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 |
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A0PC02 | UCP1_OCHDA | MVGTTATDVAPTMGVKIFSAGVAACLADVITFPLDTAKVRLQIQGECQTTSGIRYKGVLGTITTLAKTEGPLKLYSGLPAGLQRQISFASLRIGLYDTVQEFWGGEEATPSLRSKICAGLTTGGVAVFIGQPTEVVKVRLQAQSHLHGLKPRYTGTYNAYRIIATTESLSTLWKGTTPNLLRNIIINCTELVTYDLMKGALVRNDILADDVPCHLLSALIAGFCTTLLSSPVDVVKTRFINSPQGQYTSVPSCAMSMLTKEGPTAFFKGFAPSFLRLASWNVIMFVCFEKLKRELMKSRQTVDCAT | null | null | adaptive thermogenesis [GO:1990845]; cellular response to fatty acid [GO:0071398]; cellular response to hormone stimulus [GO:0032870]; cellular response to reactive oxygen species [GO:0034614]; mitochondrial transmembrane transport [GO:1990542]; proton transmembrane transport [GO:1902600]; regulation of reactive oxygen... | mitochondrial inner membrane [GO:0005743] | cardiolipin binding [GO:1901612]; long-chain fatty acid binding [GO:0036041]; oxidative phosphorylation uncoupler activity [GO:0017077]; purine ribonucleotide binding [GO:0032555] | PF00153; | 1.50.40.10; | Mitochondrial carrier (TC 2.A.29) family | PTM: May undergo sulfenylation upon cold exposure. May increase the sensitivity of UCP1 thermogenic function to the activation by noradrenaline probably through structural effects. {ECO:0000250|UniProtKB:P12242}.; PTM: May undergo ubiquitin-mediated proteasomal degradation. {ECO:0000250|UniProtKB:P04633}. | SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P12242}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P04633}. | CATALYTIC ACTIVITY: Reaction=H(+)(in) = H(+)(out); Xref=Rhea:RHEA:34979, ChEBI:CHEBI:15378; Evidence={ECO:0000250|UniProtKB:P25874}; | null | null | null | null | FUNCTION: Mitochondrial protein responsible for thermogenic respiration, a specialized capacity of brown adipose tissue and beige fat that participates in non-shivering adaptive thermogenesis to temperature and diet variations and more generally to the regulation of energy balance. Functions as a long-chain fatty acid/... | Ochotona dauurica (Daurian pika) |
A0PJ25 | GLYC_BCNVU | MGQLVSFIGEIPAIVHEALNVALIAVSIIAIMKGLINIWKSGLFQLIMFLILAGRSCSISIGHHLELQHFIINSTSLLPSMPTLCRINATNSLIRGPFSAQWGLDIFIGDLTILVNPEPGSKTKRMTATNITGCFPNNEDPDSVAQVLSWFFRGVHHDFHLDPTILCDESVTVFRIQMNLTERMYCDRIVSKLARLFGSFGDYCSKVGKKLVIIRNVTWSNQCHEDHVGSMQLILQNAHNQVMRFRKLQNFFSWSLVDSAGNSMPGGYCLEKWMLVASELKCFGNTAVAKCNINHDSEFCDMLRLFDYNKKAIVNLQDKT... | null | null | fusion of virus membrane with host endosome membrane [GO:0039654]; receptor-mediated endocytosis of virus by host cell [GO:0019065]; virion attachment to host cell [GO:0019062] | host cell endoplasmic reticulum membrane [GO:0044167]; host cell Golgi membrane [GO:0044178]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; viral envelope [GO:0019031]; virion membrane [GO:0055036] | metal ion binding [GO:0046872] | PF00798; | 6.10.140.1590;2.20.28.180; | Arenaviridae GPC protein family | PTM: Specific enzymatic cleavages in vivo yield mature proteins. GP-C polyprotein is cleaved in the endoplasmic reticulum by the host protease MBTPS1. Only cleaved glycoprotein is incorporated into virions. {ECO:0000255|HAMAP-Rule:MF_04084}.; PTM: The SSP remains stably associated with the GP complex following cleavage... | SUBCELLULAR LOCATION: [Glycoprotein G1]: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04084}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_04084}. Host endoplasmic reticulum membrane {ECO:0000255|HAMAP-Rule:MF_04084}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_04084}. Host Golgi apparatus membrane {... | null | null | null | null | null | FUNCTION: [Glycoprotein G2]: Class I viral fusion protein that directs fusion of viral and host endosomal membranes, leading to delivery of the nucleocapsid into the cytoplasm. Membrane fusion is mediated by irreversible conformational changes induced upon acidification in the endosome. {ECO:0000255|HAMAP-Rule:MF_04084... | Bear Canyon mammarenavirus (isolate Mouse/United States/AV A0070039/2000) (BCNV) |
A0PJK1 | SC5AA_HUMAN | MAANSTSDLHTPGTQLSVADIIVITVYFALNVAVGIWSSCRASRNTVNGYFLAGRDMTWWPIGASLFASSEGSGLFIGLAGSGAAGGLAVAGFEWNATYVLLALAWVFVPIYISSEIVTLPEYIQKRYGGQRIRMYLSVLSLLLSVFTKISLDLYAGALFVHICLGWNFYLSTILTLGITALYTIAGGLAAVIYTDALQTLIMVVGAVILTIKAFDQIGGYGQLEAAYAQAIPSRTIANTTCHLPRTDAMHMFRDPHTGDLPWTGMTFGLTIMATWYWCTDQVIVQRSLSARDLNHAKAGSILASYLKMLPMGLIIMPGM... | null | null | hexose transmembrane transport [GO:0008645] | apical plasma membrane [GO:0016324]; extracellular exosome [GO:0070062]; plasma membrane [GO:0005886] | fructose:sodium symporter activity [GO:0140930]; glucose:sodium symporter activity [GO:0005412]; mannose:sodium symporter activity [GO:0140929]; solute:sodium symporter activity [GO:0015370] | PF00474; | 1.20.1730.10; | Sodium:solute symporter (SSF) (TC 2.A.21) family | null | SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000250|UniProtKB:Q5SWY8}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: [Isoform 1]: Reaction=D-mannose(out) + Na(+)(out) = D-mannose(in) + Na(+)(in); Xref=Rhea:RHEA:72907, ChEBI:CHEBI:4208, ChEBI:CHEBI:29101; Evidence={ECO:0000269|PubMed:22212718, ECO:0000269|PubMed:24573086}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:72908; Evidence={ECO:0000250|UniProtKB:Q... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.45 mM for D-mannose {ECO:0000269|PubMed:22212718}; KM=0.62 mM for D-fructopyranose {ECO:0000269|PubMed:22212718}; | null | null | null | FUNCTION: [Isoform 1]: Electrogenic Na+-coupled sugar symporter that actively transports D-mannose or D-fructose at the plasma membrane, with a Na+ to sugar coupling ratio of 1:1. Transporter activity is driven by a transmembrane Na+ electrochemical gradient set by the Na+/K+ pump. Exclusively recognizes sugar substrat... | Homo sapiens (Human) |
A0PJY2 | FEZF1_HUMAN | MDSSCHNATTKMLATAPARGNMMSTSKPLAFSIERIMARTPEPKALPVPHFLQGALPKGEPKHSLHLNSSIPCMIPFVPVAYDTSPKAGVTGSEPRKASLEAPAAPAAVPSAPAFSCSDLLNCALSLKGDLARDALPLQQYKLVRPRVVNHSSFHAMGALCYLNRGDGPCHPAAGVNIHPVASYFLSSPLHPQPKTYLAERNKLVVPAVEKYPSGVAFKDLSQAQLQHYMKESAQLLSEKIAFKTSDFSRGSPNAKPKVFTCEVCGKVFNAHYNLTRHMPVHTGARPFVCKVCGKGFRQASTLCRHKIIHTQEKPHKCNQ... | null | null | axon guidance [GO:0007411]; cell dedifferentiation [GO:0043697]; forebrain anterior/posterior pattern specification [GO:0021797]; interneuron migration [GO:1904936]; negative regulation of cell population proliferation [GO:0008285]; olfactory bulb development [GO:0021772]; positive regulation of DNA-templated transcrip... | cytosol [GO:0005829]; nucleoplasm [GO:0005654] | DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription repressor activity, RNA polymerase II-specific [GO:0001227]; metal ion binding [GO:0046872]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978] | PF00096;PF13912; | 3.30.160.60; | Krueppel C2H2-type zinc-finger protein family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19318583}. | null | null | null | null | null | FUNCTION: Transcription repressor. Involved in the axonal projection and proper termination of olfactory sensory neurons (OSN). Plays a role in rostro-caudal patterning of the diencephalon and in prethalamic formation. Expression is required in OSN to cell-autonomously regulate OSN axon projections. Regulates non-cell-... | Homo sapiens (Human) |
A0PK00 | T120B_HUMAN | MSGQLERCEREWHELEGEFQELQETHRIYKQKLEELAALQTLCSSSISKQKKHLKDLKLTLQRCKRHASREEAELVQQMAANIKERQDVFFDMEAYLPKKNGLYLNLVLGNVNVTLLSNQAKFAYKDEYEKFKLYLTIILLLGAVACRFVLHYRVTDEVFNFLLVWYYCTLTIRESILISNGSRIKGWWVSHHYVSTFLSGVMLTWPNGPIYQKFRNQFLAFSIFQSCVQFLQYYYQRGCLYRLRALGERNHLDLTVEGFQSWMWRGLTFLLPFLFCGHFWQLYNAVTLFELSSHEECREWQVFVLAFTFLILFLGNFLT... | null | null | fat cell differentiation [GO:0045444]; protein heterooligomerization [GO:0051291] | nuclear inner membrane [GO:0005637] | null | PF07851; | null | TMEM120 family | null | SUBCELLULAR LOCATION: Nucleus inner membrane {ECO:0000250|UniProtKB:Q3TA38}; Multi-pass membrane protein {ECO:0000255}. | null | null | null | null | null | FUNCTION: Necessary for efficient adipogenesis. Does not show ion channel activity. {ECO:0000250|UniProtKB:Q3TA38}. | Homo sapiens (Human) |
A0PK11 | CLRN2_HUMAN | MPGWFKKAWYGLASLLSFSSFILIIVALVVPHWLSGKILCQTGVDLVNATDRELVKFIGDIYYGLFRGCKVRQCGLGGRQSQFTIFPHLVKELNAGLHVMILLLLFLALALALVSMGFAILNMIQVPYRAVSGPGGICLWNVLAGGVVALAIASFVAAVKFHDLTERIANFQEKLFQFVVVEEQYEESFWICVASASAHAANLVVVAISQIPLPEIKTKIEEATVTAEDILY | null | null | auditory receptor cell stereocilium organization [GO:0060088]; sensory perception of sound [GO:0007605]; stereocilium maintenance [GO:0120045] | stereocilium bundle [GO:0032421]; stereocilium membrane [GO:0060171] | null | null | 1.20.140.150; | Clarin family | null | SUBCELLULAR LOCATION: Cell projection, stereocilium membrane {ECO:0000250|UniProtKB:B2RVW2}; Multi-pass membrane protein {ECO:0000255}. | null | null | null | null | null | FUNCTION: Plays a key role to hearing function. Required for normal organization and maintenance of the stereocilia bundle and for mechano-electrical transduction. {ECO:0000250|UniProtKB:B2RVW2}. | Homo sapiens (Human) |
A0PVU7 | KGD_MYCUA | MANISSPFGQNEWLVEEMYRKFRDDPSSVDPSWHEFLVDYNPESTQEATEPAVVKPAAAPAKPAPAPAPAKPAAGPPAAGNGSPAAAPSAKPAAAPAKAPAPPPAEGDEMQVLRGAAAAVVKNMSASLDVPTATSVRAVPAKLLIDNRIVINNQLKRNRGGKISFTHLLGYALVQAVKKFPNMNRHYLDVDGKPNAVTPAHTNLGLAIDLQGKDGKRALVVAGIKRCETMRFAQFVTAYEDIVRRARDGKLTAEDFSGVTISLTNPGTIGTVHSVPRLMAGQGAIIGVGAMEYPAEFQGASEERIAELGIGKLITLTSTY... | 1.2.4.2; 2.2.1.5; 2.3.1.61; 4.1.1.71 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; COFACTOR: Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937; Evidence={ECO:0000250}; | tricarboxylic acid cycle [GO:0006099] | cytosol [GO:0005829]; oxoglutarate dehydrogenase complex [GO:0045252] | 2-hydroxy-3-oxoadipate synthase activity [GO:0050439]; 2-oxoglutarate decarboxylase activity [GO:0008683]; dihydrolipoyllysine-residue succinyltransferase activity [GO:0004149]; magnesium ion binding [GO:0000287]; oxoglutarate dehydrogenase (succinyl-transferring) activity [GO:0004591]; thiamine pyrophosphate binding [... | PF00198;PF16078;PF00676;PF16870;PF02779; | 3.40.50.12470;3.40.50.970;3.30.559.10;3.40.50.11610;1.10.287.1150; | 2-oxoacid dehydrogenase family, Kgd subfamily | null | null | CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + glyoxylate + H(+) = 2-hydroxy-3-oxoadipate + CO2; Xref=Rhea:RHEA:14341, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:36655, ChEBI:CHEBI:57712; EC=2.2.1.5; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + H(+) = CO2 + succinate semialdehyde; Xref=Rhea:RH... | null | PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; succinate from 2-oxoglutarate (transferase route): step 1/2.; PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; succinyl-CoA from 2-oxoglutarate (dehydrogenase route): step 1/1. | null | null | FUNCTION: Shows three enzymatic activities that share a first common step, the attack of thiamine-PP on 2-oxoglutarate (alpha-ketoglutarate, KG), leading to the formation of an enamine-thiamine-PP intermediate upon decarboxylation. Thus, displays KGD activity, catalyzing the decarboxylation from five-carbon 2-oxoglutar... | Mycobacterium ulcerans (strain Agy99) |
A0Q5Y3 | CAS9_FRATN | MNFKILPIAIDLGVKNTGVFSAFYQKGTSLERLDNKNGKVYELSKDSYTLLMNNRTARRHQRRGIDRKQLVKRLFKLIWTEQLNLEWDKDTQQAISFLFNRRGFSFITDGYSPEYLNIVPEQVKAILMDIFDDYNGEDDLDSYLKLATEQESKISEIYNKLMQKILEFKLMKLCTDIKDDKVSTKTLKEITSYEFELLADYLANYSESLKTQKFSYTDKQGNLKELSYYHHDKYNIQEFLKRHATINDRILDTLLTDDLDIWNFNFEKFDFDKNEEKLQNQEDKDHIQAHLHHFVFAVNKIKSEMASGGRHRSQYFQEIT... | 3.1.-.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:26875867}; | defense response to virus [GO:0051607] | null | DNA binding [GO:0003677]; endonuclease activity [GO:0004519]; metal ion binding [GO:0046872]; RNA binding [GO:0003723] | PF21069; | 1.10.30.50; | CRISPR-associated protein Cas9 family, Subtype II-B 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 ... | Francisella tularensis subsp. novicida (strain U112) |
A0Q7Q2 | CS12A_FRATN | MSIYQEFVNKYSLSKTLRFELIPQGKTLENIKARGLILDDEKRAKDYKKAKQIIDKYHQFFIEEILSSVCISEDLLQNYSDVYFKLKKSDDDNLQKDFKSAKDTIKKQISEYIKDSEKFKNLFNQNLIDAKKGQESDLILWLKQSKDNGIELFKANSDITDIDEALEIIKSFKGWTTYFKGFHENRKNVYSSNDIPTSIIYRIVDDNLPKFLENKAKYESLKDKAPEAINYEQIKKDLAEELTFDIDYKTSEVNQRVFSLDEVFEIANFNNYLNQSGITKFNTIIGGKFVNGENTKRKGINEYINLYSQQINDKTLKKYK... | 3.1.21.1; 4.6.1.22 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:26593719}; Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:26422227, ECO:0000269|PubMed:26593719, ECO:0000269|PubMed:27096362, ECO:0000269|PubMed:28562584}; Note=Cleavage of dsDNA requires Mg(2+) (PubMed:26422227, PubMed:28562... | defense response to virus [GO:0051607] | null | Bacillus subtilis ribonuclease activity [GO:0033898]; deoxyribonuclease I activity [GO:0004530]; DNA binding [GO:0003677]; lyase activity [GO:0016829]; RNA binding [GO:0003723] | PF18510;PF18501;PF18516; | null | CRISPR-associated endonuclease Cas12a family | null | null | CATALYTIC ACTIVITY: Reaction=Endonucleolytic cleavage to 5'-phosphodinucleotide and 5'-phosphooligonucleotide end-products.; EC=3.1.21.1; Evidence={ECO:0000269|PubMed:28431230}; CATALYTIC ACTIVITY: Reaction=RNA = a 5'-hydroxy-ribonucleotide + n nucleoside-2',3'-cyclophosphates.; EC=4.6.1.22; Evidence={ECO:0000269|PubMe... | 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 sequences complementary to antecedent mobile elements and target invading ... | Francisella tularensis subsp. novicida (strain U112) |
A0QNE0 | GYRB_MYCS2 | MAAQKNNAPKEYGADSITILEGLEAVRKRPGMYIGSTGERGLHHLIWEVVDNAVDEAMAGFATRVDVKIHADGSVEVRDDGRGIPVEMHATGMPTIDVVMTQLHAGGKFDGETYAVSGGLHGVGVSVVNALSTRLEATVLRDGYEWFQYYDRSVPGKLKQGGETKETGTTIRFWADPEIFETTDYNFETVARRLQEMAFLNKGLTIELTDERVTAEEVVDDVVKDTAEAPKTADEKAAEATGPSKVKHRVFHYPGGLVDYVKHINRTKTPIQQSIIDFDGKGPGHEVEIAMQWNAGYSESVHTFANTINTHEGGTHEEGF... | 5.6.2.2 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_01898}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000255|HAMAP-Rule:MF_01898}; Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000255|HAMAP-Rule:MF_01898}; Note=Binds two Mg(2+) per subunit. The magnesium ions form salt bri... | DNA topological change [GO:0006265]; DNA-templated DNA replication [GO:0006261] | chromosome [GO:0005694]; cytoplasm [GO:0005737] | ATP binding [GO:0005524]; DNA binding [GO:0003677]; DNA negative supercoiling activity [GO:0034335]; metal ion binding [GO:0046872] | PF00204;PF00986;PF02518;PF01751; | 3.30.230.10;3.40.50.670;3.30.565.10; | Type II topoisomerase GyrB family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01898}. | CATALYTIC ACTIVITY: Reaction=ATP-dependent breakage, passage and rejoining of double-stranded DNA.; EC=5.6.2.2; Evidence={ECO:0000255|HAMAP-Rule:MF_01898}; | null | null | null | null | FUNCTION: A type II topoisomerase that negatively supercoils closed circular double-stranded (ds) DNA in an ATP-dependent manner (PubMed:8878580) to modulate DNA topology and maintain chromosomes in an underwound state. Negative supercoiling favors strand separation, and DNA replication, transcription, recombination an... | Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) |
