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 |
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
I6LNY0 | BSR_PSEPU | MPFRRTLLAASLVLLITGQAPLYAAPPLSMDNGTNALTVQNSNAWVEVSASALQHNIRTLQAELAGKSRLCAVLKADAYGHGIGLVMPSIIAQGVPCVAVASNEEARVVRASGFTGQLVRVRAASLSELEDALQYDMEELVGSAEFARQADAIAARHGKTLRIHLAFNSSGMSRNGVEMATWSGRGEALQITDQKHLELVALMTHFAVEDKDDVRKGLAAFNEQTDWLIKHARLDRSKLTLHAANSFATLEVPEARLDMVRTGGALFGDTVPGRTEYKRAMQFKSRVAAVHSYPAGNTVGYDRTFTLARDSRLANITVGY... | 5.1.1.10 | COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000255|HAMAP-Rule:MF_02212, ECO:0000269|PubMed:22806802, ECO:0000269|PubMed:23118975}; | peptidoglycan biosynthetic process [GO:0009252] | cytosol [GO:0005829]; periplasmic space [GO:0042597] | alanine racemase activity [GO:0008784]; arginine racemase activity [GO:0047679]; lysine racemase activity [GO:0018113]; pyridoxal phosphate binding [GO:0030170] | PF00842;PF01168; | 3.20.20.10; | Alanine racemase family, Bsr subfamily | null | SUBCELLULAR LOCATION: Periplasm {ECO:0000250|UniProtKB:Q88GJ9, ECO:0000255|HAMAP-Rule:MF_02212}. | CATALYTIC ACTIVITY: Reaction=an L-alpha-amino acid = a D-alpha-amino acid; Xref=Rhea:RHEA:18317, ChEBI:CHEBI:59869, ChEBI:CHEBI:59871; EC=5.1.1.10; Evidence={ECO:0000255|HAMAP-Rule:MF_02212, ECO:0000269|PubMed:23118975}; CATALYTIC ACTIVITY: Reaction=L-lysine = D-lysine; Xref=Rhea:RHEA:22864, ChEBI:CHEBI:32551, ChEBI:CH... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=10.34 mM for L-alanine {ECO:0000269|PubMed:22806802}; KM=25.4 mM for L-lysine {ECO:0000269|PubMed:23118975}; KM=14.5 mM for L-arginine {ECO:0000269|PubMed:23118975}; Vmax=18.73 mmol/min/mg enzyme with L-alanine as substrate {ECO:0000269|PubMed:22806802}; Note=kcat ... | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 9.0. {ECO:0000269|PubMed:22806802}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 37 degrees Celsius. {ECO:0000269|PubMed:22806802}; | FUNCTION: Amino-acid racemase that catalyzes the interconversion of L-lysine and D-lysine, and L-arginine and D-arginine (PubMed:23118975). To a lesser extent, is also able to interconvert alanine and isoleucine enantiomers (PubMed:22806802, PubMed:23118975). {ECO:0000269|PubMed:22806802, ECO:0000269|PubMed:23118975}. | Pseudomonas putida (Arthrobacter siderocapsulatus) |
I6PL68 | HEI10_ORYSJ | MKCNACWRELEGQAVSTTCGHLLCTEDAKKILSNDAACPICDQVLSKSHMRPVDTNPNDDWTNMSMAGVSPQILMKSAYRSVMFYIGQKELEMQYKMNRIVGQCRQKCELMQAKFTEKLEEVHTAYQKMAKKCQLMEQEVENLSRDKQELQEKFAEKSRQKRKLDEMYDQLRSEYESAKRSAIQPANNYFPRAQPDLFSGVPNIMDSSDPLRQGLAGLPETPGRRDEGWAPPPRQRRSTSGPFELSAGSPAHNAAPPVDIRPRQPARPVFGTAMNNTSAALRNMIISPVKRPQLSRNRPHMFT | 2.3.2.27 | null | chiasma assembly [GO:0051026]; homologous chromosome pairing at meiosis [GO:0007129]; protein ubiquitination [GO:0016567]; reciprocal meiotic recombination [GO:0007131] | chiasma [GO:0005712]; chromosome [GO:0005694] | metal ion binding [GO:0046872]; transferase activity [GO:0016740] | PF14634; | 3.30.40.10; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:22792078}. Chromosome {ECO:0000269|PubMed:22792078}. Note=Dynamic localization on the meiotic chromosomes. Initially appears as distinct foci. Later observed along the chromosomes and finally restrict to prominent foci that specially localize to chiasma sites. Extends a... | 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. {ECO:0000305}. | null | null | FUNCTION: Ubiquitin E3 ligase required for class I crossover (CO) formation during meiosis. {ECO:0000269|PubMed:22792078}. | Oryza sativa subsp. japonica (Rice) |
I6VSD2 | TM147_CAPHI | MTLFHFGNCFALAYFPYFITYKCSGLSEYNAFWKCVQAGVTYLFVQLCKMLFLATFFPTWEGGIYDFIGEFMKASVDVADLIGLNLVMSRNAGKGEYKIMVAALGWATAELIMSRCIPLWVGARGIEFDWKYIQMSIDSNISLVHYIVASAQVWMITRYDLYHTYRPAVLLLMFLSVYKAFVMETFVHLCSLGSWTALLARALVTGLLALSTLALYVAVVNVHS | null | null | multi-pass transmembrane protein insertion into ER membrane [GO:0160063]; protein localization to nuclear inner membrane [GO:0036228]; regulation of apoptotic process [GO:0042981]; regulation of cytokine production [GO:0001817]; regulation of mononuclear cell proliferation [GO:0032944]; regulation of nitric oxide biosy... | endoplasmic reticulum membrane [GO:0005789]; nuclear membrane [GO:0031965]; plasma membrane [GO:0005886] | ribosome binding [GO:0043022] | PF09767; | null | TMEM147 family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9BVK8}; Multi-pass membrane protein {ECO:0000255}. Nucleus membrane {ECO:0000250|UniProtKB:Q9BVK8}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000269|PubMed:27337943}; Multi-pass membrane protein {ECO:0000255}. | null | null | null | null | null | FUNCTION: Component of the multi-pass translocon (MPT) complex that mediates insertion of multi-pass membrane proteins into the lipid bilayer of membranes. The MPT complex takes over after the SEC61 complex: following membrane insertion of the first few transmembrane segments of proteins by the SEC61 complex, the MPT c... | Capra hircus (Goat) |
I6WU39 | OLIAC_CANSA | MAVKHLIVLKFKDEITEAQKEEFFKTYVNLVNIIPAMKDVYWGKDVTQKNKEEGYTHIVEVTFESVETIQDYIIHPAHVGFGDVYRSFWEKLLIFDYTPRK | 4.4.1.26 | null | cannabinoid biosynthetic process [GO:1901696]; olivetolic acid biosynthetic process [GO:1901697]; pollen tube adhesion [GO:0009865]; terpenoid biosynthetic process [GO:0016114] | cytoplasm [GO:0005737] | cyclase activity [GO:0009975]; lyase activity [GO:0016829]; metal ion binding [GO:0046872] | PF07876; | 3.30.70.100; | null | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22802619}. | CATALYTIC ACTIVITY: Reaction=3,5,7-trioxododecanoyl-CoA = CoA + H(+) + olivetolate; Xref=Rhea:RHEA:34123, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:66950, ChEBI:CHEBI:66957; EC=4.4.1.26; Evidence={ECO:0000269|PubMed:22802619, ECO:0000269|PubMed:26783002}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:341... | null | PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis. {ECO:0000303|PubMed:30468448}. | null | null | FUNCTION: Involved in the biosynthesis of cannabinoids-related terpenophenolic natural products, which have pharmacological activity (PubMed:22802619). Polyketide cyclase which functions in concert with OLS/TKS to form olivetolic acid (PubMed:22802619, PubMed:26783002). Has no intrinsic polyketide synthase activity and... | Cannabis sativa (Hemp) (Marijuana) |
I6WXK4 | PTPB_MYCTU | MAVRELPGAWNFRDVADTATALRPGRLFRSSELSRLDDAGRATLRRLGITDVADLRSSREVARRGPGRVPDGIDVHLLPFPDLADDDADDSAPHETAFKRLLTNDGSNGESGESSQSINDAATRYMTDEYRQFPTRNGAQRALHRVVTLLAAGRPVLTHCFAGKDRTGFVVALVLEAVGLDRDVIVADYLRSNDSVPQLRARISEMIQQRFDTELAPEVVTFTKARLSDGVLGVRAEYLAAARQTIDETYGSLGGYLRDAGISQATVNRMRGVLLG | 3.1.3.-; 3.1.3.16; 3.1.3.48 | null | dephosphorylation [GO:0016311]; symbiont-mediated suppression of host defense-related programmed cell death [GO:0034054]; symbiont-mediated suppression of host inflammatory response [GO:0052036] | extracellular region [GO:0005576]; host cell cytoplasm [GO:0030430]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020] | myosin phosphatase activity [GO:0017018]; phosphatase activity [GO:0016791]; phosphatidylinositol-4,5-bisphosphate phosphatase activity [GO:0106019]; phosphatidylinositol-4-phosphate phosphatase activity [GO:0043812]; protein tyrosine phosphatase activity [GO:0004725]; ubiquitin binding [GO:0043130] | PF13350; | 3.90.190.10; | Protein-tyrosine phosphatase family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10986245}. Host cytoplasm {ECO:0000269|PubMed:36227980}. Host cell membrane {ECO:0000269|PubMed:36227980}. Note=Further investigation is required to determine whether PtpB is direct substrate for SecA2, the ESX/type VII secretion system, or an alternate mechanism. {ECO... | CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620; EC=3.1.3.48; Evidence={ECO:0000269|PubMed:10986245, ECO:0000269|PubMed:1627188... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.291 mM for P-tyr {ECO:0000269|PubMed:17584180}; KM=0.44 mM for P-Ser {ECO:0000269|PubMed:17584180}; KM=0.253 mM for P-Thr {ECO:0000269|PubMed:17584180}; KM=0.217 mM for P-Tyr insulin {ECO:0000269|PubMed:17584180}; KM=0.327 mM for P-Tyr EGFR {ECO:0000269|PubMed:17... | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is near 5.5. {ECO:0000269|PubMed:16271885}; | null | FUNCTION: Essential virulence factor that promotes mycobacterial survival within host macrophages (PubMed:14617138, PubMed:16256440, PubMed:20167798, PubMed:29888212, PubMed:36227980). Acts as a phosphatase that possesses triple substrate specificity toward phosphotyrosine, phosphoserine/threonine and phosphoinositides... | Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) |
I6WZG6 | ENCAP_MYCTU | MNNLYRDLAPVTEAAWAEIELEAARTFKRHIAGRRVVDVSDPGGPVTAAVSTGRLIDVKAPTNGVIAHLRASKPLVRLRVPFTLSRNEIDDVERGSKDSDWEPVKEAAKKLAFVEDRTIFEGYSAASIEGIRSASSNPALTLPEDPREIPDVISQALSELRLAGVDGPYSVLLSADVYTKVSETSDHGYPIREHLNRLVDGDIIWAPAIDGAFVLTTRGGDFDLQLGTDVAIGYASHDTDTVRLYLQETLTFLCYTAEASVALSH | null | null | null | encapsulin nanocompartment [GO:0140737]; extracellular region [GO:0005576]; plasma membrane [GO:0005886] | null | PF04454; | 3.30.2400.30;3.30.2320.10; | Encapsulin family, Family 1 subfamily | PTM: The initiator methionine is partially removed. When isolated from culture filtrate isoelectric focusing gives 3 bands, none of which are glycosylated. {ECO:0000269|PubMed:9596740}. | SUBCELLULAR LOCATION: Encapsulin nanocompartment {ECO:0000269|PubMed:24855650}. Secreted {ECO:0000269|PubMed:9596740}. Cell membrane {ECO:0000269|PubMed:9596740}; Peripheral membrane protein {ECO:0000269|PubMed:9596740}. Note=Encapsulin microcompartments of this protein encapsulating DyP are found in situ (PubMed:34751... | null | null | null | null | null | FUNCTION: Shell component of a type 1 encapsulin nanocompartment in situ; its cargo protects against oxidative stress at low pH. In situ and in E.coli assembles into proteinaceous shells about 22 nm in diameter with 2.5 nm thick walls (PubMed:24855650, PubMed:34751132). Cargo proteins are targeted to the interior via t... | Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) |
I6X235 | ADPP_MYCTU | MAEHDFETISSETLHTGAIFALRRDQVRMPGGGIVTREVVEHFGAVAIVAMDDNGNIPMVYQYRHTYGRRLWELPAGLLDVAGEPPHLTAARELREEVGLQASTWQVLVDLDTAPGFSDESVRVYLATGLREVGRPEAHHEEADMTMGWYPIAEAARRVLRGEIVNSIAIAGVLAVHAVTTGFAQPRPLDTEWIDRPTAFAARRAER | 3.6.1.13; 3.6.1.58 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:12906832, ECO:0000269|PubMed:27683242}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:27683242}; Note=Binds 3 Mg(2+) ions per subunit (PubMed:12906832). Activity is highest with Mn(2+). Can also use Zn(2+) or Co(2+), with lo... | DNA repair [GO:0006281]; DNA replication [GO:0006260]; nucleoside phosphate metabolic process [GO:0006753]; ribose phosphate metabolic process [GO:0019693] | cytosol [GO:0005829] | 8-oxo-dGDP phosphatase activity [GO:0044715]; 8-oxo-GDP phosphatase activity [GO:0044716]; ADP-ribose diphosphatase activity [GO:0047631]; ADP-sugar diphosphatase activity [GO:0019144]; bis(5'-adenosyl)-pentaphosphatase activity [GO:0034432]; guanosine-3',5'-bis(diphosphate) 3'-diphosphatase activity [GO:0008893]; meta... | PF00293; | 3.90.79.10; | Nudix hydrolase family | null | null | CATALYTIC ACTIVITY: Reaction=ADP-D-ribose + H2O = AMP + D-ribose 5-phosphate + 2 H(+); Xref=Rhea:RHEA:10412, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57967, ChEBI:CHEBI:78346, ChEBI:CHEBI:456215; EC=3.6.1.13; Evidence={ECO:0000269|PubMed:27683242}; CATALYTIC ACTIVITY: Reaction=8-oxo-dGDP + H2O = 8-oxo-dGMP + H... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=200 uM for ADPR (in the presence of Mg(2+) ions) {ECO:0000269|PubMed:27683242}; KM=554 uM for ADPR (in the presence of Mn(2+) ions) {ECO:0000269|PubMed:27683242}; KM=9.5 uM for 8-oxo-dGDP {ECO:0000269|PubMed:23463507}; Vmax=0.04 pmol/min/ng enzyme with 8-oxo-dGDP a... | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.0. {ECO:0000269|PubMed:27683242}; | null | FUNCTION: Catalyzes the hydrolysis of ADP-ribose (ADPR) to AMP and ribose-5-phosphate. Can also hydrolyze ADP-mannose and ADP-glucose, with lower efficiency. Has weaker activity with NAD, GDP-sugars and UDP-sugars (PubMed:27683242). Also catalyzes the conversion of 8-oxo-dGDP to 8-oxo-dGMP, and 8-oxo-GDP to 8-oxo-GMP. ... | Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) |
I6X8D2 | PKS13_MYCTU | MADVAESQENAPAERAELTVPEMRQWLRNWVGKAVGKAPDSIDESVPMVELGLSSRDAVAMAADIEDLTGVTLSVAVAFAHPTIESLATRIIEGEPETDLAGDDAEDWSRTGPAERVDIAIVGLSTRFPGEMNTPEQTWQALLEGRDGITDLPDGRWSEFLEEPRLAARVAGARTRGGYLKDIKGFDSEFFAVAKTEADNIDPQQRMALELTWEALEHARIPASSLRGQAVGVYIGSSTNDYSFLAVSDPTVAHPYAITGTSSSIIANRVSYFYDFHGPSVTIDTACSSSLVAIHQGVQALRNGEADVVVAGGVNALITP... | 2.3.1.- | null | DIM/DIP cell wall layer assembly [GO:0071770]; fatty acid biosynthetic process [GO:0006633]; secondary metabolite biosynthetic process [GO:0044550] | cytoplasm [GO:0005737]; plasma membrane [GO:0005886] | 3-oxoacyl-[acyl-carrier-protein] synthase activity [GO:0004315]; fatty acid synthase activity [GO:0004312]; phosphopantetheine binding [GO:0031177] | PF00698;PF16197;PF00109;PF02801;PF00550;PF00975; | 3.40.47.10;1.10.1200.10;3.40.50.1820;3.30.70.250;3.40.366.10; | null | PTM: 4'-phosphopantetheine is transferred from CoA to specific serines of apo-Pks13 by PptT. {ECO:0000269|PubMed:16709676, ECO:0000269|PubMed:19436070}. | null | null | null | PATHWAY: Lipid metabolism; mycolic acid biosynthesis. {ECO:0000269|PubMed:19436070, ECO:0000269|PubMed:23770708, ECO:0000269|PubMed:25467124}. | null | null | FUNCTION: Involved in the biosynthesis of mycolic acids (PubMed:19436070, PubMed:23770708, PubMed:25467124). Forms, with FadD32, the initiation module of the mycolic condensation system (PubMed:19436070, PubMed:19477415, PubMed:25467124). Synthesizes, in coupled reaction with FadD32, the biosynthetic precursors of myco... | Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) |
I6XD65 | PNCA_MYCTU | MRALIIVDVQNDFCEGGSLAVTGGAALARAISDYLAEAADYHHVVATKDFHIDPGDHFSGTPDYSSSWPPHCVSGTPGADFHPSLDTSAIEAVFYKGAYTGAYSGFEGVDENGTPLLNWLRQRGVDEVDVVGIATDHCVRQTAEDAVRNGLATRVLVDLTAGVSADTTVAALEEMRTASVELVCSS | 3.5.1.-; 3.5.1.19 | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:18201201}; Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000269|PubMed:18201201, ECO:0000269|PubMed:21283666}; Note=PncA contains Mn(2+) and Fe(2+) in a molecular ratio of 1:1. PncA has only one metal center. It is believed that PncA bind... | nicotinamide metabolic process [GO:0006769]; pyridine nucleotide biosynthetic process [GO:0019363]; response to antibiotic [GO:0046677]; xenobiotic metabolic process [GO:0006805] | null | ferrous iron binding [GO:0008198]; manganese ion binding [GO:0030145]; nicotinamidase activity [GO:0008936] | PF00857; | 3.40.50.850; | Isochorismatase family | null | null | CATALYTIC ACTIVITY: Reaction=H2O + nicotinamide = NH4(+) + nicotinate; Xref=Rhea:RHEA:14545, ChEBI:CHEBI:15377, ChEBI:CHEBI:17154, ChEBI:CHEBI:28938, ChEBI:CHEBI:32544; EC=3.5.1.19; Evidence={ECO:0000269|PubMed:18201201}; CATALYTIC ACTIVITY: Reaction=H2O + pyrazinamide = NH4(+) + pyrazine-2-carboxylate; Xref=Rhea:RHEA:... | null | PATHWAY: Cofactor biosynthesis; nicotinate biosynthesis; nicotinate from nicotinamide: step 1/1. {ECO:0000250|UniProtKB:P21369}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.0 for the hydrolysis of nicotinamide. The enzyme activity decreases rapidly below pH 6.0 or above pH 8.0. {ECO:0000269|PubMed:18201201}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 40 degrees Celsius for the hydrolysis of nicotinamide. Below 25 or above 70 degrees Celsius, the enzyme loses its activity rapidly. {ECO:0000269|PubMed:18201201}; | FUNCTION: Catalyzes the deamidation of nicotinamide (NAM) into nicotinate (PubMed:18201201). Likely functions in the cyclical salvage pathway for production of NAD from nicotinamide (By similarity). {ECO:0000250|UniProtKB:P21369, ECO:0000269|PubMed:18201201}.; FUNCTION: Is involved in the activation of the first-line a... | Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) |
I6XD69 | PKS12_MYCTU | MVDQLQHATEALRKALVQVERLKRTNRALLERSSEPIAIVGMSCRFPGGVDSPEGLWQMVADARDVMSEFPTDRGWDLAGLFDPDPDVRHKSYARTGGFVDGVADFDPAFFGISPSEALAMDPQHRMLLELSWEALERAGIDPTGLRGSATGVFAGLIVGGYGMLAEEIEGYRLTGMTSSVASGRVAYVLGLEGPAVSVDTACSSSLVALHMAVGSLRSGECDLALAGGVTVNATPTVFVEFSRHRGLAPDGRCKPYAGRADGVGWSEGGGMLVLQRLSDARRLGHPVLAVVVGSAVNQDGASNGLTAPNGPSQQRVVRA... | 2.3.1.295 | null | DIM/DIP cell wall layer assembly [GO:0071770]; fatty acid biosynthetic process [GO:0006633] | cytoplasm [GO:0005737]; plasma membrane [GO:0005886] | 3-oxoacyl-[acyl-carrier-protein] synthase activity [GO:0004315]; fatty acid synthase activity [GO:0004312]; identical protein binding [GO:0042802]; oxidoreductase activity [GO:0016491]; phosphopantetheine binding [GO:0031177] | PF00698;PF08240;PF13602;PF16197;PF00109;PF02801;PF08659;PF21089;PF00550;PF14765; | 3.30.70.3290;3.40.47.10;1.10.1200.10;3.40.366.10;3.90.180.10;3.40.50.720;3.10.129.110; | null | null | null | CATALYTIC ACTIVITY: Reaction=5 (S)-methylmalonyl-CoA + a medium-chain fatty acyl-CoA + 32 H(+) + 5 malonyl-CoA + 22 NADPH = a mycoketide-CoA + 10 CO2 + 10 CoA + 11 H2O + 22 NADP(+); Xref=Rhea:RHEA:58028, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57327, ChEBI:CHEBI:57384, Ch... | null | PATHWAY: Lipid metabolism; fatty acid metabolism. {ECO:0000305}. | null | null | FUNCTION: Involved in the synthesis of beta-D-mannosyl phosphomycoketide (MPM), an antigenic mycobacterial polyketide (PubMed:15611286, PubMed:18613748). Binds a fatty acyl-CoA as a starter unit, and extends it by five rounds of alternative additions of malonyl-CoA and methylmalonyl-CoA extender units. Depending on the... | Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) |
I6XFS7 | RDMTR_MYCTU | MTRIIGGVAGGRRIAVPPRGTRPTTDRVRESLFNIVTARRDLTGLAVLDLYAGSGALGLEALSRGAASVLFVESDQRSAAVIARNIEALGLSGATLRRGAVAAVVAAGTTSPVDLVLADPPYNVDSADVDAILAALGTNGWTREGTVAVVERATTCAPLTWPEGWRRWPQRVYGDTRLELAERLFANV | 2.1.1.-; 2.1.1.171 | null | rRNA methylation [GO:0031167] | extracellular region [GO:0005576]; host cell cytoplasm [GO:0030430]; host cell nucleolus [GO:0044196] | methyltransferase activity [GO:0008168]; nucleic acid binding [GO:0003676] | PF03602; | 3.40.50.150; | Methyltransferase superfamily | PTM: Glycosylated. {ECO:0000269|PubMed:25824946}.; PTM: Phosphorylated (PubMed:25824946). In vitro, is phosphorylated by multiple mycobacterial kinases (PknA, PknB, PknD, PknH, PknJ and PknL) and by mammalian kinases (PubMed:25824946). {ECO:0000269|PubMed:25824946}. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:25824946}. Host cytoplasm {ECO:0000269|PubMed:25824946}. Host nucleus {ECO:0000269|PubMed:25824946}. Host nucleus, host nucleolus {ECO:0000269|PubMed:25824946}. Note=Secreted into the host cell upon mycobacterial infection (PubMed:25824946). Localizes to the nucleus in... | CATALYTIC ACTIVITY: Reaction=guanosine(966) in 16S rRNA + S-adenosyl-L-methionine = H(+) + N(2)-methylguanosine(966) in 16S rRNA + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:23548, Rhea:RHEA-COMP:10211, Rhea:RHEA-COMP:10212, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:74269, ChEBI:CHEBI:74481; E... | null | null | null | null | FUNCTION: SAM-dependent methyltransferase that binds both to RNA and DNA (PubMed:21474448). Specifically methylates the guanine in position 966 of 16S rRNA in the 30S particle (PubMed:21474448). In addition, can methylate and modulate host cellular DNA within an infected mammalian cell, altering the host epigenetic mac... | Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) |
I6XHI4 | FADA5_MYCTU | MGYPVIVEATRSPIGKRNGWLSGLHATELLGAVQKAVVDKAGIQSGLHAGDVEQVIGGCVTQFGEQSNNISRVAWLTAGLPEHVGATTVDCQCGSGQQANHLIAGLIAAGAIDVGIACGIEAMSRVGLGANAGPDRSLIRAQSWDIDLPNQFEAAERIAKRRGITREDVDVFGLESQRRAQRAWAEGRFDREISPIQAPVLDEQNQPTGERRLVFRDQGLRETTMAGLGELKPVLEGGIHTAGTSSQISDGAAAVLWMDEAVARAHGLTPRARIVAQALVGAEPYYHLDGPVQSTAKVLEKAGMKIGDIDIVEINEAFAS... | 2.3.1.16 | null | cholesterol catabolic process [GO:0006707]; fatty acid beta-oxidation [GO:0006635]; phenylacetate catabolic process [GO:0010124] | null | acetyl-CoA C-acyltransferase activity [GO:0003988]; identical protein binding [GO:0042802] | PF02803;PF00108; | 3.40.47.10; | Thiolase-like superfamily, Thiolase family | null | null | 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:0000269|PubMed:19822655, ECO:0000269|PubMed:25482540}; CATALYTIC ACTIVITY: Reaction=3-oxochol-4-en-22-oyl-CoA + acet... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=3.1 uM for CoA {ECO:0000269|PubMed:25482540}; KM=15 uM for CoA {ECO:0000269|PubMed:19822655}; KM=11.8 uM for 3,22-dioxochol-4-en-24-oyl-CoA {ECO:0000269|PubMed:25482540}; KM=464 uM for AcAcCoA {ECO:0000269|PubMed:19822655}; Note=kcat is 0.725 sec(-1) for 3,22-dioxo... | PATHWAY: Steroid metabolism; cholesterol degradation. {ECO:0000269|PubMed:19822655}. | null | null | FUNCTION: Involved in the beta-oxidation of the cholesterol side chain (PubMed:19822655). It is important for utilization of cholesterol as a sole carbon source in vitro and for full virulence in the chronic stage of mouse lung infection (PubMed:19822655). Catalyzes the thiolysis of 3,22-dioxochol-4-en-24-oyl-CoA to yi... | Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) |
