea:RHEA-COMP:10033, Rhea:RHEA-COMP:10034, ChEBI:CHEBI:15378, ChEBI:CHEBI:18246, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885; EC=2.4.1.12; Evidence={ECO:0000305};
null
PATHWAY: Glycan metabolism; plant cellulose biosynthesis.
null
null
FUNCTION: Catalytic subunit of cellulose synthase terminal complexes ('rosettes'), required for beta-1,4-glucan microfibril crystallization, a major mechanism of the cell wall formation. Involved in the primary cell wall formation. {ECO:0000269|PubMed:12068120, ECO:0000269|PubMed:17085513, ECO:0000269|PubMed:17878303}.
Arabidopsis thaliana (Mouse-ear cress)
O48963
PHOT1_ARATH
MEPTEKPSTKPSSRTLPRDTRGSLEVFNPSTQLTRPDNPVFRPEPPAWQNLSDPRGTSPQPRPQQEPAPSNPVRSDQEIAVTTSWMALKDPSPETISKKTITAEKPQKSAVAAEQRAAEWGLVLKTDTKTGKPQGVGVRNSGGTENDPNGKKTTSQRNSQNSCRSSGEMSDGDVPGGRSGIPRVSEDLKDALSTFQQTFVVSDATKPDYPIMYASAGFFNMTGYTSKEVVGRNCRFLQGSGTDADELAKIRETLAAGNNYCGRILNYKKDGTSFWNLLTIAPIKDESGKVLKFIGMQVEVSKHTEGAKEKALRPNGLPES...
2.7.11.1
COFACTOR: Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000269|PubMed:18585389, ECO:0000269|PubMed:24316821}; Note=Binds 2 FMN per subunit. {ECO:0000269|PubMed:18585389, ECO:0000269|PubMed:24316821};
cellular response to blue light [GO:0071483]; chloroplast accumulation movement [GO:0009904]; chloroplast avoidance movement [GO:0009903]; circadian rhythm [GO:0007623]; negative regulation of anion channel activity by blue light [GO:0010362]; phototropism [GO:0009638]; protein autophosphorylation [GO:0046777]; regulat...
cell surface [GO:0009986]; cytoplasm [GO:0005737]; cytoplasmic side of plasma membrane [GO:0009898]; nucleus [GO:0005634]; plant-type vacuole [GO:0000325]
ATP binding [GO:0005524]; blue light photoreceptor activity [GO:0009882]; FMN binding [GO:0010181]; identical protein binding [GO:0042802]; kinase activity [GO:0016301]; mRNA binding [GO:0003729]; protein kinase activity [GO:0004672]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity...
PF13426;PF00069;
3.30.450.20;1.10.510.10;
Protein kinase superfamily, AGC Ser/Thr protein kinase family
PTM: Autophosphorylated at Ser-185, Ser-350 and Ser-410 in response to blue light irradiation. {ECO:0000269|PubMed:11537679, ECO:0000269|PubMed:16777956, ECO:0000269|PubMed:20031924, ECO:0000269|PubMed:28358053, ECO:0000269|PubMed:9831559, ECO:0000305}.; PTM: 2 molecules of FMN bind covalently to cysteines after exposu...
SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein. Cytoplasm.
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:16777956, ECO:000026...
null
null
null
null
FUNCTION: Protein kinase that acts as a blue light (BL) photoreceptor in a signal-transduction pathway for photo-induced movements (PubMed:14739272, PubMed:15821287, PubMed:29101334, PubMed:31904040). Triggers the phosphorylation of AHA1 and AHA2 C-terminal penultimate Thr in guard cells to activate them and induce sto...
Arabidopsis thaliana (Mouse-ear cress)
O49006
PME3_ARATH
MAPSMKEIFSKDNFKKNKKLVLLSAAVALLFVAAVAGISAGASKANEKRTLSPSSHAVLRSSCSSTRYPELCISAVVTAGGVELTSQKDVIEASVNLTITAVEHNYFTVKKLIKKRKGLTPREKTALHDCLETIDETLDELHETVEDLHLYPTKKTLREHAGDLKTLISSAITNQETCLDGFSHDDADKQVRKALLKGQIHVEHMCSNALAMIKNMTDTDIANFEQKAKITSNNRKLKEENQETTVAVDIAGAGELDSEGWPTWLSAGDRRLLQGSGVKADATVAADGSGTFKTVAAAVAAAPENSNKRYVIHIKAGVYR...
3.1.1.11
null
cell wall modification [GO:0042545]; defense response to bacterium [GO:0042742]; defense response to fungus [GO:0050832]; defense response to Gram-negative bacterium [GO:0050829]; negative regulation of seed germination [GO:0010187]; pectin catabolic process [GO:0045490]; regulation of gene expression [GO:0010468]; reg...
apoplast [GO:0048046]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; plant-type cell wall [GO:0009505]
aspartyl esterase activity [GO:0045330]; mRNA binding [GO:0003729]; pectinesterase activity [GO:0030599]; pectinesterase inhibitor activity [GO:0046910]
PF01095;PF04043;
1.20.140.40;2.160.20.10;
PMEI family; Pectinesterase family
null
SUBCELLULAR LOCATION: Secreted, extracellular space, apoplast {ECO:0000269|PubMed:15593128}. Secreted, cell wall {ECO:0000269|PubMed:26183897}. Note=Present in hypocotyl cell walls. {ECO:0000269|PubMed:26183897}.
CATALYTIC ACTIVITY: Reaction=[(1->4)-alpha-D-galacturonosyl methyl ester](n) + n H2O = [(1->4)-alpha-D-galacturonosyl](n) + n H(+) + n methanol; Xref=Rhea:RHEA:22380, Rhea:RHEA-COMP:14570, Rhea:RHEA-COMP:14573, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17790, ChEBI:CHEBI:140522, ChEBI:CHEBI:140523; EC=3.1.1.11;...
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=12 uM for HG96B82 {ECO:0000269|PubMed:26183897}; KM=5 uM for HG96B69 {ECO:0000269|PubMed:26183897}; KM=9 uM for HG96B20 {ECO:0000269|PubMed:26183897}; KM=6 uM for HG97B77P63 {ECO:0000269|PubMed:26183897}; KM=224 uM for HG96P64 {ECO:0000269|PubMed:26183897}; Vmax=0....
PATHWAY: Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-gluconate from pectin: step 1/5. {ECO:0000305}.
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5 on homogalacturonan (HG) substrates with a degree of methylesterification between 60 and 80% and a random distribution of methyl esters. {ECO:0000269|PubMed:26183897};
null
FUNCTION: Acts in the modification of cell walls via demethylesterification of cell wall pectin (PubMed:21171891, PubMed:26183897). Required for zinc Zn(2+) homeostasis and to monitor Zn(2+) influence on cell wall-controlled growth processes such as root cell elongation (PubMed:23826687). Monitors seed germination and ...
Arabidopsis thaliana (Mouse-ear cress)
O49048
VPS45_ARATH
MVLVTSVRDYINRMLQDISGMKVLILDSETVSNVSIVYSQSELLQKEVFLVEMIDSISVSKESMSHLKAVYFIRPTSDNIQKLRYQLANPRFGEYHLFFSNLLKDTQIHILADSDEQEVVQQVQEYYADFVSGDPYHFTLNMASNHLYMIPAVVDPSGLQRFSDRVVDGIAAVFLALKRRPVIRYQRTSDTAKRIAHETAKLMYQHESALFDFRRTESSPLLLVIDRRDDPVTPLLNQWTYQAMVHELIGLQDNKVDLKSIGSLPKDQQVEVVLSSEQDAFFKSNMYENFGDIGMNIKRMVDDFQQVAKSNQNIQTVEDM...
null
null
auxin-activated signaling pathway [GO:0009734]; intracellular protein transport [GO:0006886]; pollen germination [GO:0009846]; positive regulation of cell growth [GO:0030307]; regulation of auxin polar transport [GO:2000012]; regulation of root morphogenesis [GO:2000067]; regulation of vesicle fusion [GO:0031338]; vesi...
early endosome [GO:0005769]; Golgi membrane [GO:0000139]; mitochondrion [GO:0005739]; plant-type vacuole membrane [GO:0009705]; SNARE complex [GO:0031201]; trans-Golgi network [GO:0005802]
null
PF00995;
1.25.40.60;3.40.50.1910;3.40.50.2060;
STXBP/unc-18/SEC1 family
null
SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane {ECO:0000269|PubMed:10888666}; Peripheral membrane protein {ECO:0000269|PubMed:10888666}. Early endosome {ECO:0000269|PubMed:23737757}. Note=Binds to trans-Golgi network membranes through interaction with other proteins. {ECO:0000269|PubMed:10888666}.
null
null
null
null
null
FUNCTION: Involved in the protein transport to the vacuole, probably at the level of vesicle fusion at the trans-Golgi network (TGN) and not in transport from the TGN to the prevacuolar compartment, by promoting the recycling of vacuolar sorting receptors back to the TGN (PubMed:19251905). Involved in early endosomal v...
Arabidopsis thaliana (Mouse-ear cress)
O49139
CMT1_ARATH
MAARNKQKKRAEPESDLCFAGKPMSVVESTIRWPHRYQSKKTKLQAPTKKPANKGGKKEDEEIIKQAKCHFDKALVDGVLINLNDDVYVTGLPGKLKFIAKVIELFEADDGVPYCRFRWYYRPEDTLIERFSHLVQPKRVFLSNDENDNPLTCIWSKVNIAKVPLPKITSRIEQRVIPPCDYYYDMKYEVPYLNFTSADDGSDASSSLSSDSALNCFENLHKDEKFLLDLYSGCGAMSTGFCMGASISGVKLITKWSVDINKFACDSLKLNHPETEVRNEAAEDFLALLKEWKRLCEKFSLVSSTEPVESISELEDEEVE...
2.1.1.37
null
chromatin organization [GO:0006325]; DNA-mediated transformation [GO:0009294]; methylation [GO:0032259]
nucleus [GO:0005634]
chromatin binding [GO:0003682]; DNA (cytosine-5-)-methyltransferase activity [GO:0003886]; DNA binding [GO:0003677]
PF01426;PF00385;PF00145;
2.30.30.490;3.90.120.10;3.40.50.150;
Class I-like SAM-binding methyltransferase superfamily, C5-methyltransferase family
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CATALYTIC ACTIVITY: Reaction=a 2'-deoxycytidine in DNA + S-adenosyl-L-methionine = a 5-methyl-2'-deoxycytidine in DNA + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:13681, Rhea:RHEA-COMP:11369, Rhea:RHEA-COMP:11370, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:85452, ChEBI:CHEBI:85454; EC=2....
null
null
null
null
FUNCTION: May be involved in the CpXpG methylation and in gene silencing. {ECO:0000250}.
Arabidopsis thaliana (Mouse-ear cress)
O49163
HM1_MAIZE
MAEKESNGVRVCVTGGAGFIGSWLVRKLLEKGYTVHATLRNTGDEAKAGLLRRLVPGAAERLRLFQADLFDAATFAPAIAGCQFVFLVATPFGLDSAGSQYKSTAEAVVDAVHAILRQCEESRTVKRVIHTASVAAASPLLEEEVPASGVGYRDFIDESCWTSLNVDYPLRSAHFDKYILSKLQSEQELLSYNNGESPAFEVVTLPLGLVAGDTVLGRAPETVESAVAPVSRSEPYFGLLRILQQLLGSLPLVHVDDVCDALVFCMERRPSVAGRFLCAAAYPTIHDVVAHYASKFPHLDILKETTEAVATVRPARDRLG...
1.3.1.-
null
defense response to fungus [GO:0050832]; toxin catabolic process [GO:0009407]
null
aldo-keto reductase (NADP) activity [GO:0004033]; oxidoreductase activity [GO:0016491]
PF01370;
3.40.50.720;
NAD(P)-dependent epimerase/dehydratase family
null
null
null
null
null
null
null
FUNCTION: In tandem with Hm2, NADPH-dependent Helminthosporium carbonum (HC) toxin reductase (HCTR), which inactivates HC toxin, a cyclic tetrapeptide produced by the fungus Cochliobolus carbonum to permit infection and acting as an inhibitor of host histone deacetylases (HDACs), thus conferring resistance against C.ca...
Zea mays (Maize)
O49196
APK2_ARATH
MEGLAIRASRPSVFCSIPGLGGDSHRKPPSDGFLKLPASSIPADSRKLVANSTSFHPISAVNVSAQASLTADFPALSETILKEGRNNGKEKAENIVWHESSICRCDRQQLLQQKGCVVWITGLSGSGKSTVACALSKALFERGKLTYTLDGDNVRHGLNRDLTFKAEHRTENIRRIGEVAKLFADVGVICIASLISPYRRDRDACRSLLPDGDFVEVFMDVPLHVCESRDPKGLYKLARAGKIKGFTGIDDPYEAPVNCEVVLKHTGDDESCSPRQMAENIISYLQNKGYLEG
2.7.1.25
null
cysteine biosynthetic process [GO:0019344]; hydrogen sulfide biosynthetic process [GO:0070814]; phosphorylation [GO:0016310]; sulfate assimilation [GO:0000103]
chloroplast [GO:0009507]; plastid [GO:0009536]
adenylylsulfate kinase activity [GO:0004020]; ATP binding [GO:0005524]
PF01583;
3.40.50.300;
APS kinase family
null
SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000269|PubMed:19304933}.
CATALYTIC ACTIVITY: Reaction=adenosine 5'-phosphosulfate + ATP = 3'-phosphoadenylyl sulfate + ADP + H(+); Xref=Rhea:RHEA:24152, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:58243, ChEBI:CHEBI:58339, ChEBI:CHEBI:456216; EC=2.7.1.25;
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1 uM for adenylyl sulfate {ECO:0000269|PubMed:19304933}; Vmax=10.6 mmol/min/mg enzyme {ECO:0000269|PubMed:19304933};
PATHWAY: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from sulfate: step 2/3.
null
null
FUNCTION: Catalyzes the synthesis of activated sulfate. Essential for plant reproduction and viability. Required for the production of glucosinolates. {ECO:0000269|PubMed:11488606, ECO:0000269|PubMed:19304933, ECO:0000269|PubMed:19903478, ECO:0000269|PubMed:23218016}.
Arabidopsis thaliana (Mouse-ear cress)
O49203
NDK3_ARATH
MSSQICRSASKAAKSLLSSAKNARFFSEGRAIGAAAAVSASGKIPLYASNFARSSGSGVASKSWITGLLALPAAAYMIQDQEVLAAEMERTFIAIKPDGVQRGLISEIISRFERKGFKLVGIKVIVPSKDFAQKHYHDLKERPFFNGLCDFLSSGPVIAMVWEGDGVIRYGRKLIGATDPQKSEPGTIRGDLAVTVGRNIIHGSDGPETAKDEISLWFKPQELVSYTSNSEKWLYGDN
2.7.4.6
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CTP biosynthetic process [GO:0006241]; GTP biosynthetic process [GO:0006183]; phosphorylation [GO:0016310]; UTP biosynthetic process [GO:0006228]
chloroplast thylakoid lumen [GO:0009543]; cytosol [GO:0005829]; mitochondrial inner membrane [GO:0005743]; mitochondrial intermembrane space [GO:0005758]; mitochondrion [GO:0005739]
ATP binding [GO:0005524]; cobalt ion binding [GO:0050897]; nucleoside diphosphate kinase activity [GO:0004550]; zinc ion binding [GO:0008270]
PF00334;
3.30.70.141;
NDK family
null
SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid lumen. Mitochondrion intermembrane space.