A0QNG1 | PKNB_MYCS2 | MTTPQHLSDRYELGEILGFGGMSEVHLARDLRLHRDVAVKVLRADLARDPSFYLRFRREAQNAAALNHPAIVAVYDTGEAETPNGPLPYIVMEYVDGVTLRDIVHTDGPIAPRRAIEIIADACQALNFSHQHGIIHRDVKPANIMISKNNAVKVMDFGIARALADTGNSVTQTAAVIGTAQYLSPEQARGETVDARSDVYSLGCVLYEILTGEPPFIGDSPVAVAYQHVREDPVPPSRRHADVTPELDAVVLKALAKNPDNRYQTAAEMRADLIRVHEGQAPDAPKVLTDAERTSMLAAPPADRAGAATQDMPVPRPAGY... | 2.7.11.1 | null | phosphorylation [GO:0016310]; regulation of cellular biosynthetic process [GO:0031326]; regulation of primary metabolic process [GO:0080090] | plasma membrane [GO:0005886] | ATP binding [GO:0005524]; metal ion binding [GO:0046872]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF03793;PF00069; | 3.30.10.20;1.10.510.10; | Protein kinase superfamily, Ser/Thr protein kinase family | PTM: Autophosphorylated. Dephosphorylated by PstP (By similarity). {ECO:0000250}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[pr... | null | null | null | null | FUNCTION: Protein kinase that regulates many aspects of mycobacterial physiology. Is a key component of a signal transduction pathway that regulates cell growth, cell shape and cell division via phosphorylation of target proteins (By similarity). Probably phosphorylates RseA (PubMed:20025669). {ECO:0000250|UniProtKB:P9... | Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) |
A0QP27 | MMPL3_MYCS2 | MFAWWGRTVYQFRYIVIGVMVALCLGGGVYGISLGNHVTQSGFYDEGSQSVAASLIGDEVYGRDRTSHVVAILTPPDDKKVTDKAWQKKVTEELDQVVKDHEDQIVGWVGWLKAPDTTDPTVSAMKTQDLRHTFISIPLQGDDDDEILKNYQVVEPELQQVNGGDIRLAGLNPLASELTGTIGEDQKRAEVAAIPLVAVVLFFVFGTVIAAALPAIIGGLAIAGALGIMRLVAEFTPVHFFAQPVVTLIGLGIAIDYGLFIVSRFREEIAEGYDTEAAVRRTVMTSGRTVVFSAVIIVASSVPLLLFPQGFLKSITYAII... | null | null | cell wall biogenesis [GO:0042546]; cell wall organization [GO:0071555]; mycolate cell wall layer assembly [GO:0071769]; mycolic acid biosynthetic process [GO:0071768]; phospholipid transport [GO:0015914]; regulation of membrane potential [GO:0042391]; response to antibiotic [GO:0046677]; response to xenobiotic stimulus... | cell pole [GO:0060187]; cell septum [GO:0030428]; cell tip [GO:0051286]; plasma membrane [GO:0005886] | cardiolipin binding [GO:1901612]; diacylglycerol binding [GO:0019992]; phosphatidylethanolamine binding [GO:0008429]; phosphatidylethanolamine transfer activity [GO:1904121]; phosphatidylglycerol binding [GO:1901611]; phosphatidylinositol binding [GO:0035091]; trehalose transmembrane transporter activity [GO:0015574] | PF03176; | 1.20.1640.10; | Resistance-nodulation-cell division (RND) (TC 2.A.6) family, MmpL subfamily | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:28698380, ECO:0000269|PubMed:30682372, ECO:0000269|PubMed:31113875}; Multi-pass membrane protein {ECO:0000255, ECO:0000305|PubMed:30682372, ECO:0000305|PubMed:31113875}. Cell septum {ECO:0000269|PubMed:31239378}. Cell tip {ECO:0000269|PubMed:31239378}. Note=... | null | null | null | null | null | FUNCTION: Transports trehalose monomycolate (TMM) to the cell wall (PubMed:22520756, PubMed:28698380, PubMed:31239378). Flips TMM across the inner membrane. Membrane potential is not required for this function (PubMed:28698380). Transports probably phosphatidylethanolamine (PE) as well. Binds specifically both TMM and ... | Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) |
A0QQF4 | TTFA_MYCS2 | MVPLWFTLSALCFVGAAVLLYVDIDRRRGLGRRRKSWAKSHGFDYEYESEDLLKRWKRGVMSTVGDVTAKNVVLGQIRGEAVFIFDIEEVATVIALHRKVGTNVVVDLRLKGLKEPRENDIWLLGAIGPRMVYSTNLDAARRACDRRMVTFAHTAPDCAEIMWNEQNWTLVAMPVTSNRAQWDEGLRTVRQFNDLLRVLPPVPQNGSQAALPRRGGSPSRPLAPTPAGRRELPPGRADVPPARGDVSRFAPRPEAGRSDAFRRPPPARNGREASHFQR | null | null | cell wall organization [GO:0071555]; lipid transport [GO:0006869] | cell septum [GO:0030428]; cell tip [GO:0051286]; plasma membrane [GO:0005886] | null | null | null | null | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:31239378}; Single-pass membrane protein {ECO:0000255}. Cell septum {ECO:0000269|PubMed:31239378}. Cell tip {ECO:0000269|PubMed:31239378}. Note=Colocalizes with MmpL3 to the cell poles and septa. Trehalose monomycolate (TMM) synthesis is not required for loca... | null | null | null | null | null | FUNCTION: Required for MmpL3-dependent trehalose monomycolate (TMM) transport to the cell wall. Required for growth and cell elongation. {ECO:0000269|PubMed:31239378}. | Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) |
A0QQJ4 | FGD_MYCS2 | MAELKLGYKASAEQFAPRELVELAVLAESAGMDSATVSDHFQPWRHEGGHAPFSLAWMTAVGERTKNLVLGTSVLTPTFRYNPAVIAQAFATMGCLYPGRIFLGVGTGEALNEIATGYAGEWPEFKERFARLRESVRLMRELWLGDRVDFDGEYYRTKGASIYDVPEGGIPVYIAAGGPVVAKYAGRAGDGFICTSGKGEELYAEKLIPAVKEGAAAADRDADAIDRMIEIKISYDTDPELALENTRFWAPLSLTAEQKHSIDDPIEMEKAADALPIEQVAKRWIVASDPDEAVEKVGQYVKWGLNHLVFHAPGHDQRRF... | 1.1.98.2 | null | carbohydrate metabolic process [GO:0005975] | null | coenzyme F420 binding [GO:0070967]; glucose-6-phosphate dehydrogenase (coenzyme F420) activity [GO:0052749]; oxidoreductase activity, acting on CH-OH group of donors [GO:0016614]; oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen [GO:0016705]; protein homodimerization... | PF00296; | 3.20.20.30; | F420-dependent glucose-6-phosphate dehydrogenase family | null | null | CATALYTIC ACTIVITY: Reaction=D-glucose 6-phosphate + H(+) + oxidized coenzyme F420-(gamma-L-Glu)(n) = 6-phospho-D-glucono-1,5-lactone + reduced coenzyme F420-(gamma-L-Glu)(n); Xref=Rhea:RHEA:27294, Rhea:RHEA-COMP:12939, Rhea:RHEA-COMP:14378, ChEBI:CHEBI:15378, ChEBI:CHEBI:57955, ChEBI:CHEBI:61548, ChEBI:CHEBI:133980, C... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.004 mM for coenzyme F420 (at pH 7 and 40 degrees Celsius) {ECO:0000269|PubMed:8631674}; KM=1.6 mM for D-glucose 6-phosphate (at pH 7 and 40 degrees Celsius) {ECO:0000269|PubMed:8631674}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pHs are 5.5 and 8.0. {ECO:0000269|PubMed:8631674}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 60 degrees Celsius. {ECO:0000269|PubMed:8631674}; | FUNCTION: Catalyzes the coenzyme F420-dependent oxidation of glucose 6-phosphate (G6P) to 6-phosphogluconolactone. Appears to have a role in resistance to oxidative stress, via its consumption of G6P that serves as a source of reducing power to combat oxidative stress in mycobacteria. Cannot use NAD, NADP, FAD or FMN i... | Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) |
A0QQU5 | CH602_MYCS2 | MAKTIAYDEEARRGLERGLNSLADAVKVTLGPKGRNVVLEKKWGAPTITNDGVSIAKEIELEDPYEKIGAELVKEVAKKTDDVAGDGTTTATVLAQALVREGLRNVAAGANPLGLKRGIEKAVEKVTETLLKSAKEVETKEQIAATAGISAGDQSIGDLIAEAMDKVGNEGVITVEESNTFGLQLELTEGMRFDKGYISGYFVTDAERQEAVLEDPYILLVSSKVSTVKDLLPLLEKVIQSGKPLLIIAEDVEGEALSTLVVNKIRGTFKSVAVKAPGFGDRRKAMLQDMAILTGGQVISEEVGLSLETADVSLLGKARK... | 5.6.1.7 | null | chaperone cofactor-dependent protein refolding [GO:0051085]; mitochondrial unfolded protein response [GO:0034514]; positive regulation of interferon-alpha production [GO:0032727]; positive regulation of interleukin-6 production [GO:0032755]; positive regulation of T cell activation [GO:0050870]; positive regulation of ... | capsule [GO:0042603]; cell surface [GO:0009986]; extracellular region [GO:0005576]; GroEL-GroES complex [GO:1990220] | ATP binding [GO:0005524]; ATP-dependent protein folding chaperone [GO:0140662]; isomerase activity [GO:0016853]; protein-folding chaperone binding [GO:0051087]; unfolded protein binding [GO:0051082] | PF00118; | 3.50.7.10;1.10.560.10;3.30.260.10; | Chaperonin (HSP60) family | null | SUBCELLULAR LOCATION: Secreted, capsule {ECO:0000250|UniProtKB:P9WPE7}. Cell surface {ECO:0000250|UniProtKB:P9WPE7}. Secreted, cell wall {ECO:0000250|UniProtKB:P9WPE7}. | CATALYTIC ACTIVITY: Reaction=ATP + H2O + a folded polypeptide = ADP + phosphate + an unfolded polypeptide.; EC=5.6.1.7; Evidence={ECO:0000255|HAMAP-Rule:MF_00600}; | null | null | null | null | FUNCTION: Together with its co-chaperonin GroES, plays an essential role in assisting protein folding. The GroEL-GroES system forms a nano-cage that allows encapsulation of the non-native substrate proteins and provides a physical environment optimized to promote and accelerate protein folding. {ECO:0000255|HAMAP-Rule:... | Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) |
A0QR29 | MSPA_MYCS2 | MKAISRVLIAMVAAIAALFTSTGTSHAGLDNELSLVDGQDRTLTVQQWDTFLNGVFPLDRNRLTREWFHSGRAKYIVAGPGADEFEGTLELGYQIGFPWSLGVGINFSYTTPNILIDDGDITAPPFGLNSVITPNLFPGVSISADLGNGPGIQEVATFSVDVSGAEGGVAVSNAHGTVTGAAGGVLLRPFARLIASTGDSVTTYGEPWNMN | null | null | iron ion transport [GO:0006826] | cell outer membrane [GO:0009279]; extracellular region [GO:0005576]; pore complex [GO:0046930] | porin activity [GO:0015288] | PF09203; | 2.60.40.1650;2.10.300.10; | Mycobacterial porin (TC 1.B.24) family | null | SUBCELLULAR LOCATION: Cell outer membrane. Secreted, cell wall. | null | null | null | null | null | FUNCTION: The major porin in this organism, forms a water-filled channel which favors the permeation of cations, amino acids, iron Fe(3+) and less efficiently phosphate. Does not transport Fe-ExoMS, the predominant siderophore. Plays a role in transport of beta-lactamase and hydrophilic fluoroquinolone antibiotics such... | Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) |
A0QS29 | RECB_MYCS2 | MKVFDLLGPLPAPNTTTVLEASAGTGKTFALAGLVTRFVAEGVATLDQMLLITFGRAASQELRERVRAQIVAALVALDDPSRACNDLEEYLVKTDQQARRRRLRDALAGFDAATIATTHQFCQIVLKSLGVAGDSDAGVTLVESLDDLVSEIVDDLYLAHFGGQKDDPELSYPEALKLARVVVGNPATQLRPRDPDPDSPAAVRLKFARDVLAELEIRKRRRGVLGYDDLLTRLADALEPEDSPARVRMQQRWPIVMVDEFQDTDPVQWQVIERAFSGRSTLVLIGDPKQAIYAFRGGDIATYLRAAATAGDKQTLGTNW... | 3.1.11.5; 5.6.2.4 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_01485}; Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01485}; | double-strand break repair via homologous recombination [GO:0000724] | cytosol [GO:0005829]; exodeoxyribonuclease V complex [GO:0009338] | 3'-5' DNA helicase activity [GO:0043138]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; DNA binding [GO:0003677]; exodeoxyribonuclease V activity [GO:0008854]; isomerase activity [GO:0016853]; magnesium ion binding [GO:0000287] | PF00580;PF13361; | 3.90.320.10;3.40.50.300; | Helicase family, UvrD subfamily | null | null | CATALYTIC ACTIVITY: Reaction=Exonucleolytic cleavage (in the presence of ATP) in either 5'- to 3'- or 3'- to 5'-direction to yield 5'-phosphooligonucleotides.; EC=3.1.11.5; Evidence={ECO:0000255|HAMAP-Rule:MF_01485}; CATALYTIC ACTIVITY: Reaction=Couples ATP hydrolysis with the unwinding of duplex DNA by translocating i... | null | null | null | null | FUNCTION: A helicase/nuclease that prepares dsDNA breaks (DSB) for recombinational DNA repair. Binds to DSBs and unwinds DNA via a highly rapid and processive ATP-dependent bidirectional helicase activity. Holoenzyme degrades any linearized DNA that is unable to undergo homologous recombination. In the holoenzyme this ... | Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) |
A0QS56 | SIWR_MYCS2 | MARTVDTTGRVVQLLGLLQSRRVWTGEELAERLGVTGRSVRRDIERLRELGYPVHASKGQGGGYQLGAGMALPPLLLDPDEAVAMAVCLRLAAGGSVAGVGESALRALSKLDQVMPARLRSQVAAIHDATVTLGPNATDTAVAPDVLMTLARACRDREHVSTGYTDLRGNQTQRRLEPYQLVTTGRRWYLMAYDRDREDWRSLRLDRMSDVRATGTTFTARPAPDAAAYVGRAISASAYPYVARVRYFAPEKVVAQRFPPGTATFEPDGPDACIVTSGAEYPEQLAMYFATVGHDFEVLEPAEVIDAVGAMADRLRRAVR | null | null | DNA damage response, signal transduction resulting in transcription [GO:0042772]; regulation of cellular response to stress [GO:0080135] | null | core promoter sequence-specific DNA binding [GO:0001046]; DNA-binding transcription activator activity [GO:0001216]; protein homodimerization activity [GO:0042803]; single-stranded DNA binding [GO:0003697] | PF08279;PF13280; | 1.10.10.10; | null | null | null | null | null | null | null | null | FUNCTION: Transcriptional activator (PubMed:38042942). Acts as a transcriptional activator of the MSMEG_1357-56 operon upon genotoxic stress (PubMed:38042942). Controls adjacent genes that belong to the DinB/YfiT-like putative metalloenzymes superfamily by upregulating their expression in response to various genotoxic ... | Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) |
A0QTP2 | SIGH_MYCS2 | MTDVDRVEPETPPEREETDAELTARFERDAIPLLDQLYGGALRMTRNPADAEDLLQETMVKAYAGFRSFREGTNLKAWLYRILTNTYINSYRKKQRQPSEYPTDEITDWQLASNAEHSSTGLRSAEVEALEALPDTEIKAALQALPEEFRMAVYYADVEGFPYKEIAEIMETPIGTVMSRLHRGRRQLRDLLAGVARDRGFIRGPQLGEPEEVTS | null | null | DNA-templated transcription initiation [GO:0006352]; response to abiotic stimulus [GO:0009628]; response to stress [GO:0006950] | null | DNA binding [GO:0003677]; sigma factor activity [GO:0016987] | PF04542;PF08281; | 1.10.1740.10;1.10.10.10; | Sigma-70 factor family, ECF subfamily | null | null | null | null | null | null | null | FUNCTION: Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. Extracytoplasmic function (ECF) sigma factors are held in an inactive form by an anti-sigma factor until released. This sigma factor is involved in heat shock and oxidative st... | Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) |
A0QUA1 | MBTM_MYCS2 | MNVLSAALTEAMTTSSADLVVFEPETRTWHRHPWGQVHLRAQNVAERIGQDGSSAVGIVGEPTVEGVAAILGALLAGSAVSILPGLVRGADPDQWADSTLNRFANIGVTTVFSHGSYLEQLRTRDSSLVIHDDAEVAHAQRSTTLELGAPLGEFAVLQGTAGSTGTPRTAQLRPDAVLANLRGLAERVGLAGSDIGCSWLPLYHDMGLTFLLSAAVGGTETWQAPTTAFASAPFSWVHWLTESRATLTAAPNMAYGLIGKYSRRLTDVDLSAMRFALNGGEPVDIDGTARFGTELSRFGFDPGALSPSYGLAESSCAVTV... | 6.2.1.20; 6.2.1.47 | null | fatty acid biosynthetic process [GO:0006633] | cytosol [GO:0005829]; plasma membrane [GO:0005886] | adenylyltransferase activity [GO:0070566]; ATP binding [GO:0005524]; long-chain fatty acid [acyl-carrier-protein] ligase activity [GO:0008922] | PF00501; | 3.30.300.30;3.40.50.12780; | ATP-dependent AMP-binding enzyme family | PTM: Acetylated on Lys-511 and Lys-260 by Pat. Lys-511 is the major acetylation site. Acetylation results in the inactivation of the enzyme. {ECO:0000269|PubMed:23935107}. | null | CATALYTIC ACTIVITY: Reaction=a long-chain fatty acid + ATP + holo-[ACP] = a long-chain fatty acyl-[ACP] + AMP + diphosphate; Xref=Rhea:RHEA:45588, Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:12682, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57560, ChEBI:CHEBI:64479, ChEBI:CHEBI:133243, ChEBI:CHEBI:456215; EC=6.2.1.20; E... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=129 uM for hexanoic acid {ECO:0000269|PubMed:23935107}; KM=121 uM for decanoic acid {ECO:0000269|PubMed:23935107}; KM=21 uM for lauric acid {ECO:0000269|PubMed:23935107}; KM=1.9 uM for palmitic acid {ECO:0000269|PubMed:23935107}; KM=15 uM for ATP {ECO:0000269|PubMe... | PATHWAY: Siderophore biosynthesis; mycobactin biosynthesis. {ECO:0000269|PubMed:23935107}. | null | null | FUNCTION: Activates lipidic moieties required for mycobactin biosynthesis (PubMed:23935107). Converts medium- to long-chain aliphatic fatty acids into acyl adenylate, which is further transferred on to the phosphopantetheine arm of the carrier protein MbtL (PubMed:23935107). Shows a strong preference for palmitic acid ... | Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) |