I6XU97 | EST45_MYCTU | MLSDDELTGLDEFALLAENAEQAGVNGPLPEVERVQAGAISALRWGGSAPRVIFLHGGGQNAHTWDTVIVGLGEPALAVDLPGHGHSAWREDGNYSPQLNSETLAPVLRELAPGAEFVVGMSLGGLTAIRLAAMAPDLVGELVLVDVTPSALQRHAELTAEQRGTVALMHGEREFPSFQAMLDLTIAAAPHRDVKSLRRGVFHNSRRLDNGNWVWRYDAIRTFGDFAGLWDDVDALSAPITLVRGGSSGFVTDQDTAELHRRATHFRGVHIVEKSGHSVQSDQPRALIEIVRGVLDTR | 3.1.1.1 | null | metabolic process [GO:0008152] | null | carboxylesterase activity [GO:0106435]; hydrolase activity [GO:0016787] | PF12697; | 3.40.50.1820; | AB hydrolase superfamily | null | null | CATALYTIC ACTIVITY: Reaction=a carboxylic ester + H2O = a carboxylate + an alcohol + H(+); Xref=Rhea:RHEA:21164, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29067, ChEBI:CHEBI:30879, ChEBI:CHEBI:33308; EC=3.1.1.1; Evidence={ECO:0000269|PubMed:20957207, ECO:0000269|PubMed:25354081}; CATALYTIC ACTIVITY: Reaction=a ... | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.0 for the hydrolysis of p-nitrophenyl hexanoate. {ECO:0000269|PubMed:20957207}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 39 degrees Celsius for the hydrolysis of p-nitrophenyl hexanoate. {ECO:0000269|PubMed:20957207}; | FUNCTION: Esterase likely involved in ester/lipid metabolism. Shows strong substrate selectivity toward short, straight chain alkyl esters with the highest activity toward four atom chains. The physiological substrate is unknown (PubMed:25354081). Is able to hydrolyze ester bonds within a wide range of p-nitrophenyl de... | Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) |
I6Y0R5 | FOLC_MYCTU | MNSTNSGPPDSGSATGVVPTPDEIASLLQVEHLLDQRWPETRIDPSLTRISALMDLLGSPQRSYPSIHIAGTNGKTSVARMVDALVTALHRRTGRTTSPHLQSPVERISIDGKPISPAQYVATYREIEPLVALIDQQSQASAGKGGPAMSKFEVLTAMAFAAFADAPVDVAVVEVGMGGRWDATNVINAPVAVITPISIDHVDYLGADIAGIAGEKAGIITRAPDGSPDTVAVIGRQVPKVMEVLLAESVRADASVAREDSEFAVLRRQIAVGGQVLQLQGLGGVYSDIYLPLHGEHQAHNAVLALASVEAFFGAGAQRQ... | 6.3.2.12; 6.3.2.17 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P08192}; Note=Binds 2 Mg(2+) ions per subunit. {ECO:0000305|PubMed:18566510}; | folic acid biosynthetic process [GO:0046656]; folic acid-containing compound biosynthetic process [GO:0009396]; response to antibiotic [GO:0046677]; tetrahydrofolate biosynthetic process [GO:0046654] | cytoplasm [GO:0005737]; cytosol [GO:0005829] | ATP binding [GO:0005524]; dihydrofolate synthase activity [GO:0008841]; metal ion binding [GO:0046872]; tetrahydrofolylpolyglutamate synthase activity [GO:0004326] | PF02875;PF08245; | 3.90.190.20;3.40.1190.10; | Folylpolyglutamate synthase family | null | null | CATALYTIC ACTIVITY: Reaction=7,8-dihydropteroate + ATP + L-glutamate = 7,8-dihydrofolate + ADP + H(+) + phosphate; Xref=Rhea:RHEA:23584, ChEBI:CHEBI:15378, ChEBI:CHEBI:17839, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57451, ChEBI:CHEBI:456216; EC=6.3.2.12; Evidence={ECO:0000269|PubMed:2311801... | null | PATHWAY: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 7,8-dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate and 4-aminobenzoate: step 2/2. {ECO:0000305|PubMed:23118010}.; PATHWAY: Cofactor biosynthesis; tetrahydrofolylpolyglutamate biosynthesis. {ECO:0000250|UniProtKB:P08192... | null | null | FUNCTION: Catalyzes the addition of a glutamate residue to dihydropteroate (7,8-dihydropteroate or H2Pte) to form dihydrofolate (7,8-dihydrofolate monoglutamate or H2Pte-Glu) (PubMed:23118010). Also catalyzes successive additions of L-glutamate to tetrahydrofolate, leading to folylpolyglutamate derivatives (By similari... | Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) |
I6Y2J4 | LIPY_MYCTU | MVSYVVALPEVMSAAATDVASIGSVVATASQGVAGATTTVLAAAEDEVSAAIAALFSGHGQDYQALSAQLAVFHERFVQALTGAAKGYAAAELANASLLQSEFASGIGNGFATIHQEIQRAPTALAAGFTQVPPFAAAQAGIFTGTPSGAAGFDIASLWPVKPLLSLSALETHFAIPNNPLLALIASDIPPLSWFLGNSPPPLLNSLLGQTVQYTTYDGMSVVQITPAHPTGEYVVAIHGGAFILPPSIFHWLNYSVTAYQTGATVQVPIYPLVQEGGTAGTVVPAMAGLISTQIAQHGVSNVSVVGDSAGGNLALAAAQ... | 3.1.1.3 | null | lipid catabolic process [GO:0016042] | cell surface [GO:0009986]; cytoplasm [GO:0005737]; extracellular region [GO:0005576] | acetylesterase activity [GO:0008126]; triglyceride lipase activity [GO:0004806] | PF07859;PF00934; | 3.40.50.1820;1.10.287.850; | Mycobacterial PE family, PGRS subfamily; 'GDXG' lipolytic enzyme family | PTM: Upon export, the PE domain is removed by proteolytic cleavage (PubMed:21471225, PubMed:31662454). Cleavage occurs at the cell surface and is not required for secretion (PubMed:31662454). Cleaved after Gly-149 by the aspartic protease PecA. May also be cleaved before Leu-98 and after Ala-136 (PubMed:31662454). {ECO... | SUBCELLULAR LOCATION: [Cytosolic triacylglycerol lipase]: Cytoplasm {ECO:0000269|PubMed:29986895}.; SUBCELLULAR LOCATION: [Extracellular triacylglycerol lipase]: Secreted {ECO:0000269|PubMed:21471225, ECO:0000269|PubMed:29986895, ECO:0000269|PubMed:31034693, ECO:0000269|PubMed:31662454}. Secreted, cell wall {ECO:000026... | 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=3.1.1.3; Evidence={ECO:0000269|PubMed:16354661}; CATALYTIC ACTIVITY: Reaction=1,2,3-tri-(9Z-octadecenoyl)... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=7.57 mM for triolein (glyceryl trioleate) {ECO:0000269|PubMed:16354661}; Vmax=653.3 nmol/min/mg enzyme with triolein (glyceryl trioleate) as substrate {ECO:0000269|PubMed:16354661}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is between 8 and 9. {ECO:0000269|PubMed:16354661}; | null | FUNCTION: Catalyzes the hydrolysis of both intracellular and extracellular triacylglycerol (TAG) (PubMed:16354661, PubMed:17938218, PubMed:21471225, PubMed:29986895, PubMed:31034693). In vitro, can also hydrolyze p-nitrophenyl (pNP) esters with various chain lengths, including pNP-acetate (C2), pNP-butyrate (C4), pNP-c... | Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) |
I6Y3Q0 | CHSE5_MYCTU | MDFTTTEAAQDLGGLVDTIVDAVCTPEHQRELDKLEQRFDRELWRKLIDAGILSSAAPESLGGDGFGVLEQVAVLVALGHQLAAVPYLESVVLAAGALARFGSPELQQGWGVSAVSGDRILTVALDGEMGEGPVQAAGTGHGYRLTGTRTQVGYGPVADAFLVPAETDSGAAVFLVAAGDPGVAVTALATTGLGSVGHLELNGAKVDAARRVGGTDVAVWLGTLSTLSRTAFQLGVLERGLQMTAEYARTREQFDRPIGSFQAVGQRLADGYIDVKGLRLTLTQAAWRVAEDSLASRECPQPADIDVATAGFWAAEAGHR... | 1.3.99.- | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|PubMed:26161441}; Note=Binds 1 FAD per heterodimer. {ECO:0000269|PubMed:26161441}; | cholesterol catabolic process [GO:0006707] | null | acyl-CoA dehydrogenase activity [GO:0003995]; flavin adenine dinucleotide binding [GO:0050660] | PF00441;PF02771; | 1.10.540.10;2.40.110.10;1.20.140.10; | Acyl-CoA dehydrogenase family | null | null | CATALYTIC ACTIVITY: Reaction=(25S)-3-oxocholest-4-en-26-oyl-CoA + A = 3-oxo-cholest-4,24-dien-26-oyl-CoA + AH2; Xref=Rhea:RHEA:46688, ChEBI:CHEBI:13193, ChEBI:CHEBI:17499, ChEBI:CHEBI:83819, ChEBI:CHEBI:86414; Evidence={ECO:0000269|PubMed:26161441}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=2.6 uM for 3-OCO-CoA (at pH 8.5 and 25 degrees Celsius) {ECO:0000269|PubMed:26161441}; KM=3.3 uM for 3-OPC-CoA (at pH 8.5 and 25 degrees Celsius) {ECO:0000269|PubMed:26161441}; KM=3.4 uM for 3-OCS-CoA (at pH 8.5 and 25 degrees Celsius) {ECO:0000269|PubMed:26161441}... | PATHWAY: Steroid metabolism; cholesterol degradation. {ECO:0000305|PubMed:26161441}. | null | null | FUNCTION: Involved in the first cycle of side chain dehydrogenation in the beta-oxidation of cholesterol catabolism (PubMed:26161441). It contributes partly to the virulence by increasing the efficiency of beta-oxidation. Catalyzes the dehydrogenation of acyl-CoA ester side chains of (25S)-3-oxo-cholest-4-en-26-oyl-CoA... | Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) |
I6Y4D2 | PEPAM_MYCTU | MIVGVLVAAATPIISSASATPANIAGMVVFIDPGHNGANDASIGRQVPTGRGGTKNCQASGTSTNSGYPEHTFTWETGLRLRAALNALGVRTALSRGNDNALGPCVDERANMANALRPNAIVSLHADGGPASGRGFHVNYSAPPLNAIQAGPSVQFARIMRDQLQASGIPKANYIGQDGLYGRSDLAGLNLAQYPSILVELGNMKNPADSALMESAEGRQKYANALVRGVAGFLATQGQAR | 3.5.1.28 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:24019530, ECO:0000269|PubMed:24311595}; | cell wall macromolecule catabolic process [GO:0016998]; cell wall organization [GO:0071555]; cytokinesis [GO:0000910]; peptidoglycan catabolic process [GO:0009253] | outer membrane-bounded periplasmic space [GO:0030288] | metal ion binding [GO:0046872]; N-acetylmuramoyl-L-alanine amidase activity [GO:0008745] | PF01520; | 3.40.630.40; | N-acetylmuramoyl-L-alanine amidase 3 family | null | SUBCELLULAR LOCATION: Periplasm {ECO:0000305|PubMed:24019530}. | CATALYTIC ACTIVITY: Reaction=Hydrolyzes the link between N-acetylmuramoyl residues and L-amino acid residues in certain cell-wall glycopeptides.; EC=3.5.1.28; Evidence={ECO:0000269|PubMed:24019530, ECO:0000269|PubMed:24311595}; | null | PATHWAY: Cell wall degradation; peptidoglycan degradation. {ECO:0000269|PubMed:24019530, ECO:0000269|PubMed:24311595}. | null | null | FUNCTION: Cell-wall hydrolase that hydrolyzes the amide bond between N-acetylmuramic acid and L-alanine in cell-wall glycopeptides (PubMed:24019530, PubMed:24311595). Is able to hydrolyze the cell walls of several bacterial species (i.e. Paenibacillus sp., B.avium, E.coli DH5alpha, E.aerogenes, L.acidophilus, B.thuring... | Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) |
I6Y4U9 | DYP_MYCTU | MAVPAVSPQPILAPLTPAAIFLVATIGADGEATVHDALSKISGLVRAIGFRDPTKHLSVVVSIGSDAWDRLFAGPRPTELHPFVELTGPRHTAPATPGDLLFHIRAETMDVCFELAGRILKSMGDAVTVVDEVHGFRFFDNRDLLGFVDGTENPSGPIAIKATTIGDEDRNFAGSCYVHVQKYVHDMASWESLSVTEQERVIGRTKLDDIELDDNAKPANSHVALNVITDDDGTERKIVRHNMPFGEVGKGEYGTYFIGYSRTPTVTEQMLRNMFLGDPAGNTDRVLDFSTAVTGGLFFSPTIDFLDHPPPLPQAATPTL... | 1.11.1.7 | COFACTOR: Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000269|PubMed:24855650}; Note=Tetramer binds heme in a 1:1 ratio (PubMed:24855650). Addition of hemin to purified protein yields a tetrameric protein (Probable). {ECO:0000269|PubMed:24855650, ECO:0000305|PubMed:9634230}; | null | cytosol [GO:0005829]; encapsulin nanocompartment [GO:0140737] | heme binding [GO:0020037]; metal ion binding [GO:0046872]; peroxidase activity [GO:0004601] | PF20628;PF04261; | null | DyP-type peroxidase family | null | SUBCELLULAR LOCATION: Encapsulin nanocompartment {ECO:0000269|PubMed:24855650}. Note=Consistently identified in encapsulin nanocompartments isolated in situ (PubMed:34751132). Located inside the nanocompartment in E.coli (Probable). {ECO:0000269|PubMed:34751132, ECO:0000305|PubMed:24855650}. | CATALYTIC ACTIVITY: Reaction=2 a phenolic donor + H2O2 = 2 a phenolic radical donor + 2 H2O; Xref=Rhea:RHEA:56136, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240, ChEBI:CHEBI:139520, ChEBI:CHEBI:139521; EC=1.11.1.7; Evidence={ECO:0000269|PubMed:24855650, ECO:0000269|PubMed:34751132}; | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 4.0 or less. {ECO:0000269|PubMed:34751132}; | null | FUNCTION: Cargo of a type 1 encapsulin nanocompartment in situ; this cargo protects against oxidative stress at low pH. When expressed in the cytoplasm (absence of the encapsulin shell gene) it is almost as protective as the intact nanocompartment; its encapsulation has a modest yet significant effect on protection aga... | Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) |
I6Y778 | FABG4_MYCTU | MAPKRSSDLFSQVVNSGPGSFLARQLGVPQPETLRRYRAGEPPLTGSLLIGGAGRVVEPLRAALEKDYDLVGNNLGGRWADSFGGLVFDATGITEPAGLKGLHEFFTPVLRNLGRCGRVVVVGGTPEAAASTNERIAQRALEGFTRSLGKELRRGATTALVYLSPDAKPAATGLESTMRFLLSAKSAYVDGQVFSVGADDSTPPADWEKPLDGKVAIVTGAARGIGATIAEVFARDGAHVVAIDVESAAENLAETASKVGGTALWLDVTADDAVDKISEHLRDHHGGKADILVNNAGITRDKLLANMDDARWDAVLAVNL... | 1.1.1.212 | null | fatty acid elongation [GO:0030497] | null | 3-oxoacyl-[acyl-carrier-protein] reductase (NADH) activity [GO:0047025]; oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor [GO:0016616] | PF13561; | 3.40.50.720; | Short-chain dehydrogenases/reductases (SDR) family | null | null | CATALYTIC ACTIVITY: Reaction=a (3R)-hydroxyacyl-[ACP] + NAD(+) = a 3-oxoacyl-[ACP] + H(+) + NADH; Xref=Rhea:RHEA:19913, Rhea:RHEA-COMP:9916, Rhea:RHEA-COMP:9945, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:78776, ChEBI:CHEBI:78827; EC=1.1.1.212; Evidence={ECO:0000305|PubMed:23163771}; Physiolog... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=141.9 uM for acetoacetyl-CoA {ECO:0000269|PubMed:23163771}; KM=252 uM for 3-hydroxybutanoyl-CoA {ECO:0000269|PubMed:23163771}; KM=24.2 uM for NADH {ECO:0000269|PubMed:23163771}; KM=228.3 uM for NAD(+) {ECO:0000269|PubMed:23163771}; Note=kcat is 454 sec(-1) with ace... | PATHWAY: Lipid metabolism; fatty acid metabolism. {ECO:0000305|PubMed:23163771}. | null | null | FUNCTION: Catalyzes the NADH-dependent reduction of beta-ketoacyl derivatives (PubMed:19685079, PubMed:21081168, PubMed:23163771). Can accept the beta-oxo fatty acyl group covalently linked with CoA or ACP for catalysis (PubMed:23163771). Highly specific for NADH (PubMed:19685079, PubMed:21081168). Could be involved in... | Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) |
I6Y9J2 | LDT2_MYCTU | MPKVGIAAQAGRTRVRRAWLTALMMTAVMIGAVACGSGRGPAPIKVIADKGTPFADLLVPKLTASVTDGAVGVTVDAPVSVTAADGVLAAVTMVNDNGRPVAGRLSPDGLRWSTTEQLGYNRRYTLNATALGLGGAATRQLTFQTSSPAHLTMPYVMPGDGEVVGVGEPVAIRFDENIADRGAAEKAIKITTNPPVEGAFYWLNNREVRWRPEHFWKPGTAVDVAVNTYGVDLGEGMFGEDNVQTHFTIGDEVIATADDNTKILTVRVNGEVVKSMPTSMGKDSTPTANGIYIVGSRYKHIIMDSSTYGVPVNSPNGYRT... | 2.3.2.- | null | cell wall organization [GO:0071555]; peptidoglycan-protein cross-linking [GO:0018104]; regulation of cell shape [GO:0008360] | extracellular region [GO:0005576]; plasma membrane [GO:0005886] | acyltransferase activity [GO:0016746]; metal ion binding [GO:0046872]; peptidoglycan L,D-transpeptidase activity [GO:0071972] | PF17964;PF03734; | 2.60.40.3710;2.60.40.3780;2.40.440.10; | null | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE-ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE-ProRule:PRU00303}. | null | null | PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis. | null | null | FUNCTION: Generates 3->3 cross-links in peptidoglycan, catalyzing the cleavage of the mDap(3)-D-Ala(4) bond of a tetrapeptide donor stem and the formation of a bond between the carbonyl of mDap(3) of the donor stem and the side chain of mDap(3) of the acceptor stem. Is specific for donor substrates containing a stem te... | Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) |
I6Y9Q3 | PRPC_MYCTU | MTGPLAAARSVAATKSMTAPTVDERPDIKKGLAGVVVDTTAISKVVPQTNSLTYRGYPVQDLAARCSFEQVAFLLWRGELPTDAELALFSQRERASRRVDRSMLSLLAKLPDNCHPMDVVRTAISYLGAEDPDEDDAAANRAKAMRMMAVLPTIVAIDMRRRRGLPPIAPHSGLGYAQNFLHMCFGEVPETAVVSAFEQSMILYAEHGFNASTFAARVVTSTQSDIYSAVTGAIGALKGRLHGGANEAVMHDMIEIGDPANAREWLRAKLARKEKIMGFGHRVYRHGDSRVPTMKRALERVGTVRDGQRWLDIYQVLAAE... | 2.3.3.16; 2.3.3.5 | null | carbohydrate metabolic process [GO:0005975]; propionate metabolic process, methylcitrate cycle [GO:0019679]; tricarboxylic acid cycle [GO:0006099] | cytosol [GO:0005829] | 2-methylcitrate synthase activity [GO:0050440]; citrate (Si)-synthase activity [GO:0004108]; citrate synthase activity [GO:0036440] | PF00285; | 1.10.580.10;1.10.230.10; | Citrate synthase family | null | null | CATALYTIC ACTIVITY: Reaction=H2O + oxaloacetate + propanoyl-CoA = (2S,3S)-2-methylcitrate + CoA + H(+); Xref=Rhea:RHEA:23780, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16452, ChEBI:CHEBI:57287, ChEBI:CHEBI:57392, ChEBI:CHEBI:58853; EC=2.3.3.5; Evidence={ECO:0000250|UniProtKB:H8F0D7}; CATALYTIC ACTIVITY: Reactio... | null | PATHWAY: Organic acid metabolism; propanoate degradation. {ECO:0000305|PubMed:18375549}.; PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; isocitrate from oxaloacetate: step 1/2. {ECO:0000305|PubMed:18375549}. | null | null | FUNCTION: Involved in the catabolism of short chain fatty acids (SCFA) via the tricarboxylic acid (TCA)(acetyl degradation route) and via the 2-methylcitrate cycle I (propionate degradation route). Catalyzes the Claisen condensation of propionyl-CoA and oxaloacetate (OAA) to yield 2-methylcitrate (2-MC) and CoA. Also c... | Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) |
I6YCA3 | CHSE4_MYCTU | MRISYTPQQEELRRELRSYFATLMTPERREALSSVQGEYGVGNVYRETIAQMGRDGWLALGWPKEYGGQGRSAMDQLIFTDEAAIAGAPVPFLTINSVAPTIMAYGTDEQKRFFLPRIAAGDLHFSIGYSEPGAGTDLANLRTTAVRDGDDYVVNGQKMWTSLIQYADYVWLAVRTNPESSGAKKHRGISVLIVPTTAEGFSWTPVHTMAGPDTSATYYSDVRVPVANRVGEENAGWKLVTNQLNHERVALVSPAPIFGCLREVREWAQNTKDAGGTRLIDSEWVQLNLARVHAKAEVLKLINWELASSQSGPKDAGPSP... | 1.3.99.- | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|PubMed:26161441}; Note=Binds 1 FAD per heterodimer. {ECO:0000269|PubMed:26161441}; | cholesterol catabolic process [GO:0006707] | plasma membrane [GO:0005886] | flavin adenine dinucleotide binding [GO:0050660]; oxidoreductase activity, acting on the CH-CH group of donors [GO:0016627] | PF00441;PF02770;PF02771; | 1.10.540.10;2.40.110.10;1.20.140.10; | Acyl-CoA dehydrogenase family | null | null | CATALYTIC ACTIVITY: Reaction=(25S)-3-oxocholest-4-en-26-oyl-CoA + A = 3-oxo-cholest-4,24-dien-26-oyl-CoA + AH2; Xref=Rhea:RHEA:46688, ChEBI:CHEBI:13193, ChEBI:CHEBI:17499, ChEBI:CHEBI:83819, ChEBI:CHEBI:86414; Evidence={ECO:0000269|PubMed:26161441}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=2.6 uM for 3-OCO-CoA (at pH 8.5 and 25 degrees Celsius) {ECO:0000269|PubMed:26161441}; KM=3.3 uM for 3-OPC-CoA (at pH 8.5 and 25 degrees Celsius) {ECO:0000269|PubMed:26161441}; KM=3.4 uM for 3-OCS-CoA (at pH 8.5 and 25 degrees Celsius) {ECO:0000269|PubMed:26161441}... | PATHWAY: Steroid metabolism; cholesterol degradation. {ECO:0000305|PubMed:26161441}. | null | null | FUNCTION: Involved in the first cycle of side chain dehydrogenation in the beta-oxidation of cholesterol catabolism (PubMed:26161441). It contributes partly to the virulence by increasing the efficiency of beta-oxidation. Catalyzes the dehydrogenation of acyl-CoA ester side chains of (25S)-3-oxo-cholest-4-en-26-oyl-CoA... | Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) |
I6YFP0 | BIRA_MYCTU | MTDRDRLRPPLDERSLRDQLIGAGSGWRQLDVVAQTGSTNADLLARAASGADIDGVVLIAEHQTAGRGRHGRGWAATARAQIILSVGVRVVDVPVQAWGWLSLAAGLAVLDSVAPLIAVPPAETGLKWPNDVLARGGKLAGILAEVAQPFVVLGVGLNVTQAPEEVDPDATSLLDLGVAAPDRNRIASRLLRELEARIIQWRNANPQLAADYRARSLTIGSRVRVELPGGQDVVGIARDIDDQGRLCLDVGGRTVVVSAGDVVHLR | 6.3.4.15 | null | positive regulation of cell population proliferation [GO:0008284]; protein modification process [GO:0036211] | cytoplasm [GO:0005737]; protein-containing complex [GO:0032991] | ATP binding [GO:0005524]; biotin binding [GO:0009374]; biotin-[acetyl-CoA-carboxylase] ligase activity [GO:0004077]; protein homodimerization activity [GO:0042803] | PF02237;PF03099; | 2.30.30.100; | Biotin--protein ligase family | null | null | CATALYTIC ACTIVITY: Reaction=ATP + biotin + L-lysyl-[protein] = AMP + diphosphate + H(+) + N(6)-biotinyl-L-lysyl-[protein]; Xref=Rhea:RHEA:11756, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:10505, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57586, ChEBI:CHEBI:83144, ChEBI:CHEBI:45621... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.42 uM for biotin {ECO:0000269|PubMed:18509457}; KM=21.08 uM for Mg/ATP {ECO:0000269|PubMed:18509457}; KM=0.2 mM for ATP {ECO:0000269|PubMed:24723382}; KM=5.2 uM for apo-BCCP {ECO:0000269|PubMed:18509457}; Note=kcat is 0.034 sec(-1) with biotin as substrate. kcat ... | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5-8.0. {ECO:0000269|PubMed:18509457}; | null | FUNCTION: Catalyzes the transfer of biotin onto a conserved lysine residue of the biotin carboxyl carrier protein (BCCP) domain of acetyl-CoA carboxylase and converts it to active holo-BCCP (PubMed:18509457, PubMed:24723382). Forms an acyl-adenylate intermediate (PubMed:18509457, PubMed:24723382). Cannot use GTP or des... | Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) |
I6YG32 | RIMI_MYCTU | MTADTEPVTIGALTRADAQRCAELEAQLFVGDDPWPPAAFNRELASPHNHYVGARSGGTLVGYAGISRLGRTPPFEYEVHTIGVDPAYQGRGIGRRLLRELLDFARGGVVYLEVRTDNDAALALYRSVGFQRVGLRRRYYRVSGADAYTMRRDSGDPS | 2.3.1.255; 2.3.1.258 | null | N-terminal protein amino acid acetylation [GO:0006474] | null | peptide alpha-N-acetyltransferase activity [GO:0004596]; peptide-alanine-alpha-N-acetyltransferase activity [GO:0008999] | PF00583; | 3.40.630.30; | Acetyltransferase family, RimI subfamily | null | null | CATALYTIC ACTIVITY: Reaction=acetyl-CoA + N-terminal L-methionyl-L-alanyl-[protein] = CoA + H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-alanyl-[protein]; Xref=Rhea:RHEA:50564, Rhea:RHEA-COMP:12726, Rhea:RHEA-COMP:12727, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:133398, ChEBI:CHEBI:133399;... | null | null | null | null | FUNCTION: N-alpha-acetyltransferase that specifically mediates the acetylation of N-terminal residues. Able to mediate acetylation of a wide variety of N-terminal residues, with preference for hydrophobic N-termini. Acetylates GroS/GroES and GroEL1. Able to acetylate the ribosomal protein bS18, but it is unclear whethe... | Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) |