CATALYTIC ACTIVITY: Reaction=a 2'-deoxyribonucleoside 5'-diphosphate + ATP = a 2'-deoxyribonucleoside 5'-triphosphate + ADP; Xref=Rhea:RHEA:44640, ChEBI:CHEBI:30616, ChEBI:CHEBI:61560, ChEBI:CHEBI:73316, ChEBI:CHEBI:456216; EC=2.7.4.6; CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-diphosphate + ATP = a ribonucleosid...
null
null
null
null
FUNCTION: Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate. Shows the highest specificity towards GDP (By similarity). {ECO:0000250}.
Arabidopsis thaliana (Mouse-ear cress)
O49230
ETR1_BRAOL
MEVCNCIEPQWPADELLMKYQYISDFFIAVAYFSIPLELIYFVKKSAVFPYRWVLVQFGAFIVLCGATHLINLWTFTTHSRTVALVMTTAKVLTAVVSCATALMLVHIIPDLLSVKTRELFLKNKAAELDREMGLIRTQEETGRHVRMLTHEIRSTLDRHTILKTTLVELGRTLALEECALWMPTRTGLELQLSYTLRQQHPVEYTVPIQLPVINQVFGTSRAVKISPNSPVARLRPVSGKYLLGEVVAVRVPLLHLSNFQINDWPELSTKRYALMVLMLPSDSARQWHVHELELVEVVADQVAVALSHAAILEESMRAR...
2.7.13.3
COFACTOR: Name=Cu cation; Xref=ChEBI:CHEBI:23378; Evidence={ECO:0000250}; Note=Binds 1 copper ion per dimer. {ECO:0000250};
cell division [GO:0051301]; cytokinin metabolic process [GO:0009690]; defense response by callose deposition in cell wall [GO:0052544]; defense response to bacterium [GO:0042742]; detection of ethylene stimulus [GO:0009727]; hydrogen peroxide biosynthetic process [GO:0050665]; negative regulation of ethylene-activated ...
endoplasmic reticulum membrane [GO:0005789]
ATP binding [GO:0005524]; ethylene binding [GO:0051740]; ethylene receptor activity [GO:0038199]; identical protein binding [GO:0042802]; metal ion binding [GO:0046872]; phosphorelay sensor kinase activity [GO:0000155]
PF01590;PF02518;PF00512;PF00072;
1.10.287.130;3.30.450.40;3.40.50.2300;3.30.565.10;
Ethylene receptor family
PTM: Activation probably requires a transfer of a phosphate group between a His in the transmitter domain and an Asp of the receiver domain. {ECO:0000250}.
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
CATALYTIC ACTIVITY: Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.; EC=2.7.13.3;
null
null
null
null
FUNCTION: May act early in the ethylene signal transduction pathway, possibly as an ethylene receptor, or as a regulator of the pathway. {ECO:0000250}.
Brassica oleracea (Wild cabbage)
O49255
NAC29_ARATH
MEVTSQSTLPPGFRFHPTDEELIVYYLRNQTMSKPCPVSIIPEVDIYKFDPWQLPEKTEFGENEWYFFSPRERKYPNGVRPNRAAVSGYWKATGTDKAIHSGSSNVGVKKALVFYKGRPPKGIKTDWIMHEYRLHDSRKASTKRNGSMRLDEWVLCRIYKKRGASKLLNEQEGFMDEVLMEDETKVVVNEAERRTEEEIMMMTSMKLPRTCSLAHLLEMDYMGPVSHIDNFSQFDHLHQPDSESSWFGDLQFNQDEILNHHRQAMFKF
null
null
embryo development ending in seed dormancy [GO:0009793]; flower development [GO:0009908]; fruit ripening [GO:0009835]; leaf senescence [GO:0010150]; multidimensional cell growth [GO:0009825]
nucleus [GO:0005634]
DNA-binding transcription factor activity [GO:0003700]; transcription cis-regulatory region binding [GO:0000976]
PF02365;
2.170.150.80;
null
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00353, ECO:0000269|PubMed:16640597}.
null
null
null
null
null
FUNCTION: Transcription activator that binds to, and transactivates the promoter of the abscisic aldehyde oxidase AAO3. Promotes chlorophyll degradation in leaves by enhancing transcription of AAO3, which leads to increased levels of the senescence-inducing hormone abscisic acid (ABA) (PubMed:25516602). Involved in the...
Arabidopsis thaliana (Mouse-ear cress)
O49326
JAL21_ARATH
MVQKVEARGGEIGDVWDDGAYDGVRKVYVGQGEDGIAFVKFEYVNGSQEVVGDERGKKTLLGAEEFEVDPDDYIVYVEGYHEKVFGVTTKEIISTLTFKTYKGKTSPPFGIVSGTKFVLQGGKIVGFHGRSTDVLHSLGAYISSPATPKLRGKWIKVEQKGEGPGPRCSHDIAQVGNKIFSFGGELTPNQPIDKHLYVFDLETRTWSISPATGDVPNLSCLGVRMVSIGSSLYVFGGRDASRKYNGFYSFDTTKNEWKLLTPVEQGPTPRSFHSMTADENNVYVFGGVSATVRLKTLDAYNIVDHKWVQCSTPGGSCSVR...
4.8.1.5
COFACTOR: Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000269|PubMed:19224919, ECO:0000269|PubMed:22954730};
embryo development ending in seed dormancy [GO:0009793]; glucosinolate catabolic process [GO:0019762]; nitrile biosynthetic process [GO:0080028]; seed dormancy process [GO:0010162]; seed germination [GO:0009845]
cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; nucleus [GO:0005634]
carbohydrate binding [GO:0030246]; enzyme regulator activity [GO:0030234]; lyase activity [GO:0016829]; metal ion binding [GO:0046872]
PF01419;PF01344;PF13415;
2.100.10.30;2.120.10.80;
Jacalin lectin family
null
null
CATALYTIC ACTIVITY: Reaction=a (Z)-N-(sulfonatooxy)alkanimidothioate = a nitrile + sulfate + sulfur; Xref=Rhea:RHEA:59956, ChEBI:CHEBI:16189, ChEBI:CHEBI:18379, ChEBI:CHEBI:26833, ChEBI:CHEBI:183089; EC=4.8.1.5; Evidence={ECO:0000269|PubMed:18987211, ECO:0000269|PubMed:19224919, ECO:0000269|PubMed:22954730}; CATALYTIC ...
null
null
null
null
FUNCTION: Specifier protein responsible for constitutive and herbivore-induced simple nitrile formation, especially in seeds (PubMed:27990154). Promotes simple nitriles, but not epithionitrile or thiocyanate formation (PubMed:18987211, PubMed:19224919). Converts allylglucosinolate (allyl-GSL), 2-propenylglucosinolate (...
Arabidopsis thaliana (Mouse-ear cress)
O49339
PTI12_ARATH
MRRWICCGDKKGDSDLSNEEVHLKSPWQNSEANQKNQKPQAVVKPEAQKEALPIEVPPLSVDEVKEKTDNFGSKSLIGEGSYGRVYYATLNDGKAVALKKLDVAPEAETNTEFLNQVSMVSRLKHENLIQLVGYCVDENLRVLAYEFATMGSLHDILHGRKGVQGAQPGPTLDWLTRVKIAVEAARGLEYLHEKVQPPVIHRDIRSSNVLLFEDYQAKVADFNLSNQAPDNAARLHSTRVLGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLTGRKPVDHTMPRGQQSLVTWATPRLSEDKVKQCVDPKLKGEYPPKS...
2.7.10.2
null
defense response [GO:0006952]; phosphorylation [GO:0016310]
peroxisome [GO:0005777]; plasmodesma [GO:0009506]
ATP binding [GO:0005524]; non-membrane spanning protein tyrosine kinase activity [GO:0004715]; protein kinase binding [GO:0019901]
PF07714;
1.10.510.10;
Protein kinase superfamily, Tyr protein kinase family
PTM: Autophosphorylated and phosphorylated by OXI1. {ECO:0000269|PubMed:17040918}.
null
CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.2; Evidence={ECO:0000255|PROSITE-ProRule:PRU100...
null
null
null
null
FUNCTION: Probable tyrosine-protein kinase involved in oxidative burst-mediated signaling leading to specific genes expression. {ECO:0000269|PubMed:17040918}.
Arabidopsis thaliana (Mouse-ear cress)
O49354
COQ3_ARATH
MLASVRVNQLQRLLLSARRLSSSPIIPPSRLLHQRLFSTSDTDASAASFSSSHPKIQTLEGKASNKSRSTSSTTSLNEDELAKFSAIADTWWHSEGPFKPLHQMNPTRLAFIRSTLCRHFSKDPSSAKPFEGLKFIDIGCGGGLLSEPLARMGATVTGVDAVDKNVKIARLHADMDPVTSTIEYLCTTAEKLADEGRKFDAVLSLEVIEHVANPAEFCKSLSALTIPNGATVLSTINRTMRAYASTIVGAEYILRWLPKGTHQWSSFVTPEEMSMILQRASVDVKEIAGFVYNPITGRWLLSDDISVNYIAYGTKRKDLG...
2.1.1.114; 2.1.1.64
null
methylation [GO:0032259]; ubiquinone biosynthetic process [GO:0006744]
extrinsic component of mitochondrial inner membrane [GO:0031314]; mitochondrial envelope [GO:0005740]
2-polyprenyl-6-methoxy-1,4-benzoquinone methyltransferase activity [GO:0008425]; 3,4-dihydroxy-5-polyprenylbenzoic acid O-methyltransferase activity [GO:0010420]; 3-demethylubiquinol-n 3-O-methyltransferase activity [GO:0061542]
PF08241;
3.40.50.150;
Class I-like SAM-binding methyltransferase superfamily, UbiG/COQ3 family
null
SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000255|HAMAP-Rule:MF_03190, ECO:0000305|PubMed:25732537}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_03190}; Matrix side {ECO:0000255|HAMAP-Rule:MF_03190}.
CATALYTIC ACTIVITY: Reaction=3,4-dihydroxy-5-all-trans-polyprenylbenzoate + S-adenosyl-L-methionine = 3-methoxy,4-hydroxy-5-all-trans-polyprenylbenzoate + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:44452, Rhea:RHEA-COMP:10930, Rhea:RHEA-COMP:10931, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CH...
null
PATHWAY: Cofactor biosynthesis; ubiquinone biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03190}.
null
null
FUNCTION: O-methyltransferase that catalyzes the 2 O-methylation steps in the ubiquinone biosynthetic pathway. {ECO:0000255|HAMAP-Rule:MF_03190}.
Arabidopsis thaliana (Mouse-ear cress)
O49394
C82C2_ARATH
MDTSLFSLFVPILVFVFIALFKKSKKPKHVKAPAPSGAWPIIGHLHLLSGKEQLLYRTLGKMADQYGPAMSLRLGSSETFVVSSFEVAKDCFTVNDKALASRPITAAAKHMGYDCAVFGFAPYSAFWREMRKIATLELLSNRRLQMLKHVRVSEISMVMQDLYSLWVKKGGSEPVMVDLKSWLEDMSLNMMVRMVAGKRYFGGGSLSPEDAEEARQCRKGVANFFHLVGIFTVSDAFPKLGWFDFQGHEKEMKQTGRELDVILERWIENHRQQRKVSGTKHNDSDFVDVMLSLAEQGKFSHLQHDAITSIKSTCLALILG...
1.14.14.-; 1.14.14.165
COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
cellular response to hypoxia [GO:0071456]; defense response [GO:0006952]
membrane [GO:0016020]
heme binding [GO:0020037]; indole-3-carbonyl nitrile 4-hydroxylase activity [GO:0106149]; iron ion binding [GO:0005506]; monooxygenase activity [GO:0004497]
PF00067;
1.10.630.10;
Cytochrome P450 family
null
SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
CATALYTIC ACTIVITY: Reaction=O2 + reduced [NADPH--hemoprotein reductase] + xanthotoxin = 5-hydroxyxanthotoxin + 2 H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:58064, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:18358, ChEBI:CHEB...
null
null
null
null
FUNCTION: Involved in the biosynthetic pathway to 4-hydroxyindole-3-carbonyl nitrile (4-OH-ICN), a cyanogenic metabolite required for inducible pathogen defense. Converts indole-3-carbonyl nitrile (ICN) into 4-OH-ICN (PubMed:26352477). Can hydroxylate xanthotoxin (8-methoxypsoralen) to form 5-hydroxyxanthotoxin (5-hydr...
Arabidopsis thaliana (Mouse-ear cress)
O49397
ARR10_ARATH
MTMEQEIEVLDQFPVGMRVLAVDDDQTCLRILQTLLQRCQYHVTTTNQAQTALELLRENKNKFDLVISDVDMPDMDGFKLLELVGLEMDLPVIMLSAHSDPKYVMKGVKHGACDYLLKPVRIEELKNIWQHVVRKSKLKKNKSNVSNGSGNCDKANRKRKEQYEEEEEEERGNDNDDPTAQKKPRVLWTHELHNKFLAAVDHLGVERAVPKKILDLMNVDKLTRENVASHLQKFRVALKKVSDDAIQQANRAAIDSHFMQMNSQKGLGGFYHHHRGIPVGSGQFHGGTTMMRHYSSNRNLGRLNSLGAGMFQPVSSSFPR...
null
null
callus formation [GO:1990110]; cellular response to cytokinin stimulus [GO:0071368]; cytokinin-activated signaling pathway [GO:0009736]; maintenance of shoot apical meristem identity [GO:0010492]; primary root development [GO:0080022]; regulation of anthocyanin metabolic process [GO:0031537]; regulation of chlorophyll ...
nucleus [GO:0005634]
DNA binding [GO:0003677]; DNA-binding transcription factor activity [GO:0003700]; phosphorelay response regulator activity [GO:0000156]
PF00249;PF00072;
3.40.50.2300;1.10.10.60;
ARR family, Type-B subfamily
PTM: Two-component system major event consists of a His-to-Asp phosphorelay between a sensor histidine kinase (HK) and a response regulator (RR). In plants, the His-to-Asp phosphorelay involves an additional intermediate named Histidine-containing phosphotransfer protein (HPt). This multistep phosphorelay consists of a...
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00625, ECO:0000269|PubMed:12215502}.
null
null
null
null
null
FUNCTION: Transcriptional activator that binds specifically to the DNA sequence 5'-[AG]GATT-3'. Functions as a response regulator involved in His-to-Asp phosphorelay signal transduction system. Phosphorylation of the Asp residue in the receiver domain activates the ability of the protein to promote the transcription of...
Arabidopsis thaliana (Mouse-ear cress)
O49403
HFA4A_ARATH
MDENNHGVSSSSLPPFLTKTYEMVDDSSSDSIVSWSQSNKSFIVWNPPEFSRDLLPRFFKHNNFSSFIRQLNTYGFRKADPEQWEFANDDFVRGQPHLMKNIHRRKPVHSHSLPNLQAQLNPLTDSERVRMNNQIERLTKEKEGLLEELHKQDEEREVFEMQVKELKERLQHMEKRQKTMVSFVSQVLEKPGLALNLSPCVPETNERKRRFPRIEFFPDEPMLEENKTCVVVREEGSTSPSSHTREHQVEQLESSIAIWENLVSDSCESMLQSRSMMTLDVDESSTFPESPPLSCIQLSVDSRLKSPPSPRIIDMNCEPD...
null
null
cellular response to heat [GO:0034605]; positive regulation of DNA-templated transcription [GO:0045893]; regulation of DNA-templated transcription [GO:0006355]; regulation of transcription by RNA polymerase II [GO:0006357]; response to reactive oxygen species [GO:0000302]
cytoplasm [GO:0005737]; nucleus [GO:0005634]
DNA-binding transcription factor activity [GO:0003700]; protein homodimerization activity [GO:0042803]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; transcription cis-regulatory region binding [GO:0000976]
PF00447;
1.10.10.10;
HSF family, Class A subfamily
PTM: Exhibits temperature-dependent phosphorylation. {ECO:0000250}.