A0QUZ2 | MUTT1_MYCS2 | MMPVDDLQEIPLSKDTTEKSKHTVRAAGAVLWRDASEHGGTTGHPATVEVAVIHRPRYDDWSLPKGKLDQGETEPVAAAREIHEETGHTAVLGRRLGRVTYPIPQGTKRVWYWAAKSTGGDFSPNDEVDKLVWLPVDAAMDQLQYPDDRKVLRRFVKRPVDTKTVLVVRHGTAGRRSRYKGDDRKRPLDKRGRAQAEALVAQLMAFGATTLYAADRVRCHQTIEPLAQELDQLIHNEPLLTEEAYAADHKAARKRLLEIAGRPGNPVICTQGKVIPGLIEWWCERAKVRPETTGNRKGSTWVLSLSDGELVGADYLSPPD... | 3.6.1.58; 3.6.1.61; 3.6.1.69 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:28375146, ECO:0000269|PubMed:28705712}; Note=Can also use Mn(2+), with lower efficiency. {ECO:0000269|PubMed:28705712}; | DNA repair [GO:0006281]; DNA replication [GO:0006260] | null | 8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity [GO:0008413]; 8-oxo-dGDP phosphatase activity [GO:0044715]; 8-oxo-GDP phosphatase activity [GO:0044716]; metal ion binding [GO:0046872] | PF00300;PF00293; | 3.90.79.10;3.40.50.1240; | Nudix hydrolase family | null | null | CATALYTIC ACTIVITY: Reaction=8-oxo-dGTP + H2O = 8-oxo-dGDP + H(+) + phosphate; Xref=Rhea:RHEA:59980, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:63715, ChEBI:CHEBI:77896; EC=3.6.1.69; Evidence={ECO:0000269|PubMed:28375146}; CATALYTIC ACTIVITY: Reaction=8-oxo-GTP + H2O = 8-oxo-GDP + H(+) + phosp... | null | null | null | null | FUNCTION: Catalyzes the conversion of 8-oxo-dGTP to 8-oxo-dGDP, and 8-oxo-GTP to 8-oxo-GDP (PubMed:16585780, PubMed:28375146). At high enzyme concentrations, can also catalyze the conversion of 8-oxo-dGDP to 8-oxo-dGMP, and 8-oxo-GDP to 8-oxo-GMP (PubMed:28375146). In addition, catalyzes the hydrolysis of the diadenosi... | Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) |
A0QVH8 | RIP1_MYCS2 | MMFGIGIVLFALAILVSVALHECGHMWVARATGMKVRRYFVGFGPTLWSTRRANRLGSTEYGIKAIPLGGFCDIAGMTSVDEIAPEDRPYAMYKQKVWKRVAVLFAGPAMNFVIGLVLIYGIAIVWGLPNLHQPTTAIVGETGCVAPQITLEEMGECTGPGPAALAGIQAGDEIVKVGDTEVKDFAGMAAAVRKLDGPTRIEFKRDGRVMDTVVDVTPTQRFTSADASAPSTVGAIGVSAVPVQPPAQYNPITAVPATFAFTGDLAVELGKSLAKIPTKIGALVEAIGGGERDKETPISVVGASIIGGETVDAGLWVAFW... | 3.4.24.- | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; | proteolysis [GO:0006508] | plasma membrane [GO:0005886] | metal ion binding [GO:0046872]; metalloendopeptidase activity [GO:0004222] | PF17820;PF02163; | 2.30.42.10; | Peptidase M50B family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. | null | null | null | null | null | FUNCTION: A probable intramembrane site-2 protease (S2P) that cleaves type-2 transmembrane proteins within their membrane-spanning domains. Degrades PbpB (PBP3, FtsI) under conditions of oxidatives stress; degradation is inhibited by Wag31-PbpB interaction. Also cleaves anti-sigma factors RskA, RslA and RslM. Site-1 pr... | Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) |
A0QWG5 | ACYLT_MYCS2 | MTLSGRIPLGGQVTDLGYAAGWRLVRAMPEAMAQGVFGAGARYAARNGGPEQLRRNLARVVGKPPADVPDDLIRASLASYARYWREAFRLPAMDHGRLGEQLDVIDIDHLWSALDAGRGAVLALPHSGNWDMAGVWLVQNYGPFTTVAERLKPESLYRRFVEYRESLGFEVLPLTGGERPPFEVLAERLTDNRPICLMAERDLTRSGVQVDFFGEATRMPAGPAKLAIETGAALFPVHCWFEGDGWGMRVYPELDTSSGDVTAITQALADRFAANIATYPADWHMLQPQWIADLSDERRARLGT | 2.3.1.265 | null | glycolipid biosynthetic process [GO:0009247]; phosphatidylinositol metabolic process [GO:0046488]; phospholipid biosynthetic process [GO:0008654] | plasma membrane [GO:0005886] | acyltransferase activity [GO:0016746] | PF03279; | null | LpxL/LpxM/LpxP family | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:12851411, ECO:0000269|PubMed:26965057, ECO:0000269|PubMed:29185694}; Peripheral membrane protein {ECO:0000269|PubMed:26965057, ECO:0000269|PubMed:29185694}; Cytoplasmic side {ECO:0000269|PubMed:26965057, ECO:0000269|PubMed:29185694}. Note=Permanently associa... | CATALYTIC ACTIVITY: Reaction=a 2,6-O-bis(alpha-D-mannopyranosyl)-1-phosphatidyl-1D-myo-inositol + an acyl-CoA = 2-O-(alpha-D-mannosyl)-6-O-(6-O-acyl-alpha-D-mannosyl)-1-phosphatidyl-1D-myo-inositol + CoA; Xref=Rhea:RHEA:52436, ChEBI:CHEBI:57287, ChEBI:CHEBI:58342, ChEBI:CHEBI:136624, ChEBI:CHEBI:136625; EC=2.3.1.265; E... | null | PATHWAY: Phospholipid metabolism; phosphatidylinositol metabolism. {ECO:0000269|PubMed:12851411}. | null | null | FUNCTION: Catalyzes the transfer of a palmitoyl moiety from palmitoyl-CoA to the 6-position of the mannose ring linked to the 2-position of myo-inositol in phosphatidyl-myo-inositol monomannoside (PIM1) or dimannoside (PIM2). {ECO:0000269|PubMed:12851411, ECO:0000269|PubMed:24810911, ECO:0000269|PubMed:26965057, ECO:00... | Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) |
A0QWG6 | PIMA_MYCS2 | MRIGMVCPYSFDVPGGVQSHVLQLAEVLRDAGHEVSVLAPASPHVKLPDYVVSGGKAVPIPYNGSVARLRFGPATHRKVKKWIAEGDFDVLHIHEPNAPSLSMLALQAAEGPIVATFHTSTTKSLTLSVFQGILRPYHEKIIGRIAVSDLARRWQMEALGSDAVEIPNGVDVASFADAPLLDGYPREGRTVLFLGRYDEPRKGMAVLLAALPKLVARFPDVEILIVGRGDEDELREQAGDLAGHLRFLGQVDDATKASAMRSADVYCAPHLGGESFGIVLVEAMAAGTAVVASDLDAFRRVLADGDAGRLVPVDDADGMA... | 2.4.1.345 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P9WMZ5}; | glycolipid biosynthetic process [GO:0009247]; phosphatidylinositol metabolic process [GO:0046488]; phospholipid biosynthetic process [GO:0008654]; sulfolipid biosynthetic process [GO:0046506] | plasma membrane [GO:0005886] | GDP-Man:Man3GlcNAc2-PP-Dol alpha-1,2-mannosyltransferase activity [GO:0004377]; phosphatidylinositol alpha-mannosyltransferase activity [GO:0043750]; UDP-sulfoquinovose:DAG sulfoquinovosyltransferase activity [GO:0046510] | PF13692;PF13439; | 3.40.50.2000; | Glycosyltransferase group 1 family, Glycosyltransferase 4 subfamily | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:12068013, ECO:0000305|PubMed:19520856}; Peripheral membrane protein {ECO:0000305|PubMed:19520856}; Cytoplasmic side {ECO:0000305|PubMed:19520856}. | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + GDP-alpha-D-mannose = a 1,2-diacyl-sn-glycero-3-phospho-[alpha-D-mannopyranosyl-(1<->6)-D-myo-inositol] + GDP + H(+); Xref=Rhea:RHEA:47368, ChEBI:CHEBI:15378, ChEBI:CHEBI:57527, ChEBI:CHEBI:57880, ChEBI:CHEBI:58189, ChEBI:CHEBI:87673; EC... | null | PATHWAY: Phospholipid metabolism; phosphatidylinositol metabolism. {ECO:0000305|PubMed:19638342}. | null | null | FUNCTION: Involved in the biosynthesis of phosphatidyl-myo-inositol mannosides (PIM) which are early precursors in the biosynthesis of lipomannans (LM) and lipoarabinomannans (LAM). Catalyzes the addition of a mannosyl residue from GDP-D-mannose (GDP-Man) to the position 2 of the carrier lipid phosphatidyl-myo-inositol... | Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) |
A0QWS8 | IHF_MYCS2 | MALPQLTDEQRAAALEKAAAARRARAELKDRLKRGGTNLKQVLTDAETDEVLGKMKVSALLEALPKVGKVKAQEIMTELEIAPTRRLRGLGDRQRKALLEKFDQS | null | null | chromosome condensation [GO:0030261]; DNA integration [GO:0015074]; DNA recombination [GO:0006310]; establishment of integrated proviral latency [GO:0075713]; symbiont entry into host cell [GO:0046718]; viral genome integration into host DNA [GO:0044826] | cytoplasm [GO:0005737]; nucleoid [GO:0009295] | DNA binding [GO:0003677] | null | 1.10.8.50; | Actinobacterial IHF (aIHF) family | null | SUBCELLULAR LOCATION: Cytoplasm, nucleoid {ECO:0000269|PubMed:36960278}. Note=Found along the cell length in a bead-like pattern corresponding to DNA. Association with the chromosome is dynamic and responds to changes in DNA topology, colocalizes with HupB (hup). {ECO:0000269|PubMed:36960278}. | null | null | null | null | null | FUNCTION: A nucleoid-associated protein (NAP) that binds DNA without any sequence specificity (PubMed:31733417, PubMed:36960278, PubMed:8986825). Compacts DNA (PubMed:31733417). Binds along the whole chromosome in a dynamic manner, has equal affinity for the oriC site, attB and a randon 62% GC-rich sequence (PubMed:369... | Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) |
A0QWT2 | COABC_MYCS2 | MSARKRIVVGVAGGIAAYKACTVVRQLTEAGHSVRVVPTESALRFVGAATFEALSGNPVHTGVFTDVHEVQHVRIGQQADLVVIAPATADLLARAVAGRADDLLTATLLTARCPVLFAPAMHTEMWLHPATVDNVATLRRRGAVVLEPASGRLTGADSGPGRLPEAEEITTLAQLLLERADALPYDMAGVKALVTAGGTREPLDPVRFIGNRSSGKQGYAVARVLAQRGADVTLIAGNTAGLIDPAGVEMVHIGSATQLRDAVSKHAPDANVLVMAAAVADFRPAHVAAAKIKKGASEPSSIDLVRNDDVLAGAVRARAD... | 4.1.1.36; 6.3.2.5 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_02225}; COFACTOR: Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000255|HAMAP-Rule:MF_02225}; Note=Binds 1 FMN per subunit. {ECO:0000255|HAMAP-Rule:MF_02225}; | coenzyme A biosynthetic process [GO:0015937]; pantothenate catabolic process [GO:0015941] | phosphopantothenoylcysteine decarboxylase complex [GO:0071513] | FMN binding [GO:0010181]; metal ion binding [GO:0046872]; phosphopantothenate--cysteine ligase activity [GO:0004632]; phosphopantothenoylcysteine decarboxylase activity [GO:0004633] | PF04127;PF02441; | 3.40.50.10300;3.40.50.1950; | HFCD (homo-oligomeric flavin containing Cys decarboxylase) superfamily; PPC synthetase family | null | null | CATALYTIC ACTIVITY: Reaction=H(+) + N-[(R)-4-phosphopantothenoyl]-L-cysteine = (R)-4'-phosphopantetheine + CO2; Xref=Rhea:RHEA:16793, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:59458, ChEBI:CHEBI:61723; EC=4.1.1.36; Evidence={ECO:0000255|HAMAP-Rule:MF_02225}; CATALYTIC ACTIVITY: Reaction=(R)-4'-phosphopantothena... | null | PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 2/5. {ECO:0000255|HAMAP-Rule:MF_02225}.; PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 3/5. {ECO:0000255|HAMAP-Rule:MF_02225}. | null | null | FUNCTION: Catalyzes two sequential steps in the biosynthesis of coenzyme A. In the first step cysteine is conjugated to 4'-phosphopantothenate to form 4-phosphopantothenoylcysteine. In the second step the latter compound is decarboxylated to form 4'-phosphopantotheine. {ECO:0000255|HAMAP-Rule:MF_02225}. | Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) |
A0QX20 | ACNA_MYCS2 | MSSENTGKSSLNSFGARDTLTVGDQSYEIYRLNAVPGTEKLPYSLKVLAENLLRTEDGANITKDHIEAIANWDPNAEPSIEIQFTPARVIMQDFTGVPCIVDLATMREAVAALGGDPNKVNPLAPAELVIDHSVILDVFGNASAFERNVELEYERNAERYQFLRWGQGAFDDFKVVPPGTGIVHQVNIEYLARTVMVRDGVAYPDTCVGTDSHTTMVNGLGVLGWGVGGIEAEAAMLGQPVSMLIPRVVGFKLSGEIKPGVTATDVVLTVTDMLRRHGVVGKFVEFYGKGVAEVPLANRATLGNMSPEFGSTAAIFPIDE... | 4.2.1.3; 4.2.1.99 | COFACTOR: Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250|UniProtKB:P09339}; Note=Binds 1 [4Fe-4S] cluster per subunit. {ECO:0000250|UniProtKB:P09339}; | citrate metabolic process [GO:0006101]; tricarboxylic acid cycle [GO:0006099] | cytosol [GO:0005829] | 2-methylisocitrate dehydratase activity [GO:0047456]; 4 iron, 4 sulfur cluster binding [GO:0051539]; aconitate hydratase activity [GO:0003994]; iron-responsive element binding [GO:0030350]; metal ion binding [GO:0046872]; mRNA 3'-UTR binding [GO:0003730]; mRNA binding [GO:0003729] | PF00330;PF00694; | 6.10.190.10;3.30.499.10;3.20.19.10; | Aconitase/IPM isomerase family | null | null | CATALYTIC ACTIVITY: Reaction=citrate = D-threo-isocitrate; Xref=Rhea:RHEA:10336, ChEBI:CHEBI:15562, ChEBI:CHEBI:16947; EC=4.2.1.3; Evidence={ECO:0000250|UniProtKB:O53166}; CATALYTIC ACTIVITY: Reaction=(2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate = 2-methyl-cis-aconitate + H2O; Xref=Rhea:RHEA:17941, ChEBI:CHEBI:15377, C... | null | PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; isocitrate from oxaloacetate: step 2/2. {ECO:0000250|UniProtKB:O53166}.; PATHWAY: Organic acid metabolism; propanoate degradation. {ECO:0000250|UniProtKB:O53166}. | null | null | FUNCTION: Involved in the catabolism of short chain fatty acids (SCFA) via the tricarboxylic acid (TCA)(acetyl degradation route) and probably via the 2-methylcitrate cycle I (propionate degradation route). Catalyzes the reversible isomerization of citrate to isocitrate via cis-aconitate. The apo form of AcnA functions... | Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) |
A0QX22 | RIPA_MYCS2 | MRRTVRALATRVHGRVCAVPLVVGMLLATALYGGGPAAADPAAPDNLATLVAKVASADQKLQELGAAIQTQQETVNKAIVDVQAARDAAAAAQRELEAGQRGVADANAAIEAAQKRFDSFAAATYMNGPSRSYLTATDPADIVNTTATGQALIASSQQVMAKLQRARTEQVNRESAARLAKEKADQAARDAESSQDNAVAALKQAQQTFNAQQGELERLAAERAAAQAELDSVRKVSATGNAAPAAAPAAAPAPAAAPAPVPNSAPAPVPGAQPNPQAAAGNWDRAPSGPASSGQNWAVWDPTLPAIPSAFVSGDPIAII... | 3.4.-.- | null | cell division [GO:0051301]; cell wall macromolecule catabolic process [GO:0016998]; cell wall organization [GO:0071555]; cell wall organization or biogenesis [GO:0071554]; peptidoglycan catabolic process [GO:0009253]; proteolysis [GO:0006508]; regulation of cell shape [GO:0008360] | extracellular region [GO:0005576] | cysteine-type peptidase activity [GO:0008234] | PF00877; | 6.10.250.3150;3.90.1720.10; | Peptidase C40 family | null | SUBCELLULAR LOCATION: Secreted. Note=Localizes to the septa. {ECO:0000250}. | null | null | null | null | null | FUNCTION: Peptidoglycan endopeptidase that cleaves the bond between D-glutamate and meso-diaminopimelate. Binds and degrades high-molecular weight peptidoglycan. Required for normal separation of daughter cells after cell division and for cell wall integrity (By similarity). {ECO:0000250, ECO:0000269|PubMed:18463693}. | Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) |
A0QXD8 | ELTD_MYCS2 | MSNQVPEKMQAVVCHGPHDYRLEEVAVPQRKPGEALIRVEAVGICASDLKCYHGAAKFWGDENRPAWAETMVIPGHEFVGRVVELDDEAAQRWGIAVGDRVVSEQIVPCWECLFCKRGQYHMCQPHDLYGFKRRTPGAMASYMVYPAEALVHKVSPDIPAQHAAFAEPLSCSLHAVERAQITFEDTVVVAGCGPIGLGMIAGAKAKSPMRVIALDMAPDKLKLAEKCGADLTINIAEQDAEKIIKDLTGGYGADVYIEGTGHTSAVPQGLNLLRKLGRYVEYGVFGSDVTVDWSIISDDKELDVLGAHLGPYCWPAAIKM... | 1.1.1.- | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:O58389}; Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:O58389}; | carbohydrate catabolic process [GO:0016052]; carbohydrate utilization [GO:0009758]; cellular response to carbohydrate stimulus [GO:0071322] | null | carbohydrate binding [GO:0030246]; metal ion binding [GO:0046872]; oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor [GO:0016616] | PF08240;PF00107; | 3.90.180.10;3.40.50.720; | Zinc-containing alcohol dehydrogenase family | null | null | CATALYTIC ACTIVITY: Reaction=erythritol + NAD(+) = D-erythrulose + H(+) + NADH; Xref=Rhea:RHEA:48756, ChEBI:CHEBI:15378, ChEBI:CHEBI:16023, ChEBI:CHEBI:17113, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; Evidence={ECO:0000269|PubMed:26560079}; CATALYTIC ACTIVITY: Reaction=L-threitol + NAD(+) = H(+) + L-erythrulose + NADH; Xre... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.64 mM for L-threitol {ECO:0000269|PubMed:26560079}; KM=1.5 mM for erythritol {ECO:0000269|PubMed:26560079}; KM=1.47 mM for L-arabitol {ECO:0000269|PubMed:26560079}; KM=2.76 mM for xylitol {ECO:0000269|PubMed:26560079}; KM=2.21 mM for ribitol {ECO:0000269|PubMed:2... | PATHWAY: Carbohydrate metabolism; erythritol degradation. {ECO:0000269|PubMed:26560079}.; PATHWAY: Carbohydrate metabolism; L-threitol degradation. {ECO:0000269|PubMed:26560079}. | null | null | FUNCTION: Catalyzes the NAD-dependent reversible oxidation of erythritol and L-threitol. Involved in the degradation pathways of erythritol and L-threitol, that allow M.smegmatis to grow on these compounds as the sole carbon source. {ECO:0000269|PubMed:26560079}. | Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) |