I7C2V3 | SPXN_CARAU | MKDLRTLAAYALALLLLATFVSYSRSAPMGSFQRRNWTPQAMLYLKGTQGRRFVSEDRNEGDLYDTIRLESQSQNTENLSISKAAAFLLNVLQQARDEGEPY | null | null | long-chain fatty acid import into cell [GO:0044539]; negative regulation of appetite [GO:0032099]; negative regulation of heart rate [GO:0010459]; negative regulation of renal sodium excretion [GO:0035814]; positive regulation of gastro-intestinal system smooth muscle contraction [GO:1904306]; positive regulation of sy... | extracellular space [GO:0005615]; transport vesicle [GO:0030133] | neuropeptide hormone activity [GO:0005184]; type 2 galanin receptor binding [GO:0031765]; type 3 galanin receptor binding [GO:0031766] | PF15171; | null | Spexin family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Secreted, extracellular space {ECO:0000250}. Cytoplasmic vesicle, secretory vesicle {ECO:0000250}. | null | null | null | null | null | FUNCTION: Plays a role in the regulation of food intake and body weight and in reproduction. May also play a role as a central modulator of cardiovascular and renal function and nociception (By similarity). {ECO:0000250}.; FUNCTION: [Spexin-1]: Brain administration of the peptide inhibits food consumption. May function... | Carassius auratus (Goldfish) |
I7CA98 | TODT_PSEPT | MPARWGCLFPGKYPCQTGLRHMSDRASVIYILDDDNAVLEALSSLVRSIGLSVECFSSASVFLNDVNRSACGCLILDVRMPEMSGLDVQRQLKELGEQIPIIFISGHGDIPMAVKAIKAGAVDFFTKPFREEELLGAIRAALKLAPQQRSNAPRVSELKENYESLSKREQQVLKFVLRGYLNKQTALELDISEATVKVHRHNIMRKMKVSSIQDLVRVTERLKDSLE | null | null | phosphorelay signal transduction system [GO:0000160] | cytoplasm [GO:0005737]; protein-DNA complex [GO:0032993] | DNA-binding transcription activator activity [GO:0001216]; transcription cis-regulatory region binding [GO:0000976] | PF00196;PF00072; | 3.40.50.2300;1.10.10.10; | null | PTM: Phosphorylated by TodS. {ECO:0000269|PubMed:16702539, ECO:0000269|PubMed:19240030}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. | null | null | null | null | null | FUNCTION: Member of the two-component regulatory system TodS/TodT involved in the regulation of toluene degradation. Phosphorylated TodT activates transcription of the tod operon (todXFC1C2BADEGIH). Binds specifically to three boxes in the tod promoter region in a cooperative manner. Boxes-1 and -2 are pseudopalindrome... | Pseudomonas putida (strain DOT-T1E) |
I7H727 | TPS2_TOOSI | MSVPVSQIPSLKAKGVIMRRNANYHPNIWGDRFINYVPVDKMNHTCHLQAIEELKDAVRRELLTATGLSQLNLIDAIQRLGVGYHFERELEEALQHVYHKNHYHDDTEDNLYSISLRFRLLRQHGYYVSCDILNKFKDEKDNFKESLTTDVPGMLSLYEAAHPGVHGEDILDEAIAFTTTHLKSLAIDHLRNPSLASQVIHALRQPLHRGVPRLENRRYISIYQDEVSHNKALVKLFKLDFNLVQSLHKKELSEISRWWKELDLANKLPFARDRLVECYFWIIGVYYEPQYSLARKILTKTIAMGSIIDDIYDVYGTPEE... | 4.2.3.-; 4.2.3.104; 4.2.3.198 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:A0A1C9J6A7}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:A0A1C9J6A7}; Note=Binds 3 Mg(2+) or Mn(2+) ions per subunit. {ECO:0000250|UniProtKB:A0A1C9J6A7}; | diterpenoid biosynthetic process [GO:0016102]; sesquiterpene biosynthetic process [GO:0051762] | null | beta-elemene synthase activity [GO:0102889]; magnesium ion binding [GO:0000287]; sesquiterpene synthase activity [GO:0010334] | PF01397;PF03936; | 1.10.600.10;1.50.10.130; | Terpene synthase family, Tpsa subfamily | null | null | CATALYTIC ACTIVITY: Reaction=(2E,6E)-farnesyl diphosphate = alpha-humulene + diphosphate; Xref=Rhea:RHEA:31895, ChEBI:CHEBI:5768, ChEBI:CHEBI:33019, ChEBI:CHEBI:175763; EC=4.2.3.104; Evidence={ECO:0000269|PubMed:21818683, ECO:0000269|PubMed:23072391}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:31896; Evidence... | null | PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis. {ECO:0000269|PubMed:21818683, ECO:0000269|PubMed:23072391}. | null | null | FUNCTION: Sesquiterpene synthase involved in the biosynthesis of volatile compounds known for their medicinal efficacy for treating enteritis, dysentery, itch and some cancers (PubMed:21818683, PubMed:23072391). Mediates the conversion of (2E,6E)-farnesyl diphosphate (FPP) into beta-elemene, alpha-humulene, delta-cadin... | Toona sinensis (Chinese mahogany) (Cedrela sinensis) |
I7HJS4 | ZN683_MOUSE | MKALDGLRESLYPSLDFQLYQDDQVCSADASQPLADSVGAHDLAWSERMCPLPLAPAKSPLLACPESPDLCLCALQKTPLGRAPQDLGEDASNMRHQPPSLYKASTDSEKLTIKDSLNREEMGNEPERGAYPHLPPRTSSFPDAGLDRKSLSPLTFWPWLPPTLISKEPPIHIYPIFPGYPLLPLPYLFTYGALPSAQHPYLFMLPPHSTYPTVAGPSLLMTASGSGPRIPQEKTLLLHSGAFQSAGHTLHSQVESRSSRDTRTPGQAGVAAPTRRAVPGSRAGVIALPYPLKKENGKILYECNVCGKNFGQLSNLKVHL... | null | null | adaptive immune response [GO:0002250]; cell fate commitment [GO:0045165]; innate immune response [GO:0045087]; natural killer cell differentiation [GO:0001779]; NK T cell differentiation [GO:0001865]; regulation of extrathymic T cell differentiation [GO:0033082]; regulation of gene expression [GO:0010468]; regulation o... | cytoplasm [GO:0005737]; nucleus [GO:0005634] | DNA-binding transcription factor activity [GO:0003700]; metal ion binding [GO:0046872]; promoter-specific chromatin binding [GO:1990841]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978] | PF00096; | 3.30.160.60; | Krueppel C2H2-type zinc-finger protein family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. | null | null | null | null | null | FUNCTION: Transcription factor that mediates a transcriptional program in various innate and adaptive immune tissue-resident lymphocyte T-cell types such as tissue-resident memory T (Trm), natural killer (trNK) and natural killer T (NKT) cells and negatively regulates gene expression of proteins that promote the egress... | Mus musculus (Mouse) |
J3KML8 | GFY_MOUSE | MQPFSPIFFHLLFLLNGLSSRAAPSPGQPVVADLQGMLQPSGMPTGTLENLTRDQPTPGSSASHPPEHSETPPSASPHISTKILRETPSPSPFLSLETPIPDQLTSVAESQGTSQMSPSRATLGKPSETPKPDPTGISPSDSPETPKPNPSNTSPPESPESVYTDPTPTLHHESPEISKRDTPKLSPGEESKIPSPRPTQFLSSKSLETYDPSATRHLNSALEPTTHPDPTESPQSVFLTTHNSNPTVVPQTQFPTSPSQNVTETARTSDLEPSSSLPTQPTTFREEATTPSEPGLSPSPEAPAVTRVATPGLSTSDSPG... | null | null | non-motile cilium assembly [GO:1905515]; protein localization to non-motile cilium [GO:0097499]; response to stimulus [GO:0050896]; sensory perception of smell [GO:0007608] | Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139] | null | null | null | null | null | SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000269|PubMed:23926254}; Single-pass type I membrane protein {ECO:0000269|PubMed:23926254}. | null | null | null | null | null | FUNCTION: Required for proper function of the olfactory system. May be involved in establishing the acuity of olfactory sensory signaling. {ECO:0000269|PubMed:23926254}. | Mus musculus (Mouse) |
J3QMI4 | CAHM3_MOUSE | MDRFRMLFQHLQSSSESVMNGICLLLAAVTVKIYSSLDFNCPCLERYNALYGLGLLLTPPLALFLCGLLVNRQSVLMVEEWRRPAGHRRKDLGIIRYMCSSVLQRALAAPLVWILLALLDGKCFVCAFSNSVDPEKFLDFANMTPRQVQLFLAKVPCKEDELVKNSPARKAVSRYLRCLSQAIGWSITLLVIVVAFLARCLRPCFDQTVFLQRRYWSNYMDLEQKLFDETCCEHARDFAHRCVLHFFANMQSELRALGLRRDPAGGIPESQESSEPPELREDRDSGNGKAHLRAISSREQVDQLLSTWYSSKPPLDLAAS... | null | null | ATP transport [GO:0015867]; protein heterooligomerization [GO:0051291]; response to stimulus [GO:0050896]; sensory perception of taste [GO:0050909] | basolateral plasma membrane [GO:0016323]; plasma membrane [GO:0005886] | monoatomic cation channel activity [GO:0005261]; voltage-gated monoatomic ion channel activity [GO:0005244] | PF14798; | null | CALHM family | PTM: N-glycosylated. {ECO:0000269|PubMed:33788965}.; PTM: Palmitoylated by ZDHHC3 and ZDHHC15. Palmitoylation positively regulates CALHM1:CALHM3 channel conductance. {ECO:0000269|PubMed:33788965}. | SUBCELLULAR LOCATION: Basolateral cell membrane {ECO:0000269|PubMed:30804437, ECO:0000305|PubMed:29681531}; Multi-pass membrane protein {ECO:0000255}. Note=Localizes to the basolateral membrane of epithelial cells including taste cells. {ECO:0000269|PubMed:30804437}. | CATALYTIC ACTIVITY: Reaction=ATP(in) = ATP(out); Xref=Rhea:RHEA:75687, ChEBI:CHEBI:30616; Evidence={ECO:0000269|PubMed:29681531, ECO:0000269|PubMed:33788965}; CATALYTIC ACTIVITY: Reaction=Ca(2+)(in) = Ca(2+)(out); Xref=Rhea:RHEA:29671, ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:29681531}; CATALYTIC ACTIVITY: React... | null | null | null | null | FUNCTION: Pore-forming subunit of gustatory voltage-gated ion channels required for sensory perception of sweet, bitter and umami tastes. With CALHM1 forms a fast-activating voltage-gated ATP-release channel in type II taste bud cells, ATP acting as a neurotransmitter to activate afferent neural gustatory pathways. Act... | Mus musculus (Mouse) |
J3QMK6 | AL3B3_MOUSE | MSTKGKHPRADQGTDPFEEKLQRLKEAFNTGKTKTAKFRAEQLQSLGRFLQDNSKQLHDALDGDLGKSGFESDMSEIILCENEVDLALKNLQTWMKDEPVSTNLLTKLSTAFIRKEPFGLVLIIAPWNYPVNLMIIPLVGAIAAGNCVVLKPSEISKNTEKVLAELLPQYLDQSCFAVMLGGPEETGQLLEHKFDYIFFTGSPRVGKIVMTAAAKHLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYILCSQEMQEQLVPALQNAITRFYGDNPQTSPNLGRIINQKHFKRLQGLLGCGRVAIGG... | 1.2.1.3 | null | cellular aldehyde metabolic process [GO:0006081] | cytoplasm [GO:0005737]; plasma membrane [GO:0005886] | 3-chloroallyl aldehyde dehydrogenase activity [GO:0004028]; aldehyde dehydrogenase (NAD+) activity [GO:0004029]; glyceraldehyde-3-phosphate dehydrogenase (NAD+) (non-phosphorylating) activity [GO:0043878] | PF00171; | null | Aldehyde dehydrogenase family | PTM: Geranylgeranylation is important for membrane localization and enzyme activity. {ECO:0000269|PubMed:25286108}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:25286108}; Lipid-anchor {ECO:0000305|PubMed:25286108}. | CATALYTIC ACTIVITY: Reaction=an aldehyde + H2O + NAD(+) = a carboxylate + 2 H(+) + NADH; Xref=Rhea:RHEA:16185, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17478, ChEBI:CHEBI:29067, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.2.1.3; Evidence={ECO:0000269|PubMed:25286108}; CATALYTIC ACTIVITY: Reaction=2 H(+) + hexad... | null | null | null | null | FUNCTION: Oxidizes medium and long chain aldehydes into non-toxic fatty acids. {ECO:0000269|PubMed:25286108}. | Mus musculus (Mouse) |
J3QMY9 | TO6BL_MOUSE | MERTALAVCEILRYLIIHWKCEAGTAKGTLLDGQLVISIEALRSKHLPDSLHCIITIASTRSVYGGLNFKKFLQEIQPALPRLSAKLALASEEGGRSQDASGIAPCQVTFEVDENSQSLMTDCLVIKHFLRKIIIVHHKLKFSFSVAVNGTLSAETFGAENEPTLRLDNGVTLVVGFQRYVSKPKLNWSEAHCSRIHPVLGHPAPLFIPDAKADTGLLGELTLTPAAALCPSPKGFSSQLCRISSVSIFLYGPLGLPLLSSDQDQPSTAVFRDTSYFIDWKKYNLFMVPNLDLNLDTQSVLPDVNYKAESPEGNQSQNMN... | null | null | meiotic DNA double-strand break formation [GO:0042138]; reciprocal meiotic recombination [GO:0007131] | chromosome [GO:0005694] | DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity [GO:0003918] | PF15091; | null | TOP6B-like family | null | SUBCELLULAR LOCATION: Chromosome {ECO:0000305}. Note=Localizes to meiotic chromosomes. {ECO:0000305}. | null | null | null | null | null | FUNCTION: Component of a topoisomerase 6 complex specifically required for meiotic recombination. Together with SPO11, mediates DNA cleavage that forms the double-strand breaks (DSB) that initiate meiotic recombination. The complex promotes relaxation of negative and positive supercoiled DNA and DNA decatenation throug... | Mus musculus (Mouse) |
J3QPC3 | ACTMP_MOUSE | MTSPCSFPLKPTISPIIHETPDTNIPPPLPLNPPDLALPSPPCSLHTSISSPLPPPPPPPAPPPPPPPPPLPSAVEPVLPHVYGLKNSQLLKEALEKAGPAPKGKEDVKRLLKLHKDRFRSDLQWILFCADLPSCIQEGPQCGLVALWMAEALLSTPDSVSLERLVQVAKERGYTAQGEMFSVADMAKLAQETLDCQAELLCGGLGGPNRERVLQHLITGHPLLIPYDEDFNHEPCQKKGHKAHWAVSAGVLIGVQNVPSPGYIEDSELPGLFHPVPGAPHQPPSFPEESSPGALFLLSKQGKSWHYQLWDYSQVRESNL... | 3.4.11.- | null | protein processing [GO:0016485] | cytoplasm [GO:0005737] | cysteine-type aminopeptidase activity [GO:0070005]; initiator methionyl aminopeptidase activity [GO:0004239] | PF21646; | null | ACTMAP family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:36173861}. | CATALYTIC ACTIVITY: [Actin maturation protease]: Reaction=H2O + N-terminal N(alpha)-acetyl-L-methionyl-L-aspartyl-[protein] = N(alpha)-acetyl-L-methionine + N-terminal L-aspartyl-[protein]; Xref=Rhea:RHEA:74571, Rhea:RHEA-COMP:12669, Rhea:RHEA-COMP:12693, ChEBI:CHEBI:15377, ChEBI:CHEBI:64720, ChEBI:CHEBI:71670, ChEBI:C... | null | null | null | null | FUNCTION: Actin maturation protease that specifically mediates the cleavage of immature acetylated N-terminal actin, thereby contributing to actin maturation (PubMed:36173861). Cleaves N-terminal acetylated methionine of immature cytoplasmic beta- and gamma-actins Actb and Actg1 after translation (PubMed:36173861). Cle... | Mus musculus (Mouse) |
J3S6Y1 | TSEAR_MOUSE | MSALLMLCAVLLLLGTPSRGARPWEPCTDLRPLDILAEVVPLNGATSGIRMVQVEGVRGLQFSATEPRTTSFPASRIFSSCDFFPEEFSIIVTLRVPNLPPKKNEYLLSLLAEERDTLLLGLRYSPTQLHFLFLSEDLAGAWQTRVSFWSPGLMDSRWHTLILAVSQGSFSLTTDCGLPVDIMADVSFPPTLSVRGARFFIGSRKRTKGLFTGVIRQLVLLPGSDATPQLCPSRNARLAELSIPQVLKRLTGKPDDNEVLNYPYEADMKVTLGSRPPCTKAEGAQFWFDAAQKGLYLCAGSEWVSVLAAKTKLDYVEEHQ... | null | null | hair cycle process [GO:0022405]; Notch signaling pathway [GO:0007219]; regulation of Notch signaling pathway [GO:0008593]; sensory perception of sound [GO:0007605]; signal transduction [GO:0007165]; tooth mineralization [GO:0034505] | cell surface [GO:0009986]; ciliary membrane [GO:0060170]; extracellular region [GO:0005576]; stereocilium [GO:0032420] | null | PF03736; | 2.60.120.200; | null | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:22678063}. Cell surface {ECO:0000269|PubMed:22678063}. Cell projection, stereocilium {ECO:0000269|PubMed:22678063}. Note=Secreted protein which may bind to the cell surface via a membrane receptor. {ECO:0000269|PubMed:22678063}. | null | null | null | null | null | FUNCTION: Plays a critical role in tooth and hair follicle morphogenesis through regulation of the Notch signaling pathway. May play a role in development or function of the auditory system. {ECO:0000250|UniProtKB:Q8WU66}. | Mus musculus (Mouse) |
J3TRD1 | L_HTRV | MNLEALCSRVLSERGLSTGEPGVYDQIFERPGLPNLEVTVDSTGVVVDVGAIPDSASQLGSSINAGVLTIPLSEAYKINHDFTFSGLTKTTDRKLSEVFPLVHDGSDSMTPDVIHTRLDGTVVVIEFTTTRSTNMGGLEAAYRSKLEKYRDPLNRRTDIMPDASIYFGIIVVSASGVLTNMPLTQDEAEELMFRFCVANEIYSQARAMDAEVELQKSEEEYEAISRARAFFTLFDYDDGKLSEAFPNSDIEMLRRFLSQPVDTSFVTTTLKEKEQEAYKRMCEEHYLKSGMSTKERLEANRSDAIDKTRALMERLHNMSS... | 2.7.7.48; 3.1.-.- | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:P27316}; Note=For endonuclease activity. Binds 2 Mn(2+) ions in the active site (By similarity). The divalent metal ions are crucial for catalytic activity (PubMed:31948728). {ECO:0000250|UniProtKB:P27316, ECO:0000269|PubMed:31948728}; COFAC... | DNA-templated transcription [GO:0006351]; viral RNA genome replication [GO:0039694] | host cell endoplasmic reticulum [GO:0044165]; host cell endoplasmic reticulum-Golgi intermediate compartment [GO:0044172]; host cell Golgi apparatus [GO:0044177]; virion component [GO:0044423] | hydrolase activity [GO:0016787]; metal ion binding [GO:0046872]; nucleotide binding [GO:0000166]; RNA-dependent RNA polymerase activity [GO:0003968] | PF04196;PF12603;PF15518; | null | Bunyavirales RNA polymerase family | null | SUBCELLULAR LOCATION: Host Golgi apparatus {ECO:0000250|UniProtKB:I0DF35}. Host endoplasmic reticulum {ECO:0000250|UniProtKB:I0DF35}. Host endoplasmic reticulum-Golgi intermediate compartment {ECO:0000250|UniProtKB:I0DF35}. Virion {ECO:0000250|UniProtKB:P20470}. | CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395; EC=2.7.7.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU00539}; | null | null | null | null | FUNCTION: RNA-dependent RNA polymerase, which is responsible for the replication and transcription of the viral RNA genome using antigenomic RNA as an intermediate (By similarity). During transcription, synthesizes subgenomic RNAs and assures their capping by a cap-snatching mechanism, which involves the endonuclease a... | Heartland virus (HTRV) |
J3WAX0 | GP_HTRV | MIVPIVLFLTLCPSELSAWGSPGDPIVCGVRTETNKSIQIEWKEGRSEKLCQIDRLGHVTSWLRNHSSFQGLIGQVKGRPSVSYFPEGASYPRWSGLLSPCDAEWLGLIAVSKAGDTDMIVPGPTYKGKIFVERPTYNGYKGWGCADGKSLSHSGTYCETDSSVSSGLIQGDRVLWVGEVVCQRGTPVPEDVFSELVSLSQSEFPDVCKIDGVALNQCEQESIPQPLDVAWIDVGRSHKVLMREHKTKWVQESSAKDFVCFKVGQGPCSKQEEDDCMSKGNCHGDEVFCRMAGCSARMQDNQEGCRCELLQKPGEIIVNY... | null | null | fusion of virus membrane with host endosome membrane [GO:0039654]; symbiont entry into host cell [GO:0046718]; virion attachment to host cell [GO:0019062] | host cell endoplasmic reticulum membrane [GO:0044167]; host cell Golgi membrane [GO:0044178]; membrane [GO:0016020]; virion membrane [GO:0055036] | null | PF19019;PF07243;PF07245; | 2.60.40.3770;2.60.98.50; | Phlebovirus envelope glycoprotein family | PTM: [Envelopment polyprotein]: Specific enzymatic cleavages in vivo yield mature proteins Glycoprotein C, and Glycoprotein N. {ECO:0000250|UniProtKB:P21401}.; PTM: [Glycoprotein N]: Glycosylated. {ECO:0000250|UniProtKB:P09613}.; PTM: [Glycoprotein C]: Glycosylated. {ECO:0000250|UniProtKB:P09613}.; PTM: [Glycoprotein C... | SUBCELLULAR LOCATION: [Glycoprotein N]: Virion membrane {ECO:0000250|UniProtKB:P09613}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P09613}. Host Golgi apparatus membrane {ECO:0000250|UniProtKB:P03518}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P09613}. Host endoplasmic reticulum membran... | null | null | null | null | null | FUNCTION: [Glycoprotein N]: Structural component of the virion that interacts with glycoprotein C (By similarity). It shields the hydrophobic fusion loops of the glycoprotein C, preventing premature fusion (By similarity). The glycoprotein protrusions are arranged on an icosahedral lattice, with T=12 triangulation (By ... | Heartland virus (HTRV) |
J4KMC1 | TENS_BEAB2 | MSPMKQNESESHSVSEPIAIVGSAYRFPGGCNTPSKLWDLLQQPRDILKELDPERLNLRRYYHPDGETHGSTDVSNKAYTLEEDISRFDASFFGISPLEAASMDPQQRTLLEVVYESTETAGIPLDKLRGSLTSVHVGVMTTDWAQVQRRDPETMPQYTATGIASSIISNRISYIFDLKGASETIDTACSSSLVALHNAARALQSGDCEKAIVAGVNLILDPDPFIYESKLHMLSPDARSRMWDAAANGYARGEGAAAVVLKTLGHALRDGDRIEGVIRSTFVNSDGLSSGLTMPSSAAQTALIRQTYRKAGLDPVRDRP... | 2.3.1.-; 6.3.2.- | null | amide biosynthetic process [GO:0043604]; fatty acid biosynthetic process [GO:0006633]; heterocycle biosynthetic process [GO:0018130]; methylation [GO:0032259]; organic cyclic compound biosynthetic process [GO:1901362]; organonitrogen compound biosynthetic process [GO:1901566]; toxin biosynthetic process [GO:0009403] | null | fatty acid synthase activity [GO:0004312]; ligase activity [GO:0016874]; methyltransferase activity [GO:0008168]; oxidoreductase activity [GO:0016491]; phosphopantetheine binding [GO:0031177] | PF00698;PF00501;PF00668;PF16197;PF00109;PF02801;PF08659;PF08242;PF07993;PF21089;PF00550;PF14765; | 3.30.300.30;3.30.70.3290;3.40.47.10;1.10.1200.10;3.30.559.10;3.40.366.10;3.40.50.12780;3.40.50.720;3.30.559.30;3.10.129.110;3.40.50.150; | NRP synthetase family | null | null | null | null | PATHWAY: Secondary metabolite biosynthesis. {ECO:0000269|PubMed:17216664, ECO:0000269|PubMed:18266306, ECO:0000269|PubMed:20575135, ECO:0000269|PubMed:34903054}. | null | null | FUNCTION: Hybrid PKS-NRPS synthetase; part of the gene cluster that mediates the biosynthesis of tenellin-type 2-pyridones, iron-chelating compounds involved in iron stress tolerance, competition with the natural competitor fungus Metarhizium robertsii and insect hosts infection (PubMed:17216664, PubMed:18266306, PubMe... | Beauveria bassiana (strain ARSEF 2860) (White muscardine disease fungus) (Tritirachium shiotae) |
J4UHQ6 | OPS1_BEAB2 | MPSFFPVFSGLGSGSVFSEENVGRAEENALSPECAVLLQSCHRTFREQVSDAIARNILPEDSIDLDDFAEPASLIRPLSKYSRNVVMQHAALYLHQILAYMTSQKELGNLIGSAGFCTGLLPAAVAAASQTSVITLISQSHHFFQVALWIGIRSEQYRVDHLTNDTQDADGESMLPCSYVLEGVSEAAAQDLLHKTNMGNEVFVSAILSPTRVTISGIPTKLSTFISKHLPANCRTTVAVVHSLYHHESLLEVRNLVMADLERQDTLLQARVELSAPILSTKTGKPLALSSVTTLEQVACAILDLIFIEKVDWLNLQQSI... | 2.3.1.- | null | fatty acid biosynthetic process [GO:0006633]; organic cyclic compound biosynthetic process [GO:1901362]; secondary metabolite biosynthetic process [GO:0044550] | cytoplasm [GO:0005737]; fatty acid synthase complex [GO:0005835]; plasma membrane [GO:0005886] | 3-oxoacyl-[acyl-carrier-protein] synthase activity [GO:0004315]; fatty acid synthase activity [GO:0004312]; phosphopantetheine binding [GO:0031177] | PF00698;PF00109;PF02801;PF00550;PF16073;PF00975; | 3.30.70.3290;3.40.47.10;1.10.1200.10;3.40.50.1820;3.30.70.250;3.40.366.10;3.10.129.110; | null | null | null | CATALYTIC ACTIVITY: Reaction=acetyl-CoA + 2 H(+) + 3 malonyl-CoA = 3 CO2 + 4 CoA + orsellinate; Xref=Rhea:RHEA:62972, ChEBI:CHEBI:15378, ChEBI:CHEBI:16162, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384; Evidence={ECO:0000269|PubMed:26305932}; PhysiologicalDirection=left-to-right; Xref=Rhea:... | null | PATHWAY: Secondary metabolite biosynthesis. {ECO:0000269|PubMed:26305932}. | null | null | FUNCTION: Non-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of the bibenzoquinone oosporein, a metabolite required for fungal virulence that acts by evading host immunity to facilitate fungal multiplication in insects (PubMed:26305932). The non-reducing polyketide synthase OpS1 p... | Beauveria bassiana (strain ARSEF 2860) (White muscardine disease fungus) (Tritirachium shiotae) |