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Nucleus {ECO:0000305}.
null
null
null
null
null
FUNCTION: Transcriptional activator that specifically binds DNA sequence 5'-AGAAnnTTCT-3' known as heat shock promoter elements (HSE).
Arabidopsis thaliana (Mouse-ear cress)
O49429
MORF1_ARATH
MAMISHRLRRALLTATSYVNRSISSSITPASDFPSVSAAVLKRSVIGRSTEVATRAPARLFSTRQYKLYKEGDEITEDTVLFEGCDYNHWLITMDFSKEETPKSPEEMVAAYEETCAQGLGISVEEAKQRMYACSTTTYQGFQAIMTEQESEKFKDLPGVVFILPDSYIDPQNKEYGGDKYENGVITHRPPPIQSGRARPRPRFDRSGGGSGGPQNFQRNTQYGQQPPMQGGGGSYGPQQGYATPGQGQGTQAPPPFQGGYNQGPRSPPPPYQAGYNQGQGSPVPPYQAGYNQVQGSPVPPYQGTQSSYGQGGSGNYSQG...
null
null
chloroplast RNA modification [GO:1900865]; cytidine to uridine editing [GO:0016554]; mitochondrial mRNA modification [GO:0080156]; mitochondrial RNA modification [GO:1900864]; mRNA processing [GO:0006397]
chloroplast [GO:0009507]; mitochondrion [GO:0005739]
protein dimerization activity [GO:0046983]
null
3.30.70.80;
MORF family
null
SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:25583991}.
null
null
null
null
null
FUNCTION: Involved in organellar RNA editing. Required for the processing of numerous RNA editing sites in mitochondria (PubMed:22411807, PubMed:23818871). Binds to the mitochondrial MEF19 and MEF21 factors, two pentatricopeptide repeat-containing proteins involved in RNA editing (PubMed:22411807). {ECO:0000269|PubMed:...
Arabidopsis thaliana (Mouse-ear cress)
O49432
QRT3_ARATH
MELRKSQVAMPVFLAIMSLMVSQVVFAEKDSGSMSPHDRALAEMQALKASLVRRNLPALVSPPPTPPQAVPGPRVYQVISYGADPTGKLDSTDAILKAMEEAFDGPNHGVLMQGINDLGGARIDLQGGSYLISRPLRFPSAGAGNLLISGGTLRASNDFPVDRYLIELKDESSKLQYIFEYITLRDLLIDCNYRGGAIAVINSLRTSIDNCYITRFGDTNGILVKSGHETYIRNSFLGQHITAGGDRGERSFSGTAINLMGNDNAVTDTVIFSARIGVMVSGQANLLSGVHCYNKATGFGGTGIYLRLPGLTQNRIVNSY...
3.2.1.15
null
cell wall organization [GO:0071555]; metabolic process [GO:0008152]; microsporogenesis [GO:0009556]; pollen exine formation [GO:0010584]
extracellular region [GO:0005576]
polygalacturonase activity [GO:0004650]
null
2.160.20.10;
Glycosyl hydrolase 28 family
null
SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000269|PubMed:14551328}.
CATALYTIC ACTIVITY: Reaction=(1,4-alpha-D-galacturonosyl)n+m + H2O = (1,4-alpha-D-galacturonosyl)n + (1,4-alpha-D-galacturonosyl)m.; EC=3.2.1.15;
null
null
null
null
FUNCTION: Polygalacturonase required for degrading the pollen mother cell wall during microspore development. {ECO:0000269|PubMed:14551328}.
Arabidopsis thaliana (Mouse-ear cress)
O49434
AAH_ARATH
MAVPHPSSSSSRSHPFLSHVYHTSFHHHHHHNHPSLVLFWCLVFSLLSPLALSSSSSSSSSSSDSSSSSSSHISLGIGETEGTKHDLHQAILRDEAVARLHELGQVSDAATHLERTFMSPASIRAIPLIRGWMEDAGLSTWVDYMGNVHGRVEPKNGSSQALLIGSHMDTVIDAGKYDGSLGIISAISALKVLKIDGRLGELKRPVEVIAFSDEEGVRFQSTFLGSAALAGIMPVSRLEVTDKSGISVQDALKENSIDITDENLMQLKYDPASVWGYVEVHIEQGPVLEWVGYPLGVVKGIAGQTRLKVTVKGSQGHAGT...
3.5.3.9
COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:18065556}; Note=Binds 2 manganese ions per subunit. {ECO:0000250|UniProtKB:Q8VXY9};
purine nucleobase catabolic process [GO:0006145]; ureide catabolic process [GO:0010136]
endoplasmic reticulum [GO:0005783]
allantoate deiminase activity [GO:0047652]; metal ion binding [GO:0046872]
PF07687;PF01546;
3.30.70.360;3.40.630.10;
Peptidase M20A family
null
SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000269|PubMed:18065556}.
CATALYTIC ACTIVITY: Reaction=allantoate + 2 H(+) + H2O = (S)-2-ureidoglycine + CO2 + NH4(+); Xref=Rhea:RHEA:27485, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:17536, ChEBI:CHEBI:28938, ChEBI:CHEBI:59947; EC=3.5.3.9; Evidence={ECO:0000269|PubMed:16496096, ECO:0000269|PubMed:18065556};
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: Note=kcat is 27.2 sec(-1) for allantoate. {ECO:0000269|PubMed:18065556};
null
null
null
FUNCTION: Involved in the catabolism of purine nucleotides. Can use allantoate as substrate, but not Nalpha-carbamoyl-L-Asp, Nalpha-carbamoyl-L-Ala or Nalpha-carbamoyl-Gly. The sequential activity of AAH, UGLYAH and UAH allows a complete purine breakdown without the intermediate generation of urea (PubMed:16496096, Pub...
Arabidopsis thaliana (Mouse-ear cress)
O49447
ADT3_ARATH
MDGSKHPSVFQKLHGQSYLINRLSPSVQARGYCVSGAYVNGGLQSLLQPTSHGVGSSLIPHGSFPVLAHAPSEKTGTGFLIDFLMGGVSAAVSKTAAAPIERVKLLIQNQDEMIKAGRLSEPYKGISDCFARTVKDEGMLALWRGNTANVIRYFPTQALNFAFKDYFKRLFNFKKEKDGYWKWFAGNLASGGAAGASSLLFVYSLDYARTRLANDAKAAKKGGQRQFNGMVDVYKKTIASDGIVGLYRGFNISCVGIVVYRGLYFGLYDSLKPVVLVDGLQDSFLASFLLGWGITIGAGLASYPIDTVRRRMMMTSGEAV...
null
null
mitochondrial ADP transmembrane transport [GO:0140021]; mitochondrial ATP transmembrane transport [GO:1990544]; negative regulation of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway [GO:1901029]; purine nucleotide transport [GO:0015865]
chloroplast envelope [GO:0009941]; membrane [GO:0016020]; mitochondrial inner membrane [GO:0005743]; mitochondrion [GO:0005739]; plasma membrane [GO:0005886]
ATP:ADP antiporter activity [GO:0005471]
PF00153;
1.50.40.10;
Mitochondrial carrier (TC 2.A.29) family
null
SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:14671022}; Multi-pass membrane protein {ECO:0000255}.
CATALYTIC ACTIVITY: Reaction=ADP(in) + ATP(out) = ADP(out) + ATP(in); Xref=Rhea:RHEA:34999, ChEBI:CHEBI:30616, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:P48962}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35000; Evidence={ECO:0000250|UniProtKB:P48962};
null
null
null
null
FUNCTION: ADP:ATP antiporter that mediates import of ADP into the mitochondrial matrix for ATP synthesis, and export of ATP out to fuel the cell (By similarity). Cycles between the cytoplasmic-open state (c-state) and the matrix-open state (m-state): operates by the alternating access mechanism with a single substrate-...
Arabidopsis thaliana (Mouse-ear cress)
O49472
INDH_ARATH
MATVALLRSLRRRELHAAHISAYKFSSASAGGRTTELRLHGVKDIIAVASGKGGVGKSSTAVNLAVALANKCELKIGLLDADVYGPSVPIMMNINQKPQVNQDMKMIPVENYGVKCMSMGLLVEKDAPLVWRGPMVMSALAKMTKGVDWGDLDILVVDMPPGTGDAQISISQNLKLSGAVIVSTPQDVALADANRGISMFDKVRVPILGLVENMSCFVCPHCNEPSFIFGKEGARRTAAKKGLKLIGEIPLEMSIREGSDEGVPVVVSSPGSIVSKAYQDLAQNVVKGLKELRENPDNEIQMKLNVPHSSHSS
null
COFACTOR: Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250|UniProtKB:Q6CE48}; Note=Binds 1 [4Fe-4S] cluster. {ECO:0000250|UniProtKB:Q6CE48};
iron-sulfur cluster assembly [GO:0016226]; mitochondrial respiratory chain complex I assembly [GO:0032981]; mitochondrial translation [GO:0032543]
chloroplast stroma [GO:0009570]; cytosol [GO:0005829]; mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739]
4 iron, 4 sulfur cluster binding [GO:0051539]; ATP binding [GO:0005524]; ATP-dependent FeS chaperone activity [GO:0140663]; metal ion binding [GO:0046872]
PF10609;
3.40.50.300;
Mrp/NBP35 ATP-binding proteins family
null
SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000269|PubMed:24179128}.
null
null
null
null
null
FUNCTION: Essential during early vegetative growth (PubMed:24179128). Required for the assembly of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) (PubMed:24179128). Involved in mitochondrial translation activity (PubMed:24179128). May deliver of one or more Fe-S clusters to complex I subuni...
Arabidopsis thaliana (Mouse-ear cress)
O49482
CADH5_ARATH
MGIMEAERKTTGWAARDPSGILSPYTYTLRETGPEDVNIRIICCGICHTDLHQTKNDLGMSNYPMVPGHEVVGEVVEVGSDVSKFTVGDIVGVGCLVGCCGGCSPCERDLEQYCPKKIWSYNDVYINGQPTQGGFAKATVVHQKFVVKIPEGMAVEQAAPLLCAGVTVYSPLSHFGLKQPGLRGGILGLGGVGHMGVKIAKAMGHHVTVISSSNKKREEALQDLGADDYVIGSDQAKMSELADSLDYVIDTVPVHHALEPYLSLLKLDGKLILMGVINNPLQFLTPLLMLGRKVITGSFIGSMKETEEMLEFCKEKGLSS...
1.1.1.195
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:16633561}; Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000269|PubMed:16633561};
lignin biosynthetic process [GO:0009809]
cytosol [GO:0005829]
cinnamyl-alcohol dehydrogenase activity [GO:0045551]; coniferyl-alcohol dehydrogenase activity [GO:0050268]; sinapyl alcohol dehydrogenase activity [GO:0052747]; zinc ion binding [GO:0008270]
PF08240;PF00107;
3.90.180.10;3.40.50.720;
Zinc-containing alcohol dehydrogenase family
null
null
CATALYTIC ACTIVITY: Reaction=(E)-cinnamyl alcohol + NADP(+) = (E)-cinnamaldehyde + H(+) + NADPH; Xref=Rhea:RHEA:10392, ChEBI:CHEBI:15378, ChEBI:CHEBI:16731, ChEBI:CHEBI:33227, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.195; Evidence={ECO:0000269|PubMed:14745009}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA...
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=13 uM for 4-coumaraldehyde (at pH 6.25-6.5 and 30 degrees Celsius) {ECO:0000269|PubMed:14745009}; KM=68 uM for caffeyl aldehyde (at pH 6.0-6.25 and 30-35 degrees Celsius) {ECO:0000269|PubMed:14745009}; KM=35 uM for coniferaldehyde (at pH 6.0-6.25 and 30-35 degrees ...
PATHWAY: Aromatic compound metabolism; phenylpropanoid biosynthesis. {ECO:0000305|PubMed:14745009}.
null
null
FUNCTION: Involved in lignin biosynthesis in the floral stem. Catalyzes the final step specific for the production of lignin monomers. Catalyzes the NADPH-dependent reduction of coniferaldehyde, 5-hydroxyconiferaldehyde, sinapaldehyde, 4-coumaraldehyde and caffeyl aldehyde to their respective alcohols. {ECO:0000269|Pub...
Arabidopsis thaliana (Mouse-ear cress)
O49484
ASK11_ARATH
MSSKMIVLMSSDGQSFEVEEAVAIQSQTIAHMVEDDCVADGIPLANVESKILVKVIEYCKKHHVDEANPISEEDLNNWDEKFMDLEQSTIFELILAANYLNIKSLLDLTCQTVADMIKGKTPEEIRSTFNIENDFTPEEEEAVRKENQWAFE
null
null
auxin-activated signaling pathway [GO:0009734]; jasmonic acid mediated signaling pathway [GO:0009867]; protein ubiquitination [GO:0016567]; response to auxin [GO:0009733]; response to jasmonic acid [GO:0009753]; SCF-dependent proteasomal ubiquitin-dependent protein catabolic process [GO:0031146]
cytoplasm [GO:0005737]; nucleus [GO:0005634]; SCF ubiquitin ligase complex [GO:0019005]
cullin family protein binding [GO:0097602]
PF01466;PF03931;
null
SKP1 family
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
null
null
PATHWAY: Protein modification; protein ubiquitination.
null
null
FUNCTION: Involved in ubiquitination and subsequent proteasomal degradation of target proteins. Together with CUL1, RBX1 and a F-box protein, it forms a SCF E3 ubiquitin ligase complex. The functional specificity of this complex depends on the type of F-box protein. In the SCF complex, it serves as an adapter that link...
Arabidopsis thaliana (Mouse-ear cress)
O49485
SERA1_ARATH
MSATAAASSSIAVATNSLRNVTLSSRSPLPSAISVAFPSRGRNTLQRRLVLVSCSTGDGSKPTILVAEKLGDAGIKLLEDVANVDCSYNMTPEELNIKISLCDALIVRSGTKVGREVFESSHGRLKVVGRAGVGIDNVDLSAATEFGCLVVNAPTANTIAAAEHGIALMAAMARNVAQADASVKAGEWKRNKYVGVSLVGKTLAVLGFGKVGTEVARRAKGLGMRVIAHDPYAPADRAHAIGVDLVSFDEALATADFISLHMPLTPTTSKILNDETFAKMKKGVRIVNVARGGVIDEDALVRALDAGIVAQAALDVFTKE...
1.1.1.95
null
embryo development ending in seed dormancy [GO:0009793]; L-serine biosynthetic process [GO:0006564]; megagametogenesis [GO:0009561]; pollen development [GO:0009555]; sulfur amino acid metabolic process [GO:0000096]
chloroplast [GO:0009507]; chloroplast stroma [GO:0009570]; mitochondrion [GO:0005739]; plasma membrane [GO:0005886]; plastid [GO:0009536]
ATP binding [GO:0005524]; NAD binding [GO:0051287]; phosphoglycerate dehydrogenase activity [GO:0004617]
PF00389;PF02826;PF01842;PF19304;
3.30.70.260;3.40.50.720;
D-isomer specific 2-hydroxyacid dehydrogenase family
null
SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000269|PubMed:24058165, ECO:0000269|PubMed:24368794}.