A0QXE4 | DERK_MYCS2 | MTKLFNDPARFTEDMLVGFLDANSRYVVGVPGGVVRAQTTRPGKVAVVIGGGSGHYPAFCGTVGPGFADGAVVGNIFTSPSAEEAASVARAAHSDAGVLLTTGNYAGDVMNFNLAVDQLRSEGIEAQYFAVTDDVASAERGQEAKRRGIAGDFTVFKCASAAAEEGLDLAGVVRVAEAANAATRTLGVAFDGCTLPGADHPLFTVPEGHMGLGLGIHGEPGVSEEKMPTAAGLAATLVDGVLGDRPDAPEKRIAVILNGLGRTKYEELFVVWGEVSRLLRDRGYTIVEPEVGELVTSLDMAGCSLTVMWLDEELERYWAA... | 2.7.1.210 | null | carbohydrate catabolic process [GO:0016052]; carbohydrate utilization [GO:0009758]; cellular response to carbohydrate stimulus [GO:0071322]; glycerol catabolic process [GO:0019563] | cytosol [GO:0005829] | ATP binding [GO:0005524]; carbohydrate binding [GO:0030246]; carbohydrate kinase activity [GO:0019200]; glycerone kinase activity [GO:0004371] | PF02733;PF02734; | 1.25.40.340; | null | null | null | CATALYTIC ACTIVITY: Reaction=ATP + D-erythrulose = ADP + D-erythrulose 4-phosphate + H(+); Xref=Rhea:RHEA:48768, ChEBI:CHEBI:15378, ChEBI:CHEBI:16023, ChEBI:CHEBI:30616, ChEBI:CHEBI:90796, ChEBI:CHEBI:456216; EC=2.7.1.210; Evidence={ECO:0000269|PubMed:26560079}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=4.6 uM for D-erythrulose {ECO:0000269|PubMed:26560079}; KM=396 uM for L-erythrulose {ECO:0000269|PubMed:26560079}; KM=339 uM for dihydroxyacetone {ECO:0000269|PubMed:26560079}; Note=kcat is 2.88 sec(-1) with D-erythrulose as substrate. kcat is 0.091 sec(-1) with L-... | PATHWAY: Carbohydrate metabolism; erythritol degradation. {ECO:0000269|PubMed:26560079}.; PATHWAY: Carbohydrate metabolism; D-threitol degradation. {ECO:0000269|PubMed:26560079}. | null | null | FUNCTION: Catalyzes the phosphorylation of D-erythrulose to D-erythrulose-4P. Involved in the degradation pathways of erythritol and D-threitol, that allow M.smegmatis to grow on these compounds as the sole carbon source. {ECO:0000269|PubMed:26560079}. | Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) |
A0QXX7 | KATG2_MYCS2 | MSSDTSDSRPPNPDTKTASTSESENPAIPSPKPKSGAPLRNQDWWPNQIDVSRLHPHPPQGNPLGEDFDYAEEFAKLDVNALKADLTALMTQSQDWWPADYGHYGGLFIRMSWHSAGTYRIHDGRGGGGQGAQRFAPINSWPDNVSLDKARRLLWPIKQKYGNKISWADLLVFTGNVALESMGFKTFGFGFGREDIWEPEEILFGEEDEWLGTDKRYGGGEQRQLAEPYGATTMGLIYVNPEGPEGQPDPLAAAHDIRETFGRMAMNDEETAALIVGGHTFGKTHGAGDASLVGPEPEAAPIEQQGLGWKSSYGTGKGPD... | 1.11.1.21 | COFACTOR: Name=heme b; Xref=ChEBI:CHEBI:60344; Note=Binds 2 heme B (iron-protoporphyrin IX) groups per tetramer.; | cellular response to hydrogen peroxide [GO:0070301]; hydrogen peroxide catabolic process [GO:0042744] | cytosol [GO:0005829] | catalase activity [GO:0004096]; heme binding [GO:0020037]; metal ion binding [GO:0046872] | PF00141; | 1.10.520.10;1.10.420.10; | Peroxidase family, Peroxidase/catalase subfamily | PTM: Formation of the three residue Trp-Tyr-Met cross-link is important for the catalase, but not the peroxidase activity of the enzyme. {ECO:0000255|HAMAP-Rule:MF_01961}. | null | CATALYTIC ACTIVITY: Reaction=AH2 + H2O2 = A + 2 H2O; Xref=Rhea:RHEA:30275, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240, ChEBI:CHEBI:17499; EC=1.11.1.21; Evidence={ECO:0000255|HAMAP-Rule:MF_01961}; CATALYTIC ACTIVITY: Reaction=2 H2O2 = 2 H2O + O2; Xref=Rhea:RHEA:20309, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, C... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.4 mM for H(2)O(2) for the catalase reaction {ECO:0000269|PubMed:7673210}; KM=0.19 mM for o-dianisidine for the peroxidase reaction {ECO:0000269|PubMed:7673210}; KM=0.17 mM for NADPH for the peroxidase reaction {ECO:0000269|PubMed:7673210}; KM=0.23 mM for NADH for... | null | null | null | FUNCTION: Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity. May play a role in the intracellular survival of mycobacteria. | Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) |
A0QYC2 | DTHD_MYCS2 | MTQAQELSVDFDFRLDGKVALVTGAASGIGAAIASAYATKGARIAAVDLNAEGAEALAAQLGGDRGAHRGFACDVADAASVQAAADAVAAEFGRIDILVNSAGVARLAPAEELSLQDWDSTLAINLSGTFLMCQAVGKRMLEAGGGAIVNMASQAATVALDQHVAYCASKFGVVGVSKVLAAEWGGRGVRVNTISPTVVLTELGHKAWDGPRGDALKKLIPTGRFAYPDEIAAAAVFLASDAAAMINGADLVIDGGYTIK | 1.1.1.403 | null | carbohydrate catabolic process [GO:0016052]; carbohydrate utilization [GO:0009758]; cellular response to carbohydrate stimulus [GO:0071322] | null | carbohydrate binding [GO:0030246]; erythrulose reductase activity [GO:0047880] | PF13561; | 3.40.50.720; | Short-chain dehydrogenases/reductases (SDR) family | null | null | CATALYTIC ACTIVITY: Reaction=D-threitol + NAD(+) = D-erythrulose + H(+) + NADH; Xref=Rhea:RHEA:48748, ChEBI:CHEBI:15378, ChEBI:CHEBI:16023, ChEBI:CHEBI:48300, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.403; Evidence={ECO:0000269|PubMed:26560079}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.52 mM for D-threitol {ECO:0000269|PubMed:26560079}; KM=1.2 mM for D-threose {ECO:0000269|PubMed:26560079}; KM=0.048 mM for D-erythrulose {ECO:0000269|PubMed:26560079}; Note=kcat is 6.97 sec(-1) with D-threitol as substrate. kcat is 0.71 sec(-1) with D-threose as ... | PATHWAY: Carbohydrate metabolism; D-threitol degradation. {ECO:0000269|PubMed:26560079}. | null | null | FUNCTION: Catalyzes the NAD-dependent reversible oxidation of D-threitol. Involved in the degradation pathway of D-threitol, that allows M.smegmatis to grow on this compound as the sole carbon source. Does not catalyze the oxidation of xylitol, L-sorbitol, and L-sorbose. {ECO:0000269|PubMed:26560079}. | Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) |
A0QYE8 | GUAB1_MYCS2 | MRFLDGHTPAYDLTYNDVFVVPGRSDVASRFDVDLSTVDGSGTTIPVVVANMTAVAGRRMAETVARRGGIVVLPQDLPITAVSETVDFVKSRDLVVDTPVTLSPEDSVSDANALLHKRAHGAAVVVFEGRPIGLVTEANCAGVDRFARVRDIALSDFVTAPVGTDPREVFDLLEHAPIDVAVMTAPDGTLAGVLTRTGAIRAGIYTPAVDAKGRLRIAAAVGINGDVGAKAQALAEAGADLLVIDTAHGHQAKMLDAIKAVASLDLGLPLVAGNVVSAEGTRDLIEAGASIVKVGVGPGAMCTTRMMTGVGRPQFSAVVE... | 1.7.1.7 | COFACTOR: Name=a monovalent cation; Xref=ChEBI:CHEBI:60242; Evidence={ECO:0000255|HAMAP-Rule:MF_02250, ECO:0000269|PubMed:35338694}; Note=Activity is highest with Rb(+), followed by K(+), NH4(+) and Cs(+). {ECO:0000269|PubMed:35338694}; | IMP salvage [GO:0032264]; purine ribonucleoside salvage [GO:0006166] | cytosol [GO:0005829] | GMP reductase activity [GO:0003920]; IMP dehydrogenase activity [GO:0003938] | PF00571;PF00478; | 3.20.20.70; | IMPDH/GMPR family, GuaB1 subfamily | null | null | CATALYTIC ACTIVITY: Reaction=IMP + NADP(+) + NH4(+) = GMP + 2 H(+) + NADPH; Xref=Rhea:RHEA:17185, ChEBI:CHEBI:15378, ChEBI:CHEBI:28938, ChEBI:CHEBI:57783, ChEBI:CHEBI:58053, ChEBI:CHEBI:58115, ChEBI:CHEBI:58349; EC=1.7.1.7; Evidence={ECO:0000255|HAMAP-Rule:MF_02250, ECO:0000269|PubMed:35338694}; PhysiologicalDirection=... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=30 uM for NADPH (at pH 7.8) {ECO:0000269|PubMed:35338694}; KM=63 uM for NADPH (at pH 6.6) {ECO:0000269|PubMed:35338694}; | PATHWAY: Purine metabolism; IMP biosynthesis via salvage pathway. {ECO:0000255|HAMAP-Rule:MF_02250, ECO:0000305|PubMed:35338694}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.4-7.8. {ECO:0000269|PubMed:35338694}; | null | FUNCTION: Involved in the purine-salvage pathway (PubMed:35338694). Catalyzes the NADPH-dependent conversion of GMP to IMP (PubMed:35338694). Is not essential for viability, but may contribute to the regulation of the purine nucleotide pool by recycling GMP to IMP (PubMed:35338694). {ECO:0000269|PubMed:35338694}. | Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) |
A0QYV1 | LYSX_MYCS2 | MTVISRVEHLPARPASRVAWVPAAAGWTVGVIATLSLIASVSPLVRSLIRVPREFVNDFIFNFPDTSFAWAFVLALLAAALAARKRIAWWVLVLYLVGAIGWNVGDLAAGGDTVADDIGELIGIAFHVAAIVFLVVARKEFWAKVRRGALLKSAAVLVAGNLIGIVVAWGLLQAFPGTLDPEWRLPYAVNRVSGFATVPTEVFEGYSHTFLNAIFGLFGALALMAAAIVLFQSQRASNALTGEDESAIRGLLELYGKNDSLGYFATRRDKSVVFAPNGRAAITYRVEVGVCLASGDPVGDPKSWPQAIAAWLQLCQAYGW... | 2.3.2.3; 6.1.1.6 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000250}; | diadenosine tetraphosphate biosynthetic process [GO:0015966]; lipid metabolic process [GO:0006629]; lysyl-tRNA aminoacylation [GO:0006430]; positive regulation of macrophage activation [GO:0043032]; response to antibiotic [GO:0046677] | aminoacyl-tRNA synthetase multienzyme complex [GO:0017101]; cytosol [GO:0005829]; extracellular space [GO:0005615]; plasma membrane [GO:0005886] | ATP adenylyltransferase activity [GO:0003877]; ATP binding [GO:0005524]; lysine-tRNA ligase activity [GO:0004824]; magnesium ion binding [GO:0000287]; phosphatidylglycerol lysyltransferase activity [GO:0050071]; tRNA binding [GO:0000049] | PF09924;PF00152;PF16995;PF01336; | 2.40.50.140; | LPG synthetase family; Class-II aminoacyl-tRNA synthetase family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=ATP + L-lysine + tRNA(Lys) = AMP + diphosphate + L-lysyl-tRNA(Lys); Xref=Rhea:RHEA:20792, Rhea:RHEA-COMP:9696, Rhea:RHEA-COMP:9697, ChEBI:CHEBI:30616, ChEBI:CHEBI:32551, ChEBI:CHEBI:33019, ChEBI:CHEBI:78442, ChEBI:CHEBI:78529, ChEBI:CHEBI:456215; EC=6.1.1.6; CATALYTIC ACTIVITY: Reaction=1,2... | null | null | null | null | FUNCTION: Catalyzes the production of L-lysyl-tRNA(Lys)transfer and the transfer of a lysyl group from L-lysyl-tRNA(Lys) to membrane-bound phosphatidylglycerol (PG), which produces lysylphosphatidylglycerol (LPG), one of the components of the bacterial membrane with a positive net charge. LPG synthesis contributes to t... | Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) |
A0QZ13 | LNT_MYCS2 | MIPAVTDDDPLEDPLDDDVAPGLDDAEPEPEPRDEHDEPSRPATGSRIGGWVARRGSRFGKGVLDRCAPLSAAIGGGLALWLSFPPIGWWFTAFPGLALLGWVLTRTATTKAGGFGYGVLFGLAFYVPLLPWISGLVGAVPWLALAFAESLFCGLFGLGAVVVVRLPGWPLWFATLWVAAEWAKSTFPFGGFPWGASSYGQTNGPLLALARIGGAPLVSFAVALIGFSLTLLTAQIVWWWRHGHKPGVPAPAVMLPGVAIAASLLVTALVWPQVRQSGTGAGDDTAVTVAAVQGNVPRLGLEFNAQRRAVLDNHVKETLR... | 2.3.1.269 | null | lipoprotein biosynthetic process [GO:0042158] | plasma membrane [GO:0005886] | N-acyltransferase activity [GO:0016410] | PF00795;PF20154; | 3.60.110.10; | CN hydrolase family, Apolipoprotein N-acyltransferase subfamily | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01148, ECO:0000269|PubMed:12427759}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01148, ECO:0000269|PubMed:12427759}. | CATALYTIC ACTIVITY: Reaction=a glycerophospholipid + N-terminal S-1,2-diacyl-sn-glyceryl-L-cysteinyl-[lipoprotein] = a 2-acyl-sn-glycero-3-phospholipid + H(+) + N-acyl-S-1,2-diacyl-sn-glyceryl-L-cysteinyl-[lipoprotein]; Xref=Rhea:RHEA:48228, Rhea:RHEA-COMP:14681, Rhea:RHEA-COMP:14684, ChEBI:CHEBI:15378, ChEBI:CHEBI:136... | null | PATHWAY: Protein modification; lipoprotein biosynthesis (N-acyl transfer). {ECO:0000255|HAMAP-Rule:MF_01148}. | null | null | FUNCTION: Catalyzes the phospholipid dependent N-acylation of the N-terminal cysteine of apolipoprotein, the last step in lipoprotein maturation. Can transfer a number of fatty acids (C16 and C19, palmitic and probably tuberculostearic acids respectively are shown) (PubMed:19661058). Enhances the polyprenol monophospho... | Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) |
A0QZ48 | PUP_MYCS2 | MAQEQTKRGGGGGEDDDLPGASAAGQERREKLTEETDDLLDEIDDVLEENAEDFVRAYVQKGGQ | null | null | modification-dependent protein catabolic process [GO:0019941]; proteasomal protein catabolic process [GO:0010498]; protein pupylation [GO:0070490] | null | proteasome binding [GO:0070628]; protein tag activity [GO:0031386] | PF05639; | null | Prokaryotic ubiquitin-like protein family | PTM: Is modified by deamidation of its C-terminal glutamine to glutamate probably by the deamidase Dop, a prerequisite to the subsequent pupylation process. {ECO:0000269|PubMed:19028679}. | null | null | null | PATHWAY: Protein degradation; proteasomal Pup-dependent pathway. | null | null | FUNCTION: Protein modifier that is covalently attached to lysine residues of substrate proteins, thereby targeting them for proteasomal degradation. The tagging system is termed pupylation. Among the identified substrates are the SodA and Ino1 proteins. {ECO:0000269|PubMed:19028679}. | Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) |
A0QZ49 | DOP_MYCS2 | MQRIIGTEVEYGISSPSDPTANPILTSTQAVLAYAAAAGIQRAKRTRWDYEVESPLRDARGFDLSRSSGPPPIVDADEVGAANMILTNGARLYVDHAHPEYSAPECTDPMDAVIWDKAGERVMEAAARHVASVPGAAKLQLYKNNVDGKGASYGSHENYLMSRQTPFSAVIAGLTPFMVSRQVVTGSGRVGIGPSGDEPGFQLSQRADYIEVEVGLETTLKRGIINTRDEPHADADKYRRLHVIIGDANLAETSTYLKLGTTSLVLDLIEEGVDLSDLALARPVHAVHVISRDPSLRATVALADGRELTALALQRIYLDR... | 3.4.-.-; 3.5.1.119 | COFACTOR: Name=ATP; Xref=ChEBI:CHEBI:30616; Evidence={ECO:0000269|PubMed:20025664}; Note=ATP is required for the deamidation reaction but is not hydrolyzed during this reaction. {ECO:0000269|PubMed:20025664}; | modification-dependent protein catabolic process [GO:0019941]; proteasomal protein catabolic process [GO:0010498]; protein pupylation [GO:0070490] | null | ATP binding [GO:0005524]; hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides [GO:0016811]; metal ion binding [GO:0046872]; peptidase activity [GO:0008233] | PF03136; | null | Pup ligase/Pup deamidase family, Pup deamidase subfamily | null | null | CATALYTIC ACTIVITY: Reaction=[prokaryotic ubiquitin-like protein]-C-terminal-L-glutamine + H2O = [prokaryotic ubiquitin-like protein]-C-terminal-L-glutamate + NH4(+); Xref=Rhea:RHEA:47952, Rhea:RHEA-COMP:11959, Rhea:RHEA-COMP:11960, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938, ChEBI:CHEBI:78525, ChEBI:CHEBI:88115; EC=3.5.1.11... | null | PATHWAY: Protein degradation; proteasomal Pup-dependent pathway. | null | null | FUNCTION: Specifically catalyzes the deamidation of the C-terminal glutamine of the prokaryotic ubiquitin-like protein Pup to glutamate, thereby rendering Pup competent for conjugation. Probably also displays depupylase (DPUP) activity, removing conjugated Pup from target proteins; thus may be involved in the recycling... | Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) |
A0QZY0 | MSHC_MYCS2 | MQSWSAPAIPVVPGRGPALRLFDSADRQVRPVTPGPTATMYVCGITPYDATHLGHAATYLTFDLVHRLWLDAGHTVQYVQNVTDVDDPLFERAERDGIDWRTLGDRETQLFREDMAALRVLPPHDYVAATDAIAEVVEMVEKLLASGAAYIVEDAEYPDVYFRADATAQFGYESGYDRDTMLTLFAERGGDPDRPGKSDQLDALLWRAERPGEPSWPSPFGRGRPGWHVECSAIALTRIGTGLDIQGGGSDLIFPHHEYSAAHAESVTGERRFARHYVHTGMIGWDGHKMSKSRGNLVLVSQLRAQGVDPSAIRLGLFSG... | 6.3.1.13 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Note=Binds 1 zinc ion per subunit.; | cysteinyl-tRNA aminoacylation [GO:0006423]; mycothiol biosynthetic process [GO:0010125] | cytoplasm [GO:0005737] | ATP binding [GO:0005524]; cysteine-glucosaminylinositol ligase activity [GO:0035446]; cysteine-tRNA ligase activity [GO:0004817]; zinc ion binding [GO:0008270] | PF01406; | 1.20.120.640;3.40.50.620; | Class-I aminoacyl-tRNA synthetase family, MshC subfamily | null | null | CATALYTIC ACTIVITY: Reaction=1D-myo-inositol 2-amino-2-deoxy-alpha-D-glucopyranoside + ATP + L-cysteine = 1D-myo-inositol 2-(L-cysteinylamino)-2-deoxy-alpha-D-glucopyranoside + AMP + diphosphate + H(+); Xref=Rhea:RHEA:26176, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:35235, ChEBI:CHEBI:58886, ... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=40 uM for L-cysteine {ECO:0000269|PubMed:12033919, ECO:0000269|PubMed:17848100}; KM=72 uM for GlcN-Ins {ECO:0000269|PubMed:12033919, ECO:0000269|PubMed:17848100}; KM=1.84 mM for ATP {ECO:0000269|PubMed:12033919, ECO:0000269|PubMed:17848100}; Vmax=83 nmol/min/mg enz... | null | null | null | FUNCTION: Catalyzes the ATP-dependent condensation of GlcN-Ins and L-cysteine to form L-Cys-GlcN-Ins. | Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) |