J4W0G2 | ATG1_BEAB2 | MTSRQEGASSHGSRRSSRHVGSFIIDREIGKGSFAQVYMGWHKESKAAVAIKSVELERLNKKLKENLYGEIQILKTLRHPHIVALHDCVESSTHINLIMEYCELGDLSLFIKKRDKLITHPATHDMARKYPSAPNSGLHEVVIRHFLKQLSSALEFLRAKNYVHRDVKPQNLLLLPSQAFREERALPIMEASQDSLIPISGLASLPMLKLADFGFARVLPSTSLADTLCGSPLYMAPEILRYERYDAKADLWSVGTVLYEMITGRPPFRARNHVELLRKIEAAEDVIKFPREVSVTPDLKALVRSLLKRSPVERLSFENF... | 2.7.11.1 | null | autophagosome assembly [GO:0000045]; axon extension [GO:0048675]; negative regulation of collateral sprouting [GO:0048671]; phosphorylation [GO:0016310]; piecemeal microautophagy of the nucleus [GO:0034727]; positive regulation of autophagy [GO:0010508]; protein transport [GO:0015031]; response to starvation [GO:004259... | Atg1/ULK1 kinase complex [GO:1990316]; autophagosome membrane [GO:0000421]; cytosol [GO:0005829]; phagophore [GO:0061908]; phagophore assembly site membrane [GO:0034045]; vacuole-isolation membrane contact site [GO:0120095] | ATP binding [GO:0005524]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF12063;PF21127;PF00069; | 1.10.510.10; | Protein kinase superfamily, Ser/Thr protein kinase family, APG1/unc-51/ULK1 subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P53104}. Preautophagosomal structure membrane {ECO:0000250|UniProtKB:P53104}; Peripheral membrane protein {ECO:0000250|UniProtKB:P53104}. | 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:0000250|UniProtKB:P53104}; CATALYTI... | null | null | null | null | FUNCTION: Serine/threonine protein kinase involved in the cytoplasm to vacuole transport (Cvt) and found to be essential in autophagy, where it is required for the formation of autophagosomes (PubMed:27197558). Involved in the clearance of protein aggregates which cannot be efficiently cleared by the proteasome (By sim... | Beauveria bassiana (strain ARSEF 2860) (White muscardine disease fungus) (Tritirachium shiotae) |
J5JV76 | BSLS_BEAB2 | MEPPNNANTGQLGPTLPNGTVDLPTDLSREITRHFGLEQDEIEEILPCTPFQRDVIECASDDKRRAVGHVVYEIPEDVDTERLAAAWKATVRYTPALRTCIFTSETGNAFQVVLRDCFIFARMYCPSAHLKSAIVKDEATAAVAGPRCNRYVLTGEPNSKRRVLVWTFSHSFVDSAFQGRILQQVLAAYKDEHGRVFSLQPTTDLVESENGDCLSTPASERTVGIERATQFWQEKLHGLDASVFPHLPSHKRVPAIDARADHYLPCPPFIQHEWSSTTVCRTALAILLARYTHSSEALFGVVTEQSHEEHPLLLDGPTST... | 2.1.1.-; 6.1.2.- | null | amino acid activation for nonribosomal peptide biosynthetic process [GO:0043041]; methylation [GO:0032259]; secondary metabolite biosynthetic process [GO:0044550] | cytosol [GO:0005829] | isomerase activity [GO:0016853]; ligase activity [GO:0016874]; methyltransferase activity [GO:0008168]; phosphopantetheine binding [GO:0031177] | PF00501;PF00668;PF00550; | 3.30.300.30;3.40.50.980;1.10.1200.10;3.40.50.1820;3.30.559.10;3.40.50.12780;3.30.559.30;3.40.50.150; | NRP synthetase family | null | null | null | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.46 uM for L-phenylalanyl-N-acetyl-cysteamine thioester (by the MT domain) {ECO:0000269|PubMed:31388353}; KM=2.8 uM for L-leucyl-N-acetyl-cysteamine thioester(by the MT domain) {ECO:0000269|PubMed:31388353}; Vmax=0.41 uM/min/mg enzyme toward L-phenylalanyl-N-acety... | null | null | null | FUNCTION: Bassianolide nonribosomal synthetase that mediates the biosynthesis of bassianolide (BSL), a non-ribosomal cyclodepsipeptide that shows insecticidal and cancer cell antiproliferative activity (PubMed:19285149, PubMed:23608474, PubMed:23727842, PubMed:29163920, PubMed:31388353, PubMed:31471217). BSLS first cat... | Beauveria bassiana (strain ARSEF 2860) (White muscardine disease fungus) (Tritirachium shiotae) |
J7FIX8 | IDTG_CLAPA | MAPSPIMPRYHVGPMASTRRAISKKGFPRTRSFPVLTAPLDYLRDSPGKDIRSGLTDAFNEFLCVPEDKVVTIKRIIDLLHNASLLIDDIQDDSKLRRGVPVAHSIFGIAQTINSANLAYFLAQQELKKLSNPDAFAIYTDELINLHRGQGMELHWRESLHCPTEEEYMRMVQNKTGGLFRLAIRLLQGESRSDRDYVPLVDTLGTLFQIRDDYQNLQSDVYSKNKGFCEDISEGKFSYPVIHSIRARPGDLRLLNILKQRSEDLMVKQYAVSYINSTGSFEFCRGKIDCLAQWANLQLAALEEAEGAGRGDKLRAVLRL... | 2.5.1.-; 2.5.1.1; 2.5.1.10; 2.5.1.29 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q12051}; Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000250|UniProtKB:Q12051}; | alcohol biosynthetic process [GO:0046165]; isoprenoid biosynthetic process [GO:0008299]; ketone biosynthetic process [GO:0042181]; mycotoxin biosynthetic process [GO:0043386] | null | dimethylallyltranstransferase activity [GO:0004161]; farnesyltranstransferase activity [GO:0004311]; geranyltranstransferase activity [GO:0004337]; metal ion binding [GO:0046872] | PF00348; | 1.10.600.10; | FPP/GGPP synthase family | null | null | CATALYTIC ACTIVITY: Reaction=dimethylallyl diphosphate + isopentenyl diphosphate = (2E)-geranyl diphosphate + diphosphate; Xref=Rhea:RHEA:22408, ChEBI:CHEBI:33019, ChEBI:CHEBI:57623, ChEBI:CHEBI:58057, ChEBI:CHEBI:128769; EC=2.5.1.1; Evidence={ECO:0000250|UniProtKB:Q12051}; CATALYTIC ACTIVITY: Reaction=(2E)-geranyl dip... | null | PATHWAY: Secondary metabolite biosynthesis. {ECO:0000269|PubMed:29457197}. | null | null | FUNCTION: Geranylgeranyl pyrophosphate synthase; part of the gene cluster that mediates the biosynthesis of paspalitrems, indole-diterpene (IDT) mycotoxins that are potent tremorgens in mammals (PubMed:23468653, PubMed:29457197, PubMed:32077051). The geranylgeranyl diphosphate (GGPP) synthase idtG is proposed to cataly... | Claviceps paspali (Rye ergot fungus) |
J7GQ11 | TYRDC_LEVBR | MEKSNRSLKDLDLNALFIGDKAENGQLYKDLLNKLVDEHLGWRKNYIPSDPNMIGPEDQNSPAFKKTVGHMKTVLDQLSERIRTESVPWHSAGRYWGHMNSETLMPALLAYNYAMLWNGNNVAYESSPATSQMEEEVGQEFARLMGYDYGWGHIVADGSLANLEGLWYARNIKSLPFAMKEVNPELVAGKSDWELLNMPTKEIMDLLENAGSQIDEVKKRSARSGKNLQRLGKWLVPQTKHYSWMKAADIIGIGLDQVVPVPIDSNYRMDIQALESIIRKYAAEKTPILGVVGVAGSTEEGAVDGIDKIVALRQKLQKEG... | 4.1.1.25 | COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000269|PubMed:24211777}; | carboxylic acid metabolic process [GO:0019752] | null | L-dopa decarboxylase activity [GO:0036468]; pyridoxal phosphate binding [GO:0030170]; tyrosine decarboxylase activity [GO:0004837] | PF00282;PF21391; | 3.40.640.10; | Group II decarboxylase family, Tyrosine decarboxylase subfamily | null | null | CATALYTIC ACTIVITY: Reaction=H(+) + L-tyrosine = CO2 + tyramine; Xref=Rhea:RHEA:14345, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:58315, ChEBI:CHEBI:327995; EC=4.1.1.25; Evidence={ECO:0000269|PubMed:24211777, ECO:0000269|PubMed:27292129}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14346; Evidence={ECO:... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.59 mM for L-tyrosine {ECO:0000269|PubMed:24211777}; KM=0.6 mM for L-tyrosine {ECO:0000269|PubMed:27292129}; KM=0.8 mM for L-dopa {ECO:0000269|PubMed:27292129}; Vmax=147.1 umol/min/mg enzyme for the decarboxylation of L-tyrosine {ECO:0000269|PubMed:24211777}; Note... | PATHWAY: Amino-acid metabolism. {ECO:0000305|PubMed:24211777}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5.0 for the decarboxylation of L-tyrosine. Is not active at pH below 3.5 or above 9.0. More than 90% of activity remains over pH range from 5.0 to 6.0, and activity decreases rapidly at pH below 5.0 or higher than 6.0. {ECO:0000269|PubMed:24211777}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 50 degrees Celsius. Only 8.5% of activity remains at 70 degrees Celsius. However, the enzyme shows poor stability at 50 degrees Celsius, the relative activity dropped to 14% after 1 h of incubation. {ECO:0000269|PubMed:24211777}; | FUNCTION: Catalyzes the decarboxylation of L-tyrosine to produce tyramine (PubMed:24211777, PubMed:27292129). Cannot use other aromatic L-amino acids as substrates like L-phenylalanine, L-tryptophan and L-glutamate (PubMed:24211777). {ECO:0000269|PubMed:24211777, ECO:0000269|PubMed:27292129}.; FUNCTION: Is also able to... | Levilactobacillus brevis (Lactobacillus brevis) |
J7H670 | OXLA_LACMT | MNVFFMFSLLFLAALGSCADDRNPLGECFRETDYEEFLEIAKNGLRATSNPKHVVIVGAGMSGLSAAYVLAEAGHQVTVLEASERAGGRVRTYRNDKEGWYANLGPMRLPEKHRIVREYIRKFGLQLNEFHQENDNAWHFIKNIRKRVGEVKEDPGLLQYPVKPSEEGKSAGQLYEESLGKVAEELKRTNCSYILNKYDTYSTKEYLLKEGNLSPGAVDMIGDLLNEDSGYYVSFIESLKHDDIFGYEKRFDEIVDGMDKLPTSMYQAIKEKVRFNARVIKIQQNDREVTVTYQTSANEMSPVTADYVIVCTTSRATRRI... | 1.4.3.2 | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000305|PubMed:22963728}; | amino acid catabolic process [GO:0009063] | extracellular region [GO:0005576] | L-phenylalaine oxidase activity [GO:0106329]; toxin activity [GO:0090729] | PF01593; | 3.90.660.10;3.50.50.60;1.10.405.10; | Flavin monoamine oxidase family, FIG1 subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:22963728}. | CATALYTIC ACTIVITY: Reaction=an L-alpha-amino acid + H2O + O2 = a 2-oxocarboxylate + H2O2 + NH4(+); Xref=Rhea:RHEA:13781, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:35179, ChEBI:CHEBI:59869; EC=1.4.3.2; Evidence={ECO:0000269|PubMed:22963728}; CATALYTIC ACTIVITY: Reaction=H2O... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.97 mM for L-Leu {ECO:0000269|PubMed:22963728}; Vmax=0.063 umol/min/mg enzyme for L-Leu {ECO:0000269|PubMed:22963728}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.0 for L-Leu. {ECO:0000269|PubMed:22963728}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 4 degrees Celsius. {ECO:0000269|PubMed:22963728}; | FUNCTION: Catalyzes an oxidative deamination of predominantly hydrophobic and aromatic L-amino acids, thus producing hydrogen peroxide that may contribute to the diverse toxic effects of this enzyme (PubMed:22963728). Is highly active on L-Met=L-Leu>>L-Phe>L-Trp>L-Tyr>L-Ile, and weakly or not active on L-His, L-Arg, L-... | Lachesis muta (South American bushmaster) |
J7I4B7 | WBDD_ECOLX | MTKDLNTLVSELPEIYQTIFGHPEWDGDAARDCNQRLDLITEQYDNLSRALGRPLNVLDLGCAQGFFSLSLASKGATIVGIDFQQENINVCRALAEENPDFAAEFRVGRIEEVIAALEEGEFDLAIGLSVFHHIVHLHGIDEVKRLLSRLADVTQAVILELAVKEEPFYWGVSQPDDPRELIEQCAFYRLIGEFDTHLSPVPRPMYLVSNHRVLINDFNQPFQHWQNQPYAGAGLAHKRSRRYFFGEDYVCKFFYYDMPHGILTAEESQRNKYELHNEIKFLTQPPAGFDAPAVLAHGENAQSGWLVMEKLPGRLLSDML... | 2.1.1.294; 2.7.1.181 | null | methylation [GO:0032259]; O antigen biosynthetic process [GO:0009243]; phosphorylation [GO:0016310] | plasma membrane [GO:0005886] | ATP binding [GO:0005524]; methyltransferase activity [GO:0008168]; protein kinase activity [GO:0004672] | PF13847;PF00069; | 1.10.510.10;3.40.50.150; | WbdD family | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:19734145}; Peripheral membrane protein {ECO:0000269|PubMed:19734145}; Cytoplasmic side {ECO:0000269|PubMed:19734145}. | CATALYTIC ACTIVITY: Reaction=3-O-phospho-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-[alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)](n)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-GlcNAc-di-trans,octa-cis-undecaprenyl diphosphate + S-adenosyl-L-methionine = 3-O-methylphospho... | null | PATHWAY: Bacterial outer membrane biogenesis; LPS O-antigen biosynthesis. {ECO:0000269|PubMed:15184370, ECO:0000269|PubMed:21990359}. | null | null | FUNCTION: Regulates the length of the LPS O-antigen polysaccharide chain (PubMed:15184370, PubMed:19734145, PubMed:21990359). Stops the polymerization of the chain by phosphorylating and then methylating the phosphate on the terminal sugar (PubMed:15184370, PubMed:21990359). This terminal modification is essential for ... | Escherichia coli |
J7QLC0 | CYAA_BORP1 | MQQSHQAGYANAADRESGIPAAVLDGIKAVAKEKNATLMFRLVNPHSTSLIAEGVATKGLGVHAKSSDWGLQAGYIPVNPNLSKLFGRAPEVIARADNDVNSSLAHGHTAVDLTLSKERLDYLRQAGLVTGMADGVVASNHAGYEQFEFRVKETSDGRYAVQYRRKGGDDFEAVKVIGNAAGIPLTADIDMFAIMPHLSNFRDSARSSVTSGDSVTDYLARTRRAASEATGGLDRERIDLLWKIARAGARSAVGTEARRQFRYDGDMNIGVITDFELEVRNALNRRAHAVGAQDVVQHGTEQNNPFPEADEKIFVVSATG... | 4.6.1.1 | null | cAMP biosynthetic process [GO:0006171]; hemolysis in another organism [GO:0044179] | extracellular region [GO:0005576]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020] | ATP binding [GO:0005524]; calcium ion binding [GO:0005509]; calcium ion sequestering activity [GO:0140314]; calcium- and calmodulin-responsive adenylate cyclase activity [GO:0008294]; calmodulin binding [GO:0005516]; channel activity [GO:0015267]; ion binding [GO:0043167]; toxin activity [GO:0090729] | PF03497;PF06594;PF00353;PF02382; | 1.10.150.920;3.30.70.1720;3.90.1760.10;2.150.10.10; | Adenylyl cyclase class-2 family; RTX prokaryotic toxin family | PTM: Released in a processed form. {ECO:0000250|UniProtKB:P0DKX7}.; PTM: [Hemolysin]: Palmitoylated at Lys-860 and Lys-983 by CyaC (PubMed:11031260). The toxin only becomes active when modified in position Lys-983 (PubMed:11031260). Palmitoylation Lys-983 is required for efficient membrane insertion and pore formation ... | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:2905265}.; SUBCELLULAR LOCATION: [Hemolysin]: Host cell membrane {ECO:0000305|PubMed:7525549}; Multi-pass membrane protein {ECO:0000305}. | CATALYTIC ACTIVITY: [Calmodulin-sensitive adenylate cyclase]: Reaction=ATP = 3',5'-cyclic AMP + diphosphate; Xref=Rhea:RHEA:15389, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:58165; EC=4.6.1.1; Evidence={ECO:0000250|UniProtKB:P0DKX7}; | null | null | null | null | FUNCTION: Bifunctional adenylate cyclase toxin-hemolysin that plays a crucial role in host colonization (PubMed:2905265). It causes whooping cough by acting on mammalian cells by elevating cAMP-concentration and thus disrupts normal cell function (PubMed:2905265). {ECO:0000269|PubMed:2905265}.; FUNCTION: [Calmodulin-se... | Bordetella pertussis (strain ATCC 9797 / DSM 5571 / NCTC 10739 / 18323) |
J7RUA5 | CAS9_STAAU | MKRNYILGLDIGITSVGYGIIDYETRDVIDAGVRLFKEANVENNEGRRSKRGARRLKRRRRHRIQRVKKLLFDYNLLTDHSELSGINPYEARVKGLSQKLSEEEFSAALLHLAKRRGVHNVNEVEEDTGNELSTKEQISRNSKALEEKYVAELQLERLKKDGEVRGSINRFKTSDYVKEAKQLLKVQKAYHQLDQSFIDTYIDLLETRRTYYEGPGEGSPFGWKDIKEWYEMLMGHCTYFPEELRSVKYAYNADLYNALNDLNNLVITRDENEKLEYYEKFQIIENVFKQKKKPTLKQIAKEILVNEEDIKGYRVTSTGK... | 3.1.-.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_01480}; | defense response to virus [GO:0051607]; maintenance of CRISPR repeat elements [GO:0043571] | null | DNA binding [GO:0003677]; endonuclease activity [GO:0004519]; metal ion binding [GO:0046872]; RNA binding [GO:0003723] | PF18070;PF21574;PF18061;PF13395;PF18541; | 3.30.420.10; | CRISPR-associated Cas9 family, Subtype II-A subfamily | null | null | null | null | null | null | null | FUNCTION: CRISPR (clustered regularly interspaced short palindromic repeat) is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain spacers, sequences complementary to antecedent mobile elements, and target ... | Staphylococcus aureus |
J7SHB8 | FLDH_CLOS1 | MKILAYCVRPDEIDSFKNFSEKYGHTVDLIPDSFGPNVAHLAKGYDGISILGNDTCNREALEKIKDCGIKYLATRTAGVNNIDFDAAKEFGINVANVPAYSPNSVSEFTVGLALSLTRKIPFALKRVELNNFALGGLIGVELRNLTLGVIGTGRIGLKVIEGFSGFGMKKMIGYDIFENEKAKEYIEYKSLDEVYKEADIITLHAPLTDDNYHMIGKESIAKMKDGVFIINAARGALIDSEALIEGLKSGKIAGAALDSYEYEQGVFHNNKMNEIMKDDTLERLKSFPNVVITPHLGFYTDEAVSNMVEITLMNLQEFEL... | 1.1.1.110 | null | L-phenylalanine catabolic process [GO:0006559]; tryptophan catabolic process [GO:0006569]; tyrosine catabolic process [GO:0006572] | null | 4-phosphoerythronate dehydrogenase activity [GO:0033711]; D-lactate dehydrogenase activity [GO:0008720]; hydroxyphenylpyruvate reductase activity [GO:0047995]; indolelactate dehydrogenase (NADH) activity [GO:0047722]; NAD binding [GO:0051287]; phenyllactate dehydrogenase activity [GO:0097256] | PF00389;PF02826; | 3.40.50.720; | D-isomer specific 2-hydroxyacid dehydrogenase family | null | null | CATALYTIC ACTIVITY: Reaction=(R)-3-phenyllactate + NAD(+) = 3-phenylpyruvate + H(+) + NADH; Xref=Rhea:RHEA:38351, ChEBI:CHEBI:11009, ChEBI:CHEBI:15378, ChEBI:CHEBI:18005, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.110; Evidence={ECO:0000269|PubMed:29168502, ECO:0000269|PubMed:4384683}; PhysiologicalDirection=right-... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.075 mM for p-hydroxyphenylpyruvate {ECO:0000269|PubMed:4384683}; KM=0.106 mM for phenylpyruvate {ECO:0000269|PubMed:4384683}; KM=0.0142 mM for NADH (in the presence of indolepyruvate) {ECO:0000269|PubMed:4384683}; KM=1.03 mM for indolelactate {ECO:0000269|PubMed:... | PATHWAY: Amino-acid degradation. {ECO:0000269|PubMed:29168502}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.0 for indolepyruvate reduction. Optimum pH is 8.5 for indolelactate oxidation. {ECO:0000269|PubMed:4384683}; | null | FUNCTION: Essential for the reductive metabolism of L-phenylalanine, L-tyrosine and L-tryptophan (PubMed:29168502). Catalyzes the conversion of phenylpyruvic acid to phenyllactic acid, 4-hydroxy-phenylpyruvic acid to 4-hydroxy-phenyllactic acid, and indolepyruvic acid to indolelactic acid (PubMed:29168502, PubMed:43846... | Clostridium sporogenes (strain ATCC 15579) |
J8G6Z1 | THSA_BACCS | MKMNPIVELFIKDFTKEVMEENAAIFAGAGLSMSVGYVSWAKLLEPIAQEIGLDVNKENDLVSLAQYYCNENQGNRGRINQIILDEFSRKVDLTENHKILARLPIHTYWTTNYDRLIEKALEEENKIADVKYTVKQLATTKVKRDAVVYKMHGDVEHPSEAVLIKDDYEKYSIKMDPYIKALSGDLVSKTFLFVGFSFTDPNLDYILSRVRSAYERDQRRHYCLIKKEERRPDELEADFEYRVRKQELFISDLSRFNIKTIVLNNYNEITEILQRIENNIKTKTVFLSGSAVEYNHWETEHAEQFIHQLSKELIRKDFNI... | 3.2.2.5 | null | defense response to virus [GO:0051607] | cytoplasm [GO:0005737] | hydrolase activity [GO:0016787]; nucleotide binding [GO:0000166] | PF13289;PF18185; | null | Soluble Thoeris ThsA family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:29371424}. | 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=3.2.2.5; Evidence={ECO:0000269|PubMed:32499527, ECO:0000269|PubMed:36048923}; PhysiologicalDirection=left-to-right; Xref... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=269.8 uM for NAD(+) {ECO:0000269|PubMed:32499527}; Note=kcat is 33.9 min(-1) (PubMed:32499527). {ECO:0000269|PubMed:32499527}; | null | null | null | FUNCTION: NAD(+) hydrolyzing component (NADase) of the Thoeris antiviral defense system, composed of ThsA and ThsB. Activated by a signal molecule generated by endogenous ThsB (AC J8G8J6) or ThsB' (AC J8CSK2, probably 3'cADPR), by TIR1 and TIR2 from B.dafuensis or by BdTIR from B.distachyon (AC I1GTC2, probably 2'cADPR... | Bacillus cereus (strain MSX-D12) |
J8H9C1 | GAJA_BACC6 | MKFSNITIKNFRNFEKVNINLDNKNVIFGMNDIGKTNFLYALRFLLDKEIRKFGFNKSDYHKHDTSKKIEIILTLDLSNYEKDEDTKKLISVVKGARTSANADVFYIALESKYDDKELYGNIILKWGSELDNLIDIPGRGNINALDNVFKVIYINPLVDLDKLFAQNKKYIFEESQGNESDEGILNNIKSLTDQVNQQIGEMTIIKGFQQEITSEYRSLKKEEVSIELKSEMAIKGFFSDIIPYIKKDGDSNYYPTSGDGRRKMLSYSIYNYLAKKKYEDKIVIYLIEEPEISLHRSMQIALSKQLFEQSTYKYFFLSTH... | 3.1.-.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:33885789}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:33885789}; Note=Rapid, sequence-specific cleavage at physiological concentrations of Mg(2+) (4-5 mM) or Mn(2+) (15 uM). In presence of >20 uM Mn(2+) has rapid non-spec... | defense response to virus [GO:0051607] | null | endonuclease activity [GO:0004519]; metal ion binding [GO:0046872] | PF13175;PF20469; | 3.40.50.300; | null | null | null | null | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 9.0. {ECO:0000269|PubMed:33885789}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 37-42 degrees Celsius. {ECO:0000269|PubMed:33885789}; | FUNCTION: Component of antiviral defense system Gabija type I, composed of GajA and GajB (PubMed:29371424). Endonuclease that nicks double-stranded DNA within the sequence 5'-TNNNCGGGNNA-3' in the absence of nucleotides (NTP, dNTP and NDPs), cleaving after C-1 (PubMed:33885789, PubMed:37992757). Has no detected ATPase ... | Bacillus cereus (strain VD045) |
J9VE33 | CRZ1_CRYNH | MADPASPPSFDAIFAQQPVRRSSSTSTSSFANYTYSALQQHQQFNSDAPLVDEPQSLSEQARKQQRDPSKDGNNKRYLDMMSGLADGYGVINGRRQESLRKESLPFNPQEDSTLIATAPKRGERNGLGRNGYSSPIGDIMFGPEQTIPNQPQQPSQQPPWGEGRMSEQSVHYASVQQPQYSSFQSSGPGAGSAGIDYLPRGTTSSMNDSMLSSQISPYLNHDVASEGQPPQQQQQQQQQQQGEWGQEFIGVEQQQQYAQGEGQSNGMEDMLTMGDESPFESELQRVISNTSHPSQYPSRTSSPFPQQSQSNMVPASTVNQ... | null | null | calcineurin-mediated signaling [GO:0097720]; negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of transcription by RNA polymerase II [GO:0045944]; positive regulation of transepithelial migration of symbiont in host [GO:0140471]; regulation of fungal-type cell wall organization... | chromatin [GO:0000785]; cytosol [GO:0005829]; nucleus [GO:0005634] | DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; metal ion binding [GO:0046872]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978] | PF00096; | 3.30.160.60; | null | PTM: Phosphorylated (PubMed:21487010, PubMed:27611567). Dephosphorylated by calcineurin (CNA1) which promotes nuclear localization (PubMed:27611567). {ECO:0000269|PubMed:21487010, ECO:0000269|PubMed:27611567}. | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:23251520, ECO:0000269|PubMed:27611567, ECO:0000269|PubMed:28376087, ECO:0000269|PubMed:28898238, ECO:0000269|PubMed:31266771}. Nucleus {ECO:0000269|PubMed:21487010, ECO:0000269|PubMed:23251520, ECO:0000269|PubMed:24520056, ECO:0000269|PubMed:27611567, ECO:000... | null | null | null | null | null | FUNCTION: DNA-binding transcriptional activator that interacts with calcineurin-dependent response element (CDRE) promoters (PubMed:28376087). Activates expression of genes required to maintain cell wall integrity during stress (PubMed:23251520, PubMed:28376087). Activates expression of genes required for transepitheli... | Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 / CBS 10515 / FGSC 9487) (Filobasidiella neoformans var. grubii) |