CATALYTIC ACTIVITY: Reaction=(2R)-3-phosphoglycerate + NAD(+) = 3-phosphooxypyruvate + H(+) + NADH; Xref=Rhea:RHEA:12641, ChEBI:CHEBI:15378, ChEBI:CHEBI:18110, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:58272; EC=1.1.1.95; Evidence={ECO:0000269|PubMed:24368794};
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.308 mM for 3-phospho-D-glycerate (at pH 8.1) {ECO:0000269|PubMed:24368794}; KM=0.39 mM for NAD(+) (at pH 8.1) {ECO:0000269|PubMed:24368794}; KM=2.11 mM for 3-phospho-D-glycerate (at pH 7.2) {ECO:0000269|PubMed:24368794}; KM=0.377 mM for NAD(+) (at pH 7.2) {ECO:00...
PATHWAY: Amino-acid biosynthesis; L-serine biosynthesis; L-serine from 3-phospho-D-glycerate: step 1/3.
null
null
FUNCTION: Involved in the plastidial phosphorylated pathway of serine biosynthesis (PPSB). Required for mature pollen development. {ECO:0000269|PubMed:24058165, ECO:0000269|PubMed:24368794}.
Arabidopsis thaliana (Mouse-ear cress)
O49499
CAMT4_ARATH
MATTTTEATKTSSTNGEDQKQSQNLRHQEVGHKSLLQSDDLYQYILETSVYPREPESMKELREVTAKHPWNIMTTSADEGQFLNMLIKLVNAKNTMEIGVYTGYSLLATALALPEDGKILAMDVNRENYELGLPIIEKAGVAHKIDFREGPALPVLDEIVADEKNHGTYDFIFVDADKDNYINYHKRLIDLVKIGGVIGYDNTLWNGSVVAPPDAPMRKYVRYYRDFVLELNKALAADPRIEICMLPVGDGITICRRIS
2.1.1.104
COFACTOR: Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; Evidence={ECO:0000250|UniProtKB:Q40313}; Note=Binds 1 divalent metal cation per subunit. {ECO:0000250|UniProtKB:Q40313};
coumarin biosynthetic process [GO:0009805]; lignin biosynthetic process [GO:0009809]; methylation [GO:0032259]
cytosol [GO:0005829]; plasma membrane [GO:0005886]
caffeoyl-CoA O-methyltransferase activity [GO:0042409]; metal ion binding [GO:0046872]
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; Evidence={ECO:0000269|PubMed:18547395};
null
PATHWAY: Aromatic compound metabolism; phenylpropanoid biosynthesis.
null
null
FUNCTION: Methylates caffeoyl-CoA to feruloyl-CoA. Has a very low activity with caffeic acid and esculetin. Involved in scopoletin biosynthesis in roots. {ECO:0000269|PubMed:17594112, ECO:0000269|PubMed:18547395, ECO:0000269|PubMed:22258746}.
Arabidopsis thaliana (Mouse-ear cress)
O49500
MBR2_ARATH
MQGPRSTGDSSTGINYADGEPICSTNSETTSNNILNPVDVQFPNNTTGSGRPTYASSSSHVVQNHNWWSFGESSSRLGPSDHLNSNGSKTDRQLLSDGYGFEEGQSGMLLPGESFLRGSSSSHMLSHVNLGKDMDIGSGLQTSGVVIRHNNCETSLGSSSQTAEERSSGPGSSLGGLGSSCKRKALEGAPSHSFPGESHGCFFQTENGAWNEGLAQYDASSSLSLSMPSQNSPNVNNQSGLPEPRFGLGGGRAVTASAFPSTRSTETISRPGRRLNPGQPPESVAFSFTQSGSSVRQQQQLPATSPFVDPLDARAIPVTG...
2.3.2.27
null
flower development [GO:0009908]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; protein ubiquitination [GO:0016567]; vegetative to reproductive phase transition of meristem [GO:0010228]
null
metal ion binding [GO:0046872]; ubiquitin protein ligase activity [GO:0061630]
PF13639;
3.30.40.10;
RING-type zinc finger family
null
null
CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27;
null
PATHWAY: Protein modification; protein ubiquitination.
null
null
FUNCTION: E3 ubiquitin-protein ligase that functions as a regulator of MED25 stability by targeting MED25 for degradation in a RING-H2-dependent way. Proteasome-dependent degradation of MED25 seems to activate its function as positive regulator of FLOWERING LOCUS T (FT) and is important to induce the expression of FT a...
Arabidopsis thaliana (Mouse-ear cress)
O49506
GLO5_ARATH
MEITNVMEYEKIAKEKLPKMVYDYYASGAEDQWTLQENRNAFSRILFRPRILIDVSKIDVSTTVLGFNISMPIMIAPTAMQKMAHPDGELATARATSAAGTIMTLSSWATCSVEEVASTGPGIRFFQLYVYKDRNVVIQLVKRAEEAGFKAIALTVDTPRLGRRESDIKNRFALPRGLTLKNFEGLDLGKIDKTNDSGLASYVAGQVDQSLSWKDIKWLQSITSLPILVKGVITAEDARIAVEYGAAGIIVSNHGARQLDYVPATIVALEEVVKAVEGRIPVFLDGGVRRGTDVFKALALGASGVFVGRPSLFSLAADGE...
1.1.3.15
COFACTOR: Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000250|UniProtKB:P05414};
defense response to bacterium [GO:0042742]; fatty acid alpha-oxidation [GO:0001561]; hydrogen peroxide biosynthetic process [GO:0050665]; lactate oxidation [GO:0019516]; oxidative photosynthetic carbon pathway [GO:0009854]
peroxisome [GO:0005777]; plasma membrane [GO:0005886]
(S)-2-hydroxy-acid oxidase activity [GO:0003973]; FMN binding [GO:0010181]; L-lactate dehydrogenase activity [GO:0004459]
PF01070;
3.20.20.70;
FMN-dependent alpha-hydroxy acid dehydrogenase family
null
SUBCELLULAR LOCATION: Peroxisome {ECO:0000250}.
CATALYTIC ACTIVITY: Reaction=glycolate + O2 = glyoxylate + H2O2; Xref=Rhea:RHEA:25311, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:29805, ChEBI:CHEBI:36655; EC=1.1.3.15; Evidence={ECO:0000250|UniProtKB:Q9LRR9}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25312; Evidence={ECO:0000250|UniProtKB:Q9LRR9};
null
PATHWAY: Photosynthesis; photorespiration; glycine from 2-phosphoglycolate: step 2/3. {ECO:0000250|UniProtKB:Q9LRR9}.
null
null
FUNCTION: Catalyzes the oxidation of glycolate to glyoxylate, with a reduction of O2 to H2O2. Is a key enzyme in photorespiration in green plants. {ECO:0000250|UniProtKB:Q9LRR9}.
Arabidopsis thaliana (Mouse-ear cress)
O49519
CLE2_ARATH
MAKLSFTFCFLLFLLLSSIAAGSRPLEGARVGVKVRGLSPSIEATSPTVEDDQAAGSHGKSPERLSPGGPDPQHH
null
null
cell fate commitment [GO:0045165]; cell-cell signaling [GO:0007267]
apoplast [GO:0048046]
receptor serine/threonine kinase binding [GO:0033612]
null
null
CLV3/ESR signal peptide family
PTM: [CLE2p]: The O-glycosylation (arabinosylation) of the hydroxyproline Pro-70 enhances binding affinity of the CLE2p peptide for its receptor. {ECO:0000269|PubMed:19525968}.
SUBCELLULAR LOCATION: [CLE2p]: Secreted, extracellular space {ECO:0000269|PubMed:19525968}.
null
null
null
null
null
FUNCTION: [CLE2p]: Extracellular signal peptide that regulates cell fate. May act with CLV1 as a ligand-receptor pair in a signal transduction pathway, coordinating growth between adjacent meristematic regions. {ECO:0000269|PubMed:16489133, ECO:0000269|PubMed:19525968}.
Arabidopsis thaliana (Mouse-ear cress)
O49523
DSEL_ARATH
MKRKKKEEEEEKLIVTREFAKRWRDLSGQNHWKGMLQPLDQDLREYIIHYGEMAQAGYDTFNINTESQFAGASIYSRKDFFAKVGLEIAHPYTKYKVTKFIYATSDIHVPESFLLFPISREGWSKESNWMGYVAVTDDQGTALLGRRDIVVSWRGSVQPLEWVEDFEFGLVNAIKIFGERNDQVQIHQGWYSIYMSQDERSPFTKTNARDQVLREVGRLLEKYKDEEVSITICGHSLGAALATLSATDIVANGYNRPKSRPDKSCPVTAFVFASPRVGDSDFRKLFSGLEDIRVLRTRNLPDVIPIYPPIGYSEVGDEFP...
3.1.1.-
null
diacylglycerol catabolic process [GO:0046340]; lipid storage [GO:0019915]; monoacylglycerol catabolic process [GO:0052651]; negative regulation of seed germination [GO:0010187]
cytoplasm [GO:0005737]
acylglycerol lipase activity [GO:0047372]; phospholipase A1 activity [GO:0008970]
PF01764;
3.40.50.1820;
AB hydrolase superfamily, Lipase family
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21477884}.
null
null
null
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5-6 with 1,3-DAG as substrate and at 30 degrees Celsius. {ECO:0000269|PubMed:21477884};
null
FUNCTION: Acylhydrolase that catalyzes the hydrolysis of 1,3-diacylglycerol (1,3-DAG) and 1-monoacylglycerol (1-MAG) at the sn-1 position. High activity toward 1,3-DAG and 1-MAG, but low activity toward 1,2-diacylglycerol (1,2-DAG) and 1-lysophosphatidylcholine (1-LPC), and no activity toward phosphatidylcholine (PC), ...
Arabidopsis thaliana (Mouse-ear cress)
O49543
MNIF1_ARATH
MASKVISATIRRTLTKPHGTFSRCRYLSTAAAATEVNYEDESIMMKGVRISGRPLYLDMQATTPIDPRVFDAMNASQIHEYGNPHSRTHLYGWEAENAVENARNQVAKLIEASPKEIVFVSGATEANNMAVKGVMHFYKDTKKHVITTQTEHKCVLDSCRHLQQEGFEVTYLPVKTDGLVDLEMLREAIRPDTGLVSIMAVNNEIGVVQPMEEIGMICKEHNVPFHTDAAQAIGKIPVDVKKWNVALMSMSAHKIYGPKGVGALYVRRRPRIRLEPLMNGGGQERGLRSGTGATQQIVGFGAACELAMKEMEYDEKWIKG...
2.8.1.7
COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000269|PubMed:22511606};
[2Fe-2S] cluster assembly [GO:0044571]; iron-sulfur cluster assembly [GO:0016226]
cytosol [GO:0005829]; mitochondrion [GO:0005739]; nucleus [GO:0005634]; plastid [GO:0009536]
ATP binding [GO:0005524]; cysteine desulfurase activity [GO:0031071]; iron-sulfur cluster binding [GO:0051536]; pyridoxal phosphate binding [GO:0030170]; zinc ion binding [GO:0008270]
PF00266;
3.90.1150.10;3.40.640.10;
Class-V pyridoxal-phosphate-dependent aminotransferase family, NifS/IscS subfamily
null
SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:14671022, ECO:0000269|PubMed:17417719}.
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:0000269|PubMed:17417719};
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: Vmax=21.2 nmol/min/mg enzyme with cysteine as substrate {ECO:0000269|PubMed:22511606};
null
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.5. {ECO:0000303|PubMed:17417719};
null
FUNCTION: Catalyzes the removal of elemental sulfur from cysteine to produce alanine. Supplies the inorganic sulfur for iron-sulfur (Fe-S) clusters. {ECO:0000269|PubMed:16437155, ECO:0000269|PubMed:17417719}.
Arabidopsis thaliana (Mouse-ear cress)
O49545
BAME1_ARATH
MKLFLLLLFLLHISHTFTASRPISEFRALLSLKTSLTGAGDDKNSPLSSWKVSTSFCTWIGVTCDVSRRHVTSLDLSGLNLSGTLSPDVSHLRLLQNLSLAENLISGPIPPEISSLSGLRHLNLSNNVFNGSFPDEISSGLVNLRVLDVYNNNLTGDLPVSVTNLTQLRHLHLGGNYFAGKIPPSYGSWPVIEYLAVSGNELVGKIPPEIGNLTTLRELYIGYYNAFEDGLPPEIGNLSELVRFDGANCGLTGEIPPEIGKLQKLDTLFLQVNVFSGPLTWELGTLSSLKSMDLSNNMFTGEIPASFAELKNLTLLNLFR...
2.7.11.1
null
cell differentiation [GO:0030154]; floral organ development [GO:0048437]; gametophyte development [GO:0048229]; phosphorylation [GO:0016310]; regulation of meristem growth [GO:0010075]; regulation of meristem structural organization [GO:0009934]
plasma membrane [GO:0005886]
ATP binding [GO:0005524]; identical protein binding [GO:0042802]; protein self-association [GO:0043621]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; receptor serine/threonine kinase binding [GO:0033612]
PF00560;PF08263;PF00069;
3.80.10.10;1.10.510.10;
Protein kinase superfamily, Ser/Thr protein kinase family
null
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:14506206, ECO:0000269|PubMed:20626648}; Single-pass type I membrane protein {ECO:0000269|PubMed:14506206, ECO:0000269|PubMed:20626648}.
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-[pr...
null
null
null
null
FUNCTION: Necessary for male gametophyte development, as well as ovule specification and function. Involved in cell-cell communication process required during early anther development, and regulating cell division and differentiation to organize cell layers. Required for the development of high-ordered vascular strands...
Arabidopsis thaliana (Mouse-ear cress)
O49562
PDRP1_ARATH
MALLSAMKLQGRPPPISSNLNPNSKPAGSDSVSLNASEPGSERKPRKFSSQLNRWNRARTLRSGAKLDSTITNGSNNTTGPMRPIESSSRTDVSTLDSDVSSSSNGVSEADMTAAKSIYIVSDGTGWTAEHAVNAALGQFDYCLVDRGCPVNTHLFSGIEDGEKLMEIIKQAAREGAMVIYTLADPSMAEATMRACKLWKIPSLDILGPITESISSHLGTNPSGLSRGITNSSLNEDYFKRIEAIEFTIKHDDGALPENLEKADIVLVGVSRTGKTPLSTYLAQKGYKVSNVPIVNGVDLPKTLFEIDPRKVFGLMINPL...
2.7.11.32; 2.7.4.27
null
phosphorylation [GO:0016310]
chloroplast [GO:0009507]; chloroplast stroma [GO:0009570]
ATP binding [GO:0005524]; phosphoprotein phosphatase activity [GO:0004721]; phosphotransferase activity, phosphate group as acceptor [GO:0016776]; protein kinase activity [GO:0004672]; protein serine/threonine kinase activity [GO:0004674]
PF03618;
null
Pyruvate, phosphate/water dikinase regulatory protein family, PDRP subfamily
null
SUBCELLULAR LOCATION: Plastid, chloroplast stroma {ECO:0000269|PubMed:17996018}.
CATALYTIC ACTIVITY: Reaction=ADP + N(tele)-phospho-L-histidyl/L-threonyl-[pyruvate, phosphate dikinase] = AMP + H(+) + N(tele)-phospho-L-histidyl/O-phospho-L-threonyl-[pyruvate, phosphate dikinase]; Xref=Rhea:RHEA:43692, Rhea:RHEA-COMP:10650, Rhea:RHEA-COMP:10651, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:61977...
null
null
null
null
FUNCTION: Bifunctional serine/threonine kinase and phosphorylase involved in the dark/light-mediated regulation of PPDK by catalyzing its phosphorylation/dephosphorylation. Dark/light-induced changes in stromal concentrations of the competing ADP and Pi substrates govern the direction of the reaction. In the dark, phos...