A0R066 | ILVE_MYCS2 | MNSGPLEFTVSANTNPATDAVRESILANPGFGKYYTDHMVSIDYTVDEGWHNAQVIPYGPIQLDPSAIVLHYGQEIFEGLKAYRWADGSIVSFRPEANAARLQSSARRLAIPELPEEVFIESLRQLIAVDEKWVPPAGGEESLYLRPFVIATEPGLGVRPSNEYRYLLIASPAGAYFKGGIKPVSVWLSHEYVRASPGGTGAAKFGGNYAASLLAQAQAAEMGCDQVVWLDAIERRYVEEMGGMNLFFVFGSGGSARLVTPELSGSLLPGITRDSLLQLATDAGFAVEERKIDVDEWQKKAGAGEITEVFACGTAAVITP... | 2.6.1.42 | COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000269|PubMed:20445230}; | amino acid biosynthetic process [GO:0008652]; branched-chain amino acid metabolic process [GO:0009081]; isoleucine biosynthetic process [GO:0009097]; leucine biosynthetic process [GO:0009098]; protein-pyridoxal-5-phosphate linkage via peptidyl-N6-pyridoxal phosphate-L-lysine [GO:0018272]; valine biosynthetic process [G... | null | branched-chain-amino-acid transaminase activity [GO:0004084]; 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]; pyridoxal phosphate binding [GO:0030170] | PF01063; | 3.30.470.10;3.20.10.10; | Class-IV pyridoxal-phosphate-dependent aminotransferase family | null | null | CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-isoleucine = (S)-3-methyl-2-oxopentanoate + L-glutamate; Xref=Rhea:RHEA:24801, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:35146, ChEBI:CHEBI:58045; EC=2.6.1.42; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-valine = 3-methyl-2-oxobutanoate + L-glutamate; Xref=Rhe... | null | PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 4/4.; PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 4/4.; PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine from pyruvate: step 4/4. | null | null | FUNCTION: Catalyzes the reversible transfers of an amino group from glutamate to the alpha-ketoacid of the respective amino acid in the final step in the biosynthesis of branchedchain amino acids. The amino acids can be ranked in the following order with respect to their efficiency as amino donor: Leu > Ile > Val. {ECO... | Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) |
A0R0S4 | DPDS_MYCS2 | MATTRGKKTYPQLPPAPDDYPTFPDKSTWPVVFPEIPAGTNGRFARPPQHTSKAAAPKIPADQVPNHVAVVMDGNGRWATQRGLGRTEGHKMGEAVLIDITCGAIEIGIKHLTVYAFSTENWKRSTEEVRFLMGFNREVVRRRRENLNDMGVRMRWVGSRPRMWRSVIKEFDIAEQMTVDNDVITINYCVNYGGRTEIVEAARALAQEAVDGKINPARISEAMFAKHLHRADIPDVDLFIRTSGEQRASNFLLWQAAYAEYVFQDKLWPDYDRRDLWAACEEYVNRNRRFGRA | 2.5.1.86; 2.5.1.87 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Binds 2 magnesium ions per subunit. {ECO:0000250}; | polyprenol biosynthetic process [GO:0016094] | cytosol [GO:0005829]; plasma membrane [GO:0005886] | dehydrodolichyl diphosphate synthase activity [GO:0045547]; di-trans,poly-cis-undecaprenyl-diphosphate synthase activity [GO:0008834]; magnesium ion binding [GO:0000287]; manganese ion binding [GO:0030145]; polyprenyltransferase activity [GO:0002094]; Z-farnesyl diphosphate synthase activity [GO:0033850] | PF01255; | 3.40.1180.10; | UPP synthase family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11004176}. | CATALYTIC ACTIVITY: Reaction=(2Z,6E)-farnesyl diphosphate + 7 isopentenyl diphosphate = (2Z,6Z,10Z,14Z,18Z,22Z,26Z,30Z,34E)-decaprenyl diphosphate + 7 diphosphate; Xref=Rhea:RHEA:47096, ChEBI:CHEBI:33019, ChEBI:CHEBI:87356, ChEBI:CHEBI:128769, ChEBI:CHEBI:162247; EC=2.5.1.86; CATALYTIC ACTIVITY: Reaction=(2E,6E)-farnes... | null | null | null | null | FUNCTION: Catalyzes the sequential condensation of isopentenyl diphosphate (IPP) in the cis configuration with (2Z,6E)-farnesyl diphosphate (Z-FPP or EZ-FPP) generating the 50 carbon product trans,polycis-decaprenyl diphosphate. When (2E,6E)-farnesyl diphosphate (E-FPP or EE-FPP) is used in vitro, both primary products... | Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) |
A0R0S7 | ERA_MYCS2 | MTEFRSGFVCFVGRPNTGKSTLTNALVGQKVAITSNRPQTTRHTIRGIVHREDFQIILVDTPGLHRPRTLLGQRLNDLVKDTYSEVDVIGMCIPADEAIGPGDRWIYQQIRAVAPRTTLIGIVTKIDKVPKDRVAAQLLAVSELMGPDAEIVPVSATSGEQLDVLTNVLVSQLPPGPAYYPDGELTDEPEEVLMAELIREAALEGVRDELPHSLAVVIDEVSQREDRDDLIDVHAILYVERDSQKGIVIGKGGARLREVGTAARKQIEKLLGTKVYLDLRVKIAKNWQRDPKQLGKLGF | null | null | ribosomal small subunit assembly [GO:0000028] | cytosol [GO:0005829]; envelope [GO:0031975]; extracellular region [GO:0005576] | GTP binding [GO:0005525]; GTPase activity [GO:0003924]; ribosomal small subunit binding [GO:0043024]; rRNA binding [GO:0019843] | PF07650;PF01926; | 3.30.300.20;3.40.50.300; | TRAFAC class TrmE-Era-EngA-EngB-Septin-like GTPase superfamily, Era GTPase family | null | SUBCELLULAR LOCATION: Cell envelope {ECO:0000255|HAMAP-Rule:MF_00367}. Secreted, cell wall {ECO:0000255|HAMAP-Rule:MF_00367}. | null | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=285 uM for GTP {ECO:0000269|PubMed:35917161}; | null | null | null | FUNCTION: Exhibits GTPase activity (PubMed:35917161). Binds RNA but is probably not involved in ribosome assembly in mycobacteria (PubMed:35917161). Cannot use ATP (PubMed:35917161). {ECO:0000269|PubMed:35917161}. | Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) |
A0R152 | RNE_MYCS2 | MAEDAHTEDLSTQTPQQEGLPERLRVHSLARVLGTTSRRVLDALAEFDGRQRSAHSTVDKADAERVRAALTESPAAETPPEEAPAAETPVADLVVVQAEQVEVVTVSEAGPAEPAEPAEPEAPAAEAEAEAETEVADEAETPEPTFRGAVLVGDEPESRLILEHANIPPARETQTERPDYLPLFVAPQPVSFEPAVVDDEDEDDDTETGAESDFDSGADSDSDDDQADRPRRRRRGRRGRGRGRGEQNDDATSDADTDSTEDQTDGDEQESGEDSDDSGDEDSTTTEGGTRRRRRRRRRKSGSGDSDDAVSPDDPPNTVV... | 3.1.26.12 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P21513}; Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250|UniProtKB:P21513}; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:P21513}; Note=Binds 2 Zn(2+) ions per homotetramer. Zinc ions are bound between subu... | mRNA processing [GO:0006397]; rRNA processing [GO:0006364]; tRNA processing [GO:0008033] | cytoplasm [GO:0005737] | metal ion binding [GO:0046872]; RNA nuclease activity [GO:0004540]; rRNA binding [GO:0019843]; tRNA binding [GO:0000049] | PF10150; | 1.10.10.2480;2.40.50.140; | RNase E/G family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:35521527}. Note=Has dynamic expression patterns, often present as foci near the mid-cell or new cell pole in addition to a weaker overall cytoplasmic distribution. Colocalizes with HupB (PubMed:35521527). {ECO:0000269|PubMed:35521527}. | CATALYTIC ACTIVITY: Reaction=Endonucleolytic cleavage of single-stranded RNA in A- and U-rich regions.; EC=3.1.26.12; | null | null | null | null | FUNCTION: Endoribonuclease that plays a central role in RNA processing and decay. Plays a major role in pre-16S rRNA maturation, probably generating the mature 5'-end, and a minor role in pre-5S and pre-23S rRNA maturation (PubMed:22014150). Probably also processes tRNA (By similarity). RNase E and HupB jointly contrib... | Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) |
A0R1E8 | PKS5_MYCS2 | MTQNCVAPVAIIGMACRLPGAINSPQQLWEALLRGDDFVTEIPTGRWDAEEYYDPEPGVPGRSVSKWGAFLDDPAAFDPEFFGITEREAAAIDPQHRLLLETAWEAVEHSGLNPAGLAGSATGVFMGLTHNDYAHLAADAKALEGPYGFTGTSFSLASGRIAYALGVHGPAITVDTACSSSLSAIHMACRSLHDGESDVALAGGVSVLLEPRKAAGGSAAGMLSPTGHCHAFDTAADGFVSAEGCVVLTLKRLDDAVADGDRILAVIRGTATNQDGRTVNIATPSADAQAKVYRMALKAAGVEPGTVGLVEAHGTGTPVG... | 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]; oxidoreductase activity [GO:0016491]; phosphopantetheine binding [GO:0031177] | PF00698;PF08240;PF13602;PF16197;PF00109;PF02801;PF08659;PF21089;PF00550;PF14765; | 3.40.47.10;1.10.1200.10;3.30.70.250;3.40.366.10;3.90.180.10;3.40.50.720;3.10.129.110; | null | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE-ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE-ProRule:PRU00303}. | null | null | PATHWAY: Lipid metabolism; fatty acid biosynthesis. {ECO:0000269|PubMed:19181796}. | null | null | FUNCTION: Polyketide synthase involved in the biosynthesis of 2,4-dimethyl-2-eicosenoic acid, a lipid component of the lipooligosaccharides (LOS) which are not located at the bacterial surface but rather in deeper compartments of the cell envelope of M.smegmatis. {ECO:0000269|PubMed:19181796}. | Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) |
A0R2B1 | KGD_MYCS2 | MSSSPSPFGQNEWLVEEMYRKFRDDPSSVDPSWHEFLVDYSPEPTTDSASNGRTTTAAPVTPPTPAPAPAPEPKAAPKPAAKTEAKPAKPAKSATPAKGDESQILRGAAAAVVKNMNASLEVPTATSVRAIPAKLMIDNRVVINNHLKRTRGGKISFTHLLGYAIVQAVKKFPNMNRHFAVVDGKPTAITPAHTNLGLAIDLQGKDGNRSLVVAAIKRCETMRFGQFIAAYEDIVRRARDGKLTAEDFSGVTISLTNPGTLGTVHSVPRLMQGQGAIIGAGAMEYPAEFQGASEERIADLGIGKLITLTSTYDHRIIQGA... | 1.2.4.2; 2.2.1.5; 2.3.1.61; 4.1.1.71 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:21867916}; COFACTOR: Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937; Evidence={ECO:0000269|PubMed:21867916}; | tricarboxylic acid cycle [GO:0006099] | cytosol [GO:0005829]; oxoglutarate dehydrogenase complex [GO:0045252] | 2-hydroxy-3-oxoadipate synthase activity [GO:0050439]; 2-oxoglutarate decarboxylase activity [GO:0008683]; dihydrolipoyllysine-residue succinyltransferase activity [GO:0004149]; magnesium ion binding [GO:0000287]; oxoglutarate dehydrogenase (succinyl-transferring) activity [GO:0004591]; thiamine pyrophosphate binding [... | PF00198;PF16078;PF00676;PF16870;PF02779; | 3.40.50.12470;3.40.50.970;3.30.559.10;3.40.50.11610;1.10.287.1150; | 2-oxoacid dehydrogenase family, Kgd subfamily | null | null | CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + glyoxylate + H(+) = 2-hydroxy-3-oxoadipate + CO2; Xref=Rhea:RHEA:14341, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:36655, ChEBI:CHEBI:57712; EC=2.2.1.5; Evidence={ECO:0000269|PubMed:21867916}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + H(+) = CO... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.54 mM for alpha-ketoglutarate {ECO:0000269|PubMed:19019160}; | PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; succinate from 2-oxoglutarate (transferase route): step 1/2. {ECO:0000269|PubMed:21867916}.; PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; succinyl-CoA from 2-oxoglutarate (dehydrogenase route): step 1/1. {ECO:0000269|PubMed:21867916}. | null | null | FUNCTION: Shows three enzymatic activities that share a first common step, the attack of thiamine-PP on 2-oxoglutarate (alpha-ketoglutarate, KG), leading to the formation of an enamine-thiamine-PP intermediate upon decarboxylation. Thus, displays KGD activity, catalyzing the decarboxylation from five-carbon 2-oxoglutar... | Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) |
A0R2E6 | GPGS_MYCS2 | MGHRWLTDHSWNRPSWTVADLEAAKAGRTVSVVLPALNEEETVGSVVETIKPLLGGLVDELIVLDSGSTDETEIRAVAAGAKVVSREAALPEVPPQPGKGEVLWRSLAATTGDIIAFVDSDLIDPDPMFVPKLLGPLLTCDGVHLVKGFYRRPLKVSGAEDANGGGRVTELVARPLLASLRPELNCVLQPLGGEYAGTRELLTSVPFAPGYGVEIGLLVDTYDRLGLDGIAQVNLGVRAHRNRPLTELASMSRQVIATLLSRCGISDSGVGLTQFFADGDDFTPRVSSVSLADRPPMTTLRPR | 2.4.1.266 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:18221489}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:P9WMW9}; Note=Requires divalent cations for activity. The maximum activity is observed at 20 mM of MgCl(2). {ECO:0000269|PubMed:18221489}; | null | null | glycosyltransferase activity [GO:0016757]; metal ion binding [GO:0046872] | PF00535; | null | Glycosyltransferase 2 family | null | null | CATALYTIC ACTIVITY: Reaction=(2R)-3-phosphoglycerate + an NDP-alpha-D-glucose = (2R)-2-O-(alpha-D-glucopyranosyl)-3-phospho-glycerate + a ribonucleoside 5'-diphosphate + H(+); Xref=Rhea:RHEA:47244, ChEBI:CHEBI:15378, ChEBI:CHEBI:57930, ChEBI:CHEBI:58272, ChEBI:CHEBI:62600, ChEBI:CHEBI:76533; EC=2.4.1.266; Evidence={ECO... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.24 mM for 3-PGA (at 37 degrees Celsius) {ECO:0000269|PubMed:18221489}; KM=1.28 mM for UDP-glucose (at 37 degrees Celsius) {ECO:0000269|PubMed:18221489}; KM=6.08 mM for ADP-glucose (at 37 degrees Celsius) {ECO:0000269|PubMed:18221489}; KM=32.04 mM for GDP-glucose ... | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8. {ECO:0000269|PubMed:18221489}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 45 degrees Celsius. The activity is undetectable below 20 and above 55 degrees Celsius. {ECO:0000269|PubMed:18221489}; | FUNCTION: Involved in the biosynthesis of 6-O-methylglucose lipopolysaccarides (MGLPs) (PubMed:18221489, PubMed:19421329). Catalyzes the transfer of the glucose moiety from a nuleotide sugar such as UDP-alpha-D-glucose to the position 2 of 3-phospho-D-glycerate (3-PGA) to form glucosyl-3-phosphoglycerate (GPG). It can ... | Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) |
A0R2K8 | PIME_MYCS2 | MRVNGYRGAKVGAVDTTSPPEVPASARLQRLAPMLLVVSILARLAWTYLVPNGANFVDLHVYVGGADALDGPGALYDYVYADQTPDFPLPFTYPPFAAIVFYPLHLLPFGVVAFIWQIGIIAALYGVVRVSQRLMGLQSQRRVAMLWTALGIWTEPLRSTFDYGQVNVVLVLAVLCAVSTTRWWLSGLLVGLAAGIKLTPAVAGLYFLGARRWAAVACSAAVFFATVGVSWLVVGAQARRYFTELLGDADRIGPIGTSFNQSWRGGISRILGHDAGFGPLVLIGIGITAVLALLAWRAIGGAQDRLGGILVVSLFGLVLS... | 2.4.1.- | null | glycolipid biosynthetic process [GO:0009247]; phosphatidylinositol metabolic process [GO:0046488]; phospholipid biosynthetic process [GO:0008654] | plasma membrane [GO:0005886] | GDP-Man:Man3GlcNAc2-PP-Dol alpha-1,2-mannosyltransferase activity [GO:0004377]; phosphatidylinositol alpha-mannosyltransferase activity [GO:0043750] | PF09594; | null | Glycosyltransferase 87 family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16803893}; Multi-pass membrane protein {ECO:0000255}. Note=Localizes in the plasma membrane-cell wall (PM-CW) fraction. {ECO:0000269|PubMed:16803893}. | null | null | PATHWAY: Phospholipid metabolism; phosphatidylinositol metabolism. {ECO:0000269|PubMed:16803893}. | null | null | FUNCTION: Catalyzes the alpha-1,2 addition of a mannose residue from polyprenol-phosphate-mannose (PPM) to a monoacyl phosphatidylinositol tetramannoside (AcPIM4) to generate a monoacyl phosphatidylinositol pentamannoside (AcPIM5). {ECO:0000269|PubMed:16803893}. | Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) |
A0R2N3 | NDP_MYCS2 | MQVTVLSGAGISAESGVPTFRDAETGLWAQVDPYEISSTDGWQRNPEKVWAWYLWRHYMMARVAPNEAHRTVAAWEDHLDVRVVTQNIDDLHERAGSTNVYHLHGSLFEFRCDACGSAFEGNLPEMPEPVETIDPPVCPCSGLIRPSVVWFGEPLPDAAWNRSVLAVSSADVVIVVGTSSIVYPAAGLPEAALAAGKPVIEVNPERTPLSDSATVSLRETASEALPTLLQRLPELLNRSA | 2.3.1.286 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|HAMAP-Rule:MF_01121}; Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01121}; | cellular response to ionizing radiation [GO:0071479]; double-strand break repair via nonhomologous end joining [GO:0006303] | cytoplasm [GO:0005737] | NAD+ binding [GO:0070403]; NAD-dependent histone deacetylase activity [GO:0017136]; protein-malonyllysine demalonylase activity [GO:0036054]; protein-succinyllysine desuccinylase activity [GO:0036055]; transferase activity [GO:0016740]; zinc ion binding [GO:0008270] | PF02146; | 3.30.1600.10;3.40.50.1220; | Sirtuin family, Class III subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01121}. | CATALYTIC ACTIVITY: Reaction=H2O + N(6)-succinyl-L-lysyl-[protein] + NAD(+) = 2''-O-succinyl-ADP-D-ribose + L-lysyl-[protein] + nicotinamide; Xref=Rhea:RHEA:47668, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:11877, ChEBI:CHEBI:15377, ChEBI:CHEBI:17154, ChEBI:CHEBI:29969, ChEBI:CHEBI:57540, ChEBI:CHEBI:87830, ChEBI:CHEBI:87832;... | null | null | null | null | FUNCTION: NAD-dependent lysine deacetylase and desuccinylase that specifically removes acetyl and succinyl groups on target proteins. Modulates the activities of several proteins which are inactive in their acylated form. {ECO:0000255|HAMAP-Rule:MF_01121}.; FUNCTION: Involved in non-homologous end joining (NHEJ) repair... | Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) |