J9VHN6 | X325_CRYNH | MFALKSILVTSLITSTALAHFTLDYPQSRGFVDDTENQFCGGFNTVEARQPFPLGSGPVHIDSHHALATIVAFISTSSNPTSFDDFNTTSNGTAIPLASSIFQVPQGEKCFNIDLQSLNVGLTNGSEVTLQIQYDGGDGNLYQCSDLVLIEGYEVPSNETCTNDASKASNATSTSSGSATATSAAATSSSSGTSGAIKEVVGFGALSLALGIAGLIIL | null | COFACTOR: Name=Cu(2+); Xref=ChEBI:CHEBI:29036; Evidence={ECO:0000269|PubMed:31932719}; Note=Binds 1 copper ion per subunit. {ECO:0000269|PubMed:31932719}; | null | plasma membrane [GO:0005886]; side of membrane [GO:0098552] | metal ion binding [GO:0046872] | PF20238; | null | X325 family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000255}; Lipid-anchor, GPI-anchor {ECO:0000255}. Note=Proteins attached to a GPI anchor via their C terminus are found in the outer leaflet of the lipid bilayer facing the extracellular environment. GPI anchors can also be considered as predetermined breaking points, which allo... | null | null | null | null | null | FUNCTION: Lytic polysaccharide monooxygenase-like protein that has diverged to biological functions other than polysaccharide degradation since it does not perform oxidative cleavage of polysaccharides (Probable). Cell surface-bound protein that functions in the copper-accumulation pathway shared by the CUF1-dependent ... | Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 / CBS 10515 / FGSC 9487) (Filobasidiella neoformans var. grubii) |
J9VI03 | DMT5_CRYNH | MTTALTFGGGLFKDNTKFDIDMRGTADGAVNGGNIPNSQSQKRKRASPSPEIESEEDGDDWYEIDYIADSRVIRRKGRQILQYLIHWAGYAVHERTWEDEDGIGGEDCALVQEFYRKNPGKPRLSPSSVRKEVKLARMVEVVITTRRIDGKSRAASSTDQPSPHRLGITSPQANNIGGEDPNPSLTRRPVRSTVSEIAKRPTSKKVHPNKKCKASSDDESDFVFEEGEWDEDEDDDNDVDFRSSEDDEDDEQERSAEEPESDEEIIKPAKKTKSSLPKAKLRPKPANLGGFVTGVRPLNQGLDIKAAVRNMSDDLPPISD... | 3.6.4.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:32437639}; | DNA methylation-dependent heterochromatin formation [GO:0006346]; methylation [GO:0032259]; nucleotide-excision repair [GO:0006289] | chromosome [GO:0005694]; nucleus [GO:0005634] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATP-dependent chromatin remodeler activity [GO:0140658]; ATP-dependent DNA (cytosine-5-)-methyltransferase activity [GO:0120328]; chromatin binding [GO:0003682]; DNA (cytosine-5-)-methyltransferase activity [GO:0003886]; sequence-specific DNA binding [GO:0... | PF00385;PF00145;PF00271;PF00176; | 2.40.50.40;3.40.50.300;3.40.50.10810;3.40.50.150; | Class I-like SAM-binding methyltransferase superfamily, C5-methyltransferase family; SNF2/RAD54 helicase family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:31955845}. Chromosome {ECO:0000269|PubMed:31955845}. Note=Localizes to heterochromatin characterized by trimethylation of histone H3 'Lys-9'. {ECO:0000269|PubMed:31955845}. | CATALYTIC ACTIVITY: Reaction=a 2'-deoxycytidine in DNA + ATP + H2O + S-adenosyl-L-methionine = a 5-methyl-2'-deoxycytidine in DNA + ADP + 2 H(+) + phosphate + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:68984, Rhea:RHEA-COMP:11369, Rhea:RHEA-COMP:11370, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.9 uM for ATP (in the presence of unmethylated DNA and at 23 degrees Celsius) {ECO:0000269|PubMed:32437639}; KM=6.2 uM for ATP (in the presence of hemimethylated DNA and at 23 degrees Celsius) {ECO:0000269|PubMed:32437639}; Note=kcat is 5.0 min(-1) for ATP (in the... | null | null | null | FUNCTION: ATP-dependent cytosine methylase that maintains DNA methylation by acting at hemimethylated palindromic 5'-CG-3' sites to produce symmetrically methylated DNA strands (PubMed:24630728, PubMed:31955845, PubMed:32437639). DNA methylation may play a role in transcriptional silencing, particularly at transposable... | Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 / CBS 10515 / FGSC 9487) (Filobasidiella neoformans var. grubii) |
J9VJP1 | PUR9_CRYNH | MSSEAPIALLSVYDKTGLLPFAKSLKELGFRLLGSGGTAKMIREAGMEIEDVSNITKAPEMLGGRVKTLHPAVHGGILSRDIPSDLADLATNKISPITLVVCNLYPFVLQTAKPDCTLAGAIEEIDIGGVTLLRAAAKNHGRVSIISSPSDYETIVAELRAKGEVSAETRRGLAIKAFEDTKSYDEAISDYFRKVYATPGVEEEMKAGAGVGYQRLGLRYGANPHQKPAQAFVEQGEMPIKVLSGSPGYINLLDALNSWALVKELAAGLDLPAAASFKHVSPAGAAVGLPLDERAAKVFGVEDLKELSPLACAYARARGA... | 2.1.2.3; 3.5.4.10 | null | 'de novo' IMP biosynthetic process [GO:0006189] | cytosol [GO:0005829] | IMP cyclohydrolase activity [GO:0003937]; phosphoribosylaminoimidazolecarboxamide formyltransferase activity [GO:0004643] | PF01808;PF02142; | 1.10.287.440;3.40.140.20;3.40.50.1380; | PurH family | null | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P54113}. | CATALYTIC ACTIVITY: Reaction=(6R)-10-formyltetrahydrofolate + 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide = (6S)-5,6,7,8-tetrahydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide; Xref=Rhea:RHEA:22192, ChEBI:CHEBI:57453, ChEBI:CHEBI:58467, ChEBI:CHEBI:58475, ChEBI:CHEBI:195366; EC=2.... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=130 uM for 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide (with (6S)-10-formyltetrahydrofolate as cosubstrate) (at pH 7.5 and 37 degrees Celsius) {ECO:0000269|PubMed:36063996}; KM=30 uM for 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide (at... | PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide (10-formyl THF route): step 1/1. {ECO:0000269|PubMed:36063996}.; PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; IMP ... | null | null | FUNCTION: Bifunctional enzyme that catalyzes the last two steps of purine biosynthesis (PubMed:36063996). Acts as a transformylase that incorporates a formyl group to the AMP analog AICAR (5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide) to produce the intermediate formyl-AICAR (FAICAR) (PubMed:36063996). A... | Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 / CBS 10515 / FGSC 9487) (Filobasidiella neoformans var. grubii) |
J9VLJ9 | SODC_CRYNH | MVKAVVVLKGESYVHGTVCFTQESENAPVCITGEIKDMDADAKRGMHVHEFGDNTNGCTSAGPHYNPFKKHHGAPTDSERHVGDLGNIQTNSCGAAQLDFSDKIISLYGPHSIIGRSLVVHASTDDLGKGGNEESLKTGNAGARLACGVIGIST | 1.15.1.1 | COFACTOR: Name=Cu cation; Xref=ChEBI:CHEBI:23378; Evidence={ECO:0000250|UniProtKB:P00445}; Note=Binds 1 copper ion per subunit. {ECO:0000250|UniProtKB:P00445}; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:P00445}; Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P00445}; | removal of superoxide radicals [GO:0019430]; symbiont defense to host-produced reactive oxygen species [GO:0052164] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; mitochondrion [GO:0005739]; nucleus [GO:0005634]; peroxisome [GO:0005777]; plasma membrane raft [GO:0044853] | copper ion binding [GO:0005507]; superoxide dismutase activity [GO:0004784] | PF00080; | 2.60.40.200; | Cu-Zn superoxide dismutase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:33567338}. Mitochondrion {ECO:0000269|PubMed:33567338}. Cell membrane {ECO:0000269|PubMed:16524904}; Peripheral membrane protein {ECO:0000305}. Note=Localizes to lipid rafts in the cell membrane. {ECO:0000269|PubMed:16524904}. | CATALYTIC ACTIVITY: Reaction=2 H(+) + 2 superoxide = H2O2 + O2; Xref=Rhea:RHEA:20696, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:18421; EC=1.15.1.1; Evidence={ECO:0000305|PubMed:12496163, ECO:0000305|PubMed:16524904}; | null | null | null | null | FUNCTION: Destroys radicals which are normally produced within the cells and which are toxic to biological systems (PubMed:12496163, PubMed:16524904). Destroys radicals produced by host defense mechanisms (PubMed:12496163). {ECO:0000269|PubMed:12496163, ECO:0000269|PubMed:16524904}. | Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 / CBS 10515 / FGSC 9487) (Filobasidiella neoformans var. grubii) |
J9VND2 | CDA2_CRYNH | MIPSTAAALLTLTAGAAFAHTGCGGHEIGRRNVGGPMLYRRAVTDEASAAVSTDINTECTAYSYAPVTELISSFPTIWQTASIPSNDTEAQQLFGKINSTLNTKIPNDVPHGTPTGDWTGVNYSNSDPDCWWTHNKCTTPSNDTGLQADISIAPEPMTWGLGFDDGPNCSHNALYDLLLENNQKATMFFIGSNVLDWPLQAMRAHDEGHEICVHTWSHQYMTALSNEVVFAELYYTQKAIKAVLGVTPQCWRPPYGDVDNRVRMIAEGLNLTTIIWSDDTDDWAAGTNGVTEQDVTNNYQSVIDKAGNGTYTTHGPVVLN... | 3.5.1.41 | COFACTOR: Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000250|UniProtKB:Q6DWK3}; | cell wall chitin catabolic process [GO:0006039]; cell wall organization [GO:0071555]; fungal-type cell wall biogenesis [GO:0009272]; polysaccharide catabolic process [GO:0000272] | extracellular region [GO:0005576]; fungal-type cell wall [GO:0009277]; plasma membrane [GO:0005886]; side of membrane [GO:0098552] | chitin binding [GO:0008061]; chitin deacetylase activity [GO:0004099]; metal ion binding [GO:0046872] | PF01522; | 3.20.20.370; | Polysaccharide deacetylase family | PTM: The GPI anchor is required for the attachment to the cell membrane but not for cell surface targeting. {ECO:0000269|PubMed:22354955}. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:22354955}. Secreted, cell wall {ECO:0000269|PubMed:22354955}. Cell membrane {ECO:0000269|PubMed:22354955}; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:22354955}. Note=GPI-anchored cell membrane protein (GPI-PMP) (PubMed:22354955). Non-covalently associated to the cell... | CATALYTIC ACTIVITY: Reaction=[(1->4)-N-acetyl-beta-D-glucosaminyl](n) + n H2O = n acetate + chitosan; Xref=Rhea:RHEA:10464, Rhea:RHEA-COMP:9593, Rhea:RHEA-COMP:9597, ChEBI:CHEBI:15377, ChEBI:CHEBI:17029, ChEBI:CHEBI:30089, ChEBI:CHEBI:57704; EC=3.5.1.41; Evidence={ECO:0000305|PubMed:17400891, ECO:0000305|PubMed:2235495... | null | null | null | null | FUNCTION: Hydrolyzes the N-acetamido groups of N-acetyl-D-glucosamine residues in chitin to form chitosan and acetate (PubMed:17400891, PubMed:22354955). Chitosan is required to anchor melanin to the cell wall, for maintenance of cell wall integrity, and for proper cytokinesis (PubMed:17400891). Chitosan offers an adva... | Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 / CBS 10515 / FGSC 9487) (Filobasidiella neoformans var. grubii) |
J9VNT4 | CHS5_CRYNH | MAQQPPPSRFLGVTDLSSLAVTEDTVLVTLQERYISHKPYTSLSPAALVFLSPYSHLPIDDEESLLHYVEEYYQCNNEEGGSRNEQGWWKKKMEQPHVFQLALSAYYNMRRTGQDQVIIASGPTGSGKSELKRLAIEAITQVSLANPGKKGSKIGLQVSSAEFILKCFGNAHTLSNDEASRFGTYTELQFNERGRLEGLKTIVYYFERSRVSQAPINGERNFHAFYYLVSGAPEEERNFLKLGDVSDYRYLNCRVRRVGVDDRHRYSQLRQAFKLMGISSRLIAQIFQLLASILHIGNLRFSPSDGIQEGASVINVETLD... | 2.4.1.16 | null | cell wall organization [GO:0071555]; fungal-type cell wall chitin biosynthetic process [GO:0034221] | cell septum [GO:0030428]; myosin complex [GO:0016459]; plasma membrane [GO:0005886] | actin binding [GO:0003779]; ATP binding [GO:0005524]; chitin synthase activity [GO:0004100]; cytoskeletal motor activity [GO:0003774] | PF03142;PF00173;PF08766;PF00063; | 1.10.10.820;1.20.58.530;3.10.120.10;1.10.10.60;3.40.850.10;1.20.120.720; | TRAFAC class CC myosin-kinesin ATPase superfamily, Myosin family; Chitin synthase family, Class V subfamily | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=[(1->4)-N-acetyl-beta-D-glucosaminyl](n) + UDP-N-acetyl-alpha-D-glucosamine = [(1->4)-N-acetyl-beta-D-glucosaminyl](n+1) + H(+) + UDP; Xref=Rhea:RHEA:16637, Rhea:RHEA-COMP:9593, Rhea:RHEA-COMP:9595, ChEBI:CHEBI:15378, ChEBI:CHEBI:17029, ChEBI:CHEBI:57705, ChEBI:CHEBI:58223; EC=2.4.1.16; Evi... | null | null | null | null | FUNCTION: Polymerizes chitin, a structural polymer of the cell wall and septum, by transferring the sugar moiety of UDP-GlcNAc to the non-reducing end of the growing chitin polymer (PubMed:16278457). Produces a large proportion of the chitin that is not deacetylated to chitosan (PubMed:16278457). {ECO:0000269|PubMed:16... | Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 / CBS 10515 / FGSC 9487) (Filobasidiella neoformans var. grubii) |
J9VP29 | MRJ1_CRYNH | MLSFQATVRPLAVSSRLHSPAAHIWRRNAHTAAMSDDSLDQGSSSSYGDSASQPHLGKGKGRQDSLAQSYRFPEKGMNGGPPDPFEVMALDRSATQQEVKQQYYKLALLLHPDSSHPSSSPDHFATLNKAYNLLSKQSSRSAFLKTGYGWDVSTSSGGNQTWSDSLMRAEIARRRNGGAAAWNGASRRYRDSDAGRGAWGGFDGSQGWRPYEDPSKGFSPPTSGPAEERYMSNPRFLAVVGVASAVIAWVHWHRLGYAAETHRDMLDKQNIDASRALAQARYEAATHGHIRREQIRRRVREAEVLKELEKADQGHIAVAG... | null | null | chaperone cofactor-dependent protein refolding [GO:0051085]; mitochondrial electron transport, ubiquinol to cytochrome c [GO:0006122]; protein refolding [GO:0042026] | mitochondrion [GO:0005739]; respirasome [GO:0070469] | unfolded protein binding [GO:0051082] | PF00226; | 1.10.287.110; | DnaJ family | null | SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:32518190}. | null | null | null | null | null | FUNCTION: Mitochondrial co-chaperone required for ubiquinol-cytochrome c oxidoreductase (mitochondrial respiratory chain complex III) activity. {ECO:0000269|PubMed:32518190}. | Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 / CBS 10515 / FGSC 9487) (Filobasidiella neoformans var. grubii) |
J9VPD7 | CDA1_CRYNH | MFTFAAFSALLISLAGVVAQTTGTSVDSSILTKTADSTGPSGFSIPALSELTSGAPTDSTVALYSTFAAGATPTVSGAPVLPTSALTIADYPALDVTPPTNSSLVKDWMAKIDLSKVPSYNVTTGDCSTDAAAISDGRCWWTCGGCTRETDIVECPDKNVWGLSYDDGPSPFTPLLIDYLQEKNIKTTFFVVGSRVLSRPEMLQTEYMSGHQISIHTWSHPALTTLTNEEIVAELGWTMKVIKDTLGVTPNTFRPPYGDIDDRVRAIAAQMGLTPVIWTSYTDGSTTVNFDTNDWHISGGTATGASSYETFEKILTEYAP... | 3.5.1.41 | COFACTOR: Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000250|UniProtKB:Q6DWK3}; | cell wall chitin catabolic process [GO:0006039]; cell wall organization [GO:0071555]; evasion of host immune response [GO:0042783]; fungal-type cell wall biogenesis [GO:0009272]; polysaccharide catabolic process [GO:0000272] | extracellular region [GO:0005576]; fungal-type cell wall [GO:0009277]; plasma membrane [GO:0005886]; side of membrane [GO:0098552] | chitin binding [GO:0008061]; chitin deacetylase activity [GO:0004099]; metal ion binding [GO:0046872] | PF01522; | 3.20.20.370; | Polysaccharide deacetylase family | null | SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000269|PubMed:30459196}. Cell membrane {ECO:0000269|PubMed:30459196}; Lipid-anchor, GPI-anchor {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=[(1->4)-N-acetyl-beta-D-glucosaminyl](n) + n H2O = n acetate + chitosan; Xref=Rhea:RHEA:10464, Rhea:RHEA-COMP:9593, Rhea:RHEA-COMP:9597, ChEBI:CHEBI:15377, ChEBI:CHEBI:17029, ChEBI:CHEBI:30089, ChEBI:CHEBI:57704; EC=3.5.1.41; Evidence={ECO:0000305|PubMed:17400891, ECO:0000305|PubMed:3045919... | null | null | null | null | FUNCTION: Hydrolyzes the N-acetamido groups of N-acetyl-D-glucosamine residues in chitin to form chitosan and acetate (PubMed:17400891, PubMed:30459196). Chitosan is required to anchor melanin to the cell wall, for maintenance of cell wall integrity, and for proper cytokinesis (PubMed:17400891). Plays a major role in s... | Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 / CBS 10515 / FGSC 9487) (Filobasidiella neoformans var. grubii) |
J9VWU3 | ATM1_CRYNH | MGFGSCSRHALFTPAAFSGSFTTMTTSCFKRVYTAQIHGGDALGKRLPSVSSFSGQLPRHGLHRQSLAFFSTSHRRQTSPPPSPRTTSQSPTVPSKASTTPPTSLNTSKPIATESQDKTDWSIIVKLAGNIWPKNNPNVKFRVIGALTLLVAGKVLNVQVPFFFKTIVDSLNVPITESTTVWVLAGASIAGYGAARILTTLFGELRNAVFASVAQNAIRKVARETFEHLLNMDMKFHLERQTGGLTRAIDRGTKGISFILSSIVFHVIPTALEISMVCGILSWKFGWDFAAVTAITMLLYTWFTIKTTAWRTTFRKQANA... | 7.-.-.- | null | intracellular iron ion homeostasis [GO:0006879]; iron-sulfur cluster assembly [GO:0016226]; iron-sulfur cluster export from the mitochondrion [GO:0140466] | mitochondrial inner membrane [GO:0005743]; mitochondrial membrane [GO:0031966] | ABC-type transporter activity [GO:0140359]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887] | PF00664;PF00005; | 1.20.1560.10;3.40.50.300; | ABC transporter superfamily, ABCB family, Heavy Metal importer (TC 3.A.1.210) subfamily | null | SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000305|PubMed:29089435, ECO:0000305|PubMed:29420779}; Multi-pass membrane protein {ECO:0000255}. | null | null | null | null | null | FUNCTION: Performs an essential function in the generation of cytoplasmic iron-sulfur proteins by mediating the ATP-dependent export of mitochondrial Fe/S cluster precursors synthesized by NFS1 and other mitochondrial proteins (PubMed:29089435, PubMed:29420779). Hydrolyzes ATP (By similarity). Binds glutathione and may... | Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 / CBS 10515 / FGSC 9487) (Filobasidiella neoformans var. grubii) |
J9VWW9 | SODM_CRYNH | MITAITRTALPRATLRTSLATMSTIRAKHTLPPLPYAYDALEPSISAEIMNLHHTKHHQTYVNGLNAAEESLQKASADGDFKTAISLQPALKFNGGGHINHSLFWKNLAPTGSAQVKVPTSGVFYDQVQADFGGFENLKKEMNAKTAAIQGSGWGWLGYNKATKKLEIVTTPNQDPLLSHVPIIGIDIWEHAFYLQYKNVKPDYLNAIWNVINYEEAESRLKAAQ | 1.15.1.1 | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:Q9UQX0}; Note=Binds 1 Mn(2+) ion per subunit. {ECO:0000250|UniProtKB:Q9UQX0}; | removal of superoxide radicals [GO:0019430]; symbiont defense to host-produced reactive oxygen species [GO:0052164] | cytosol [GO:0005829]; mitochondrion [GO:0005739] | metal ion binding [GO:0046872]; superoxide dismutase activity [GO:0004784] | PF02777;PF00081; | 1.10.287.990;3.55.40.20; | Iron/manganese superoxide dismutase family | null | SUBCELLULAR LOCATION: [Isoform 1]: Mitochondrion {ECO:0000269|PubMed:33567338}. Note=Localizes to the mitochondrion both in copper-replete and copper-limiting conditions. {ECO:0000269|PubMed:33567338}.; SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm {ECO:0000269|PubMed:33567338}. | CATALYTIC ACTIVITY: Reaction=2 H(+) + 2 superoxide = H2O2 + O2; Xref=Rhea:RHEA:20696, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:18421; EC=1.15.1.1; Evidence={ECO:0000305|PubMed:33567338}; | null | null | null | null | FUNCTION: Destroys radicals which are normally produced within the cells and which are toxic to biological systems. {ECO:0000269|PubMed:15643059, ECO:0000269|PubMed:16524904}.; FUNCTION: [Isoform 1]: Destroys mitochondrial radicals produced by oxidative stress. {ECO:0000269|PubMed:33567338}.; FUNCTION: [Isoform 2]: Des... | Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 / CBS 10515 / FGSC 9487) (Filobasidiella neoformans var. grubii) |
J9VXM5 | CHS3_CRYNH | MSRPHLQQNVSFQDTKPPSRRAGRDDIPPRPPTKSDPSKASLTTTTTVQSVGGYNNHQLDFDDNAYVDAGSSNPQGFSDYNGVRRKKSMVRPERERIDPNHRLWHYREHAAEDQVDIQPSSTGNQPYNQYNNQRPGANLRRGKSLLARETDDVDDSSGLNIFKRGATIRRKASRATPRQAPTGAQSNRVSAGQKEDEECCCLGNFAPGPKNCWMIYCYLLTICIPGFVIAKVFGKKTPDAQRAWREKIGIVSIVLYLMGAVGFITFGFTQTVCGDTQLRLPGGSANTGSLVINGYDYDFSTWRHPVAGDTFNGTTSPLYM... | 2.4.1.16 | null | cell wall organization [GO:0071555]; fungal-type cell wall chitin biosynthetic process [GO:0034221]; protein localization to bud neck [GO:0097271] | cell septum [GO:0030428]; cellular bud neck [GO:0005935]; chitosome [GO:0045009]; incipient cellular bud site [GO:0000131]; plasma membrane [GO:0005886] | chitin synthase activity [GO:0004100] | PF03142; | null | Chitin synthase family, Class IV subfamily | PTM: Palmitoylated by PFA4; required for proper subcellular localization. {ECO:0000269|PubMed:25970403}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:25970403}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=[(1->4)-N-acetyl-beta-D-glucosaminyl](n) + UDP-N-acetyl-alpha-D-glucosamine = [(1->4)-N-acetyl-beta-D-glucosaminyl](n+1) + H(+) + UDP; Xref=Rhea:RHEA:16637, Rhea:RHEA-COMP:9593, Rhea:RHEA-COMP:9595, ChEBI:CHEBI:15378, ChEBI:CHEBI:17029, ChEBI:CHEBI:57705, ChEBI:CHEBI:58223; EC=2.4.1.16; Evi... | null | null | null | null | FUNCTION: Polymerizes chitin, a structural polymer of the cell wall and septum, by transferring the sugar moiety of UDP-GlcNAc to the non-reducing end of the growing chitin polymer (PubMed:16278457). Activated by CSR2, it produces chitin that is deacetyled to chitosan, which is required to maintain cell wall integrity ... | Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 / CBS 10515 / FGSC 9487) (Filobasidiella neoformans var. grubii) |