Arabidopsis thaliana (Mouse-ear cress)
O49595
HMGB1_ARATH
MKTAKGKDKVKTTKEALKPVDDRKVGKRKAPAEKPTKRETRKEKKAKKDPNKPKRAPSAFFVFLEDFRVTFKKENPNVKAVSAVGKAGGQKWKSMSQAEKAPYEEKAAKRKAEYEKQMDAYNKNLEEGSDESEKSRSEINDEDEASGEEELLEKEAAGDDEEEEEEEDDDDDDDEEED
null
null
chromatin organization [GO:0006325]
chromatin [GO:0000785]; nucleus [GO:0005634]
chromatin binding [GO:0003682]; DNA binding [GO:0003677]; DNA-binding transcription factor activity [GO:0003700]; structural constituent of chromatin [GO:0030527]
PF00505;
1.10.30.10;
HMGB family
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00267, ECO:0000269|PubMed:17114349, ECO:0000269|PubMed:18822296}. Note=Displays a highly dynamic speckle distribution pattern in interphase chromatin but does not associate with mitotic chromosomes.
null
null
null
null
null
FUNCTION: Binds preferentially double-stranded DNA. Modulates general plant growth and stress tolerance. Confers sensitivity to salt and genotoxic (methyl methanesulfonate, MMS) stresses. {ECO:0000269|PubMed:17114349, ECO:0000269|PubMed:9461286}.
Arabidopsis thaliana (Mouse-ear cress)
O49596
HMGB2_ARATH
MKGAKSKTETRSSKLSVTKKPAKGAGRGKAAAKDPNKPKRPASAFFVFMEDFRETFKKENPKNKSVATVGKAAGDKWKSLSDSEKAPYVAKAEKRKVEYEKNIKAYNKKLEEGPKEDEESDKSVSEVNDEDDAEDGSEEEEDDD
null
null
chromatin organization [GO:0006325]
chromatin [GO:0000785]; cytosol [GO:0005829]; nucleus [GO:0005634]
chromatin binding [GO:0003682]; DNA binding [GO:0003677]; DNA-binding transcription factor activity [GO:0003700]; structural constituent of chromatin [GO:0030527]
PF00505;
1.10.30.10;
HMGB family
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00267, ECO:0000269|PubMed:20123078}. Cytoplasm, cytosol {ECO:0000269|PubMed:20123078}.
null
null
null
null
null
FUNCTION: Binds preferentially double-stranded DNA. Confers sensitivity to salt and drought stresses. {ECO:0000269|PubMed:17169924, ECO:0000269|PubMed:9461286}.
Arabidopsis thaliana (Mouse-ear cress)
O49597
HMGB5_ARATH
MKDNQTEVESRSTDDRLKVRGNKVGKKTKDPNRPKKPPSPFFVFLDDFRKEFNLANPDNKSVGNVGRAAGKKWKTMTEEERAPFVAKSQSKKTEYAVTMQQYNMELANGNKTTGDDEKQEKAADD
null
null
chromatin organization [GO:0006325]
chromatin [GO:0000785]; cytoplasm [GO:0005737]; nucleus [GO:0005634]
chromatin binding [GO:0003682]; DNA binding [GO:0003677]; DNA-binding transcription factor activity [GO:0003700]; structural constituent of chromatin [GO:0030527]
PF00505;
1.10.30.10;
HMGB family
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00267, ECO:0000269|PubMed:17114349}. Note=Displays a highly dynamic speckle distribution pattern in interphase chromatin.
null
null
null
null
null
FUNCTION: Binds preferentially double-stranded DNA. Confers resistance to salt and drought stresses. {ECO:0000269|PubMed:17169924, ECO:0000269|PubMed:9461286}.
Arabidopsis thaliana (Mouse-ear cress)
O49623
DPNP2_ARATH
MSYEKELAAAKKAVTLAARLSQEVQKTLLQSQVWKKSDRSPVTAADYGSQAVVSLVLERELQPDKLSLVAEEETGDLRKNGSEAFLEDIAKLVKDTLASEESYTSSPLSTDDVLNAIDCGKSEGGCKGSHWVLDPIDGTRGFVRGEQYAVGLALLVEGKVVLGVMACPNLPLASAVCATDNSSQEDVGCLFFATTGSGTYVQSLKGNSLPQKVQVSSNENLDEAKFLESYHKPIPIHGTIAKKLGIKALPVRIDSQAKYAALSRGDAEIYLRFTLNGYRECIWDHAPGSIITTEAGGVVCDATGKSLDFSKGKYLAHKTG...
3.1.3.57; 3.1.3.7
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:10205895};
sulfate assimilation [GO:0000103]
null
3'(2'),5'-bisphosphate nucleotidase activity [GO:0008441]; inositol bisphosphate phosphatase activity [GO:0016312]; inositol-1,4-bisphosphate 1-phosphatase activity [GO:0004441]; metal ion binding [GO:0046872]
PF00459;
3.40.190.80;3.30.540.10;
Inositol monophosphatase superfamily
null
null
CATALYTIC ACTIVITY: Reaction=adenosine 3',5'-bisphosphate + H2O = AMP + phosphate; Xref=Rhea:RHEA:10040, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:58343, ChEBI:CHEBI:456215; EC=3.1.3.7; Evidence={ECO:0000269|PubMed:10205895}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10041; Evidence={ECO:0000305|PubM...
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=20 uM for adenosine 3',5'-bisphosphate {ECO:0000269|PubMed:10205895}; KM=830 uM for 1D-myo-inositol 1,4-bisphosphate {ECO:0000269|PubMed:10205895};
PATHWAY: Signal transduction; phosphatidylinositol signaling pathway. {ECO:0000305}.
null
null
FUNCTION: Phosphatase that converts adenosine 3'-phosphate 5'-phosphosulfate (PAPS) to adenosine 5'-phosphosulfate (APS) and 3'-phosphoadenosine 5'-phosphate (3'-PAP) to AMP (PubMed:10205895). May regulate the flux of sulfur in the sulfur-activation pathway by converting PAPS to APS (By similarity). Prevents both the t...
Arabidopsis thaliana (Mouse-ear cress)
O49627
ISU1_ARATH
MMLKQAAKKALGLTSRQSTPWSVGILRTYHENVIDHYDNPRNVGSFDKNDPNVGTGLVGAPACGDVMKLQIKVDEKTGQIVDARFKTFGCGSAIASSSVATEWVKGKAMEDVLTIKNTEIAKHLSLPPVKLHCSMLAEDAIKAAVKDYKEKRVKTNGAAAAGETTQA
null
COFACTOR: Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; Evidence={ECO:0000269|PubMed:17417719}; Note=Binds 1 [2Fe-2S] cluster per subunit. {ECO:0000269|PubMed:17417719};
intracellular iron ion homeostasis [GO:0006879]; iron-sulfur cluster assembly [GO:0016226]
cytosol [GO:0005829]; mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739]
2 iron, 2 sulfur cluster binding [GO:0051537]; ferrous iron binding [GO:0008198]; structural molecule activity [GO:0005198]
PF01592;
3.90.1010.10;
NifU family
null
SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000269|PubMed:15792798, ECO:0000269|PubMed:17417719, ECO:0000269|PubMed:19865480}. Cytoplasm, cytosol {ECO:0000269|PubMed:19865480}. Note=Localizes to the cytosol when interacting with HSCB. {ECO:0000269|PubMed:19865480}.
null
null
PATHWAY: Cofactor biosynthesis; iron-sulfur cluster biosynthesis. {ECO:0000250|UniProtKB:Q03020}.
null
null
FUNCTION: Scaffold protein for the de novo synthesis of iron-sulfur (Fe-S) clusters within mitochondria, which is required for maturation of both mitochondrial and cytoplasmic [2Fe-2S] and [4Fe-4S] proteins (PubMed:15507320, PubMed:17417719). First, a [2Fe-2S] cluster is transiently assembled on the scaffold protein IS...
Arabidopsis thaliana (Mouse-ear cress)
O49686
PYR1_ARATH
MPSELTPEERSELKNSIAEFHTYQLDPGSCSSLHAQRIHAPPELVWSIVRRFDKPQTYKHFIKSCSVEQNFEMRVGCTRDVIVISGLPANTSTERLDILDDERRVTGFSIIGGEHRLTNYKSVTTVHRFEKENRIWTVVLESYVVDMPEGNSEDDTRMFADTVVKLNLQKLATVAEAMARNSGDGSGSQVT
null
null
abscisic acid-activated signaling pathway [GO:0009738]; positive regulation of response to water deprivation [GO:1902584]; regulation of protein serine/threonine phosphatase activity [GO:0080163]
cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleus [GO:0005634]; plant-type vacuole membrane [GO:0009705]; plasma membrane [GO:0005886]; protein phosphatase inhibitor complex [GO:0062049]
abscisic acid binding [GO:0010427]; identical protein binding [GO:0042802]; protein homodimerization activity [GO:0042803]; protein phosphatase inhibitor activity [GO:0004864]; signaling receptor activity [GO:0038023]; ubiquitin-like protein ligase binding [GO:0044389]
PF10604;
3.30.530.20;
PYR/PYL/RCAR abscisic acid intracellular receptor family
PTM: Ubiquitynated and degraded by the proteasome upon binding to the E3 ubiquitin-protein ligase RSL1 at the plasma membrane. {ECO:0000269|PubMed:25330042}.; PTM: Phosphorylated by CARK1 especially in response to abscisic acid (ABA); this phosphorylation promotes its stability and inhibitory ability to ABI1. {ECO:0000...
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9FLB1}. Cytoplasm, cytosol {ECO:0000269|PubMed:29928509}. Nucleus {ECO:0000269|PubMed:25465408}. Cell membrane {ECO:0000269|PubMed:25330042, ECO:0000269|PubMed:25465408}. Vacuole {ECO:0000269|PubMed:27495812}. Note=Localizes at the plasma membrane in the presence ...
null
null
null
null
null
FUNCTION: Receptor for abscisic acid (ABA) required for ABA-mediated responses such as stomatal closure and germination inhibition. Inhibits the activity of group-A protein phosphatases type 2C (PP2Cs) when activated by ABA (PubMed:19407142, PubMed:19624469, PubMed:19769575, PubMed:21658606, PubMed:23844015). Can be ac...
Arabidopsis thaliana (Mouse-ear cress)
O49687
MYC4_ARATH
MSPTNVQVTDYHLNQSKTDTTNLWSTDDDASVMEAFIGGGSDHSSLFPPLPPPPLPQVNEDNLQQRLQALIEGANENWTYAVFWQSSHGFAGEDNNNNNTVLLGWGDGYYKGEEEKSRKKKSNPASAAEQEHRKRVIRELNSLISGGVGGGDEAGDEEVTDTEWFFLVSMTQSFVKGTGLPGQAFSNSDTIWLSGSNALAGSSCERARQGQIYGLQTMVCVATENGVVELGSSEIIHQSSDLVDKVDTFFNFNNGGGEFGSWAFNLNPDQGENDPGLWISEPNGVDSGLVAAPVMNNGGNDSTSNSDSQPISKLCNGSSV...
null
null
anthocyanin-containing compound biosynthetic process [GO:0009718]; defense response [GO:0006952]; extracellular ATP signaling [GO:0106167]; positive regulation of DNA-templated transcription [GO:0045893]; regulation of DNA-templated transcription [GO:0006355]; regulation of secondary cell wall biogenesis [GO:2000652]; ...
nucleus [GO:0005634]
bHLH transcription factor binding [GO:0043425]; DNA-binding transcription factor activity [GO:0003700]; protein dimerization activity [GO:0046983]; transcription cis-regulatory region binding [GO:0000976]
PF14215;PF00010;
4.10.280.10;
null
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981, ECO:0000269|PubMed:21321051, ECO:0000269|PubMed:21335373}.
null
null
null
null
null
FUNCTION: Transcription factor involved in jasmonic acid (JA) gene regulation. With MYC2 and MYC3, controls additively subsets of JA-dependent responses. Can form complexes with all known glucosinolate-related MYBs to regulate glucosinolate biosynthesis. Binds to the G-box (5'-CACGTG-3') of promoters. Activates multipl...
Arabidopsis thaliana (Mouse-ear cress)
O49696
ALMTC_ARATH
MSNKVHVGSLEMEEGLSKTKWMVLEPSEKIKKIPKRLWNVGKEDPRRVIHALKVGLSLTLVSLLYLMEPLFKGIGSNAIWAVMTVVVVLEFSAGATLCKGLNRGLGTLIAGSLAFFIEFVANDSGKVLRAIFIGTAVFIIGAAATYIRFIPYIKKNYDYGVVIFLLTFNLITVSSYRVDSVINIAHDRFYTIAVGCGICLFMSLLVFPIWSGEDLHKTTVGKLQGLSRSIEACVDEYFEEKEKEKTDSKDRIYEGYQAVLDSKSTDETLALYANWEPRHTLRCHRFPCQQYVKVGAVLRQFGYTVVALHGCLQTEIQTPR...
null
null
malate transport [GO:0015743]; stomatal movement [GO:0010118]; sulfate transport [GO:0008272]
endomembrane system [GO:0012505]; plant-type vacuole membrane [GO:0009705]; plasma membrane [GO:0005886]
monoatomic anion transmembrane transporter activity [GO:0008509]
PF11744;
null
Aromatic acid exporter (TC 2.A.85) family
null
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20154005, ECO:0000269|PubMed:20626656}; Multi-pass membrane protein {ECO:0000269|PubMed:20154005, ECO:0000269|PubMed:20626656}. Note=PubMed:20626656 indicates also a not confirmed endomembrane localization.
null
null
null
null
null
FUNCTION: Malate-sensitive anion transporter permeable to chloride, nitrate, sulfate and malate. Involved in dark-, CO(2)-, abscisic acid- and water-deficient-induced stomatal closure. Belongs to the R-type anion channels. {ECO:0000269|PubMed:20154005, ECO:0000269|PubMed:20626656}.
Arabidopsis thaliana (Mouse-ear cress)
O49717
CDPKF_ARATH
MGCFSSKHRNTESDIINGSVQSSIPTNQPENHVSRDVLKPQKPPSPQIPTTTQSNHHHQQESKPVNQQIEKKHVLTQPLKPIVFRETETILGKPFEEIRKLYTLGKELGRGQFGITYTCKENSTGNTYACKSILKRKLTRKQDIDDVKREIQIMQYLSGQENIVEIKGAYEDRQSIHLVMELCGGSELFDRIIAQGHYSEKAAAGVIRSVLNVVQICHFMGVIHRDLKPENFLLASTDENAMLKATDFGLSVFIEEGKVYRDIVGSAYYVAPEVLRRSYGKEIDIWSAGIILYILLCGVPPFWSETEKGIFNEIIKGEID...
2.7.11.1
null
intracellular signal transduction [GO:0035556]; phosphorylation [GO:0016310]
cytoplasm [GO:0005737]; membrane [GO:0016020]; nucleus [GO:0005634]
ATP binding [GO:0005524]; calcium ion binding [GO:0005509]; calcium-dependent protein serine/threonine kinase activity [GO:0009931]; calmodulin binding [GO:0005516]; calmodulin-dependent protein kinase activity [GO:0004683]; protein serine kinase activity [GO:0106310]
PF13499;PF00069;
1.10.238.10;1.10.510.10;
Protein kinase superfamily, Ser/Thr protein kinase family, CDPK subfamily
null
SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}.
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-[pr...
null
null
null
null
FUNCTION: May play a role in signal transduction pathways that involve calcium as a second messenger.