A0R3C4 | MAZG_MYCS2 | MIVVLVDPRRPALVPVDAVEFLTGDVQYTEEMPVKVPWSLPSARPAYDGEDAPVLLSSDPEHPVVKARLAAGDRLIAAPEPQPGERLVDAVALMDKLRTSGPWESEQTHDSLRRYLLEETYELFDAVRSGNADELREELGDVLLQVLFHARIAEDAPHHPFSIDDVADALVRKLGNRVPAVLAGESISLDEQLAQWEERKAQEKKVKARASSMDDVPTGQPALALAQKVLARVSQAGLPAELIPASLTSVSVSADTDSENELRTAVLEFMDTVREVEAAVAAGRRGEDVPEELDVAPLGVISEDEWRAYWPGAESSASEA... | 3.6.1.8 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; | dATP catabolic process [GO:0046061]; dGTP catabolic process [GO:0006203]; dTTP catabolic process [GO:0046076]; dUTP catabolic process [GO:0046081]; TTP catabolic process [GO:0046047]; UTP catabolic process [GO:0046052] | null | ATP binding [GO:0005524]; ATP diphosphatase activity [GO:0047693]; metal ion binding [GO:0046872] | PF03819; | 1.10.287.1080; | Nucleoside triphosphate pyrophosphohydrolase family | null | null | CATALYTIC ACTIVITY: Reaction=ATP + H2O = AMP + diphosphate + H(+); Xref=Rhea:RHEA:14245, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:456215; EC=3.6.1.8; Evidence={ECO:0000269|PubMed:20529853}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.16 mM for 8-oxo-dGTP (at pH 9.6 and at 37 degrees Celsius in the presence of 5 mM magnesium) {ECO:0000269|PubMed:20529853}; KM=0.9 mM for GTP (at pH 9.6 and at 37 degrees Celsius in the presence of 5 mM magnesium) {ECO:0000269|PubMed:20529853}; Vmax=0.16 nmol/min... | null | null | null | FUNCTION: Required to maintain the full capacity of the mycobacteria to respond to oxidative stress via the degradation of the oxidation-induced damaged nucleotides. It hydrolyzes all canonical (d)NTPs, as well as the mutagenic dUTP and 8-oxo-7,8-dihydro-2'-deoxyguanosine 5'-triphosphate (8-oxo-dGTP). Also involved in ... | Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) |
A0R3F9 | PAT_MYCS2 | MAELTEVRAADLAALEFFTGCRPSALEPLATQLRPLKAEPGQVLIRQGDPALTFMLIESGRVQVSHAVADGPPIVLDIEPGLIIGEIALLRDAPRTATVVAAEPVIGWVGDRDAFDTILHLPGMFDRLVRIARQRLAAFITPIPVQVRTGEWFYLRPVLPGDVERTLNGPVEFSSETLYRRFQSVRKPTRALLEYLFEVDYADHFVWVMTEGALGPVIADARFVREGHNATMAEVAFTVGDDYQGRGIGSFLMGALIVSANYVGVQRFNARVLTDNMAMRKIMDRLGAVWVREDLGVVMTEVDVPPVDTVPFEPELIDQI... | 2.3.1.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; | cGMP-mediated signaling [GO:0019934] | null | 3',5'-cyclic-GMP phosphodiesterase activity [GO:0047555]; metal ion binding [GO:0046872]; N-acetyltransferase activity [GO:0008080] | PF13302;PF00027; | 3.40.630.30;2.60.120.10; | null | null | null | null | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=3.1 uM for acetyl-CoA (with ACS as substrate) {ECO:0000269|PubMed:20507997, ECO:0000269|PubMed:21627103}; KM=10 uM for acetyl-CoA (with USP as substrate) {ECO:0000269|PubMed:20507997, ECO:0000269|PubMed:21627103}; KM=10.2 uM for ACS {ECO:0000269|PubMed:20507997, EC... | null | null | null | FUNCTION: Catalyzes specifically the acetylation of the epsilon-amino group of a highly conserved lysine residue in acetyl-CoA synthetase (ACS) and of the universal stress protein (USP) MSMEG_4207. Acetylation results in the inactivation of ACS activity and could be important for mycobacteria to adjust to environmental... | Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) |
A0R3R7 | LIGD_MYCS2 | MARHPWGMERYERVRLTNPDKVLYPATGTTKAEVFDYYLSIAQVMVPHIAGRPVTRKRWPNGVAEEAFFEKQLASSAPSWLERGSITHKSGTTTYPIINTREGLAWVAQQASLEVHVPQWRFEDGDQGPATRIVFDLDPGEGVTMTQLCEIAHEVRALMTDLDLETYPLTSGSKGLHLYVPLAEPISSRGASVLARRVAQQLEQAMPKLVTATMTKSLRAGKVFLDWSQNNAAKTTIAPYSLRGRDHPTVAAPRTWDEIADPELRHLRFDEVLDRLDEYGDLLAPLDADAPIADKLTTYRSMRDASKTPEPVPKEIPKTG... | 6.5.1.1 | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; Note=Binds 4 Mn(2+); 2 Mn(2+) for polymerase/primase activity, 1 each for 3-phosphoesterase and ligase. {ECO:0000250}; | DNA recombination [GO:0006310]; double-strand break repair via nonhomologous end joining [GO:0006303] | null | ATP binding [GO:0005524]; DNA binding [GO:0003677]; DNA ligase (ATP) activity [GO:0003910]; DNA-directed DNA polymerase activity [GO:0003887]; exonuclease activity [GO:0004527]; metal ion binding [GO:0046872] | PF04679;PF01068;PF13298;PF21686; | 3.30.1490.70;3.30.470.30;3.90.920.10;2.40.50.140; | LigD polymerase family; LigD 3'-phosphoesterase family; ATP-dependent DNA ligase family | null | null | CATALYTIC ACTIVITY: Reaction=ATP + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + diphosphate.; EC=6.5.1.1; | null | null | null | null | FUNCTION: With Ku forms a non-homologous end joining (NHEJ) repair enzyme which repairs blunt-end and 5'-overhang DNA double strand breaks (DSB) with about 50% fidelity, and DSB with non-complementary 3' ends. Plays a partial role in NHEJ during 3'-overhang repair. NHEJ repairs DSB with blunt ends and 5' overhangs with... | Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) |
A0R4M9 | OTSA_MYCS2 | MSPESGHETISGTSDFVVVANRLPVDLERLPDGTTRWKRSPGGLVTALEPLLRKRRGSWIGWAGVADSDEEPIVQDGLQLHPVRLSADDVAKYYEGFSNATLWPLYHDLIVKPEYHREWWDRYVEVNRRFAEATARAAAEGATVWIQDYQLQLVPKMLRMLRPDVTIGFFLHIPFPPVELFMQMPWRTEIVEGLLGADLVGFHLPGGAQNFLVLSRRLVGANTSRASIGVRSRFGEVQVGFRTVKVGAFPISIDSAELDGKARNRAIRQRARQIRAELGNPRKIMLGVDRLDYTKGIDVRLRALSELLEEKRIKRDDTVL... | 2.4.1.15; 2.4.1.347 | null | cellular response to heat [GO:0034605]; trehalose biosynthetic process [GO:0005992]; trehalose metabolism in response to stress [GO:0070413] | alpha,alpha-trehalose-phosphate synthase complex (UDP-forming) [GO:0005946]; cytosol [GO:0005829] | alpha,alpha-trehalose-phosphate synthase (GDP-forming) activity [GO:0047260]; alpha,alpha-trehalose-phosphate synthase (UDP-forming) activity [GO:0003825]; trehalose-phosphatase activity [GO:0004805] | PF00982; | 3.40.50.2000; | Glycosyltransferase 20 family | null | null | CATALYTIC ACTIVITY: Reaction=ADP-alpha-D-glucose + D-glucose 6-phosphate = ADP + alpha,alpha-trehalose 6-phosphate + H(+); Xref=Rhea:RHEA:53880, ChEBI:CHEBI:15378, ChEBI:CHEBI:57498, ChEBI:CHEBI:58429, ChEBI:CHEBI:61548, ChEBI:CHEBI:456216; EC=2.4.1.347; Evidence={ECO:0000269|Ref.4}; CATALYTIC ACTIVITY: Reaction=CDP-al... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=40 uM for UDP-Glc (in the presence of polyanion) {ECO:0000269|Ref.4}; KM=1 mM for Glc-6-P (with UDP-Glc in the presence of polyanion) {ECO:0000269|Ref.4}; KM=2 mM for Glc-6-P (with GDP-Glc in the presence of polyanion) {ECO:0000269|Ref.4}; | PATHWAY: Glycan biosynthesis; trehalose biosynthesis. {ECO:0000305}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7. {ECO:0000269|Ref.4}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: About 60% of the activity is lost in the absence of FII after 10 minutes at 40 degrees Celsius, but only 35% in the presence of FII. {ECO:0000269|Ref.4}; | FUNCTION: Involved in the production of glycogen and alpha-glucan via the TreS-Pep2 branch involved in the biosynthesis of maltose-1-phosphate (M1P), and probably in the osmoprotection via the biosynthesis of trehalose (PubMed:27513637, Ref.4). Catalyzes the transfer of glucose from UDP-glucose (UDP-Glc) to glucose-6-p... | Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) |
A0R4Q6 | CP142_MYCS2 | MTQMLTRPDVDLVNGMFYADGGAREAYRWMRANEPVFRDRNGLAAATTYQAVLDAERNPELFSSTGGIRPDQPGMPYMIDMDDPQHLLRRKLVNAGFTRKRVMDKVDSIGRLCDTLIDAVCERGECDFVRDIAAPLPMAVIGDMLGVLPTERDMLLKWSDDLVCGLSSHVDEAAIQKLMDTFAAYTEFTKDVITKRRAEPTDDLFSVLVNSEVEGQRMSDDEIVFETLLILIGGDETTRHTLSGGTEQLLRHRDQWDALVADVDLLPGAIEEMLRWTSPVKNMCRTLTADTVFHGTELRAGEKIMLMFESANFDESVFGD... | 1.14.15.28 | COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000269|PubMed:23489718, ECO:0000269|PubMed:25210044}; | cholesterol catabolic process [GO:0006707] | null | cholest-4-en-3-one 26-monooxygenase activity [GO:0036199]; heme binding [GO:0020037]; iron ion binding [GO:0005506]; steroid hydroxylase activity [GO:0008395] | PF00067; | 1.10.630.10; | Cytochrome P450 family | null | null | CATALYTIC ACTIVITY: Reaction=cholest-4-en-3-one + 5 H(+) + 3 O2 + 6 reduced [2Fe-2S]-[ferredoxin] = (25R)-3-oxocholest-4-en-26-oate + 4 H2O + 6 oxidized [2Fe-2S]-[ferredoxin]; Xref=Rhea:RHEA:49996, Rhea:RHEA-COMP:10000, Rhea:RHEA-COMP:10001, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16175, Ch... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=10.3 uM for cholest-4-en-3-one {ECO:0000269|PubMed:23489718}; KM=39.8 uM for cholesteryl sulfate {ECO:0000269|PubMed:25210044}; | PATHWAY: Steroid metabolism; cholesterol degradation. {ECO:0000303|PubMed:23489718}. | null | null | FUNCTION: Involved in the utilization of cholesterol as the sole carbon and energy source by degrading the side chain. Primarily catalyzes the sequential oxidation of the terminal methyl of cholest-4-en-3-one into (25R)-26-hydroxycholest-4-en-3-one (alcohol), (25R)-26-oxocholest-4-en-3-one (aldehyde), to finally yield ... | Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) |
A0R4Y3 | CP125_MYCS2 | MPTPNIPSDFDFLDATLNLERLPVEELAELRKSEPIHWVDVPGGTGGFGDKGYWLVTKHADVKEVSRRSDVFGSSPDGAIPVWPQDMTREAVDLQRAVLLNMDAPQHTRLRKIISRGFTPRAIGRLEDELRSRAQKIAQTAAAQGAGDFVEQVSCELPLQAIAELLGVPQDDRDKLFRWSNEMTAGEDPEYADVDPAMSSFELISYAMKMAEERAVNPTEDIVTKLIEADIDGEKLSDDEFGFFVVMLAVAGNETTRNSITHGMIAFAQNPDQWELYKKERPETAADEIVRWATPVSAFQRTALEDVELGGVQIKKGQRV... | 1.14.15.29 | COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000269|PubMed:23489718, ECO:0000269|PubMed:26522442}; | cholesterol catabolic process [GO:0006707] | null | cholest-4-en-3-one 26-monooxygenase activity [GO:0036199]; heme binding [GO:0020037]; iron ion binding [GO:0005506]; steroid hydroxylase activity [GO:0008395] | PF00067; | 1.10.630.10; | Cytochrome P450 family | null | null | CATALYTIC ACTIVITY: Reaction=cholest-4-en-3-one + 5 H(+) + 3 O2 + 6 reduced [2Fe-2S]-[ferredoxin] = (25S)-3-oxocholest-4-en-26-oate + 4 H2O + 6 oxidized [2Fe-2S]-[ferredoxin]; Xref=Rhea:RHEA:51564, Rhea:RHEA-COMP:10000, Rhea:RHEA-COMP:10001, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16175, Ch... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=14 uM for cholest-4-en-3-one {ECO:0000269|PubMed:23489718}; | PATHWAY: Steroid metabolism; cholesterol degradation. {ECO:0000303|PubMed:23489718}. | null | null | FUNCTION: Involved in the utilization of cholesterol as the sole carbon and energy source by degrading the side chain. Primarily catalyzes the sequential oxidation of the terminal methyl of cholest-4-en-3-one into (25S)-26-hydroxycholest-4-en-3-one (alcohol), (25S)-26-oxocholest-4-en-3-one (aldehyde), to finally yield ... | Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) |
A0R564 | DISA_MYCS2 | MAVKSGARSGRNVVHLARPTLRETLGRLAPGTPLRDGLERILRGRTGALIVLGYDDSVEAICDGGFVLDVRYAPTRLRELSKMDGAVVLSSDGSRILRANVQLVPDPSIPTDESGTRHRSAERTAIQTGYPVISVSHSMSIVTVYVAGERHVVPDSATILSRANQTIATLERYKGRLDEVSRQLSTAEIEDFVTLRDVMTVVQRLEMVRRISLEIDADVVELGTDGRQLKLQLDELVGDNETARELIVRDYHANPDPPTAAQVAATLEELDSLSDSELLDFTVLARVFGYPSTAEAQDSAMSSRGYRAMAAIPRLQFAHV... | 2.7.7.85 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_01438}; | DNA repair [GO:0006281] | null | adenylate cyclase activity [GO:0004016]; ATP binding [GO:0005524]; diadenylate cyclase activity [GO:0106408]; DNA binding [GO:0003677] | PF02457;PF10635;PF12826; | 1.10.150.20;1.20.1260.110;3.40.1700.10; | DisA family | null | null | CATALYTIC ACTIVITY: Reaction=2 ATP = 3',3'-c-di-AMP + 2 diphosphate; Xref=Rhea:RHEA:35655, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:71500; EC=2.7.7.85; Evidence={ECO:0000255|HAMAP-Rule:MF_01438, ECO:0000269|PubMed:23760274}; | null | null | null | null | FUNCTION: Participates in a DNA-damage check-point. DisA forms globular foci that rapidly scan along the chromosomes searching for lesions. {ECO:0000255|HAMAP-Rule:MF_01438}.; FUNCTION: Has also diadenylate cyclase activity, catalyzing the condensation of 2 ATP molecules into cyclic di-AMP (c-di-AMP). c-di-AMP likely a... | Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) |
A0R5D9 | TOP1_MYCS2 | MAGGDRGSGGTGNVRRLVIVESPTKARKIAGYLGSNYVVESSRGHIRDLPRNAADVPAKFKSEPWARLGVNVDQNFEPLYIVSPEKKSTVTELKGLLKDVDELYLATDGDREGEAIAWHLLETLKPRVPVKRMVFHEITEPAIRNAAENPRDLDIALVDAQETRRILDRLYGYEVSPVLWKKVAPKLSAGRVQSVATRIIVQRERERMAFHSASYWDVTAELDASVSDPSASPPKFTAKLNTVDGRRVATGRDFDSLGQLKRPDEVLVLDEASAGALASGLRGAQLAVTSVEQKPYTRRPYAPFMTSTLQQEAARKLRFS... | 5.6.2.1 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_00952, ECO:0000269|PubMed:9593741}; | DNA topological change [GO:0006265] | null | DNA binding [GO:0003677]; DNA topoisomerase type I (single strand cut, ATP-independent) activity [GO:0003917]; metal ion binding [GO:0046872] | PF01131;PF01751;PF13368; | 3.40.50.140;1.10.460.10;2.70.20.10;1.10.290.10; | Type IA topoisomerase family | null | null | CATALYTIC ACTIVITY: Reaction=ATP-independent breakage of single-stranded DNA, followed by passage and rejoining.; EC=5.6.2.1; Evidence={ECO:0000255|HAMAP-Rule:MF_00952}; | null | null | null | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 30-42 degrees Celsius. Partially active up to 65 degrees Celsius (PubMed:9593741). {ECO:0000269|PubMed:9593741}; | FUNCTION: Releases the supercoiling and torsional tension of DNA, which is introduced during the DNA replication and transcription, by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is ... | Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) |
A0R5M8 | EGTD_MYCS2 | MTLSLANYLAADSAAEALRRDVRAGLTAAPKSLPPKWFYDAVGSDLFDQITRLPEYYPTRTEAQILRTRSAEIIAAAGADTLVELGSGTSEKTRMLLDAMRDAELLRRFIPFDVDAGVLRSAGAAIGAEYPGIEIDAVCGDFEEHLGKIPHVGRRLVVFLGSTIGNLTPAPRAEFLSTLADTLQPGDSLLLGTDLVKDTGRLVRAYDDAAGVTAAFNRNVLAVVNRELSADFDLDAFEHVAKWNSDEERIEMWLRARTAQHVRVAALDLEVDFAAGEEMLTEVSCKFRPENVVAELAEAGLRQTHWWTDPAGDFGLSLAV... | 2.1.1.44 | null | ergothioneine biosynthesis from histidine via gamma-glutamyl-hercynylcysteine sulfoxide [GO:0052704]; methylation [GO:0032259]; N-alpha,N-alpha,N-alpha-trimethyl-L-histidine biosynthesis from histidine [GO:0052707] | null | dimethylhistidine N-methyltransferase activity [GO:0030745]; protein methyltransferase activity [GO:0008276] | PF10017; | 3.40.50.150; | Methyltransferase superfamily, EgtD family | null | null | CATALYTIC ACTIVITY: Reaction=L-histidine + 3 S-adenosyl-L-methionine = 3 H(+) + hercynine + 3 S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:38471, ChEBI:CHEBI:15378, ChEBI:CHEBI:15781, ChEBI:CHEBI:57595, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789; EC=2.1.1.44; Evidence={ECO:0000269|PubMed:20420449, ECO:0000269|PubMed:25404173}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=109 uM for L-histidine {ECO:0000269|PubMed:25404173}; KM=17.7 uM for N-alpha-methyl-L-histidine {ECO:0000269|PubMed:25404173}; KM=25.3 uM for N-alpha,N-alpha-dimethyl-L-histidine {ECO:0000269|PubMed:25404173}; Note=kcat is 0.58 sec(-1) for the methylation of L-hist... | PATHWAY: Amino-acid biosynthesis; ergothioneine biosynthesis. {ECO:0000269|PubMed:23629716, ECO:0000305|PubMed:20420449}. | null | null | FUNCTION: Catalyzes the SAM-dependent triple methylation of the alpha-amino group of histidine to form hercynine, a step in the biosynthesis pathway of ergothioneine. Among all the proteinogenic amino acids, only L-histidine is a substrate. {ECO:0000269|PubMed:20420449, ECO:0000269|PubMed:25404173}. | Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) |