J9VYP5 | PUR2_CRYNH | MPEITAFPQPKSDLSILLLGAGGREHALAFKLAQSSRVARIVVCPGNGGTALMGGKVSNLALPWGAPPAFRSIVEWAQKENIDLVVPGPEQPLVDGVEGAFKKVGIPVFGPSPAAAMLEGSKSLSKEFMARHNIPTAAFRSFTSTQYEDAVAYIKSKPFTSGRSVIKASGLAAGKGVLIPETDEEAFAALKSVMVDKEFGDAGDEVVVEEYLSGPEISVLAFSDGYTIVPMPAAQDHKRIGEGDTGLNTGGMGAYAPAPIATKEIMERCVKDVLEPTIKGMREDGYPFVGMLFTGFMITADGPRVLEYNVRFGDPETQAL... | 6.3.3.1; 6.3.4.13 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|PROSITE-ProRule:PRU00409}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000255|PROSITE-ProRule:PRU00409}; Note=Binds two magnesium or manganese ions per subunit. {ECO:0000305}; | 'de novo' IMP biosynthetic process [GO:0006189]; adenine biosynthetic process [GO:0046084] | cytosol [GO:0005829] | ATP binding [GO:0005524]; metal ion binding [GO:0046872]; phosphoribosylamine-glycine ligase activity [GO:0004637]; phosphoribosylformylglycinamidine cyclo-ligase activity [GO:0004641] | PF00586;PF02769;PF01071;PF02843;PF02844; | 3.40.50.20;3.30.1490.20;3.30.470.20;3.90.600.10;3.90.650.10;3.30.1330.10; | GARS family; AIR synthase family | null | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P20772}. | CATALYTIC ACTIVITY: Reaction=2-formamido-N(1)-(5-O-phospho-beta-D-ribosyl)acetamidine + ATP = 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole + ADP + H(+) + phosphate; Xref=Rhea:RHEA:23032, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:137981, ChEBI:CHEBI:147287, ChEBI:CHEBI:456216; EC=6.3.3.1; Evi... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=48 uM for ATP (at 37 degrees Celsius) {ECO:0000269|PubMed:34416230}; KM=496 uM for glycine (at 37 degrees Celsius) {ECO:0000269|PubMed:34416230}; KM=131 uM for phosphoribosyl-amine (at 37 degrees Celsius) {ECO:0000269|PubMed:34416230}; Note=kcat is 27.3 sec(-1) for... | PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole from N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide: step 2/2. {ECO:0000305|PubMed:34416230}.; PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phos... | null | null | FUNCTION: Catalyzes the second and fifth step in the 'de novo' purine biosynthesis pathway; contains phosphoribosylamine--glycine ligase (GARS) and phosphoribosylformylglycinamidine cyclo-ligase (AIRS) activities. {ECO:0000269|PubMed:34416230}. | Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 / CBS 10515 / FGSC 9487) (Filobasidiella neoformans var. grubii) |
J9W0G9 | YPK1_CRYNH | MMSWKFGKKFKEGGFLSGKHHSSNNNSPSDTSRSTTPTPGNPHPEDAVKPPVPRSGMLKIRVTAAKGLSLPQGVSVPAPVQEALTTHPTLASRIATSPPTAIVKAAGANRDSLQRRQVWWLPYLVLEFDKNEVLVDALGGDLASPVWMYSATFDVSRISEISATVYLRTREPHAEGREKSNGEGEGEDMGNSDLCLGSIRFTPNLDSLRVTDDWVTVQGGGGSGSINVQVSFKPASGQILTIDSFELLKVIGKGSFGKVMQVRKRDTLRIYALKTIRKAHIVSRSEVTHTLAERTVLAQVNCPFIVPLKFSFQSKEKLYL... | 2.7.11.1 | null | phosphorylation [GO:0016310]; regulation of sphingolipid biosynthetic process [GO:0090153] | cytoplasm [GO:0005737]; nucleus [GO:0005634] | ATP binding [GO:0005524]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF00069;PF00433; | 1.10.510.10; | Protein kinase superfamily, AGC Ser/Thr protein kinase family, RAC subfamily | null | null | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000250|UniProtKB:Q9P7J8}; CATALYTI... | null | null | null | null | FUNCTION: Probable serine/threonine-protein kinase which may act in the sphingolipid-mediated signaling pathway (PubMed:22339665). May act downstream of TORC2 (TOR complex 2) and PDK1 to regulate sphingolipid metabolism (PubMed:22339665). {ECO:0000269|PubMed:22339665}. | Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 / CBS 10515 / FGSC 9487) (Filobasidiella neoformans var. grubii) |
K0I210 | FOMT4_OCIBA | MAVDKEVELHAQAWDHALSYITPTALSAAVELEIPDILEDHGGLMSLSELSAASGCPREPLYRLMRFLIFHGIFTKSNDCYAQSPLSRVFTRENLGPYMLMQATPVTRSPAGLSGEALKTGTPLYLKSIRGEDSWNDPAYGFHMRAFTNGMAAHARLTAAAIVTNYPTAFNGVRSVVDVGGRHGMAIGKLVEAFPWVRGIAFDLPEVVADAPPRKGVDFVGGDMFESLPKADAVMLMWVLHDWSDDKCIEILKKCKEAIPTSTGKVMIVDAIINEEGEGDEFSGARLSLDMTMMAMTTQGKERSYKEWVHLLNEAGFSKH... | 2.1.1.- | null | melatonin biosynthetic process [GO:0030187]; methylation [GO:0032259] | null | acetylserotonin O-methyltransferase activity [GO:0017096]; protein dimerization activity [GO:0046983] | PF08100;PF00891; | 3.40.50.150;1.10.10.10; | Class I-like SAM-binding methyltransferase superfamily, Cation-independent O-methyltransferase family | null | null | CATALYTIC ACTIVITY: Reaction=ladanein + S-adenosyl-L-methionine = H(+) + S-adenosyl-L-homocysteine + salvigenin; Xref=Rhea:RHEA:73247, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:192702, ChEBI:CHEBI:192703; Evidence={ECO:0000269|PubMed:22923679}; PhysiologicalDirection=left-to-right; Xref=Rhea:... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=98 nM for scutellarein-7-methyl ether (in the presence of S-adenosyl-L-methionine) {ECO:0000269|PubMed:22923679}; KM=54 nM for ladanein (in the presence of S-adenosyl-L-methionine) {ECO:0000269|PubMed:22923679}; KM=21 uM for S-adenosyl-L-methionine (in the presence... | PATHWAY: Flavonoid metabolism. {ECO:0000303|PubMed:30468448}. | null | null | FUNCTION: Flavonoid 6-O-methyltransferase involved in the biosynthesis of polymethoxylated flavonoids natural products such as nevadensin and salvigenin (SALV), aroma compounds which contribute to the flavor of sweet basil, and exhibit pharmacological activities such as anti-allergic, anti-oxidant, antibacterial, anti-... | Ocimum basilicum (Sweet basil) |
K0I7Q2 | FOMT3_OCIBA | MAVDKEVQLHAQAWEHALSYINSTALSAAVELEIPDILEDHGGLMSLSELSAASGCPREPLYRLMRFLIFHGIFTKSDDCYAQSPLSRLFTRENLGPYMLMQATPVTRSPAGLSGEALKTGTSLYLKSIRGEDSWSDPAYGYHMKAFTNAMIAHARLTAAAIVSNYPAAFDGLRSVVDVGGRHGTAIGRLVEAFPWVRGIAFDLPEIVADAPPRKGVDFVGGDMFESVPKADAVMLMWILHDWSDDKCIEILKKCKEAIPASTGKVMIVDAIINEDGEGDEFSGARLSLDMIMLAVMAQGKERTYKEWVHLLNEAGFSKH... | 2.1.1.- | null | melatonin biosynthetic process [GO:0030187]; methylation [GO:0032259] | null | acetylserotonin O-methyltransferase activity [GO:0017096]; protein dimerization activity [GO:0046983] | PF08100;PF00891; | 3.40.50.150;1.10.10.10; | Class I-like SAM-binding methyltransferase superfamily, Cation-independent O-methyltransferase family | null | null | CATALYTIC ACTIVITY: Reaction=S-adenosyl-L-methionine + scutellarein 7-methyl ether = H(+) + ladanein + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:73239, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:192701, ChEBI:CHEBI:192702; Evidence={ECO:0000269|PubMed:22923679}; PhysiologicalDirection=left-to-... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=410 nM for scutellarein-7-methyl ether (in the presence of S-adenosyl-L-methionine) {ECO:0000269|PubMed:22923679}; KM=42 nM for cirsimaritin (in the presence of S-adenosyl-L-methionine) {ECO:0000269|PubMed:22923679}; KM=130 nM for genkwanin (in the presence of S-ad... | PATHWAY: Flavonoid metabolism. {ECO:0000303|PubMed:30468448}. | null | null | FUNCTION: Flavonoid 4'-O-methyltransferase involved in the biosynthesis of polymethoxylated flavonoids natural products such as nevadensin and salvigenin, aroma compounds which contribute to the flavor of sweet basil, and exhibit pharmacological activities such as anti-allergic, anti-oxidant, antibacterial, anti-prolif... | Ocimum basilicum (Sweet basil) |
K0I977 | FOMT1_OCIBA | MGRDEEAAAQAEAWNHGFGFIKTSVIKTAIELEIPDILHNQGGPLSLSALSSAVGVPPDRLHRIMRFLAHHGVSKKTASPPGESDYYYAETAVSRSLTKDNLGPFVLLQGAQRGPSACITAQGLKSRERPGVEELGSDPLYEDPIFTEKVFRDAMTCHARVTTSAVIENYGEGFRGVGSLVDVGGSYGMTLGMLVEAFPWIRGICYDLPPVVAKAKPLHGVEFVAGSMFESVPKADVIMLMFVLHNWSDNECIDILKRCKEAIPAETGRLMIIDAIIDEDGEGDEFAGARLGLDVTMMAVTYEGKERTHREWAYILTEAG... | 2.1.1.-; 2.1.1.232 | null | melatonin biosynthetic process [GO:0030187]; methylation [GO:0032259] | null | acetylserotonin O-methyltransferase activity [GO:0017096]; protein dimerization activity [GO:0046983] | PF08100;PF00891; | 3.40.50.150;1.10.10.10; | Class I-like SAM-binding methyltransferase superfamily, Cation-independent O-methyltransferase family | null | null | CATALYTIC ACTIVITY: Reaction=(2S)-naringenin + S-adenosyl-L-methionine = (2S)-sakuranetin + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:31539, ChEBI:CHEBI:15378, ChEBI:CHEBI:17846, ChEBI:CHEBI:28927, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789; EC=2.1.1.232; Evidence={ECO:0000269|PubMed:22923679}; PhysiologicalDirection=... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=32 nM for apigenin (in the presence of S-adenosyl-L-methionine) {ECO:0000269|PubMed:22923679}; KM=240 nM for luteolin (in the presence of S-adenosyl-L-methionine) {ECO:0000269|PubMed:22923679}; KM=580 nM for scutellarein (in the presence of S-adenosyl-L-methionine)... | PATHWAY: Flavonoid metabolism. {ECO:0000303|PubMed:30468448}. | null | null | FUNCTION: Flavonoid 7-O-methyltransferase involved in the biosynthesis of polymethoxylated flavonoids natural products such as nevadensin and salvigenin, aroma compounds which contribute to the flavor of sweet basil, and exhibit pharmacological activities such as anti-allergic, anti-oxidant, antibacterial, anti-prolife... | Ocimum basilicum (Sweet basil) |
K0ICR0 | FOMT5_OCIBA | MVADEEAQLHAQAWDHALSYIKPTALSAAVELEIPDILENHGGPMTLSELSAASGCPREPLYRLMRFLIFHGIFTKSDDCYAQSPLSRLFTTENLGPYMLMQATPVTRCPTGLSGEALKTGTSLYLKSIRGEDSWSDPAYGYHMKAFTNAMTAHARLTAAAIVRNYPAAFDGVQSVVDVGSRHGTAIGKLVEAFPWVRGIAFDLPEIVADAPPRKGVDFVGGDMFESVPKADAVMLMWILHDWSDDKCIEILKKCKEAIPANIGKVMIVDAIINEDGEGDEFSGTRLSLDMIMLAVMAQGKERTYKEWVHLLNEAGFSKH... | 2.1.1.- | null | melatonin biosynthetic process [GO:0030187]; methylation [GO:0032259] | null | acetylserotonin O-methyltransferase activity [GO:0017096]; protein dimerization activity [GO:0046983] | PF08100;PF00891; | 3.40.50.150;1.10.10.10; | Class I-like SAM-binding methyltransferase superfamily, Cation-independent O-methyltransferase family | null | null | CATALYTIC ACTIVITY: Reaction=genkwanin + S-adenosyl-L-methionine = apigenin 4',7-dimethyl ether + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:73263, ChEBI:CHEBI:2769, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:192700; Evidence={ECO:0000269|PubMed:22923679}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:7326... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=36 nM for scutellarein-7-methyl ether (in the presence of S-adenosyl-L-methionine) {ECO:0000269|PubMed:22923679}; KM=87 nM for cirsimaritin (in the presence of S-adenosyl-L-methionine) {ECO:0000269|PubMed:22923679}; KM=130 nM for genkwanin (in the presence of S-ade... | PATHWAY: Flavonoid metabolism. {ECO:0000303|PubMed:30468448}. | null | null | FUNCTION: Flavonoid 4'-O-methyltransferase involved in the biosynthesis of polymethoxylated flavonoids natural products such as nevadensin and salvigenin, aroma compounds which contribute to the flavor of sweet basil, and exhibit pharmacological activities such as anti-allergic, anti-oxidant, antibacterial, anti-prolif... | Ocimum basilicum (Sweet basil) |
K0II72 | FOMT2_OCIBA | MGRDEEAAARAEAWNHGFGFIKTSVIKTAIELEIPDILHNHGAPLSLSALSSAVGVPPDRLHRIMRFLTHHGVSKKTASPPGESDYYYAETAVSRSLTKDNLGAFVLLQGAQRGPSACITAQGLKSRERPGVEELGSDPLYEDPIFTKMVFRDAMACHARLTTSAVIENYGEGFRGVGSLVDVGGSYGMTLGMLVEAFPWIRGICYDLPQVVAKAKPLHGVEFVAGSMFESVPEADVVMLMFVLHNWSDNECIDILKRCKEAIPRETGKVMIIDAIIEEDGEGDEFAEARLGLDVTMMAVTFEGKERTHREWAFILKEAG... | 2.1.1.-; 2.1.1.232 | null | melatonin biosynthetic process [GO:0030187]; methylation [GO:0032259] | null | acetylserotonin O-methyltransferase activity [GO:0017096]; protein dimerization activity [GO:0046983] | PF08100;PF00891; | 3.40.50.150;1.10.10.10; | Class I-like SAM-binding methyltransferase superfamily, Cation-independent O-methyltransferase family | null | null | CATALYTIC ACTIVITY: Reaction=S-adenosyl-L-methionine + scutellarein 4'-methyl ether = ladanein + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:73111, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:192702, ChEBI:CHEBI:192755; Evidence={ECO:0000269|PubMed:22923679}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:731... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=59 nM for apigenin (in the presence of S-adenosyl-L-methionine) {ECO:0000269|PubMed:22923679}; KM=250 nM for luteolin (in the presence of S-adenosyl-L-methionine) {ECO:0000269|PubMed:22923679}; KM=250 nM for scutellarein (in the presence of S-adenosyl-L-methionine)... | PATHWAY: Flavonoid metabolism. {ECO:0000303|PubMed:30468448}. | null | null | FUNCTION: Flavonoid 7-O-methyltransferase involved in the biosynthesis of polymethoxylated flavonoids natural products such as nevadensin and salvigenin, aroma compounds which contribute to the flavor of sweet basil, and exhibit pharmacological activities such as anti-allergic, anti-oxidant, antibacterial, anti-prolife... | Ocimum basilicum (Sweet basil) |
K0J4Q8 | AHPC_AMPXN | MSLIGTEVQPFRAQAFQSGKDFFEVTEADLKGKWSIVVFYPADFSFVCPTELEDVQKEYAELKKLGVEVYSVSTDTHFVHKAWHENSPAVGSIEYIMIGDPSQTISRQFDVLNEETGLADRGTFIIDPDGVIQAIEINADGIGRDASTLINKVKAAQYVRENPGEVCPAKWEEGGETLKPSLDIVGKI | 1.11.1.26 | null | cell redox homeostasis [GO:0045454]; cellular response to stress [GO:0033554]; hydrogen peroxide catabolic process [GO:0042744]; response to oxidative stress [GO:0006979] | cytosol [GO:0005829] | NADH-dependent peroxiredoxin activity [GO:0102039]; thioredoxin peroxidase activity [GO:0008379] | PF10417;PF00578; | 3.40.30.10; | Peroxiredoxin family, AhpC/Prx1 subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P0AE08}. | CATALYTIC ACTIVITY: Reaction=a hydroperoxide + H(+) + NADH = an alcohol + H2O + NAD(+); Xref=Rhea:RHEA:62628, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30879, ChEBI:CHEBI:35924, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.11.1.26; Evidence={ECO:0000269|PubMed:10960086}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=8.9 uM for H(2)O(2) {ECO:0000269|PubMed:10960086}; KM=10 uM for cumene hydroperoxide {ECO:0000269|PubMed:10960086}; | null | null | null | FUNCTION: Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides. {ECO:0000269|PubMed:10960086}. | Amphibacillus xylanus (strain ATCC 51415 / DSM 6626 / JCM 7361 / LMG 17667 / NBRC 15112 / Ep01) |
K0P2S0 | IF4E1_ARAHY | MVVEDTQKSSITDDQITANPNNENEDLEEGEILDDDDSSATSRPPSSSGALARNPHPLENSWTFWFDNPSAKSKQAAWGSSIRPIYTFATVEEFWSIYNNIHHPSKLAVGADFHCFKHKIEPKWEDPICANGGKWTMTFPRGKSDTSWLYTLLGMIGEQFDHGDEICGAVVNVRNRQEKIALWTKNAANEAAQVSIGKQWKEFLDYNDTIGFIFHEDAKKHDRAAKNKYVI | null | null | defense response to virus [GO:0051607] | cytoplasm [GO:0005737]; eukaryotic translation initiation factor 4F complex [GO:0016281]; nucleus [GO:0005634] | RNA 7-methylguanosine cap binding [GO:0000340]; translation initiation factor activity [GO:0003743] | PF01652; | 3.30.760.10; | Eukaryotic initiation factor 4E family | PTM: According to the redox status, the Cys-129-Cys-167 disulfide bridge may have a role in regulating protein function by affecting its ability to bind capped mRNA. {ECO:0000250|UniProtKB:P29557}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:28344571}. Cytoplasm {ECO:0000269|PubMed:28344571}. | null | null | null | null | null | FUNCTION: Component of the protein complex eIF4F, which is involved in the recognition of the mRNA cap, ATP-dependent unwinding of 5'-terminal secondary structure and recruitment of mRNA to the ribosome (By similarity). Recognizes and binds the 7-methylguanosine-containing mRNA cap during an early step in the initiatio... | Arachis hypogaea (Peanut) |
K1WG73 | CFM6_MARBU | MKYSMITLGAFAMMAVAQLSSLPACGQTCISNMLALAPTFGCTANDASCLCSDVNFAYGIRDCSNAACGAEAAGPVIAYGVEYCSSAGVGLSGSATGIDPGLGPATAVVASTPIATDGASAGSLSAITTSEFTSYVISGDSTVSTIVGSTTIYGPAAGSSSAITTSPIVSTVTSGDTSYPTTVGSTTIFGVAGVISTPTASASSALDSLSSSIASEASVITSSASAAVSSLSSRLSSAASPVSTTTSSAGGARQTAFAGLAAAAGFAAIIL | null | null | biological process involved in interaction with host [GO:0051701] | extracellular space [GO:0005615]; host cell nucleus [GO:0042025]; host cell plasma membrane [GO:0020002]; plasma membrane [GO:0005886]; side of membrane [GO:0098552] | metal ion binding [GO:0046872] | PF05730; | null | RBT5 family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000255}; Lipid-anchor, GPI-anchor {ECO:0000255}. Secreted {ECO:0000269|PubMed:36439212}. Host nucleus {ECO:0000269|PubMed:36439212}. Host cell membrane {ECO:0000269|PubMed:36439212}. Host chloroplast envelope {ECO:0000269|PubMed:36439212}. | null | null | null | null | null | FUNCTION: Appears to function during host infection, and may play a role in suppressing the host immune response. {ECO:0000269|PubMed:36439212}. | Marssonina brunnea f. sp. multigermtubi (strain MB_m1) (Marssonina leaf spot fungus) |
K1XT82 | CFM9_MARBU | MRVLKFLSLMAMLGCTIGQSGSATPGSLHLLGGPTTTDWYPECALRCWENTKYVTKCSEDQQCLCSDVNYQNSVFQCIYSQCDTVHFGSALHHAIAQCLGTDNEVFFAIPPIPDRDALRRREDEYAAGAKLFGSGSAAGYPTESAAFPVQSANYPTDSVGGPYSPSPTASVPFPYFSLTSVTSPAAKSATTTEATRNTVPASTTAPSPSPQLYTGNASTSRATVSLTVVLTVAAVYLVL | null | null | biological process involved in interaction with host [GO:0051701] | extracellular space [GO:0005615]; host cell nucleus [GO:0042025]; host cell plasma membrane [GO:0020002]; plasma membrane [GO:0005886]; side of membrane [GO:0098552] | metal ion binding [GO:0046872] | PF05730; | null | RBT5 family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000255}; Lipid-anchor, GPI-anchor {ECO:0000255}. Secreted {ECO:0000269|PubMed:36439212}. Host nucleus {ECO:0000269|PubMed:36439212}. Host cell membrane {ECO:0000269|PubMed:36439212}. | null | null | null | null | null | FUNCTION: Appears to function during host infection, and may play a role in suppressing the host immune response. {ECO:0000269|PubMed:36439212}. | Marssonina brunnea f. sp. multigermtubi (strain MB_m1) (Marssonina leaf spot fungus) |
K1XVG1 | CFM1_MARBU | MKFSAPVLAIFLASASAQSTAELAAQIPSCAQTCLATAITGAGCTAGDYACQCGTSQNTITASATPCVISACTSEEALNTQRTTSQICALVAAGSASSPSASSSASASASSSASSTSGAASASASASSSASSASAAASALTLAHPIPNPSHPPSPTIQTNLRKKVRNSNRLTPASLSSVSSALVSSASSVRASASSAVSAATTAANPAATTAAGVKEEASFFIPAAVALFAVFAV | null | null | biological process involved in interaction with host [GO:0051701] | extracellular space [GO:0005615]; host cell cytoplasm [GO:0030430]; host cell nucleus [GO:0042025]; host cell plasma membrane [GO:0020002]; plasma membrane [GO:0005886]; side of membrane [GO:0098552] | metal ion binding [GO:0046872] | PF05730; | null | RBT5 family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000255}; Lipid-anchor, GPI-anchor {ECO:0000255}. Secreted {ECO:0000269|PubMed:36439212}. Host cytoplasm {ECO:0000269|PubMed:36439212}. Host nucleus {ECO:0000269|PubMed:36439212}. Host cell membrane {ECO:0000269|PubMed:36439212}. | null | null | null | null | null | FUNCTION: Appears to function during host infection, and may play a role in suppressing the host immune response. {ECO:0000269|PubMed:36439212}. | Marssonina brunnea f. sp. multigermtubi (strain MB_m1) (Marssonina leaf spot fungus) |
K1XW16 | CFM8_MARBU | MQFSIVVMAALASLASAQSMDGIPTCALQCLAQAVVTGGCEASDQACQCGPAREAITAAATPCLLSACTDAADLATAASVGNGMCDKYKMGGDDAAPSPSVNTPAAAAPYPTAPAPNGTVPIGTAAAPSPTANTNETTTVATGSAPQNVAGGLAGIFGLVVAAAFAL | null | null | biological process involved in interaction with host [GO:0051701] | extracellular space [GO:0005615]; host cell nucleus [GO:0042025]; host cell plasma membrane [GO:0020002]; plasma membrane [GO:0005886]; side of membrane [GO:0098552] | metal ion binding [GO:0046872] | PF05730; | null | RBT5 family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000255}; Lipid-anchor, GPI-anchor {ECO:0000255}. Secreted {ECO:0000269|PubMed:36439212}. Host nucleus {ECO:0000269|PubMed:36439212}. Host cell membrane {ECO:0000269|PubMed:36439212}. | null | null | null | null | null | FUNCTION: Appears to function during host infection, and may play a role in suppressing the host immune response. {ECO:0000269|PubMed:36439212}. | Marssonina brunnea f. sp. multigermtubi (strain MB_m1) (Marssonina leaf spot fungus) |
K4BNG7 | NAP2_SOLLC | MVGKNNSNHLPPGFRFHPTDEELIMYYLRNQATSKPCPSSIIPEVDVYKFDPWELPEKTEFGEKEWYFFTPRDRKYPNGVRPNRAAVSGYWKATGTDKGIYSGTKYVGIKKALVFYKGKPPKGIKTDWIMHEYRLSESRTQPTRPNGSMRLDDWVLCRIYKKKNLERAIEMMKVEEDTQEPQIMSVTNPIHEVVASNGQQTLKLPRTCSLSHLLEMDYFGSISQLFDDNNSYNTISQNNTLMTNVNGYVMPHQAMEKFQLGEVSQISMNPSYQFQ | null | null | abscisic acid homeostasis [GO:1902265]; abscisic acid-activated signaling pathway [GO:0009738]; leaf senescence [GO:0010150]; regulation of DNA-templated transcription [GO:0006355]; regulation of reproductive fruiting body development [GO:0031155]; response to abscisic acid [GO:0009737]; response to absence of light [G... | nucleus [GO:0005634] | sequence-specific DNA binding [GO:0043565] | PF02365; | 2.170.150.80; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00353}. | null | null | null | null | null | FUNCTION: Transcription factor that binds DNA motifs 5'-CGT[AG](5N)NACG[ACT][AC][AT][ACG][ACT]-3' and 5'-CACG[ACT][AC][AT][AGT][CT]-3' in target genes promoters. Promotes leaf senescence (developmental, light-induced and ABA-induced senescence) and regulates fruit yield and sugar content, probably by establishing absci... | Solanum lycopersicum (Tomato) (Lycopersicon esculentum) |
K4C9E2 | NSY_SOLLC | METLLKPFPSLLLSSPTPYRSIVQQNPSFLSPTTKKKSRKCLLRNKSSKLFCSFLDLAPTSKPESLDVNISWVDPNSNRAQFDVIIIGAGPAGLRLAEQVSKYGIKVCCVDPSPLSMWPNNYGVWVDEFENLGLEDCLDHKWPMTCVHINDNKTKYLGRPYGRVSRKKLKLKLLNSCVENRVKFYKAKVWKVEHEEFESSIVCDDGKKIRGSLVVDASGFASDFIEYDRPRNHGYQIAHGVLVEVDNHPFDLDKMVLMDWRDSHLGNEPYLRVNNAKEPTFLYAMPFDRDLVFLEETSLVSRPVLSYMEVKRRMVARLRH... | 5.3.99.9; 5.5.1.19 | null | carotene biosynthetic process [GO:0016120]; ubiquinone biosynthetic process [GO:0006744]; xanthophyll biosynthetic process [GO:0016123] | chloroplast [GO:0009507]; mitochondrion [GO:0005739] | lycopene beta cyclase activity [GO:0045436]; neoxanthin synthase activity [GO:0034020]; oxidoreductase activity [GO:0016491]; oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen [GO:0016705] | PF05834; | 3.50.50.60; | Lycopene cyclase family | null | SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255, ECO:0000269|PubMed:11029576}. | CATALYTIC ACTIVITY: Reaction=all-trans-violaxanthin = all-trans-neoxanthin; Xref=Rhea:RHEA:10128, ChEBI:CHEBI:32446, ChEBI:CHEBI:35288; EC=5.3.99.9; Evidence={ECO:0000269|PubMed:11029576}; CATALYTIC ACTIVITY: Reaction=a carotenoid psi-end group = a carotenoid beta-end derivative; Xref=Rhea:RHEA:55620, ChEBI:CHEBI:13911... | null | PATHWAY: Carotenoid biosynthesis; neoxanthin biosynthesis. {ECO:0000305}.; PATHWAY: Carotenoid biosynthesis; beta-carotene biosynthesis. {ECO:0000305}. | null | null | FUNCTION: Involved in the synthesis of neoxanthin, the last product of carotenoid synthesis and a precursor of abscisic acid (PubMed:11029576). Involved in the beta-carotene biosynthesis (PubMed:10995464). {ECO:0000269|PubMed:10995464, ECO:0000269|PubMed:11029576}. | Solanum lycopersicum (Tomato) (Lycopersicon esculentum) |