Arabidopsis thaliana (Mouse-ear cress)
O49782
MYB51_ARATH
MVRTPCCKAELGLKKGAWTPEEDQKLLSYLNRHGEGGWRTLPEKAGLKRCGKSCRLRWANYLRPDIKRGEFTEDEERSIISLHALHGNKWSAIARGLPGRTDNEIKNYWNTHIKKRLIKKGIDPVTHKGITSGTDKSENLPEKQNVNLTTSDHDLDNDKAKKNNKNFGLSSASFLNKVANRFGKRINQSVLSEIIGSGGPLASTSHTTNTTTTSVSVDSESVKSTSSSFAPTSNLLCHGTVATTPVSSNFDVDGNVNLTCSSSTFSDSSVNNPLMYCDNFVGNNNVDDEDTIGFSTFLNDEDFMMLEESCVENTAFMKEL...
null
null
defense response by callose deposition in cell wall [GO:0052544]; defense response to bacterium [GO:0042742]; indole glucosinolate biosynthetic process [GO:0009759]; induced systemic resistance [GO:0009682]; response to bacterium [GO:0009617]; response to insect [GO:0009625]
nucleus [GO:0005634]
DNA-binding transcription factor activity [GO:0003700]; transcription cis-regulatory region binding [GO:0000976]
PF00249;
1.10.10.60;
null
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00625, ECO:0000269|PubMed:17461791}.
null
null
null
null
null
FUNCTION: Transcription factor positively regulating indolic glucosinolate biosynthetic pathway genes. {ECO:0000269|PubMed:17461791, ECO:0000269|PubMed:23580754, ECO:0000269|PubMed:23943862}.
Arabidopsis thaliana (Mouse-ear cress)
O49815
BCH1_CAPAN
MAAEISISASSRAICLQRNPFPAPKYFATAPPLLFFSPLTCNLDAILRSRRKPRLAACFVLKDDKLYTAQSGKQSDTEAIGDEIEVETNEEKSLAVRLAEKFARKKSERFTYLVAAVMSSLGITSMAVISVYYRFSWQMEGGEMPFSEMFCTFALAFGAAIGMEYWARWAHRALWHASLWHMHESHHRPREGPFELNDIFAIINAVPAIALLSFGFNHKGLIPGLCFGAGLGITVFGMAYMFVHDGLVHKRFPVGPIANVPYFQRVAAAHQLHHSDKFDGVPYGLFLGPKELEEVGVLEELEKEVNRRIKSSKRL
1.14.15.24
null
carotene metabolic process [GO:0016119]; xanthophyll biosynthetic process [GO:0016123]
chloroplast membrane [GO:0031969]
beta-carotene 3-hydroxylase activity [GO:0052611]; beta-cryptoxanthin hydroxylase activity [GO:0052610]; carotene beta-ring hydroxylase activity [GO:0010291]; hydrolase activity [GO:0016787]; iron ion binding [GO:0005506]
PF04116;
null
Sterol desaturase family
null
SUBCELLULAR LOCATION: Plastid, chloroplast membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
CATALYTIC ACTIVITY: Reaction=all-trans-beta-carotene + 4 H(+) + 2 O2 + 4 reduced [2Fe-2S]-[ferredoxin] = all-trans-zeaxanthin + 2 H2O + 4 oxidized [2Fe-2S]-[ferredoxin]; Xref=Rhea:RHEA:30331, Rhea:RHEA-COMP:10000, Rhea:RHEA-COMP:10001, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:17579, ChEBI:CH...
null
null
null
null
FUNCTION: Nonheme diiron monooxygenase involved in the biosynthesis of xanthophylls. Specific for beta-ring hydroxylations of beta-carotene. Produces beta-cryptoxanthin and zeaxanthin. Uses ferredoxin as an electron donor. {ECO:0000269|PubMed:9555077}.
Capsicum annuum (Capsicum pepper)
O49839
PBL2_ARATH
MGNCLDSSAKVDNSNHSPHANSASSGSKVSSKTSRSTGPSGLSTTSYSTDSSFGPLPTLRTEGEILSSPNLKAFTFNELKNATKNFRQDNLLGEGGFGCVFKGWIDQTSLTASRPGSGIVVAVKQLKPEGFQGHKEWLTEVNYLGQLSHPNLVLLVGYCAEGENRLLVYEFMPKGSLENHLFRRGAQPLTWAIRMKVAVGAAKGLTFLHEAKSQVIYRDFKAANILLDADFNAKLSDFGLAKAGPTGDNTHVSTKVIGTHGYAAPEYVATGRLTAKSDVYSFGVVLLELISGRRAMDNSNGGNEYSLVDWATPYLGDKRK...
2.7.11.1
null
defense response [GO:0006952]; phosphorylation [GO:0016310]; positive regulation of defense response to bacterium [GO:1900426]
nucleus [GO:0005634]; plasma membrane [GO:0005886]
ATP binding [GO:0005524]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; Tat protein binding [GO:0030957]
PF07714;
1.10.510.10;
Protein kinase superfamily, Ser/Thr protein kinase family
PTM: Uridylylated at Ser-253 and Thr-254 by Xanthomonas campestris effector AvrAC/XopAC; this uridylylation is necessary for specific recruitment to RKS1 and to trigger immunity. {ECO:0000269|PubMed:26355215}.
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21219905}; Lipid-anchor {ECO:0000305|PubMed:21219905}. Nucleus {ECO:0000269|PubMed:21219905}. Note=Predominantly localized at the plasma membrane. {ECO:0000269|PubMed:21219905}.
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:0000305}; CATALYTIC ACTIVITY: React...
null
null
null
null
FUNCTION: Involved in disease resistance signaling (PubMed:20413097, PubMed:23951354, PubMed:26355215). Contributes to pathogen-associated molecular pattern (PAMP)-triggered immunity (PTI) signaling and defense responses downstream of FLS2 (PubMed:20413097). Acts as a BIK1 decoy and enables Xanthomonas campestris AvrAC...
Arabidopsis thaliana (Mouse-ear cress)
O49840
PBL3_ARATH
MGNCLDSSAKVDSSSHSPHANSASLSSRVSSKTSRSTVPSSLSINSYSSVESLPTPRTEGEILSSPNLKAFTFNELKNATRNFRPDSLLGEGGFGYVFKGWIDGTTLTASKPGSGIVVAVKKLKTEGYQGHKEWLTEVNYLGQLSHPNLVKLVGYCVEGENRLLVYEFMPKGSLENHLFRRGAQPLTWAIRMKVAIGAAKGLTFLHDAKSQVIYRDFKAANILLDAEFNSKLSDFGLAKAGPTGDKTHVSTQVMGTHGYAAPEYVATGRLTAKSDVYSFGVVLLELLSGRRAVDKSKVGMEQSLVDWATPYLGDKRKLFR...
2.7.11.1
null
defense response [GO:0006952]; phosphorylation [GO:0016310]
cytoplasm [GO:0005737]; nucleus [GO:0005634]; plasma membrane [GO:0005886]
ATP binding [GO:0005524]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]
PF07714;
1.10.510.10;
Protein kinase superfamily, Ser/Thr protein kinase family
null
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21219905}; Lipid-anchor {ECO:0000305|PubMed:21219905}. Nucleus {ECO:0000269|PubMed:21219905}. Note=Predominantly localized at the plasma membrane. {ECO:0000269|PubMed:21219905}.
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:0000305}; CATALYTIC ACTIVITY: React...
null
null
null
null
FUNCTION: May be involved in plant defense signaling. {ECO:0000250|UniProtKB:O48814}.
Arabidopsis thaliana (Mouse-ear cress)
O50008
METE1_ARATH
MASHIVGYPRMGPKRELKFALESFWDGKSTAEDLQKVSADLRSSIWKQMSAAGTKFIPSNTFAHYDQVLDTTAMLGAVPPRYGYTGGEIGLDVYFSMARGNASVPAMEMTKWFDTNYHYIVPELGPEVNFSYASHKAVNEYKEAKALGVDTVPVLVGPVSYLLLSKAAKGVDKSFELLSLLPKILPIYKEVITELKAAGATWIQLDEPVLVMDLEGQKLQAFTGAYAELESTLSGLNVLVETYFADIPAEAYKTLTSLKGVTAFGFDLVRGTKTLDLVKAGFPEGKYLFAGVVDGRNIWANDFAASLSTLQALEGIVGKD...
2.1.1.14
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:15326182}; Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000269|PubMed:15326182};
'de novo' L-methionine biosynthetic process [GO:0071266]; DNA methylation-dependent heterochromatin formation [GO:0006346]; methionine biosynthetic process [GO:0009086]; methylation [GO:0032259]; response to zinc ion [GO:0010043]
apoplast [GO:0048046]; chloroplast [GO:0009507]; chloroplast stroma [GO:0009570]; cytosol [GO:0005829]; peroxisome [GO:0005777]; plant-type vacuole [GO:0000325]; plasma membrane [GO:0005886]; plasmodesma [GO:0009506]
5-methyltetrahydropteroyltriglutamate-homocysteine S-methyltransferase activity [GO:0003871]; copper ion binding [GO:0005507]; methionine synthase activity [GO:0008705]; mRNA binding [GO:0003729]; zinc ion binding [GO:0008270]
PF08267;PF01717;
3.20.20.210;
Vitamin-B12 independent methionine synthase family
null
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:15024005}.
CATALYTIC ACTIVITY: Reaction=5-methyltetrahydropteroyltri-L-glutamate + L-homocysteine = L-methionine + tetrahydropteroyltri-L-glutamate; Xref=Rhea:RHEA:21196, ChEBI:CHEBI:57844, ChEBI:CHEBI:58140, ChEBI:CHEBI:58199, ChEBI:CHEBI:58207; EC=2.1.1.14; Evidence={ECO:0000269|PubMed:15024005};
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=60 uM for 5-methyltetrahydrofolate {ECO:0000269|PubMed:15024005}; Vmax=26.5 nmol/min/mg enzyme toward 5-methyltetrahydrofolate {ECO:0000269|PubMed:15024005};
PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-methionine from L-homocysteine (MetE route): step 1/1. {ECO:0000269|PubMed:15024005}.
null
null
FUNCTION: Catalyzes the transfer of a methyl group from 5-methyltetrahydrofolate to homocysteine resulting in methionine formation. {ECO:0000269|PubMed:15024005}.
Arabidopsis thaliana (Mouse-ear cress)
O50055
COL1_ARATH
MLKVESNWAQACDTCRSAACTVYCRADSAYLCSSCDAQVHAANRLASRHERVRVCQSCERAPAAFFCKADAASLCTTCDSEIHSANPLARRHQRVPILPISEYSYSSTATNHSCETTVTDPENRLVLGQEEEDEDEAEAASWLLPNSGKNSGNNNGFSIGDEFLNLVDYSSSDKQFTDQSNQYQLDCNVPQRSYGEDGVVPLQIEVSKGMYQEQQNFQLSINCGSWGALRSSNGSLSHMVNVSSMDLGVVPESTTSDATVSNPRSPKAVTDQPPYPPAQMLSPRDREARVLRYREKKKMRKFEKTIRYASRKAYAEKRPR...
null
null
regulation of flower development [GO:0009909]
nucleus [GO:0005634]
DNA binding [GO:0003677]; DNA-binding transcription factor activity [GO:0003700]; identical protein binding [GO:0042802]; zinc ion binding [GO:0008270]
PF06203;PF00643;
null
CONSTANS family
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
null
null
null
null
null
FUNCTION: Putative transcription factor that may be involved in the light input to the circadian clock but does not affect flowering time.
Arabidopsis thaliana (Mouse-ear cress)
O50061
RK4_ARATH
MASSATAPNSLSFFSSSLFLSSSHQIPKTYISVSKLGSGRVSKPLSVSSQLATLPILSFEGEKVGETYLDLKAAPEDTARAVVHRAIVTDLNNKRRGTASTLTRGEVRGGGIKPYSQKKTGHARRGSQRTPLRPGGGVVFGPRPKDWSIKINRKEKKLAISTALSSAASAEGGAIVVEEFGEKFEKPKTKDFLAAMQRWGLDPKEKAMFLMIDVDENVAKSSRNIGTLRMLTPRTLNLFDILNADKLVLTPAAVEFLNARYGVDAVEEEDDDEDETEGSEEA
null
null
translation [GO:0006412]
chloroplast [GO:0009507]; chloroplast stroma [GO:0009570]; chloroplast thylakoid membrane [GO:0009535]; cytosolic ribosome [GO:0022626]; extracellular region [GO:0005576]; nucleus [GO:0005634]; plastid large ribosomal subunit [GO:0000311]; plastid ribosome [GO:0009547]; thylakoid [GO:0009579]
mRNA binding [GO:0003729]; poly(U) RNA binding [GO:0008266]; rRNA binding [GO:0019843]; structural constituent of ribosome [GO:0003735]
PF00573;
3.40.1370.10;
Universal ribosomal protein uL4 family
null
SUBCELLULAR LOCATION: Plastid, chloroplast.
null
null
null
null
null
FUNCTION: This protein binds directly and specifically to 23S rRNA (By similarity). May play a role in plastid transcriptional regulation. {ECO:0000250}.
Arabidopsis thaliana (Mouse-ear cress)
O50078
ACEA_HYPME
MAHKKTYSQLRSELLARYPVGLTKGGVSIDDIVQLRLQSPYESHLDVARAMASVMRADMAAYDRDTGKFTQSLGCWSGFHAQQMIKAVKRLRGTTKGAYVYLSGWMVAGLRNRWGHLPDQSMHEKTSVVDLIEEIYVSLRQADEVALNDLFNELKDARAKGATNKACEEIISRIDGFESHVVPIIADIDAGFGNEHATYLLAKEMIKAGACCLQIENQVSDAKQCGHQDGKVTVPREDFIEKLRACRLAFEELGVDDGVIVARTDSLGASLTQKIPVSQQAGDFASSYIKWLKTEPITDANPLSEGELAIWQSGNFARPI...
4.1.3.1
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:9395332}; Note=Can also use Mn(2+). {ECO:0000269|PubMed:9395332};
glyoxylate cycle [GO:0006097]; tricarboxylic acid cycle [GO:0006099]
glyoxysome [GO:0009514]
isocitrate lyase activity [GO:0004451]; magnesium ion binding [GO:0000287]; transition metal ion binding [GO:0046914]
PF00463;
3.20.20.60;
Isocitrate lyase/PEP mutase superfamily, Isocitrate lyase family
null
null
CATALYTIC ACTIVITY: Reaction=D-threo-isocitrate = glyoxylate + succinate; Xref=Rhea:RHEA:13245, ChEBI:CHEBI:15562, ChEBI:CHEBI:30031, ChEBI:CHEBI:36655; EC=4.1.3.1; Evidence={ECO:0000269|PubMed:9395332};
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.51 mM for D-isocitrate {ECO:0000269|PubMed:9395332};
PATHWAY: Carbohydrate metabolism; glyoxylate cycle; (S)-malate from isocitrate: step 1/2. {ECO:0000305|PubMed:9395332}.; PATHWAY: One-carbon metabolism; formaldehyde assimilation via serine pathway. {ECO:0000305|PubMed:9395332}.
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5. The enzyme is stable when incubated for 15 minutes at 30 degrees Celsius at pH 7.5-9. {ECO:0000269|PubMed:9395332};
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 45 degrees Celsius. Loss of activity is 0%, 16%, 30%, 82% and 100% when incubated at 25, 30, 40, 50 and 60 degrees Celsius for 30 minutes, respectively. {ECO:0000269|PubMed:9395332};
FUNCTION: Involved in the metabolic adaptation in response to environmental changes. Catalyzes the reversible formation of succinate and glyoxylate from isocitrate, a key step of the glyoxylate cycle, which operates as an anaplerotic route for replenishing the tricarboxylic acid cycle during growth on fatty acid substr...