A0R607 | DPRE1_MYCS2 | MSTTEFPTTTKRLMGWGRTAPTVASVLSTSDPEVIVRAVTRAAEEGGRGVIARGLGRSYGDNAQNGGGLVIDMPALNRIHSIDSGTRLVDVDAGVSLDQLMKAALPHGLWVPVLPGTRQVTVGGAIGCDIHGKNHHSAGSFGNHVRSMELLTANGEVRHLTPAGPDSDLFWATVGGNGLTGIILRATIEMTPTETAYFIADGDVTGSLDETIAFHSDGSEANYTYSSAWFDAISKPPKLGRAAISRGSLAKLDQLPSKLQKDPLKFDAPQLLTLPDIFPNGLANKFTFMPIGELWYRKSGTYRNKVQNLTQFYHPLDMFG... | 1.1.98.3 | null | capsule polysaccharide biosynthetic process [GO:0045227]; cell wall organization [GO:0071555]; response to antibiotic [GO:0046677] | membrane [GO:0016020]; periplasmic space [GO:0042597] | D-arabinono-1,4-lactone oxidase activity [GO:0003885]; FAD binding [GO:0071949] | PF04030;PF01565; | 3.30.465.10;3.30.43.10; | DprE1 family | null | SUBCELLULAR LOCATION: Periplasm {ECO:0000250|UniProtKB:P9WJF1}. | CATALYTIC ACTIVITY: Reaction=FAD + H(+) + trans,octa-cis-decaprenylphospho-beta-D-ribofuranose = FADH2 + trans,octa-cis-decaprenylphospho-beta-D-erythro-pentofuranosid-2-ulose; Xref=Rhea:RHEA:33899, ChEBI:CHEBI:15378, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:65067, ChEBI:CHEBI:66881; EC=1.1.98.3; Evidence={ECO... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.11 mM for FPR (at pH 8.5 and 25 degrees Celsius) {ECO:0000269|PubMed:22956199}; Note=kcat is 12.7 min(-1) for epimerase activity with FPR as substrate (at pH 8.5 and 25 degrees Celsius). {ECO:0000269|PubMed:22956199}; | PATHWAY: Cell wall biogenesis; cell wall polysaccharide biosynthesis. {ECO:0000305|PubMed:21346818}. | null | null | FUNCTION: Component of the DprE1-DprE2 complex that catalyzes the 2-step epimerization of decaprenyl-phospho-ribose (DPR) to decaprenyl-phospho-arabinose (DPA), a key precursor that serves as the arabinose donor required for the synthesis of cell-wall arabinans (PubMed:22188377). DprE1 catalyzes the first step of epime... | Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) |
A0R618 | FAA32_MYCS2 | MPFHNPFIKDGQIKFPDGSSIVAHVERWAKVRGDKLAYRFLDFSTERDGVPRDLTWAQFSARNRAVAARLQQVTQPGDRVAILCPQNLDYLVAFFGALYAGRIAVPLFDPSEPGHVGRLHAVLDNCHPSAILTTTEAAEGVRKFFRTRPANQRPRVIAVDAVPDDVASTWVNPDEPDETTIAYLQYTSGSTRIPTGVQITHLNLATNVVQVIEALEGEEGDRGLSWLPFFHDMGLITALLAPMIGHYFTFMTPAAFVRRPERWIRELARKEGDTGGTISVAPNFAFDHAAARGVPKPGSPPLDLSNVKAVLNGSEPISAA... | 6.2.1.20 | null | fatty acid biosynthetic process [GO:0006633] | cytosol [GO:0005829]; plasma membrane [GO:0005886] | adenylyltransferase activity [GO:0070566]; ATP binding [GO:0005524]; long-chain fatty acid [acyl-carrier-protein] ligase activity [GO:0008922] | PF00501; | 3.30.300.30;3.40.50.12780; | ATP-dependent AMP-binding enzyme family | null | null | CATALYTIC ACTIVITY: Reaction=a long-chain fatty acid + ATP + holo-[ACP] = a long-chain fatty acyl-[ACP] + AMP + diphosphate; Xref=Rhea:RHEA:45588, Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:12682, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57560, ChEBI:CHEBI:64479, ChEBI:CHEBI:133243, ChEBI:CHEBI:456215; EC=6.2.1.20; E... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=259 uM for decanoate {ECO:0000269|PubMed:23364516}; KM=25.9 uM for dodecanoate {ECO:0000269|PubMed:23364516}; KM=5.2 uM for tetradecanoate {ECO:0000269|PubMed:23364516}; KM=76 uM for ATP {ECO:0000269|PubMed:23364516}; KM=112 uM for ATP {ECO:0000269|PubMed:26900152}... | PATHWAY: Lipid metabolism; mycolic acid biosynthesis. {ECO:0000250|UniProtKB:O53580}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5. {ECO:0000269|PubMed:23364516}; | null | FUNCTION: Involved in the biosynthesis of mycolic acids (By similarity). Catalyzes the activation of long-chain fatty acids as acyl-adenylates (acyl-AMP), which are then transferred to the phosphopantetheine arm of the polyketide synthase Pks13 for further chain extension (By similarity). Can use decanoate (C10), dodec... | Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) |
A0R6D0 | NFNB_MYCS2 | MSVPTLPTGPTVDLAQAAERLIKGRRAVRAFRPDEVPEETMRAVFELAGHAPSNSNTQPWHVEVVSGAARDRLAEALVTAHAEERVTVDFPYREGLFQGVLQERRADFGSRLYAALGIARDQTDLLQGYNTESLRFYGAPHVAMLFAPNNTEARIAGDMGIYAQTLMLAMTAHGIASCPQALLSFYADTVRAELGVENRKLLMGISFGYADDTAAVNGVRIPRAGLSETTRFSR | 1.-.-.- | COFACTOR: Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000269|PubMed:20624223}; Note=Binds 1 FMN per subunit. {ECO:0000269|PubMed:20624223}; | thyroid hormone metabolic process [GO:0042403]; tyrosine metabolic process [GO:0006570]; xenobiotic catabolic process [GO:0042178] | null | FMN binding [GO:0010181]; identical protein binding [GO:0042802]; NADP binding [GO:0050661]; oxidoreductase activity [GO:0016491]; protein homodimerization activity [GO:0042803] | PF00881; | 3.40.109.10; | Nitroreductase family | null | null | null | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=10.75 uM for NADH (at pH 8.0 and 25 degrees Celsius) {ECO:0000269|PubMed:20624223}; KM=8.15 uM for NADPH (at pH 8.0 and 25 degrees Celsius) {ECO:0000269|PubMed:20624223}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5 to 9.0. {ECO:0000269|PubMed:20624223}; | null | FUNCTION: Confers resistance to antitubercular drugs benzothiazinone (BTZ) and dinitrobenzamide (DNB). Inactivates BTZ and DNB by reducing an essential nitro group of these compounds to amino group or to hydroxyl amine, respectively, using NADH or NADPH as source of reducing equivalents; two electrons are transferred (... | Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) |
A0R6E0 | TRES_MYCS2 | MEEHTQGSHVEAGIVEHPNAEDFGHARTLPTDTNWFKHAVFYEVLVRAFYDSNADGIGDLRGLTEKLDYIKWLGVDCLWLPPFYDSPLRDGGYDIRDFYKVLPEFGTVDDFVTLLDAAHRRGIRIITDLVMNHTSDQHEWFQESRHNPDGPYGDFYVWSDTSDRYPDARIIFVDTEESNWTFDPVRRQFYWHRFFSHQPDLNYDNPAVQEAMLDVLRFWLDLGIDGFRLDAVPYLFEREGTNCENLPETHAFLKRCRKAIDDEYPGRVLLAEANQWPADVVAYFGDPDTGGDECHMAFHFPLMPRIFMAVRRESRFPISE... | 3.2.1.1; 5.4.99.16 | null | glycogen biosynthetic process [GO:0005978]; glycogen metabolic process [GO:0005977]; maltose metabolic process [GO:0000023]; polysaccharide catabolic process [GO:0000272]; trehalose metabolic process [GO:0005991] | null | alpha-amylase activity [GO:0004556]; calcium ion binding [GO:0005509]; maltose alpha-D-glucosyltransferase activity [GO:0047471] | PF00128;PF16657; | 3.20.20.80;2.60.40.1180; | Glycosyl hydrolase 13 family, TreS subfamily | null | null | CATALYTIC ACTIVITY: Reaction=D-maltose = alpha,alpha-trehalose; Xref=Rhea:RHEA:15145, ChEBI:CHEBI:16551, ChEBI:CHEBI:17306; EC=5.4.99.16; Evidence={ECO:0000269|PubMed:15511231, ECO:0000269|PubMed:18505459, ECO:0000269|PubMed:21840994}; CATALYTIC ACTIVITY: Reaction=Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=8 mM for maltose (at pH 6.8 and 37 degrees Celsius) {ECO:0000269|PubMed:15511231, ECO:0000269|PubMed:18505459, ECO:0000269|PubMed:21840994}; KM=87 mM for trehalose (at pH 6.8 and at 37 degrees Celsius) {ECO:0000269|PubMed:15511231, ECO:0000269|PubMed:18505459, ECO:... | PATHWAY: Glycan biosynthesis; glycogen biosynthesis. {ECO:0000269|PubMed:20118231, ECO:0000269|PubMed:27513637}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is between 6.0-6.2 for the amylase activity and 7.0 for the trehalose synthase activity. {ECO:0000269|PubMed:15511231, ECO:0000269|PubMed:18505459}; | null | FUNCTION: Catalyzes the reversible interconversion of maltose and trehalose by transglucosylation (PubMed:15511231, PubMed:18505459, PubMed:20118231, PubMed:21840994). Maltose is the preferred substrate (PubMed:15511231, PubMed:18505459). To a lesser extent, also displays amylase activity, catalyzing the endohydrolysis... | Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) |
A0R758 | LERK_MYCS2 | MTYLLNSPDDFADEAVRGLVAANPDLLTEVPGGVVRSTETPKGQPALVIGGGSGHYPAFAGWVGPGMGHGAPCGNIFSSPSASEVYSVVRNAENGGGVILGFGNYAGDVLHFGLAAEKLRHEGIDVRIVTVSDDIASNSPENHRDRRGVAGDLPVFKIAGAAIEAGADLDEAERVAWKANDATRSFGLAFEGCTLPGATEPLFHVEKGWMGVGLGIHGEPGVRDNRLGTAAEVADMLFDEVTAEEPPRGENGYDGRVAVILNGLGTVKYEELFVVYGRIAERLAQQGFTVVRPEVGEFVTSLDMAGVSLTMVFLDDELER... | 2.7.1.209 | null | carbohydrate catabolic process [GO:0016052]; carbohydrate utilization [GO:0009758]; cellular response to carbohydrate stimulus [GO:0071322]; glycerol catabolic process [GO:0019563] | cytosol [GO:0005829] | ATP binding [GO:0005524]; carbohydrate binding [GO:0030246]; carbohydrate kinase activity [GO:0019200]; glycerone kinase activity [GO:0004371] | PF02733;PF02734; | 1.25.40.340; | null | null | null | CATALYTIC ACTIVITY: Reaction=ATP + L-erythrulose = ADP + H(+) + L-erythrulose 1-phosphate; Xref=Rhea:RHEA:48780, ChEBI:CHEBI:15378, ChEBI:CHEBI:27913, ChEBI:CHEBI:30616, ChEBI:CHEBI:58002, ChEBI:CHEBI:456216; EC=2.7.1.209; Evidence={ECO:0000269|PubMed:26560079, ECO:0000305|PubMed:26978037}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=3 uM for L-erythrulose {ECO:0000269|PubMed:26560079}; KM=10.6 uM for D-erythrulose {ECO:0000269|PubMed:26560079}; KM=37.8 uM for dihydroxyacetone {ECO:0000269|PubMed:26560079}; Note=kcat is 1.79 sec(-1) with L-erythrulose as substrate. kcat is 1.60 sec(-1) with D-e... | PATHWAY: Carbohydrate metabolism; L-threitol degradation. {ECO:0000269|PubMed:26560079}. | null | null | FUNCTION: Kinase that has a preference for L-erythrulose, producing L-erythrulose-1P. Involved in the degradation pathway of L-threitol, that allows M.smegmatis to grow on this compound as the sole carbon source. Is also able to phosphorylate D-erythrulose and dihydroxyacetone in vitro. {ECO:0000269|PubMed:26560079, EC... | Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) |
A0RV30 | FBPAP_CENSY | MRITVSAIKADVGGIGGHTLPSSGLLDAVRRKVSSSSLLIDHYIGYCGDDVHIVMTHTRGTDNSDIHKLAWDAFMEGTRVAKEEGLYGAGQDLLRDSFSGNVKGMGPGVAELEFEERANEAFTVFAADKTEPGAFNYPFYRMFVDSLSNTGLIVNKSLAEGVVINIMDVSKARTARLVLWEDKPTIEAALMYPGRFVVSSVETRDGEPIASASTDRLHNIAGTYVGKDDPICLVRTQKRFPATEEAGSCFNNPHYVAGNTRGSHHMPLMPVRLNSPASINFCIPIVEALVFSMHEGRLTGPFDGFSTPDWDDVRRTATRR... | 3.1.3.11; 4.1.2.13 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:20348906}; | gluconeogenesis [GO:0006094] | null | fructose 1,6-bisphosphate 1-phosphatase activity [GO:0042132]; fructose-bisphosphate aldolase activity [GO:0004332]; magnesium ion binding [GO:0000287]; oxidoreductase activity [GO:0016491] | PF01950; | null | FBP aldolase/phosphatase family | null | null | CATALYTIC ACTIVITY: Reaction=beta-D-fructose 1,6-bisphosphate + H2O = beta-D-fructose 6-phosphate + phosphate; Xref=Rhea:RHEA:11064, ChEBI:CHEBI:15377, ChEBI:CHEBI:32966, ChEBI:CHEBI:43474, ChEBI:CHEBI:57634; EC=3.1.3.11; Evidence={ECO:0000269|PubMed:20348906}; CATALYTIC ACTIVITY: Reaction=beta-D-fructose 1,6-bisphosph... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=40 uM for D-fructose 1,6-bisphosphate (when assaying the FBP phosphatase activity, at 48 degrees Celsius) {ECO:0000269|PubMed:20348906}; KM=110 uM for triosephosphates (when assaying the FBP aldolase activity in the anabolic direction, at 48 degrees Celsius) {ECO:0... | PATHWAY: Carbohydrate biosynthesis; gluconeogenesis. {ECO:0000305|PubMed:20348906}. | null | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Heat-stabile at 70 degrees Celsius. Displays a half-life of 20 minutes at 82 degrees Celsius. {ECO:0000269|PubMed:20348906}; | FUNCTION: Catalyzes two subsequent steps in gluconeogenesis: the aldol condensation of dihydroxyacetone phosphate (DHAP) and glyceraldehyde-3-phosphate (GA3P) to fructose-1,6-bisphosphate (FBP), and the dephosphorylation of FBP to fructose-6-phosphate (F6P). {ECO:0000269|PubMed:20348906}. | Cenarchaeum symbiosum (strain A) |
A0S864 | 3NBA_BOIIR | MKTLLLAVAVVAFVCLGSADQLGLGRQQIDWGQGQAVGPPYTLCFECNRMTSSDCSTALRCYRGSCYTLYRPDENCELKWAVKGCAETCPTAGPNERVKCCRSPRCNDD | null | null | modulation of receptor activity in another organism [GO:0044504] | extracellular region [GO:0005576] | acetylcholine receptor inhibitor activity [GO:0030550]; ion channel regulator activity [GO:0099106]; toxin activity [GO:0090729] | null | 2.10.60.10; | Snake three-finger toxin family, Ancestral subfamily, Boigatoxin sub-subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18952712}. | null | null | null | null | null | FUNCTION: This bird and reptile-specific postsynaptic neurotoxin inhibits the chick muscle alpha-1-beta-1-gamma-delta (CHRNA1-CHRNB1-CHRNG-CHNRD) nicotinic acetylcholine receptor (nAChR) 100-fold more compared with the mouse receptor. In vivo, produces rapid flaccid paralysis, dyspnea and increased respiratory rate in ... | Boiga irregularis (Brown tree snake) |
A0S865 | 3NBB_BOIIR | MKTLLLAVAVVAFVCLGSADQLGLGRQQIDWGKGQAKGPPYTLCFECNRETCSNCFKDNRCPPYHRTCYTLYRPDGNGEMKWAVKGCAKTCPTAQPGESVQCCNTPKCNDY | null | null | modulation of receptor activity in another organism [GO:0044504] | extracellular region [GO:0005576] | acetylcholine receptor inhibitor activity [GO:0030550]; ion channel regulator activity [GO:0099106]; toxin activity [GO:0090729] | PF00087; | 2.10.60.10; | Snake three-finger toxin family, Ancestral subfamily, Boigatoxin sub-subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18952712}. | null | null | null | null | null | FUNCTION: This bird and reptile-specific postsynaptic neurotoxin inhibits the chick muscle alpha-1-beta-1-gamma-delta (CHRNA1-CHRNB1-CHRNG-CHRND) nicotinic acetylcholine receptor (nAChR) 100-fold more compared with the mouse receptor. In vivo, produces rapid flaccid paralysis, dyspnea and increased respiratory rate in ... | Boiga irregularis (Brown tree snake) |
A0SVK0 | DOG1_ARATH | MGSSSKNIEQAQDSYLEWMSLQSQRIPELKQLLAQRRSHGDEDNDNKLRKLTGKIIGDFKNYAAKRADLAHRCSSNYYAPTWNSPLENALIWMGGCRPSSFFRLVYALCGSQTEIRVTQFLRNIDGYESSGGGGGASLSDLSAEQLAKINVLHVKIIDEEEKMTKKVSSLQEDAADIPIATVAYEMENVGEPNVVVDQALDKQEEAMARLLVEADNLRVDTLAKILGILSPVQGADFLLAGKKLHLSMHEWGTMRDRRRRDCMVDTEVIFDACTTVNSGPRPTETTNNERN | null | null | abscisic acid-activated signaling pathway [GO:0009738]; DNA-templated transcription [GO:0006351]; regulation of seed dormancy process [GO:2000033]; seed dormancy process [GO:0010162]; sugar mediated signaling pathway [GO:0010182] | nucleus [GO:0005634] | identical protein binding [GO:0042802]; sequence-specific DNA binding [GO:0043565] | PF14144; | null | null | PTM: A shift in isoelectric focusing of the protein occurs during after-ripening, probably leading to its loss of function. {ECO:0000269|PubMed:22829147}. | SUBCELLULAR LOCATION: [Isoform 1]: Nucleus {ECO:0000269|PubMed:22829147, ECO:0000269|PubMed:26620523, ECO:0000269|PubMed:26684465}.; SUBCELLULAR LOCATION: [Isoform 2]: Nucleus {ECO:0000269|PubMed:26620523}. | null | null | null | null | null | FUNCTION: Required for the induction of seed dormancy (PubMed:17065317, PubMed:22829147, PubMed:26620523). The level of DOG1 protein in freshly harvested seeds determines the level of seed dormancy (PubMed:22829147). Determines the temperature window for germination by regulating the expression of micropylar endosperm-... | Arabidopsis thaliana (Mouse-ear cress) |