K4CI52 | ABAH2_SOLLC | MEFVSMLCLFTFISLTLLLIHSIFKFLAFASKKLPLPPGTLGLPYIGETFQLYSQNPNVFFASKVKKYGSIFKTYILGCPCVMISSPEAAKQVLVTKANLFKPTFPASKERMLGKQAIFFHQGDYHAKLRKLVLQAFKPDSIRNIIPDIESIAITSLESFQGRLINTYQEMKTYTFNVALISIFGKDEFLYREELKKCYYILEKGYNSMPINLPGTLFNKAMKARKELAKIVAKIISTRREMKIDHGDLLGSFMGDKEGLTDEQIADNVIGVIFAARDTTASVLTWILKYLGENPSVLQAVTEEQENIMRKKEVNGEEKV... | 1.14.14.137 | COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250|UniProtKB:Q96242}; | abscisic acid catabolic process [GO:0046345]; abscisic acid metabolic process [GO:0009687]; fruit ripening [GO:0009835]; response to abscisic acid [GO:0009737]; response to water deprivation [GO:0009414]; sterol metabolic process [GO:0016125] | membrane [GO:0016020] | (+)-abscisic acid 8'-hydroxylase activity [GO:0010295]; heme binding [GO:0020037]; iron ion binding [GO:0005506]; oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen [GO:0016709] | PF00067; | 1.10.630.10; | Cytochrome P450 family | null | SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=2-cis-(+)-abscisate + O2 + reduced [NADPH--hemoprotein reductase] = (+)-8'-hydroxyabscisate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:12897, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:37569, C... | null | PATHWAY: Plant hormone degradation; abscisic acid degradation. {ECO:0000269|PubMed:25039074}. | null | null | FUNCTION: Negative regulator of fruit ripening involved in the oxidative degradation of abscisic acid (ABA). {ECO:0000269|PubMed:25039074}. | Solanum lycopersicum (Tomato) (Lycopersicon esculentum) |
K4CWS6 | U75C1_SOLLC | MVQPHVLLVTFPAQGHINPSLQFAKRLIEMGIEVTFTTSVFAHRRMAKIAASTAPKGLNLAAFSDGFDDGFKSNVDDSKRYMSEIRSRGSQTLRDVILKSSDEGRPVTSLVYTLLLPWAAEVARELHIPSALLWIQPATVLDIYYYYFNGYEDEMKCSSSNDPNWSIQLPRLPLLKSQDLPSFLVSSSSKDDKYSFALPTFKEQLDTLDGEENPKVLVNTFDALELEPLKAIEKYNLIGIGPLIPSSFLGGKDSLESSFGGDLFQKSNDDYMEWLNTKPKSSIVYISFGSLLNLSRNQKEEIAKGLIEIQRPFLWVIRDQ... | 2.4.1.121; 2.4.1.263 | null | abscisic acid-activated signaling pathway [GO:0009738]; fruit ripening [GO:0009835]; negative regulation of response to water deprivation [GO:0080148]; regulation of abscisic acid-activated signaling pathway [GO:0009787]; response to abscisic acid [GO:0009737]; seed germination [GO:0009845] | cytoplasm [GO:0005737]; nucleus [GO:0005634] | abscisic acid glucosyltransferase activity [GO:0010294]; indole-3-acetate beta-glucosyltransferase activity [GO:0047215]; quercetin 3-O-glucosyltransferase activity [GO:0080043]; quercetin 7-O-glucosyltransferase activity [GO:0080044] | PF00201; | 3.40.50.2000; | UDP-glycosyltransferase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:28482127}. Nucleus {ECO:0000269|PubMed:28482127}. | CATALYTIC ACTIVITY: Reaction=2-cis-(+)-abscisate + UDP-alpha-D-glucose = beta-D-glucopyranosyl cis-(+)-abscisate + UDP; Xref=Rhea:RHEA:31031, ChEBI:CHEBI:22151, ChEBI:CHEBI:37569, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885; EC=2.4.1.263; Evidence={ECO:0000269|PubMed:28482127}; CATALYTIC ACTIVITY: Reaction=(indol-3-yl)acetate... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.27 mM for abscisic acid {ECO:0000269|PubMed:28482127}; Vmax=0.026 umol/min/ug enzyme with abscisic acid as substrate (in the presence of UDP-glucose) {ECO:0000269|PubMed:28482127}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 3.67-8. {ECO:0000269|PubMed:28482127}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 37 degrees Celsius. {ECO:0000269|PubMed:28482127}; | FUNCTION: Glucosyltransferase acting on both abscisic acid (ABA) and auxin (IAA). Required for ABA-mediated fruit ripening, seed germination, and negative responses to drought. {ECO:0000269|PubMed:28482127}. | Solanum lycopersicum (Tomato) (Lycopersicon esculentum) |
K4L7X3 | SPCAD_ADVMD | MYELTPEQRTLQTQARELAQSVFASTAVQTDLTEQYPWDNVAQLRDAGFMGMMLPTSVGGRGLSTLDTVIVIEEMAKACATMGRITVDSNLGAIGAITKYGSEEQIKLAADLVLAGDKPAICISEPNAGSAASEMTTRADKNGDHYILNGEKYWITGGGVSKLHLIFARVFDDGVEQGIGAFITVLDDHGPEGLKVGRRLYAMGVRGIPETHLEFHDLKIHKSMMITFPDGLKRGFAALMSAYNAQRVGAGAVALGIAQCAFEEGVAYLKRREQFGRPLAEFQGLQWMVADMSVQLEAARLMLRSAAVSGETFPDINKAA... | 3.13.1.4 | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|PubMed:23354747, ECO:0000269|PubMed:26057676}; Note=Binds 1 FAD per subunit. {ECO:0000269|PubMed:26057676}; | leucine catabolic process [GO:0006552] | null | flavin adenine dinucleotide binding [GO:0050660]; hydrolase activity [GO:0016787]; isovaleryl-CoA dehydrogenase activity [GO:0008470] | PF00441;PF02770;PF02771; | 1.10.540.10;2.40.110.10;1.20.140.10; | Acyl-CoA dehydrogenase family | null | null | CATALYTIC ACTIVITY: Reaction=3-sulfinopropanoyl-CoA + H2O = H(+) + propanoyl-CoA + sulfite; Xref=Rhea:RHEA:41624, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17359, ChEBI:CHEBI:57392, ChEBI:CHEBI:78349; EC=3.13.1.4; Evidence={ECO:0000269|PubMed:23354747, ECO:0000269|PubMed:26057676}; PhysiologicalDirection=left-t... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.013 mM for 3SP-CoA {ECO:0000269|PubMed:23354747}; Vmax=4.19 umol/min/mg enzyme {ECO:0000269|PubMed:23354747}; Note=kcat is 3.13 sec(-1). {ECO:0000269|PubMed:23354747}; | null | null | null | FUNCTION: Catalyzes the conversion 3-sulfinopropanoyl-CoA (3SP-CoA) to propanoyl-CoA by abstraction of sulfite (PubMed:23354747, PubMed:26057676). Does not show dehydrogenase activity (PubMed:23354747). Involved in the degradation of 3,3'-dithiodipropionate (DTDP), a sulfur-containing precursor substrate for biosynthes... | Advenella mimigardefordensis (strain DSM 17166 / LMG 22922 / DPN7) |
K4LLQ2 | VSP_BOTBA | APKELQVSYAHKSSELVIGGDECDINEHPFLAFLYSRGNFCGLTLINQEWVLTAAHCDRRFMPIYLGIHTLSVPNDDEVIRYPKDNFICPNNNIIDEKDKDIMLIRLNRPVKNSEHIAPISLPSNLPSVGSVCRVMGWGSITAPNDTFPDVPHCANINLFNDTVCHGAYKRFPVKSRTLCAGVLQGGKDKCMGDSGGPLICNGPFHGILFWGDDPCALPRKPALYTKGFEYPPWIQSIIAKNTTETCPP | 3.4.21.- | null | regulation of systemic arterial blood pressure [GO:0003073]; zymogen activation [GO:0031638] | extracellular region [GO:0005576]; secretory granule [GO:0030141] | serine-type endopeptidase activity [GO:0004252]; toxin activity [GO:0090729] | PF00089; | 2.40.10.10; | Peptidase S1 family, Snake venom subfamily | PTM: Glycoprotein, contains approx. 52% carbohydrate which could be removed by N-glycosidase. Glycosylation is important, since deglycosylated barnettobin loses its clotting and defibrinogenating effects. {ECO:0000269|PubMed:23578498}. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:23578498}. | null | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.0-8.0. {ECO:0000269|PubMed:23578498}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 40 degrees Celsius. {ECO:0000269|PubMed:23578498}; | FUNCTION: Thrombin-like snake venom serine protease that releases only fibrinopeptide A from human Aalpha chain of fibrinogen (specific coagulant activity was 251.7 NIH thrombin units/mg). Also shows fibrino(geno)lytic activities in vitro and defibrinogenating effects in vivo. {ECO:0000269|PubMed:23578498}. | Bothrops barnetti (Barnett's lancehead) (Trimeresurus barnetti) |
K4REZ6 | ROSB_STRDJ | MALKALILNTTLRRSPSRSQTQGLIDKAVPLYEKEGIETEVVRVIDHDIEQEYWDDYDDWNAGEKARREDEWPWLLEKIREADILVIATPITLNMCTSAAHVILEKLNLMDELNGDTKQFPLYNKVAGLLMCGNEDGAHHVAGTVLNNLGRLGYSVPPNAAAYWLGPAGTGPGYIEGKGDRHFHTNKLIRFMVANTSHLARMLQETPYTTDLEACAQAAREESDDVFAIRVNVNTPAIRYKRFQKLGEVKVEESQLG | 2.6.1.114 | null | antibiotic biosynthetic process [GO:0017000]; antibiotic metabolic process [GO:0016999] | null | oxidoreductase activity [GO:0016491]; transaminase activity [GO:0008483] | PF03358; | 3.40.50.360; | SsuE family | null | null | CATALYTIC ACTIVITY: Reaction=3 A + FMN + H2O + L-glutamate + O2 = 2-oxoglutarate + 8-amino-8-demethylriboflavin 5'-phosphate + 3 AH2 + CO2 + H(+); Xref=Rhea:RHEA:54992, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:17499, ChEBI:CHEBI:29985,... | null | PATHWAY: Antibiotic biosynthesis. {ECO:0000269|PubMed:27062037}. | null | null | FUNCTION: Involved in the biosynthesis of the riboflavin analog antibiotic roseoflavin (3,8-dimethylamino-riboflavin) (PubMed:27062037). Catalyzes the site-specific substitution of the C-8 methyl group of riboflavin-5'-phosphate (FMN) by an amino group to yield 8-amino-8-demethylriboflavin 5'-phosphate, via a combined ... | Streptomyces davaonensis (strain DSM 101723 / JCM 4913 / KCC S-0913 / 768) |
K4ZRC1 | PPEP2_PAEA2 | MKWDKRVVALILAVMIVCPLFAAPAHAQEQSILDKLVVLPSGEYNHSEAAAMKQRLEKIPTSILDALYSKGVKIKLTQGAITNEPELAYLKGVVPRGWEGTGLTWDDVPGVSERVVAVRIGYSEKGKGHNSLNLEIHETLHAVDRLVLNEVSGTDEFINIFNKEASVKYKGDGYVSAYPTEYFAEAASLYLYSDATRSDLKDSMPLTYEFMAKLFAN | 3.4.24.89 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|PROSITE-ProRule:PRU01339, ECO:0000269|PubMed:29794027}; Note=Binds 1 zinc ion per subunit. {ECO:0000255|PROSITE-ProRule:PRU01339, ECO:0000269|PubMed:29794027}; | proteolysis [GO:0006508] | extracellular region [GO:0005576] | metal ion binding [GO:0046872]; metallopeptidase activity [GO:0008237] | PF07737; | 3.40.390.10; | Peptidase M34 family, Pro-Pro endopeptidase subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:29794027}. | CATALYTIC ACTIVITY: Reaction=The enzyme catalyzes the hydrolytic cleavage of peptide bonds between two proline residues.; EC=3.4.24.89; Evidence={ECO:0000269|PubMed:29794027}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=70 uM for a FRET peptide containing PLPPVP {ECO:0000269|PubMed:29794027}; KM=330 uM for a FRET peptide containing VLPPVP {ECO:0000269|PubMed:29794027}; Note=kcat is 8 sec(-1) with a FRET peptide containing PLPPVP as substrate. kcat is 3 sec(-1) with a FRET peptide ... | null | null | null | FUNCTION: Zinc-dependent endoprotease with a unique preference for proline residues surrounding the scissile bond, which cleaves in a PLP-|-PVP motif. Cleaves the cell surface protein encoded by an adjacent gene, which contains two PPEP-2 cleaving sites and putative extracellular matrix-binding domains. Thereby, may ha... | Paenibacillus alvei (strain ATCC 6344 / DSM 29 / NBRC 3343 / NCIMB 9371 / NCTC 6352) (Bacillus alvei) |
K5B7F3 | MET1_MYCHD | MTDIRDTDALFALADRVTGFMPADEGRTLYETAVRYLGDGVGVEIGTYCGKSTVLLGAAARQTGGVVFTVDHHHGSEEHQPGWEYHDPSLVDPVTGLFDTLPRLRHTLDEADLYDHVVAVVGKSAVVARGWRTPLRFLFIDGGHTEEAAQRDFDGWARWVEVGGALVIHDVFPDPKDGGQAPFHIYQRALNTGDFREVNAYGSMRVLERTSGIAGQPL | 2.1.1.365 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:30606802}; | chondroitin sulfate biosynthetic process [GO:0030206]; DIM/DIP cell wall layer assembly [GO:0071770]; methylation [GO:0032259] | plasma membrane [GO:0005886] | metal ion binding [GO:0046872]; methyltransferase activity [GO:0008168] | PF13578; | 3.40.50.150; | Methyltransferase superfamily | null | null | CATALYTIC ACTIVITY: Reaction=3,3'-di-O-methyl-4alpha-mannobiose + S-adenosyl-L-methionine = 1,3,3'-tri-O-methyl-4alpha-mannobiose + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:62408, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:145745, ChEBI:CHEBI:145746; EC=2.1.1.365; Evidence={ECO:0000269... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.25 mM for 3,3'-di-O-methyl-4alpha-mannobiose {ECO:0000269|PubMed:30606802}; KM=0.055 mM for S-adenosyl-L-methionine {ECO:0000269|PubMed:30606802}; Vmax=75 nmol/min/mg enzyme toward 3,3'-di-O-methyl-4alpha-mannobiose {ECO:0000269|PubMed:30606802}; Vmax=85 nmol/min... | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5. {ECO:0000269|PubMed:30606802}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 50-55 degrees Celsius. {ECO:0000269|PubMed:30606802}; | FUNCTION: Involved in the biosynthesis of 3-O-methylmannose polysaccharides (MMP), which are intracellular polymethylated polysaccharides implicated in the modulation of fatty acid metabolism in non-tuberculous mycobacteria (PubMed:30606802). Specifically methylates the 1-OH position of 3,3'-di-O-methyl-4alpha-mannobio... | Mycolicibacterium hassiacum (strain DSM 44199 / CIP 105218 / JCM 12690 / 3849) (Mycobacterium hassiacum) |
K5BDL0 | GGH_MYCHD | MPHDPSFTPTQLAARAAYLLRGNDLGTMTTAAPLLYPHMWSWDAAFVAIGLAPLSVERAVVELDTLLSAQWRNGMIPHIVFANGVDGYFPGPARWATATLADNAPRNRLTSGITQPPVHAIAVQRILEHARTRGRSTRAVAEAFLDRRWGDLMRWHRWLAECRDRNERGRITLYHGWESGMDNSPRWDSAYANVVPGKLPEYQRADNVIITDPSQRPSDGEYDRYLWLLEEMKAVRYDDERLPSVMSFQVEDVFFSAIFSVACQVLAEIGEDYKRPHADVKDLYLWAERFRAGVVETTDQRTGAARDFDVLAEKWLVTET... | 3.2.1.208 | null | oligosaccharide metabolic process [GO:0009311]; protein N-linked glycosylation [GO:0006487] | null | Glc3Man9GlcNAc2 oligosaccharide glucosidase activity [GO:0004573]; glucosylglycerate hydrolase activity [GO:0102547] | null | 1.50.10.10; | Glycosyl hydrolase 63 family | null | null | CATALYTIC ACTIVITY: Reaction=(2R)-2-O-(alpha-D-glucopyranosyl)-glycerate + H2O = (R)-glycerate + D-glucose; Xref=Rhea:RHEA:32059, ChEBI:CHEBI:4167, ChEBI:CHEBI:15377, ChEBI:CHEBI:16659, ChEBI:CHEBI:62510; EC=3.2.1.208; Evidence={ECO:0000269|PubMed:25341489, ECO:0000269|PubMed:31316802}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=16.7 mM for glucosylglycerate (at 37 degrees Celsius, C-terminally tagged variant) {ECO:0000269|PubMed:25341489}; KM=16.7 mM for glucosylglycerate (at 42 degrees Celsius, C-terminally tagged variant) {ECO:0000269|PubMed:25341489}; KM=11.2 mM for glucosylglycerate (... | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.0 (tag-less variant) (PubMed:31316802). Optimum pH is 5.8 (C-terminally tagged variant) (PubMed:25341489). {ECO:0000269|PubMed:25341489, ECO:0000269|PubMed:31316802}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 50-55 degrees Celsius (tag-less variant) (PubMed:31316802). Optimum temperature is 42 degrees Celsius (C-terminally tagged variant) (PubMed:25341489). {ECO:0000269|PubMed:25341489, ECO:0000269|PubMed:31316802}; | FUNCTION: Catalyzes the hydrolysis of glucosylglycerate (GG) to glycerate and glucose (PubMed:25341489, PubMed:31316802). Involved in recovery from nitrogen starvation by promoting the rapid mobilization of the glucosylglycerate that accumulates under these conditions (PubMed:25341489). Can also hydrolyze mannosylglyce... | Mycolicibacterium hassiacum (strain DSM 44199 / CIP 105218 / JCM 12690 / 3849) (Mycobacterium hassiacum) |
K6UCV4 | ADA_PLACD | MNILQEPIDFLKKDEIKNIDLSQMSKKERYKIWKRIPKCELHCHLDLCFSADFFLSCIRKYNLQPNLSDEEVLDYYLFAKGGKSLGEFVEKAIRVADIFHDYEVIEDLAKHAVFNKYKEGVVLMEFRYSPTFVAFKYKLDIELIHQAIVKGIKEVVELLDHKIHVALMCIGDTGHEAANIKASADFCLKHRADFVGFDHGGHEVDLKQYKEIFDYVRESGIPLSVHAGEDVTLPNLNTLYSAIQVLKVERIGHGIRVSESQELIDMVKEKNILLEVCPISNVLLKNAKSMDTHPIRQLYDAGVKVSVNSDDPGMFLTNIN... | 3.5.4.31; 3.5.4.4 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:A5KE01}; Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:A5KE01}; | adenosine catabolic process [GO:0006154]; hypoxanthine salvage [GO:0043103]; inosine biosynthetic process [GO:0046103]; negative regulation of adenosine receptor signaling pathway [GO:0060169]; purine ribonucleoside monophosphate biosynthetic process [GO:0009168]; purine ribonucleoside salvage [GO:0006166] | cytosol [GO:0005829]; external side of plasma membrane [GO:0009897] | 2'-deoxyadenosine deaminase activity [GO:0046936]; 5'-methylthioadenosine deaminase activity [GO:0090614]; adenosine deaminase activity [GO:0004000]; metal ion binding [GO:0046872] | PF00962; | 3.20.20.140; | Metallo-dependent hydrolases superfamily, Adenosine and AMP deaminases family | null | null | CATALYTIC ACTIVITY: Reaction=adenosine + H(+) + H2O = inosine + NH4(+); Xref=Rhea:RHEA:24408, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16335, ChEBI:CHEBI:17596, ChEBI:CHEBI:28938; EC=3.5.4.4; Evidence={ECO:0000269|PubMed:19728741}; CATALYTIC ACTIVITY: Reaction=H(+) + H2O + S-methyl-5'-thioadenosine = NH4(+) + ... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=87 uM for adenosine (at pH 8) {ECO:0000269|PubMed:19728741}; KM=8.7 uM for 5'-methylthioadenosine (MTA) (at pH 8) {ECO:0000269|PubMed:19728741}; Note=kcat is 5.3 sec(-1) with adenosine as substrate (PubMed:19728741). kcat is 0.31 sec(-1) with 5'-methylthioadenosine... | PATHWAY: Purine metabolism; purine nucleoside salvage. {ECO:0000305|PubMed:19728741}. | null | null | FUNCTION: Catalyzes the hydrolytic deamination of adenosine to produce inosine (PubMed:19728741). Unlike mammalian adenosine deaminases, also catalyzes the deamination of 5'-methylthioadenosine (MTA), a by-product of polyamine biosynthesis, to produce 5'-methylthioinosine (MTI) (PubMed:19728741). Plays an essential rol... | Plasmodium cynomolgi (strain B) |
K7EJ46 | SIM22_HUMAN | MAVSTEELEATVQEVLGRLKSHQFFQSTWDTVAFIVFLTFMGTVLLLLLLVVAHCCCCSSPGPRRESPRKERPKGVDNLALEP | null | null | lipid droplet formation [GO:0140042]; positive regulation of cell migration [GO:0030335]; regulation of actin cytoskeleton organization [GO:0032956]; regulation of cell cycle [GO:0051726]; regulation of cell population proliferation [GO:0042127] | late endosome [GO:0005770]; membrane [GO:0016020] | null | PF15831; | null | null | null | SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. Late endosome. Note=Partially colocalizedes with LAMP1 in late endosome. {ECO:0000269|PubMed:29765154}. | null | null | null | null | null | FUNCTION: May modulate lipid droplet formation throught interaction with SQLE. {ECO:0000269|PubMed:29765154}. | Homo sapiens (Human) |
K7FQW8 | SCNNB_PELSI | MNLKKYFIRVLHRLQKGPGYTYKELLVWYCDNTNTHGPKRIIREGPKKKFIWFFLTLLFASLVFWQWGILITTYLSYSVSSSLSIGFKTMKFPAVTVCNASPFKYSKVRHLLRELDELTEAALERILQSKNRDATSALPLNSSETPSQTLNLRLWNQIPLVLIDESDPERPVIIDLFETDESGSGAQPNNSSPALVNVTSEAKKQKVAMKLCSRKALPNCIYRNFTSAAQAVTEWYILQSTSIFAKIPRNETVEMGYQPEDMILACLYGAEPCSYRNFTPIYHPDHGNCYIFNWGKDEEALFSSNPGAEFGLKLILDISQ... | null | null | aldosterone metabolic process [GO:0032341]; artery smooth muscle contraction [GO:0014824]; cellular response to acidic pH [GO:0071468]; cellular response to aldosterone [GO:1904045]; epithelial fluid transport [GO:0042045]; erythrocyte homeostasis [GO:0034101]; gene expression [GO:0010467]; intracellular sodium ion hom... | apical plasma membrane [GO:0016324]; cytoplasmic vesicle membrane [GO:0030659]; external side of plasma membrane [GO:0009897]; extracellular exosome [GO:0070062]; sodium channel complex [GO:0034706] | ligand-gated sodium channel activity [GO:0015280]; WW domain binding [GO:0050699] | PF00858; | 2.60.470.10;1.10.287.770; | Amiloride-sensitive sodium channel (TC 1.A.6) family, SCNN1B subfamily | null | SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000250|UniProtKB:P37090}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P37089}. Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:P37090}. Note=Apical membrane of epithelial cells. {ECO:0000250|UniProtKB:P37090}. | null | null | null | null | null | FUNCTION: Sodium permeable non-voltage-sensitive ion channel inhibited by the diuretic amiloride. Mediates the electrodiffusion of the luminal sodium (and water, which follows osmotically) through the apical membrane of epithelial cells. Plays an essential role in electrolyte and blood pressure homeostasis, but also in... | Pelodiscus sinensis (Chinese softshell turtle) (Trionyx sinensis) |
K7MTW9 | TAP1_SOYBN | MSMLSLLRSQLFNFMPIIHCLLKLNSTRKFKSFQLKAGFWESIKSGLMKNNSMQVIDPPSTDEENVEPLSQDFVLVEKTEPDGTIEQIIFSSGGDVDVYDLQALCDKVGWPRRPLSKLAAALKNSYIVASLHSIRKSHGSEGNEQKRLIGMARATSDHAFNATIWDVLVDPGYQGQGLGKALIEKLIRTLLQRDIGNITLFADSQVVEFYRNLGFEADPEGIKGMFWYPNH | 2.3.1.48 | null | defense response [GO:0006952] | cytoplasm [GO:0005737]; nucleus [GO:0005634] | histone H2A acetyltransferase activity [GO:0043998]; histone H3 acetyltransferase activity [GO:0010484]; N-acetyltransferase activity [GO:0008080] | PF00583; | 3.40.630.30; | Acetyltransferase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:30346270}. Nucleus {ECO:0000269|PubMed:30346270}. Note=Localizes to the cytoplasm, but is relocated to the nucleus when interacting with the effector Avh52 from the pathogen Phytophtora sojae. {ECO:0000269|PubMed:30346270}. | CATALYTIC ACTIVITY: Reaction=acetyl-CoA + L-lysyl-[histone] = CoA + H(+) + N(6)-acetyl-L-lysyl-[histone]; Xref=Rhea:RHEA:21992, Rhea:RHEA-COMP:9845, Rhea:RHEA-COMP:11338, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:61930; EC=2.3.1.48; Evidence={ECO:0000269|PubMed:30346270}; | null | null | null | null | FUNCTION: Acetylates histones H2A and H3 in vitro. {ECO:0000269|PubMed:30346270}.; FUNCTION: (Microbial infection) Acts as a negative regulator of immunity when hijacked and relocated to the nucleus by the effector Avh52 from the pathogen Phytophtora sojae (PubMed:30346270). Acts as a susceptibility factor that is hija... | Glycine max (Soybean) (Glycine hispida) |