Hyphomicrobium methylovorum
O50083
RPIA_PYRHO
MNVEEMKKIAAKEALKFIEDDMVIGLGTGSTTAYFIKLLGEKLKRGEISDIVGVPTSYQAKLLAIEHDIPIASLDQVDAIDVAVDGADEVDPNLNLIKGRGAALTMEKIIEYRAGTFIVLVDERKLVDYLCQKMPVPIEVIPQAWKAIIEELSIFNAKAELRMGVNKDGPVITDNGNFIIDAKFPRIDDPLDMEIELNTIPGVIENGIFADIADIVIVGTREGVKKLER
5.3.1.6
null
D-ribose metabolic process [GO:0006014]; pentose-phosphate shunt, non-oxidative branch [GO:0009052]
cytosol [GO:0005829]; intracellular membrane-bounded organelle [GO:0043231]
ribose-5-phosphate isomerase activity [GO:0004751]
PF06026;
3.30.70.260;3.40.50.1360;
Ribose 5-phosphate isomerase family
null
null
CATALYTIC ACTIVITY: Reaction=aldehydo-D-ribose 5-phosphate = D-ribulose 5-phosphate; Xref=Rhea:RHEA:14657, ChEBI:CHEBI:58121, ChEBI:CHEBI:58273; EC=5.3.1.6; Evidence={ECO:0000255|HAMAP-Rule:MF_00170, ECO:0000269|PubMed:12057201};
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.17 mM for ribose 5-P {ECO:0000269|PubMed:12057201};
PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D-ribose 5-phosphate from D-ribulose 5-phosphate (non-oxidative stage): step 1/1. {ECO:0000255|HAMAP-Rule:MF_00170}.
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6 (at 50 degrees Celsius). {ECO:0000269|PubMed:12057201};
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is over 95 degrees Celsius. {ECO:0000269|PubMed:12057201};
FUNCTION: Involved in the first step of the non-oxidative branch of the pentose phosphate pathway. It catalyzes the reversible conversion of ribose-5-phosphate to ribulose 5-phosphate. {ECO:0000269|PubMed:12057201}.
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
O50131
ORNAT_PYRHO
MELKPNVKEIPGPKARKVIEEHHKYMATTTNDPNEYFLVIERAEGVYWIDVDGNVLLDFSSGIGVMNVGLRNPKVIEAIKKQLDLVLHAAGTDYYNPYQVELAKKLVEIAPGDIERKVFLSNSGTEANEAALKIAKWSTNRKMFIAFIGAFHGRTHGTMSLTASKPVQRSRMFPTMPGVVHVPYPNPYRNPWGIDGYENPDELINRVIDYIEEYLFEHYVPAEEVAGIFFEPIQGEGGYVVPPKNFFKELKKLADKHGILLIDDEVQMGMGRTGRMWAIEHFDIVPDIVTVAKALGGGIPIGATIFRADLDFGVSGVHSN...
2.6.1.13
COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000269|PubMed:35337912};
null
null
identical protein binding [GO:0042802]; pyridoxal phosphate binding [GO:0030170]; transaminase activity [GO:0008483]
PF00202;
3.90.1150.10;3.40.640.10;
Class-III pyridoxal-phosphate-dependent aminotransferase family
null
null
CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-ornithine = L-glutamate + L-glutamate 5-semialdehyde; Xref=Rhea:RHEA:25160, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:46911, ChEBI:CHEBI:58066; EC=2.6.1.13; Evidence={ECO:0000269|PubMed:35337912}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-lysine = (S)-2-amin...
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.106 mM for L-ornithine (in the presence of 10 mM 2-oxoglutarate) {ECO:0000269|PubMed:35337912}; KM=0.211 mM for L-lysine (in the presence of 10 mM 2-oxoglutarate) {ECO:0000269|PubMed:35337912}; KM=0.446 mM for D-ornithine (in the presence of 5 mM 2-oxoglutarate) ...
null
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.5-7.0. {ECO:0000269|PubMed:35337912};
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is higher than 90 degrees Celsius. {ECO:0000269|PubMed:35337912};
FUNCTION: Catalyzes the conversion of L-ornithine and 2-oxoglutarate to L-glutamate semialdehyde and L-glutamate (PubMed:35337912). L-ornithine is the best substrate, but the enzyme also shows good activity toward L-lysine, and low activity toward D-ornithine, D-lysine, 5-aminovalerate, 6-aminohexanoate and GABA (PubMe...
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
O50146
LYSY_THET2
MDKKTLSIVGASGYAGGEFLRLALSHPYLEVKQVTSRRFAGEPVHFVHPNLRGRTNLKFIPPEKLEPADILVLALPHGVFAREFDRYSALAPILIDLSADFRLKDPELYRRYYGEHPRPDLLGCFVYAVPELYREALKGADWIAGAGCNATATLLGLYPLLKAGVLKPTPIFVTLLISTSAAGAEASPASHHPERAGSIRVYKPTGHRHTAEVVENLPGRPEVHLTAIATDRVRGILMTAQCFVQDGWSERDVWQAYREAYAGEPFIRLVKQKKGVHRYPDPRFVQGTNYADIGFELEEDTGRLVVMTAIDNLVKGTAGH...
1.2.1.103
null
arginine biosynthetic process [GO:0006526]; lysine biosynthetic process via aminoadipic acid [GO:0019878]
cytoplasm [GO:0005737]
N-acetyl-gamma-aminoadipyl-phosphate reductase activity [GO:0043870]; N-acetyl-gamma-glutamyl-phosphate reductase activity [GO:0003942]; NAD binding [GO:0051287]; NADP+ binding [GO:0070401]; protein dimerization activity [GO:0046983]
PF01118;PF02774;
3.40.50.720;
NAGSA dehydrogenase family, Type 1 subfamily, LysY sub-subfamily
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02083}.
CATALYTIC ACTIVITY: Reaction=[amino-group carrier protein]-C-terminal-N-(1-carboxy-5-oxopentan-1-yl)-L-glutamine + NADP(+) + phosphate = [amino-group carrier protein]-C-terminal-N-(1-carboxy-5-phosphooxy-5-oxopentan-1-yl)-L-glutamine + H(+) + NADPH; Xref=Rhea:RHEA:41948, Rhea:RHEA-COMP:9712, Rhea:RHEA-COMP:9714, ChEBI:...
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=9.8 uM for [LysW]-aminoadipate 6-semialdehyde {ECO:0000269|PubMed:26966182}; KM=14 uM for NADP(+) {ECO:0000269|PubMed:26966182}; KM=12000 uM for phosphate {ECO:0000269|PubMed:26966182}; Note=kcat is 0.96 sec(-1). {ECO:0000269|PubMed:26966182};
PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via AAA pathway; L-lysine from L-alpha-aminoadipate (Thermus route): step 3/5. {ECO:0000255|HAMAP-Rule:MF_02083, ECO:0000269|PubMed:19620981}.
null
null
FUNCTION: Catalyzes the NADPH-dependent reduction of [LysW]-aminoadipate 6-phosphate to yield [LysW]-aminoadipate 6-semialdehyde. {ECO:0000255|HAMAP-Rule:MF_02083, ECO:0000269|PubMed:26966182, ECO:0000305|PubMed:19620981}.
Thermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27)
O50147
LYSZ_THET2
MIVVKVGGAEGINYEAVAKDAASLWKEGVKLLLVHGGSAETNKVAEALGHPPRFLTHPGGQVSRLTDRKTLEIFEMVYCGLVNKRLVELLQKEGANAIGLSGLDGRLFVGRRKTAVKYVENGKVKVHRGDYTGTVEEVNKALLDLLLQAGYLPVLTPPALSYENEAINTDGDQIAALLATLYGAEALVYLSNVPGLLARYPDEASLVREIPVERIEDPEYLALAQGRMKRKVMGAVEAVRGGVKRVVFADARVENPIRRALSGEGTVVR
2.7.2.17
null
arginine biosynthetic process [GO:0006526]; lysine biosynthetic process via aminoadipic acid [GO:0019878]; phosphorylation [GO:0016310]
cytoplasm [GO:0005737]
acetylglutamate kinase activity [GO:0003991]; ATP binding [GO:0005524]; N2-acetyl-L-aminoadipate kinase activity [GO:0043744]
PF00696;
3.40.1160.10;
Acetylglutamate kinase family, LysZ subfamily
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02082}.
CATALYTIC ACTIVITY: Reaction=[amino-group carrier protein]-C-terminal-N-(1,4-dicarboxybutan-1-yl)-L-glutamine + ATP = [amino-group carrier protein]-C-terminal-N-(1-carboxy-5-phosphooxy-5-oxopentan-1-yl)-L-glutamine + ADP; Xref=Rhea:RHEA:41944, Rhea:RHEA-COMP:9694, Rhea:RHEA-COMP:9712, ChEBI:CHEBI:30616, ChEBI:CHEBI:784...
null
PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via AAA pathway; L-lysine from L-alpha-aminoadipate (Thermus route): step 2/5. {ECO:0000255|HAMAP-Rule:MF_02082, ECO:0000269|PubMed:10613839, ECO:0000269|PubMed:19620981, ECO:0000305|PubMed:25392000}.
null
null
FUNCTION: Catalyzes the phosphorylation of LysW-gamma-alpha-aminoadipate. Does not phosphorylate N-acetyl-glutamate. {ECO:0000269|PubMed:25392000}.
Thermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27)
O50202
ARC_RHOER
MSSTENPDSVAAAEELHALRVEAQVLRRQLAQSPEQVRELESKVDSLSIRNSKLMDTLKEARQQLIALREEVDRLGQPPSGYGVLLSVHEDKTVDVFTSGRKMRLTCSPNIDTDTLALGQTVRLNEALTIVEAGTYEQVGEISTLREVLDDGLRALVVGHADEERIVWLAAPLAAVFADPEADIIAYDADSPTRKLRPGDSLLVDTKAGYAFERIPKAEVEDLVLEEVPDVHYDDIGGLGRQIEQIRDAVELPFLHKDLFHEYSLRPPKGVLLYGPPGCGKTLIAKAVANSLAKKIAEARGQDSKDAKSYFLNIKGPELL...
null
null
modification-dependent protein catabolic process [GO:0019941]; proteasomal protein catabolic process [GO:0010498]; retrograde protein transport, ER to cytosol [GO:0030970]
cytosol [GO:0005829]; proteasome complex [GO:0000502]; proteasome-activating nucleotidase complex [GO:0022623]
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; CTPase activity [GO:0043273]; polyubiquitin modification-dependent protein binding [GO:0031593]
PF00004;PF16450;PF17758;
1.10.8.60;1.20.5.170;2.40.50.140;3.40.50.300;
AAA ATPase family
null
null
null
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=200 uM for ATP {ECO:0000269|PubMed:9514743}; Vmax=268 pmol/min/ug enzyme {ECO:0000269|PubMed:9514743}; Note=Is also able to cleave CTP at half the rate of ATP hydrolysis, but GTP or UTP are not substrates.;
PATHWAY: Protein degradation; proteasomal Pup-dependent pathway. {ECO:0000255|HAMAP-Rule:MF_02112}.
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7-8. {ECO:0000269|PubMed:9514743};
null
FUNCTION: ATPase which is responsible for recognizing, binding, unfolding and translocation of pupylated proteins into the bacterial 20S proteasome core particle. May be essential for opening the gate of the 20S proteasome via an interaction with its C-terminus, thereby allowing substrate entry and access to the site o...
Rhodococcus erythropolis (Arthrobacter picolinophilus)
O50274
CYSNC_PSEAE
MSHQSDLISEDILAYLGQHERKELLRFLTCGNVDDGKSTLIGRLLHDSKMIYEDHLEAITRDSKKVGTTGDDVDLALLVDGLQAEREQGITIDVAYRYFSTAKRKFIIADTPGHEQYTRNMATGASTCDLAIILIDARYGVQTQTRRHSFIASLLGIRHIVVAINKMDLKDFDQGVFEQIKADYLAFAEKIGLKTSSLHFVPMSALKGDNVVNKSERSPWYAGQSLMEILETVEIAADRNLDDMRFPVQYVNRPNLNFRGFAGTLASGVVRKGDEVVALPSGKGSKVKSIVTFEGELEQAGPGQAVTLTLEDEIDVSRGD...
2.7.1.25; 2.7.7.4
null
cellular response to sulfate starvation [GO:0009970]; hydrogen sulfide biosynthetic process [GO:0070814]; phosphorylation [GO:0016310]; sulfate assimilation [GO:0000103]; sulfur compound metabolic process [GO:0006790]
null
adenylylsulfate kinase activity [GO:0004020]; ATP binding [GO:0005524]; GTP binding [GO:0005525]; GTPase activity [GO:0003924]; sulfate adenylyltransferase (ATP) activity [GO:0004781]; translation elongation factor activity [GO:0003746]
PF01583;PF00009;
3.40.50.300;2.40.30.10;
APS kinase family; TRAFAC class translation factor GTPase superfamily, Classic translation factor GTPase family, CysN/NodQ subfamily
null
null
CATALYTIC ACTIVITY: Reaction=ATP + H(+) + sulfate = adenosine 5'-phosphosulfate + diphosphate; Xref=Rhea:RHEA:18133, ChEBI:CHEBI:15378, ChEBI:CHEBI:16189, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:58243; EC=2.7.7.4; CATALYTIC ACTIVITY: Reaction=adenosine 5'-phosphosulfate + ATP = 3'-phosphoadenylyl sulfate + AD...
null
PATHWAY: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from sulfate: step 1/3.; PATHWAY: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from sulfate: step 2/3.
null
null
FUNCTION: With CysD forms the ATP sulfurylase (ATPS) that catalyzes the adenylation of sulfate producing adenosine 5'-phosphosulfate (APS) and diphosphate, the first enzymatic step in sulfur assimilation pathway. APS synthesis involves the formation of a high-energy phosphoric-sulfuric acid anhydride bond driven by GTP...
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
O50406
DITCY_MYCTU
METFRTLLAKAALGNGISSTAYDTAWVAKLGQLDDELSDLALNWLCERQLPDGSWGAEFPFCYEDRLLSTLAAMISLTSNKHRRRRAAQVEKGLLALKNLTSGAFEGPQLDIKDATVGFELIAPTLMAEAARLGLAICHEESILGELVGVREQKLRKLGGSKINKHITAAFSVELAGQDGVGMLDVDNLQETNGSVKYSPSASAYFALHVKPGDKRALAYISSIIQAGDGGAPAFYQAEIFEIVWSLWNLSRTDIDLSDPEIVRTYLPYLDHVEQHWVRGRGVGWTGNSTLEDCDTTSVAYDVLSKFGRSPDIGAVLQFE...