K7N5M8 | DYP2_AMYS7 | MPVDLSTTLSWKSATGEAATMLDELQPNILKAHVRDRLTVLFLGFGDAAEARTFLNGLSGLMKSARTHLQEVEAHKLTKAVGTPYLGVGLTAHGYATLGVTAPADPSFTAGAKAAVEKLADPAVTEWEGHYQQTIDAVLLLGDATAGPVRTLRRQVEALRPASVTVVGEESGLGLANANGDGIEHFGYVDGRSQPLFLTEDVDAERDTTDGVNDWDPSAPLEQVLVPDPAAPDPTVHFGSYFVFRKLEQNVRLFKEAERDLAHDLGLRGEDRERAGAMLVGRFEDGTPLTAQSAPGSHHPVGNDFSYDSDKLGQKCPFHA... | 1.11.1.16; 1.11.1.19; 1.11.1.7 | COFACTOR: Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000269|PubMed:23054399}; Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit. {ECO:0000269|PubMed:23054399}; COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:23054399}; | null | cytosol [GO:0005829]; extracellular region [GO:0005576] | heme binding [GO:0020037]; lactoperoxidase activity [GO:0140825]; manganese ion binding [GO:0030145]; manganese peroxidase activity [GO:0016689]; peroxidase activity [GO:0004601]; reactive-black-5:hydrogen-peroxide oxidoreductase activity [GO:0052750] | PF21105; | null | DyP-type peroxidase family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:23054399}. Note=Although no signal sequence is found, the secretory machinery for actinomycetes is not fully characterized, and the low pH optimum for DyP2 along with the observation that many DyPs have been isolated from the secreted protein fraction imply that DyP2 c... | CATALYTIC ACTIVITY: Reaction=1-(4-hydroxy-3-methoxyphenyl)-2-(2-methoxyphenoxy)propane-1,3-diol + H2O2 = glycolaldehyde + guaiacol + H2O + vanillin; Xref=Rhea:RHEA:22396, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240, ChEBI:CHEBI:17071, ChEBI:CHEBI:18346, ChEBI:CHEBI:28591, ChEBI:CHEBI:53650; EC=1.11.1.16; Evidence={ECO:0000269... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=13 uM for ABTS {ECO:0000269|PubMed:23054399}; KM=48 uM for Reactive Blue 5 {ECO:0000269|PubMed:23054399}; KM=2.4 uM for Reactive Black 5 {ECO:0000269|PubMed:23054399}; KM=1.2 mM for 2,4-dichlorophenol {ECO:0000269|PubMed:23054399}; KM=210 uM for Mn(2+) (when assayi... | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 4.5 for the H(2)O(2)-dependent oxidation of Reactive Blue 5, and 5.0 for the O(2)-dependent oxidation of 4-methoxymandelate. {ECO:0000269|PubMed:23054399}; | null | FUNCTION: Displays both high peroxidase and manganese peroxidase activity. Is likely involved in lignin degradation. Also has a Mn-dependent oxidase mode of action that expands its substrate scope in vitro; is thus able to catalyze the O(2)- and Mn-dependent oxidative decarboxylation of 4-methoxymandelate to anisaldehy... | Amycolatopsis sp. (strain ATCC 39116 / 75iv2) |
K7N6K2 | TR34B_MOUSE | MASTGPTNIQEKTTCPVCQELLTKALSLGCGHLVCQACLISNKNAVINPRGKSSCPVCGTRFSLENLQANKHLANVVERLGEVKLKPDIGTKRDLCVHHGEKLLLFCKEDKKVICWVCERSQEHRGHHTFLWEEAVRECQENLQKALTRLRKEQEKVETLEADIKEDRLSWKRQVQTERQRIQTGFNQLRRILDKEEQRELKRLREEEQMILDSLAGAEAELAQQSQLVEELISDLELRREWSDTELLQDMSGILKWSQIWTLKKPKAVSKKLSMVFQAPDLSGMLQKFRELSAVRAYWDNFTFNPENLNLNLILSEDHR... | 2.3.2.27 | null | defense response to virus [GO:0051607]; innate immune response [GO:0045087]; positive regulation of autophagy [GO:0010508]; positive regulation of canonical NF-kappaB signal transduction [GO:0043123]; protein polyubiquitination [GO:0000209]; regulation of protein localization [GO:0032880]; regulation of viral entry int... | cytoplasm [GO:0005737]; cytosol [GO:0005829]; mitochondrion [GO:0005739]; nucleoplasm [GO:0005654] | protein homodimerization activity [GO:0042803]; protein kinase binding [GO:0019901]; ubiquitin protein ligase activity [GO:0061630]; zinc ion binding [GO:0008270] | PF00622;PF00643;PF13445; | 2.60.120.920;3.30.160.60;3.30.40.10; | TRIM/RBCC family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9BYJ4}. Mitochondrion {ECO:0000250|UniProtKB:Q9BYJ4}. | 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; Evidence={ECO:0000250|UniProtKB:Q9BYJ4}; | null | PATHWAY: Protein modification; protein ubiquitination. {ECO:0000250|UniProtKB:Q9BYJ4}. | null | null | FUNCTION: Functions as antiviral protein and contributes to the defense against retroviral infections (By similarity). Acts as a capsid-specific restriction factor with the help of TRIM5 and prevents infection from non-host-adapted retroviruses. During influenza A virus infection, promotes programmed cell death by targ... | Mus musculus (Mouse) |
K7NBW3 | 74AC1_SIRGR | MEKGDTHILVFPFPSQGHINPLLQLSKRLIAKGIKVSLVTTLHVSNHLQLQGAYSNSVKIEVISDGSEDRLETDTMRQTLDRFRQKMTKNLEDFLQKAMVSSNPPKFILYDSTMPWVLEVAKEFGLDRAPFYTQSCALNSINYHVLHGQLKLPPETPTISLPSMPLLRPSDLPAYDFDPASTDTIIDLLTSQYSNIQDANLLFCNTFDKLEGEIIQWMETLGRPVKTVGPTVPSAYLDKRVENDKHYGLSLFKPNEDVCLKWLDSKPSGSVLYVSYGSLVEMGEEQLKELALGIKETGKFFLWVVRDTEAEKLPPNFVES... | 2.4.1.350 | null | null | null | quercetin 3-O-glucosyltransferase activity [GO:0080043]; quercetin 7-O-glucosyltransferase activity [GO:0080044]; UDP-glucosyltransferase activity [GO:0035251] | PF00201; | 3.40.50.2000; | UDP-glycosyltransferase family | null | null | CATALYTIC ACTIVITY: Reaction=mogrol + UDP-alpha-D-glucose = H(+) + mogroside IE + UDP; Xref=Rhea:RHEA:52044, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885, ChEBI:CHEBI:138974, ChEBI:CHEBI:138975; EC=2.4.1.350; Evidence={ECO:0000269|PubMed:25759326, ECO:0000269|Ref.3}; PhysiologicalDirection=left-to-right; Xre... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=41.4 uM for mogrol {ECO:0000269|PubMed:25759326}; KM=49.4 uM for mogrol {ECO:0000269|Ref.3}; KM=890.2 uM for UDP-alpha-D-glucose {ECO:0000269|Ref.3}; KM=58.2 uM for quercetin {ECO:0000269|PubMed:25759326}; KM=54.7 uM for naringenin {ECO:0000269|PubMed:25759326}; | null | null | null | FUNCTION: Catalyzes the transfer of a glucose moiety to the C-3 hydroxyl of mogrol to form mogroside IE (PubMed:25759326, Ref.3). Besides mogrol, UGT74AC1 also shows activity in vitro with quercetin and naringenin as substrate (PubMed:25759326). {ECO:0000269|PubMed:25759326, ECO:0000269|Ref.3}. | Siraitia grosvenorii (Monk's fruit) (Luo han guo) |
K7QHS5 | BCAT2_HUMLU | MDCAAALLPGFHPNYLLCPSRHFSSLLPKTDLSSPLKFQLQNKQLSLASSHGFSPVICNATLSDTYSETVELADIDWDNLGFGFLPTDYMYNMKCAQGESFSNGELQRFGNIELSPSAGVLNYGQGLFEGLKAYRKEDGNILLFRPEENALRMRLGAERMCMPSPTVDQFVDAVKATVLANKRWIPPVGKGSLYIRPLLMGSGAVLGLAPAPEYTFLIYVSPVGNYFKEGVAPIHLIVEDNLHRATPGGTGGVKTIGNYAAVLKAQSAAKEQGYSDVLYLDCVHKKYLEEVSSCNIFVVKGNLIFTPAIKGTILPGITRK... | 2.6.1.42 | COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000255|RuleBase:RU004516}; | amino acid biosynthetic process [GO:0008652]; isoleucine biosynthetic process [GO:0009097]; leucine biosynthetic process [GO:0009098]; valine biosynthetic process [GO:0009099] | chloroplast [GO:0009507] | L-isoleucine transaminase activity [GO:0052656]; L-leucine transaminase activity [GO:0052654]; L-leucine:2-oxoglutarate aminotransferase activity [GO:0050048]; L-valine transaminase activity [GO:0052655] | PF01063; | 3.30.470.10;3.20.10.10; | Class-IV pyridoxal-phosphate-dependent aminotransferase family | null | SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000269|PubMed:23347725}. | CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-isoleucine = (S)-3-methyl-2-oxopentanoate + L-glutamate; Xref=Rhea:RHEA:24801, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:35146, ChEBI:CHEBI:58045; EC=2.6.1.42; Evidence={ECO:0000269|PubMed:23347725}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-leucine = 4-meth... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=690 uM for glutamate {ECO:0000269|PubMed:23347725}; KM=120 uM for ketoisocarpoate {ECO:0000269|PubMed:23347725}; KM=160 uM for ketoisomethylvalerate {ECO:0000269|PubMed:23347725}; KM=200 uM for ketoisovalerate {ECO:0000269|PubMed:23347725}; KM=210 uM for 2-oxogluta... | PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 4/4. {ECO:0000305}.; PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 4/4. {ECO:0000305}.; PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine from pyru... | null | null | FUNCTION: Converts 2-oxo acids to branched-chain amino acids. Shows no kinetic preferences corresponding to anabolic or catabolic functions, but likely involved in BCAA biosynthesis. {ECO:0000269|PubMed:23347725}. | Humulus lupulus (European hop) |
K7QKH1 | BCAT1_HUMLU | MIHRGLWLHNLVQSYRVGSSSSSSTLFKLVYRYNSSTSLAKSSLKQSCELSCKSNTEPSNMDWDKLGFKLMPTDYVYSMKCSNEGNFEQGRLELHGNIELSPAAAVLNYGQGIFEGTKAYRKEDGSLLLFRPDQNGVRMRIGAERMCMPSPSVDQFVDAVKQTAIANRRWVPPSGKGSLYIRPLLMGTGAVLGVAPAPQYTFLAYASPVGNYFKEGLAPLRLYVEDEFDRASPGGTGFVKTIGNYSRCLAALSRAKNKGFSDVLFLDSVHKKYVEELSSCNIFIVQGNQISTPAANGTILSGVTRSSIIEIARDHGFKVE... | 2.6.1.42 | COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000255|RuleBase:RU004516}; | amino acid biosynthetic process [GO:0008652]; isoleucine biosynthetic process [GO:0009097]; leucine biosynthetic process [GO:0009098]; valine biosynthetic process [GO:0009099] | mitochondrion [GO:0005739] | L-isoleucine transaminase activity [GO:0052656]; L-leucine transaminase activity [GO:0052654]; L-leucine:2-oxoglutarate aminotransferase activity [GO:0050048]; L-valine transaminase activity [GO:0052655] | PF01063; | 3.30.470.10;3.20.10.10; | Class-IV pyridoxal-phosphate-dependent aminotransferase family | null | SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:23347725}. | CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-isoleucine = (S)-3-methyl-2-oxopentanoate + L-glutamate; Xref=Rhea:RHEA:24801, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:35146, ChEBI:CHEBI:58045; EC=2.6.1.42; Evidence={ECO:0000269|PubMed:23347725}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-leucine = 4-meth... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=720 uM for glutamate {ECO:0000269|PubMed:23347725}; KM=35 uM for ketoisocarpoate {ECO:0000269|PubMed:23347725}; KM=99 uM for ketoisomethylvalerate {ECO:0000269|PubMed:23347725}; KM=99 uM for ketoisovalerate {ECO:0000269|PubMed:23347725}; KM=30 uM for 2-oxoglutarate... | PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 4/4. {ECO:0000305}.; PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 4/4. {ECO:0000305}.; PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine from pyru... | null | null | FUNCTION: Converts 2-oxo acids to branched-chain amino acids (BCAA). Shows no kinetic preferences corresponding to anabolic or catabolic functions, but likely involved in BCAA catabolism. {ECO:0000269|PubMed:23347725}. | Humulus lupulus (European hop) |
K7QRJ5 | PYRE3_STRRG | MSDTVIIAGGGPVGLMLACELGLAGVDTVVLERHDAPREPSRGGAINATVVELFTQRGIMESLRDDGFEFRMAHFAHIPLAPERVPGDRAFSFAVPHAQVERRLEERARSLGVRVRRSTEITSVRQTPDGVQVTTGDGEVVEGAYLVGCDGSASLVREQAGIPFPGVDPDFHGLWGDIKVEPGAPVLERIGARQYELGLCMVAPIGPDTVRVITGEFDVPSPPADQEVGFDELRAAVARIAGVELDGVPGWLSRWTATSRQAERYREGRILLAGDAAHTLFPLGGQALGTGIEDAVNLGWKLAATVQGWAPPSLLDSYHE... | 5.5.1.- | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|PubMed:25730548, ECO:0000269|PubMed:29657086}; Note=Binds 1 FAD per subunit. The FAD cofactor does not cycle between oxidized and reduced forms and therefore does not have a typical redox role in the reaction; it plays a structural role essential for Pyr... | antibiotic biosynthetic process [GO:0017000]; ubiquinone biosynthetic process [GO:0006744] | null | 2-octaprenyl-3-methyl-6-methoxy-1,4-benzoquinol hydroxylase activity [GO:0043719]; FAD binding [GO:0071949]; isomerase activity [GO:0016853] | PF01494;PF21274; | 3.40.30.120;3.50.50.60; | PheA/TfdB FAD monooxygenase family | null | null | CATALYTIC ACTIVITY: Reaction=4-[(2E,7S,8E,10E,13R,14R,16E,18E)-14-ethyl-7,13-dihydroxy-2,16,18-trimethylicosa-2,8,10,16,18-pentaenoyl]-2-methylidene-5-oxo-2,5-dihydro-1H-pyrrol-3-olate = 4-[(1R,2R,4aS,5S,8aR)-2-[(2R,3R,5E,7E)-3-ethyl-2-hydroxy-5,7-dimethylnona-5,7-dien-1-yl]-5-hydroxy-1-methyl-1,2,4a,5,6,7,8,8a-octahyd... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=51.5 uM for 4-[(2E,7S,8E,10E,13R,14R,16E,18E)-14-ethyl-7,13-dihydroxy-2,16,18-trimethylicosa-2,8,10,16,18-pentaenoyl]-2-methylidene-5-oxo-2,5-dihydro-1H-pyrrol-3-olate {ECO:0000269|PubMed:25730548}; Note=kcat is 223.2 min(-1). {ECO:0000269|PubMed:25730548}; | PATHWAY: Antibiotic biosynthesis. {ECO:0000269|PubMed:25730548}. | null | null | FUNCTION: Involved in the biosynthesis of the spirotetramate antibiotics pyrroindomycins. Catalyzes the intramolecular cyclization forming the dialkyldecalin moiety in pyrroindomycins, via an endo-selective [4+2] cycloaddition reaction. {ECO:0000269|PubMed:25730548, ECO:0000269|PubMed:29657086}. | Streptomyces rugosporus |
K7QVW7 | PYRI4_STRRG | MTTPQIDERAMEAGAAALQETIVDPGPLDVTALAVAAALAAGLHSAADDPAAALDKCIVLDELTEFAEKLVVHDRPGGIGTTVEYVEVYEDASGVRLGTATGNAVVLKMEPHMWQFHQSVSELADGSFEAVGVIDCTAMLRRMTQVLRVTGRSGRYAGKSGFMTLAISDPNQRPPHYSVQVVLC | 5.-.-.- | null | antibiotic biosynthetic process [GO:0017000] | null | isomerase activity [GO:0016853] | PF18678; | null | null | null | null | CATALYTIC ACTIVITY: Reaction=4-[(1R,2R,4aS,5S,8aR)-2-[(2R,3R,5E,7E)-3-ethyl-2-hydroxy-5,7-dimethylnona-5,7-dien-1-yl]-5-hydroxy-1-methyl-1,2,4a,5,6,7,8,8a-octahydronaphthalene-1-carbonyl]-2-methylidene-5-oxo-2,5-dihydro-1H-pyrrol-3-olate = (1S,3R,6R,8R,9R,11R,14S,15S,19R,20R)-8-ethyl-9,15-dihydroxy-3,4,6,20-tetramethyl... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=224 uM for 4-[(1R,2R,4aS,5S,8aR)-2-[(2R,3R,5E,7E)-3-ethyl-2-hydroxy-5,7-dimethylnona-5,7-dien-1-yl]-5-hydroxy-1-methyl-1,2,4a,5,6,7,8,8a-octahydronaphthalene-1-carbonyl]-2-methylidene-5-oxo-2,5-dihydro-1H-pyrrol-3-olate {ECO:0000269|PubMed:25730548}; Note=kcat is 3... | PATHWAY: Antibiotic biosynthesis. {ECO:0000269|PubMed:25730548}. | null | null | FUNCTION: Involved in the biosynthesis of the spirotetramate antibiotics pyrroindomycins. Catalyzes the intramolecular cyclization forming the spiro-conjugate moiety in pyrroindomycins, via an exo-selective [4+2] cycloaddition reaction. {ECO:0000269|PubMed:25730548, ECO:0000269|PubMed:26877021}. | Streptomyces rugosporus |
K7SGN7 | ZAR2B_XENLA | MAGFMYAPYNVYQGYGGNFGQNPHVAQPLAKNKQAAWKSNKASEPTDYLDNFQRAQLKAILSQVNPNLTPRLRKANTKEIGVQVNPRVDTGVQCSLGPRTLRRPPPPPCSPVKAADCVRFTRPLAVYSPVVDRRLFSLPQGGRLPKKSPDSQSQPLKERAPSPEDKEREKVSEKEPDTKDELEKRPVPGTEEPGNEEQTKSAFQFLEQKYGYFHCKDCKTRWESAYVWCISGSNKVYFKQLCRKCQKGYNPYRVEAIQCQVCAKTRCSCPQKQRHIDLKRPHRQELCGRCKNKRLSCDNTYSYKYIV | null | null | negative regulation of translation [GO:0017148]; oocyte maturation [GO:0001556]; translation [GO:0006412] | cytoplasmic ribonucleoprotein granule [GO:0036464] | metal ion binding [GO:0046872]; mRNA 3'-UTR binding [GO:0003730] | PF13695; | null | ZAR1 family | null | SUBCELLULAR LOCATION: Cytoplasm, Cytoplasmic ribonucleoprotein granule {ECO:0000250|UniProtKB:C3VD30}. | null | null | null | null | null | FUNCTION: mRNA-binding protein required for maternal mRNA storage, translation and degradation during oocyte maturation (PubMed:22732570). Probably promotes formation of some phase-separated membraneless compartment that stores maternal mRNAs in oocytes: acts by undergoing liquid-liquid phase separation upon binding to... | Xenopus laevis (African clawed frog) |
K7TLS0 | MYB69_MAIZE | MGRPPCCDKAGVKKGPWTPEEDIVLVSYVQEHGPGNWRAVPVSTGLMRCSKSCRLRWTNYLRPGIRRGNFTPHEEGIIVHLQALLGNRWAAIASYLPQRTDNDIKNYWNTHLKKKLRKQQAIGAIFAPPRPSEPTAGHADCRRHDMTRSSKDSHAACPADSTPAADEVVTQLIAQQFAATDGDTSSSSSYSYASSTDNISKLLNGFMMKSASPARDDATDTIKTSSAIDIDPFDHKSGGAALPPPKKRQQQQHLSSIENWLFDDATEQLVVQLMEEISGGSCSVPMLLY | null | null | positive regulation of DNA-templated transcription [GO:0045893]; regulation of lignin biosynthetic process [GO:1901141]; response to auxin [GO:0009733] | nucleus [GO:0005634] | DNA-binding transcription factor activity [GO:0003700]; sequence-specific DNA binding [GO:0043565]; 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:35640133}. | null | null | null | null | null | FUNCTION: Transcription factor that binds to the promoter of MYB31 and MYB42 and activates directly their expression, thus repressing lignin biosynthesis. {ECO:0000269|PubMed:35640133}. | Zea mays (Maize) |
K7U9N8 | OP1_MAIZE | MSYRKGLKVWVEEKGEGWVEAEVVEAKERAVVVFSSQRKKITVSPEKLLPRDTDEDLGGGHVDDMTKLTYLNEPGVLYNLKKRYALNEIYTYTGSILIAVNPFTRLPHLYNEYMMEQYKGIRLGELSPHVFAVADASYSRAMVNDSRSQSILVSGESGAGKTETTKLIMQYLTFVGGRAALDDRTVEQQVLESNPLLEAFGNAKTVRNDNSSRFGKFVEIQFDSSGRISGAAIRTYLLERSRVVQITDPERNFHCFYQLCASGKDAELYKLGHISSFHYLNQSNTHDLEGTNNEDEYWKTKRAMDIVGISREDQDAIFRT... | null | null | actin filament organization [GO:0007015]; vesicle transport along actin filament [GO:0030050] | actin cytoskeleton [GO:0015629]; cytoplasm [GO:0005737]; membrane [GO:0016020]; myosin complex [GO:0016459]; vesicle [GO:0031982] | actin filament binding [GO:0051015]; ATP binding [GO:0005524]; calmodulin binding [GO:0005516]; microfilament motor activity [GO:0000146] | PF01843;PF00612;PF00063; | 1.10.10.820;1.20.5.190;1.20.58.530;3.30.70.1590;3.40.850.10;1.20.120.720; | TRAFAC class myosin-kinesin ATPase superfamily, Myosin family, Plant myosin class XI subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22892319}. Note=Associated with the endoplasmic reticulum membrane. {ECO:0000269|PubMed:22892319}. | null | null | null | null | null | FUNCTION: Myosin XI motor protein required for endoplasmic reticulum motility and protein body formation (PubMed:22892319). May function by binding with its tail domain to receptor proteins on membranes and exerting force with its N-terminal motor domain against actin filaments, thereby transporting its cargo along pol... | Zea mays (Maize) |
K7W9N9 | CPT6_SOLLC | MNSLFVGRPIVKSSYNVYTLPSSICGGHFFKVSNSLSLYDDHRRTRIEIIRNSELIPKHVAIIMDGNRRWAKARGLPVQEGHKFLAPNLKNICNISSKLGIQVITAFAFSTENWNRSSEEVDFLMRLFEEFFEEFMRLGVRVSLIGGKSKLPTKLQQVIELTEEVTKSNEGLHLMMALNYGGQYDMLQATKNIASKVKDGLIKLEDIDYTLFEQELTTKCAKFPKPDLLIRTGGEQRISNFLLWQLAYSELYFTNTLFPDFGEEALMDAIFSFQRRHRRFGGHTY | 2.5.1.92 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:23134568}; | plastid membrane organization [GO:0009668]; polyprenol biosynthetic process [GO:0016094]; response to cold [GO:0009409] | chloroplast [GO:0009507]; chloroplast stroma [GO:0009570] | 2-cis,6-cis-farnesyl pyrophosphate synthase activity [GO:0102059]; dehydrodolichyl diphosphate synthase activity [GO:0045547]; dimethylallylcistransferase activity [GO:0047863]; magnesium ion binding [GO:0000287]; polyprenyltransferase activity [GO:0002094]; prenyltransferase activity [GO:0004659] | PF01255; | 3.40.1180.10; | UPP synthase family | null | SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000269|PubMed:23134568}. Note=Localizes in punctuate patterns inside the chloroplasts. {ECO:0000269|PubMed:23134568}. | CATALYTIC ACTIVITY: Reaction=dimethylallyl diphosphate + 2 isopentenyl diphosphate = (2Z,6Z)-farnesyl diphosphate + 2 diphosphate; Xref=Rhea:RHEA:27810, ChEBI:CHEBI:33019, ChEBI:CHEBI:57623, ChEBI:CHEBI:60374, ChEBI:CHEBI:128769; EC=2.5.1.92; Evidence={ECO:0000269|PubMed:23134568}; PhysiologicalDirection=left-to-right;... | null | null | null | null | FUNCTION: Uses neryl diphosphate to catalyze the cis-prenyl chain elongation and produce the 15 carbon product (2Z,6Z)-farnesyl diphosphate. {ECO:0000269|PubMed:23134568}. | Solanum lycopersicum (Tomato) (Lycopersicon esculentum) |
K7WDL7 | IRIS_CATRO | MSWWWKRSIGAGKNLPNQNKENGVCKSYKSVALVVGVTGIVGSSLAEVLKLPDTPGGPWKVYGVARRPCPVWLAKKPVEYIQCDVSDNQETISKLSPLKDITHIFYVSWIGSEDCQTNATMFKNILNSVIPNASNLQHVCLQTGIKHYFGIFEEGSKVVPHDSPFTEDLPRLNVPNFYHDLEDILYEETGKNNLTWSVHRPALVFGFSPCSMMNIVSTLCVYATICKHENKALVYPGSKNSWNCYADAVDADLVAEHEIWAAVDPKAKNQVLNCNNGDVFKWKHIWKKLAEEFGIEMVGYVEGKEQVSLAELMKDKDQVW... | 1.3.1.122 | null | monoterpenoid biosynthetic process [GO:0016099] | cytosol [GO:0005829] | identical protein binding [GO:0042802]; oxidoreductase activity, acting on the CH-CH group of donors, NAD or NADP as acceptor [GO:0016628]; protein homodimerization activity [GO:0042803] | PF01370; | 3.40.50.720; | Short-chain dehydrogenases/reductases (SDR) family | null | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:23172143}. | CATALYTIC ACTIVITY: Reaction=(S)-8-oxocitronellyl enol + NADP(+) = (6E)-8-oxogeranial + H(+) + NADPH; Xref=Rhea:RHEA:62592, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:64239, ChEBI:CHEBI:144481; EC=1.3.1.122; Evidence={ECO:0000269|PubMed:23172143, ECO:0000269|PubMed:26768532, ECO:0000269|PubMed... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=4.5 uM for (6E)-8-oxogeranial {ECO:0000269|PubMed:23172143}; KM=10.6 uM for (6E)-8-oxogeranial {ECO:0000269|PubMed:26868105}; KM=4.7 uM for NADPH {ECO:0000269|PubMed:23172143}; Note=kcat is 1.6 sec(-1) with (6E)-8-oxogeranial. kcat is 2.2 sec(-1) with NADPH.; | null | null | null | FUNCTION: Iridoid synthase that catalyzes the first step in generation of the iridoid ring scaffold using the linear monoterpene (6E)-8-oxogeranial as substrate. Iridoids comprise a large family of distinctive bicyclic monoterpenes that possess a wide range of pharmacological activities, including anticancer, anti-infl... | Catharanthus roseus (Madagascar periwinkle) (Vinca rosea) |
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