5.5.1.16
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:19618417};
cellular response to magnesium starvation [GO:0010350]; geranylgeranyl diphosphate metabolic process [GO:0033385]; gibberellin biosynthetic process [GO:0009686]; response to host immune response [GO:0052572]; tuberculosinol biosynthetic process [GO:0035440]
null
halimadienyl-diphosphate synthase activity [GO:0035439]; magnesium ion binding [GO:0000287]; terpene synthase activity [GO:0010333]
PF00432;PF13243;
1.50.10.160;1.50.10.20;
Terpene synthase family
null
null
CATALYTIC ACTIVITY: Reaction=geranylgeranyl diphosphate = tuberculosinyl diphosphate; Xref=Rhea:RHEA:25621, ChEBI:CHEBI:57533, ChEBI:CHEBI:58822; EC=5.5.1.16; Evidence={ECO:0000269|PubMed:15719101, ECO:0000269|PubMed:19618417};
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=11.7 uM for GGPP (at 30 degrees Celsius and pH 7.5) {ECO:0000269|PubMed:19618417}; Vmax=186 nmol/min/mg enzyme (at 30 degrees Celsius and pH 7.5) {ECO:0000269|PubMed:19618417};
null
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5. Enzyme activity is not detected at pH values above 9.0. {ECO:0000269|PubMed:19618417};
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 30 degrees Celsius. {ECO:0000269|PubMed:19618417};
FUNCTION: Catalyzes the formation of tuberculosinyl diphosphate from geranylgeranyl diphosphate (GGPP). It could also react with (14R/S)-14,15-oxidoGGPP to generate 3alpha- and 3beta-hydroxytuberculosinyl diphosphate. {ECO:0000269|PubMed:15719101, ECO:0000269|PubMed:19618417}.
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
O50580
DT3E_PSECI
MNKVGMFYTYWSTEWMVDFPATAKRIAGLGFDLMEISLGEFHNLSDAKKRELKAVADDLGLTVMCCIGLKSEYDFASPDKSVRDAGTEYVKRLLDDCHLLGAPVFAGLTFCAWPQSPPLDMKDKRPYVDRAIESVRRVIKVAEDYGIIYALEVVNRFEQWLCNDAKEAIAFADAVDSPACKVQLDTFHMNIEETSFRDAILACKGKMGHFHLGEANRLPPGEGRLPWDEIFGALKEIGYDGTIVMEPFMRKGGSVSRAVGVWRDMSNGATDEEMDERARRSLQFVRDKLA
5.1.3.31
COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:17936787, ECO:0000269|PubMed:25655925, ECO:0000269|Ref.2};
null
null
isomerase activity [GO:0016853]; metal ion binding [GO:0046872]
PF01261;
3.20.20.150;
Hyi family
null
null
CATALYTIC ACTIVITY: Reaction=keto-D-tagatose = keto-D-sorbose; Xref=Rhea:RHEA:43048, ChEBI:CHEBI:13022, ChEBI:CHEBI:47693; EC=5.1.3.31; Evidence={ECO:0000269|PubMed:25655925, ECO:0000269|Ref.2}; CATALYTIC ACTIVITY: Reaction=D-allulose = keto-D-fructose; Xref=Rhea:RHEA:42360, ChEBI:CHEBI:27605, ChEBI:CHEBI:48095; EC=5.1...
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=55 mM for D-tagatose {ECO:0000269|Ref.2}; Vmax=30 umol/min/mg enzyme with D-tagatose as substrate {ECO:0000269|Ref.2};
null
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is between 7 and 9 at 30 degrees Celsius. The enzyme is stable from 7 to 11 at 30 degrees Celsius. {ECO:0000269|Ref.2};
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is around 60 degrees Celsius. The enzyme is stable up to 60 degrees Celsius for 10 minutes. {ECO:0000269|Ref.2};
FUNCTION: Catalyzes the epimerization of various ketoses at the C(3) position. It is able to interconvert D-tagatose and D-ribulose to D-sorbose and D-xylulose, respectively. The enzyme is also able to accept other ketopentoses such as D-psicose with lower efficiency. {ECO:0000269|PubMed:17936787, ECO:0000269|PubMed:25...
Pseudomonas cichorii
O50657
DCLO_SELRU
MKNFRLSEKEVKTLAKRIPTPFLVASLDKVEENYQFMRRHLPRAGVFYAMKANPTPEILSLLAGLGSHFDVASAGEMEILHELGVDGSQMIYANPVKDARGLKAAADYNVRRFTFDDPSEIDKMAKAVPGADVLVRIAVRNNKALVDLNTKFGAPVEEALDLLKAAQDAGLHAMGICFHVGSQSLSTAAYEEALLVARRLFDEAEEMGMHLTDLDIGGGFPVPDAKGLNVDLAAMMEAINKQIDRLFPDTAVWTEPGRYMCGTAVNLVTSVIGTKTRGEQPWYILDEGIYGCFSGIMYDHWTYPLHCFGKGNKKPSTFGG...
4.1.1.17; 4.1.1.18
COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
putrescine biosynthetic process from ornithine [GO:0033387]; spermidine biosynthetic process [GO:0008295]
cytoplasm [GO:0005737]
lysine decarboxylase activity [GO:0008923]; ornithine decarboxylase activity [GO:0004586]
PF02784;PF00278;
3.20.20.10;
Orn/Lys/Arg decarboxylase class-II family
null
null
CATALYTIC ACTIVITY: Reaction=H(+) + L-lysine = cadaverine + CO2; Xref=Rhea:RHEA:22352, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:32551, ChEBI:CHEBI:58384; EC=4.1.1.18; CATALYTIC ACTIVITY: Reaction=H(+) + L-ornithine = CO2 + putrescine; Xref=Rhea:RHEA:22964, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:4691...
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.5 mM for L-lysine; KM=0.96 mM for L-ornithine;
PATHWAY: Amine and polyamine biosynthesis; putrescine biosynthesis via L-ornithine pathway; putrescine from L-ornithine: step 1/1.
null
null
FUNCTION: Decarboxylates both L-lysine and L-ornithine with similar catalytic efficiency.
Selenomonas ruminantium
O51312
ENO_BORBU
MGFHIYEIKARQIIDSRGNPTVEADVILEDGTYGRAAVPSGASTGINEAVELRDGDKSVYMGKGVLKAIENIKNIIAPELEGMSALNQVAIDRKMLELDGTPTKEKLGANAILAVSMATAKAAAKYLGLRPYQYLGAYKANILPTPMCNIINGGAHSDNSVDFQEFMIMPIGAKTFSEAIRMAAEVFHTLKGILSGKGYATSVGDEGGFAPNLKSNEEACEVIIEAIKKAGYEPGKDIAIALDPATSELYDPKTKKYVLKWSTKEKLTSEQMVEYWAKWVEKYPIISIEDGMAEEDWDGWKKLTDKIGNKIQLVGDDLFV...
4.2.1.11
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_00318}; Note=Binds a second Mg(2+) ion via substrate during catalysis. {ECO:0000255|HAMAP-Rule:MF_00318};
evasion of host immune response [GO:0042783]; gluconeogenesis [GO:0006094]; glycolytic process [GO:0006096]; symbiont entry into host [GO:0044409]
cell surface [GO:0009986]; cytosol [GO:0005829]; external side of cell outer membrane [GO:0031240]; extracellular region [GO:0005576]; membrane [GO:0016020]; phosphopyruvate hydratase complex [GO:0000015]
magnesium ion binding [GO:0000287]; phosphopyruvate hydratase activity [GO:0004634]
PF00113;PF03952;
3.20.20.120;3.30.390.10;
Enolase family
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00318}. Secreted {ECO:0000255|HAMAP-Rule:MF_00318}. Cell surface {ECO:0000255|HAMAP-Rule:MF_00318}. Note=Fractions of enolase are present in both the cytoplasm and on the cell surface. {ECO:0000255|HAMAP-Rule:MF_00318}.
CATALYTIC ACTIVITY: Reaction=(2R)-2-phosphoglycerate = H2O + phosphoenolpyruvate; Xref=Rhea:RHEA:10164, ChEBI:CHEBI:15377, ChEBI:CHEBI:58289, ChEBI:CHEBI:58702; EC=4.2.1.11; Evidence={ECO:0000255|HAMAP-Rule:MF_00318};
null
PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 4/5. {ECO:0000255|HAMAP-Rule:MF_00318}.
null
null
FUNCTION: Catalyzes the reversible conversion of 2-phosphoglycerate (2-PG) into phosphoenolpyruvate (PEP). It is essential for the degradation of carbohydrates via glycolysis. {ECO:0000255|HAMAP-Rule:MF_00318}.
Borreliella burgdorferi (strain ATCC 35210 / DSM 4680 / CIP 102532 / B31) (Borrelia burgdorferi)
O51934
RGYR_THEMA
MAVNSKYHHSCINCGGLNTDERNERGLPCEVCLPEDSPSDIYRALLERKTLKEYRFYHEFWNEYEDFRSFFKKKFGKDLTGYQRLWAKRIVQGKSFTMVAPTGVGKTTFGMMTALWLARKGKKSALVFPTVTLVKQTLERLQKLADEKVKIFGFYSSMKKEEKEKFEKSFEEDDYHILVFSTQFVSKNREKLSQKRFDFVFVDDVDAVLKASRNIDTLLMMVGIPEEIIRKAFSTIKQGKIYERPKNLKPGILVVSSATAKPRGIRPLLFRDLLNFTVGRLVSVARNITHVRISSRSKEKLVELLEIFRDGILIFAQTEE...
5.6.2.-
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|HAMAP-Rule:MF_01125, ECO:0000269|PubMed:23209025, ECO:0000312|PDB:7FSE, ECO:0000312|PDB:7FSF, ECO:0000312|PDB:8OFB, ECO:0007744|PDB:4DDT, ECO:0007744|PDB:4DDU, ECO:0007744|PDB:4DDV, ECO:0007744|PDB:4DDW, ECO:0007744|PDB:4DDX}; Note=Binds 2 zinc ions p...
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;PF17915;
2.60.510.20;3.30.56.80;3.40.50.140;3.40.50.300;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, ECO:0000269|PubMed:18614530};
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=44 uM for ATP without DNA {ECO:0000269|PubMed:21051354}; KM=12 uM for ATP with 60 base ssDNA {ECO:0000269|PubMed:21051354}; KM=16 uM for ATP with 60 bp dsDNA {ECO:0000269|PubMed:21051354}; KM=15.6 uM for ATP with negatively supercoiled plasmid dsDNA {ECO:0000269|Pu...
null
null
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 90 degrees Celsius for production of positive supercoils (PubMed:9440516). Thermostable for at least 4 hours at 85 degrees Celsius (PubMed:9440516). Optimum temperature is 65 degrees Celsius for ATPase activity (PubMed:18614530). The necessi...
FUNCTION: Modifies the topological state of DNA by introducing positive supercoils in an ATP-dependent process (PubMed:18614530, PubMed:21051354, PubMed:23209025, PubMed:9440516). Increases the linking number in steps of +1 (Probable) (PubMed:23209025). Probably recognizes regions with a low GC content which melt and f...
Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8)
O52063
ATZC_PSESD
MSKDFDLIIRNAYLSEKDSVYDIGIVGDRIIKIEAKIEGTVKDEIDAKGNLVSPGFVDAHTHMDKSFTSTGERLPKFWSRPYTRDAAIEDGLKYYKNATHEEIKRHVIEHAHMQVLHGTLYTRTHVDVDSVAKTKAVEAVLEAKEELKDLIDIQVVAFAQSGFFVDLESESLIRKSLDMGCDLVGGVDPATRENNVEGSLDLCFKLAKEYDVDIDYHIHDIGTVGVYSINRLAQKTIENGYKGRVTTSHAWCFADAPSEWLDEAIPLYKDSGMKFVTCFSSTPPTMPVIKLLEAGINLGCASDNIRDFWVPFGNGDMVQG...
3.5.4.42
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:12218024, ECO:0000269|PubMed:26390431, ECO:0000269|Ref.3}; Note=Binds 1 Zn(2+) ion per subunit. {ECO:0000269|PubMed:12218024, ECO:0000269|PubMed:26390431, ECO:0000269|Ref.3};
atrazine catabolic process [GO:0019381]
cytoplasm [GO:0005737]
hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amidines [GO:0016814]; metal ion binding [GO:0046872]; N-isopropylammelide isopropylaminohydrolase activity [GO:0018764]
PF07969;
3.20.20.140;2.30.40.10;
Metallo-dependent hydrolases superfamily, N-acyl-D-amino-acid deacylase family
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CATALYTIC ACTIVITY: Reaction=H(+) + H2O + N-isopropylammelide = cyanurate + isopropylamine; Xref=Rhea:RHEA:23608, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17247, ChEBI:CHEBI:38028, ChEBI:CHEBI:57492; EC=3.5.4.42; Evidence={ECO:0000269|PubMed:12218024, ECO:0000269|PubMed:26390431};
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=817 uM for N-methylammelide {ECO:0000269|PubMed:12218024}; KM=308 uM for N-ethylammelide {ECO:0000269|PubMed:12218024}; KM=3860 uM for N-hydroxyethylammelide {ECO:0000269|PubMed:12218024}; KM=406 uM for N-isopropylammelide {ECO:0000269|PubMed:12218024}; KM=580 uM f...
PATHWAY: Xenobiotic degradation; atrazine degradation; cyanurate from atrazine: step 3/3.
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.25. {ECO:0000269|PubMed:26390431};
null
FUNCTION: Transforms N-isopropylammelide to cyanuric acid and isopropylamine. {ECO:0000269|PubMed:12218024, ECO:0000269|PubMed:9422605}.
Pseudomonas sp. (strain ADP)
O52378
NAGAA_RALSP
MELVVEPLNLHLNAETGSTLLDVLRSNEVPISYSCMSGRCGTCRCRVIAGHLRDNGPETGRPQAGKGTYVLACQAVLTEDCTIEIPESDEIVVHPARIVKGTVTAIDEATHDIRRLRIKLAKPLEFSPGQYATVQFTPECVRPYSMAGLPSDAEMEFQIRAVPGGHVSNYVFNELSVGASVRISGPLGTAYLRRTHTGPMLCVGGGTGLAPVLSIVRGALESGMSNPIHLYFGVRSEQDIYDEERLHALAARFPNLKVNVVVATGPAGPGRRSGLVTDLIGRDLPNLAGWRAYLCGAPAMVEALNLLVARLGIVPGHIHA...
1.18.1.7
COFACTOR: Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; Evidence={ECO:0000250|UniProtKB:Q52126, ECO:0000255|PROSITE-ProRule:PRU00465}; Note=Binds 1 [2Fe-2S] cluster. {ECO:0000255|PROSITE-ProRule:PRU00465}; COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250|UniProtKB:Q52126};
electron transport chain [GO:0022900]; naphthalene catabolic process [GO:1901170]; salicylic acid catabolic process [GO:0046244]
catalytic complex [GO:1902494]
2 iron, 2 sulfur cluster binding [GO:0051537]; ferredoxin-NAD+ reductase activity [GO:0008860]; ferredoxin-NADP+ reductase activity [GO:0004324]; metal ion binding [GO:0046872]
PF00970;PF00111;PF00175;
3.10.20.30;3.40.50.80;2.40.30.10;
Bacterial ring-hydroxylating dioxygenase ferredoxin reductase family
null
null
CATALYTIC ACTIVITY: Reaction=H(+) + NAD(+) + 2 reduced [2Fe-2S]-[ferredoxin] = NADH + 2 oxidized [2Fe-2S]-[ferredoxin]; Xref=Rhea:RHEA:16521, Rhea:RHEA-COMP:10000, Rhea:RHEA-COMP:10001, ChEBI:CHEBI:15378, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.18.1.7; Evidence={ECO:0000269|PubM...
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PATHWAY: Aromatic compound metabolism; naphthalene degradation. {ECO:0000269|PubMed:11872705, ECO:0000269|PubMed:9573207}.
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FUNCTION: Component of two multicomponent enzyme systems which are involved in the catabolism of naphthalene (PubMed:11872705, PubMed:9573207). Plays a role as an electron transfer component for both salicylate 5-hydroxylase (S5H) and naphthalene 1,2-dioxygenase (NDO) systems, by transferring electrons from NAD(P)H to ...
Ralstonia sp