A0SYQ0 | PTGES_CANLF | MPPPVLALVSGQALPAFLLCSTLLVIKMYVVAVITGQVRLRKKAFANPEDALRHGGLQYCRSDQDVDRCLRAHRNDMETIYPFLFLGFVYSFLGPDPFIAQMHFLVFFLGRMVHTVAYLGKLRAPTRSLAYTVAQLPCASMALQIVWEAACHL | 1.11.1.-; 2.5.1.18; 5.3.99.3 | COFACTOR: Name=glutathione; Xref=ChEBI:CHEBI:57925; Evidence={ECO:0000250|UniProtKB:O14684}; | cell population proliferation [GO:0008283]; negative regulation of cell population proliferation [GO:0008285]; positive regulation of prostaglandin secretion [GO:0032308]; prostaglandin biosynthetic process [GO:0001516]; regulation of fever generation [GO:0031620]; regulation of inflammatory response [GO:0050727]; sens... | membrane [GO:0016020]; nuclear envelope lumen [GO:0005641]; perinuclear region of cytoplasm [GO:0048471] | glutathione binding [GO:0043295]; glutathione peroxidase activity [GO:0004602]; glutathione transferase activity [GO:0004364]; prostaglandin-D synthase activity [GO:0004667]; prostaglandin-E synthase activity [GO:0050220] | PF01124; | 1.20.120.550; | MAPEG family | null | SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:O14684}; Multi-pass membrane protein {ECO:0000250|UniProtKB:O14684}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O14684}. Note=Colocalizes with PTGS1/COX-1 and PTGS2/COX-2 in the perinuclear compartment. {ECO:0000250|UniProtKB:O14684}. | CATALYTIC ACTIVITY: Reaction=prostaglandin H2 = prostaglandin E2; Xref=Rhea:RHEA:12893, ChEBI:CHEBI:57405, ChEBI:CHEBI:606564; EC=5.3.99.3; Evidence={ECO:0000250|UniProtKB:O14684}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12894; Evidence={ECO:0000250|UniProtKB:O14684}; CATALYTIC ACTIVITY: Reaction=2-glycery... | null | PATHWAY: Lipid metabolism; prostaglandin biosynthesis. {ECO:0000250|UniProtKB:O14684}. | null | null | FUNCTION: Terminal enzyme of the cyclooxygenase (COX)-2-mediated prostaglandin E2 (PGE2) biosynthetic pathway. Catalyzes the glutathione-dependent oxidoreduction of prostaglandin endoperoxide H2 (PGH2) to prostaglandin E2 (PGE2) in response to inflammatory stimuli (By similarity). Plays a key role in inflammation respo... | Canis lupus familiaris (Dog) (Canis familiaris) |
A0T2N3 | APJB_DANRE | MNAMDNMTADYSPDYFDDAVNSSMCEYDEWEPSYSLIPVLYMLIFILGLTGNGVVIFTVWRAQSKRRAADVYIGNLALADLTFVVTLPLWAVYTALGYHWPFGVALCKISSYVVLLNMYASVFCLTCLSLDRYMAIVHSLTSTQLRTRGHMRASLTAIWLLSGVLAAPTLLFRTTVYDVETNRTSCAMDFNLVVSQPGQETYWIAGLSISSTALGFLIPLLAMMVCYGFIGCTVTRHFNSLRKEDQRKRRLLKIITTLVVVFAACWMPFHVVKTMDALSYLNLAPDSCTFLNLLLLAHPYATCLAYVNSCLNPLLYAFFD... | null | null | angioblast cell migration from lateral mesoderm to midline [GO:0035479]; blood vessel development [GO:0001568]; brain development [GO:0007420]; calcium-mediated signaling [GO:0019722]; cardiac muscle tissue development [GO:0048738]; cell chemotaxis [GO:0060326]; cell migration [GO:0016477]; coronary vasculature develop... | external side of plasma membrane [GO:0009897]; plasma membrane [GO:0005886] | apelin receptor activity [GO:0060182]; C-C chemokine binding [GO:0019957]; C-C chemokine receptor activity [GO:0016493] | PF00001; | 1.20.1070.10; | G-protein coupled receptor 1 family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P79960}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P79960}. Note=Internalized to the cytoplasm after exposure to apelin (apln). After exposure to apelin receptor early endogenous ligand (apela), internalized from the cell surface into an endosomal recy... | null | null | null | null | null | FUNCTION: Receptor for apelin receptor early endogenous ligand (apela) and apelin (apln) hormones coupled to G proteins that inhibit adenylate cyclase activity (PubMed:17336905, PubMed:17336906, PubMed:24316148, PubMed:24407481). Plays a key role in early development such as gastrulation, blood vessels formation and he... | Danio rerio (Zebrafish) (Brachydanio rerio) |
A1A278 | MANA_BIFAA | MKTTVTKLLATVAAASTIFGMSTLPAFAAEGKSASNGNSVNISDVNATAETRALFDKLKNSGKGDLRFGQQHATDENISSSASQGDVYETTGKYPAVFGWDAGLALRGAEKPGSGADKNANAKALAQNITDADSKGAIVTLSAHWCNPGTGKDFNDTTAVASELLPGGKYSGTFNKELDAIAATAQRAKRSDGTLIPIIFRPLHENNGSWFWWGATHASASEYKELYRYIVDYLRDVKDVHNLLYAYSPGGVFNGDSTDYLATYPGDQWVDVLGYDEYDSDDSADDSSAWINTVVKDMKMVSDQASQRGKIVALTEFGRS... | 3.2.1.78 | null | cellulose catabolic process [GO:0030245]; galactomannan metabolic process [GO:0051069]; glucomannan metabolic process [GO:0010391]; mannan catabolic process [GO:0046355] | extracellular region [GO:0005576] | cellulase activity [GO:0008810]; mannan binding [GO:2001065]; mannan endo-1,4-beta-mannosidase activity [GO:0016985] | PF03425;PF02156; | 2.60.120.430;3.20.20.80;2.60.40.10; | Glycosyl hydrolase 26 family | null | SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000305}; Peptidoglycan-anchor {ECO:0000305}. Note=Is likely to be cell attached, either by the sortase mechanism (LPXTG motif) or via a C-terminal transmembrane helix. {ECO:0000269|PubMed:23064345}. | CATALYTIC ACTIVITY: Reaction=Random hydrolysis of (1->4)-beta-D-mannosidic linkages in mannans, galactomannans and glucomannans.; EC=3.2.1.78; Evidence={ECO:0000269|PubMed:23064345}; | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5.3. Retains over 90% of its activity in the pH range of 5 to 6. {ECO:0000269|PubMed:23064345}; | null | FUNCTION: Beta-mannanase likely involved in the utilization of carbohydrates in the human gut. Catalyzes the hydrolysis of different beta-1,4-linked mannans, such as ivory nut mannan, konjac glucomannan, as well as carob and guar gum galactomannans, to a mixture of oligosaccharides. The dominant product from ivory nut ... | Bifidobacterium adolescentis (strain ATCC 15703 / DSM 20083 / NCTC 11814 / E194a) |
A1A399 | BGAL_BIFAA | MSARRNFEWPELLTADGRGIAFGGDYNPDQWSEDIWDDDIRLMKQAGVNTVALAIFSWDRIQPTEDRWDFGWLDRIIDKLGNAGIVVDLASATATAPLWLYESHPEVLPRDKYGHPVNAGSRQSWSPTSPVFKEYALTLCRKLAERYGTNPYVTAWHMGNEYGWNNREDYSDNALEAFRAWCRRKYGTIDALNQAWGTTFWGQEMNGFDEVLIPRFMGADSMVNPGQKLDFERFGNDMLLDFYKAERDAIAEICPDKPFTTNFMVSTDQCCMDYAAWAKEVNFVSNDHYFHEGESHLDELACSDALMDSLALGKPWYVME... | 3.2.1.23 | null | carbohydrate metabolic process [GO:0005975] | beta-galactosidase complex [GO:0009341] | beta-galactosidase activity [GO:0004565] | PF02449;PF08532; | 3.40.50.880;3.20.20.80; | Glycosyl hydrolase 42 family | PTM: The N-terminus is blocked. | null | CATALYTIC ACTIVITY: Reaction=Hydrolysis of terminal non-reducing beta-D-galactose residues in beta-D-galactosides.; EC=3.2.1.23; Evidence={ECO:0000269|PubMed:10742215, ECO:0000269|PubMed:15480628}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=60 mM for Gal(beta1-4)Gal (at 37 degrees Celsius and pH 6.0) {ECO:0000269|PubMed:10742215, ECO:0000269|PubMed:15480628}; KM=2.2 mM for p-nitrophenyl-beta-D-galactopyranoside (PNPG) (at 40 degrees Celsius and pH 6.0) {ECO:0000269|PubMed:10742215, ECO:0000269|PubMed:... | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum is pH 6.0 using PNPG or TOS as substrate. Not active below pH 5. {ECO:0000269|PubMed:10742215, ECO:0000269|PubMed:15480628}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 50 degrees Celsius using PNPG as substrate (PubMed:15480628). Optimum temperature is 35 degrees Celsius using TOS as substrate (PubMed:10742215). Stable at 40 degrees Celsius. Half-life time at 50 degrees Celsius is 10 minutes. {ECO:0000269|... | FUNCTION: Involved in the hydrolysis of transgalactooligosaccharides (TOS). Highly active towards Gal(beta1-4)Gal and Gal(beta1-4)-Gal-containing oligosaccharides. Low activity towards Gal(beta1-3)Gal, lactose and Gal(beta1-3)GalOMe. No activity towards Gal(beta1-6)Gal, Gal(beta1-4)Man, Gal(alpha1-4)Gal, Gal(alpha1-3)G... | Bifidobacterium adolescentis (strain ATCC 15703 / DSM 20083 / NCTC 11814 / E194a) |
A1A4I4 | PKN1_BOVIN | MASDAVQSEPRSWSLLEQLGLAGADLAAPGVQQQLELERERLRREIRKELKLKEGAENLRRATTDLGRNLGPVELVLRGSSRRLALLHQQLQELHAHVVLPDPAVGVHDAPQSPGTGDSACSATNLSRVAGLEKQLAIELKVKQGAENMIQTYSNGSTKDRKLLLTAQQMLQDSKTKIDIIRMQLHRALQACQLESQAAPDEAQGSPDLGAVELRIEELRHHFRVEHAVAEGAKNVLRLLSAAKAPDRKAVSEAQEKLTESNQKLGLLREALERRLGELPADHPKGRLLREELAAASSAAFSARLAGPFPATHYSTLSKP... | 2.7.11.13 | null | B cell apoptotic process [GO:0001783]; B cell homeostasis [GO:0001782]; epithelial cell migration [GO:0010631]; hyperosmotic response [GO:0006972]; intracellular signal transduction [GO:0035556]; negative regulation of B cell proliferation [GO:0030889]; negative regulation of protein phosphorylation [GO:0001933]; post-... | cleavage furrow [GO:0032154]; cytoplasm [GO:0005737]; endosome [GO:0005768]; midbody [GO:0030496]; nucleus [GO:0005634]; protein-containing complex [GO:0032991] | ATP binding [GO:0005524]; chromatin binding [GO:0003682]; diacylglycerol-dependent serine/threonine kinase activity [GO:0004697]; histone binding [GO:0042393]; histone deacetylase binding [GO:0042826]; histone H3T11 kinase activity [GO:0035402]; nuclear androgen receptor binding [GO:0050681]; nuclear receptor coactivat... | PF02185;PF00069;PF00433; | 1.10.287.160;1.10.510.10; | Protein kinase superfamily, AGC Ser/Thr protein kinase family, PKC subfamily | PTM: Autophosphorylated; preferably on serine. Phosphorylated during mitosis. {ECO:0000250|UniProtKB:Q16512}.; PTM: Activated by limited proteolysis with trypsin. {ECO:0000250}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q16512}. Nucleus {ECO:0000250|UniProtKB:Q16512}. Endosome {ECO:0000250|UniProtKB:Q16512}. Cell membrane {ECO:0000250|UniProtKB:Q63433}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q63433}. Cleavage furrow {ECO:0000250|UniProtKB:Q16512}. Midbody {ECO:0000250|... | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.13; Evidence={ECO:0000250|UniProtKB:Q16512}; CATALYT... | null | null | null | null | FUNCTION: PKC-related serine/threonine-protein kinase involved in various processes such as regulation of the intermediate filaments of the actin cytoskeleton, cell migration, tumor cell invasion and transcription regulation. Part of a signaling cascade that begins with the activation of the adrenergic receptor ADRA1B ... | Bos taurus (Bovine) |
A1A4I9 | UFL1_BOVIN | MADAWEEIRRLAADFQRAQFAEATQRLSERNCIEIVNKLIAQKQLEVVHTLDGKEYITPAQISKEMRDELHVRGGRVNIVDLQQAINVDLTHIENRIGDIVKSEKHVQLVLGQLIDENYLDRLAEEVNDKLQESGQVTIAELCKTYDLPGNFLTQALTQRLGRIINGHIDLDNRGVIFTEAFVSRHKARIRGLFSAITRPTAVNSLISRYGFQEQLLYSVLEELVNDGRLRGTVVGGRQDKAVFIPDIYSRTQSTWVDSFLRQNGYLEFDALSRLGIPDAMSYIKKRYKTTQLLFLKAACVGQGLVDQVEASVEEAISSG... | 2.3.2.- | null | DNA damage checkpoint signaling [GO:0000077]; DNA repair [GO:0006281]; erythrocyte differentiation [GO:0030218]; hematopoietic stem cell differentiation [GO:0060218]; negative regulation of IRE1-mediated unfolded protein response [GO:1903895]; negative regulation of NF-kappaB transcription factor activity [GO:0032088];... | cytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; nucleus [GO:0005634]; site of double-strand break [GO:0035861] | UFM1 ligase activity [GO:0061666]; UFM1 transferase activity [GO:0071568] | PF09743; | null | UFL1 family | PTM: Ubiquitinated, leading to its degradation by the proteasome. Interaction with CDK5RAP3 protects both proteins against ubiquitination and degradation via the proteasome. {ECO:0000250|UniProtKB:O94874}. | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:O94874}. Cytoplasm, cytosol {ECO:0000269|PubMed:30881595, ECO:0000269|PubMed:31721015}. Nucleus {ECO:0000269|PubMed:30881595, ECO:0000269|PubMed:31721015}. Chromosome {ECO:0000250|UniProtKB:O94874}. Note=Recruited to double-strand breaks by the... | null | null | null | null | null | FUNCTION: E3 protein ligase that mediates ufmylation, the covalent attachment of the ubiquitin-like modifier UFM1 to lysine residues on target proteins, and which plays a key role in reticulophagy (also called ER-phagy) induced in response to endoplasmic reticulum stress (By similarity). In response to endoplasmic reti... | Bos taurus (Bovine) |
A1A4J1 | PFKAL_BOVIN | MASVDLEKLRTTGAGKAIGVLTSGGDAQGMNAAVRAVTRMGIYVGAKVFLIYEGYEGLVEGGENIKQANWLSVSNIIQLGGTVIGSARCKAFTTREGRRAAAYNLVQRGITNLCVIGGDGSLTGANIFRSEWGSLLEELVSEGKISEGTAQTYSHLNIAGLVGSIDNDFCGTDMTIGTDSALHRIMEVIDAITTTAQSHQRTFVLEVMGRHCGYLALVSALASGADWLFIPEAPPEDGWENFMCERLGETRSRGSRLNIIIIAEGAIDRNGKPISSRYVKDLVVQRLGFDTRVTVLGHVQRGGTPSAFDRILSSKMGMEA... | 2.7.1.11 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_03184}; | canonical glycolysis [GO:0061621]; fructose 1,6-bisphosphate metabolic process [GO:0030388]; fructose 6-phosphate metabolic process [GO:0006002]; glycolytic process [GO:0006096]; negative regulation of insulin secretion [GO:0046676]; response to glucose [GO:0009749] | 6-phosphofructokinase complex [GO:0005945]; membrane [GO:0016020] | 6-phosphofructokinase activity [GO:0003872]; AMP binding [GO:0016208]; ATP binding [GO:0005524]; fructose binding [GO:0070061]; fructose-6-phosphate binding [GO:0070095]; identical protein binding [GO:0042802]; kinase binding [GO:0019900]; metal ion binding [GO:0046872]; monosaccharide binding [GO:0048029] | PF00365; | 3.40.50.450;3.40.50.460; | Phosphofructokinase type A (PFKA) family, ATP-dependent PFK group I subfamily, Eukaryotic two domain clade 'E' sub-subfamily | PTM: GlcNAcylation at Ser-529 by OGT decreases enzyme activity, leading to redirect glucose flux through the oxidative pentose phosphate pathway. Glycosylation is stimulated by both hypoxia and glucose deprivation (By similarity). {ECO:0000250}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03184}. | CATALYTIC ACTIVITY: Reaction=ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 1,6-bisphosphate + H(+); Xref=Rhea:RHEA:16109, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:32966, ChEBI:CHEBI:57634, ChEBI:CHEBI:456216; EC=2.7.1.11; Evidence={ECO:0000255|HAMAP-Rule:MF_03184}; | null | PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 3/4. {ECO:0000255|HAMAP-Rule:MF_03184}. | null | null | FUNCTION: Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis (By similarity). Negatively regulates the phagocyte oxidative burst in response to bacterial infection by controlling cellular NADPH biosynthesis and NADPH oxidase-derived react... | Bos taurus (Bovine) |
A1A4K3 | DDB1_BOVIN | MSYNYVVTAQKPTAVNGCVTGHFTSAEDLNLLIAKNTRLEIYVVTAEGLRPVKEVGMYGKIAVMELFRPKGESKDLLFILTAKYNACILEYKQSGESIDIITRAHGNVQDRIGRPSETGIIGIIDPECRMIGLRLYDGLFKVIPLDRDNKELKAFNIRLEELHVIDVKFLYGCQAPTICFVYQDPQGRHVKTYEVSLREKEFNKGPWKQENVEAEASMVIAVPEPFGGAIIIGQESITYHNGDKYLAIAPPIIKQSTIVCHNRVDPNGSRYLLGDMEGRLFMLLLEKEEQMDGTVTLKDLRVELLGETSIAECLTYLDNG... | null | null | DNA repair [GO:0006281]; positive regulation of gluconeogenesis [GO:0045722]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; protein ubiquitination [GO:0016567]; regulation of circadian rhythm [GO:0042752]; rhythmic process [GO:0048511]; ubiquitin-dependent protein catabolic process [GO... | Cul4-RING E3 ubiquitin ligase complex [GO:0080008]; Cul4A-RING E3 ubiquitin ligase complex [GO:0031464]; Cul4B-RING E3 ubiquitin ligase complex [GO:0031465]; cytoplasm [GO:0005737]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; site of double-strand break [GO:0035861] | DNA binding [GO:0003677] | PF03178;PF10433; | 1.10.150.910;2.130.10.10; | DDB1 family | PTM: Phosphorylated by ABL1. {ECO:0000250|UniProtKB:Q3U1J4}.; PTM: Ubiquitinated by CUL4A. Subsequently degraded by ubiquitin-dependent proteolysis. {ECO:0000250|UniProtKB:Q16531}.; PTM: Acetylated, promoting interaction with CUL4 (CUL4A or CUL4B) and subsequent formation of DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein l... | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q16531}. Nucleus {ECO:0000250|UniProtKB:Q16531}. Note=Primarily cytoplasmic. Translocates to the nucleus following UV irradiation and subsequently accumulates at sites of DNA damage. More concentrated in nuclei than in cytoplasm in germinal vesicle (GV) stage oocyt... | null | null | PATHWAY: Protein modification; protein ubiquitination. {ECO:0000250|UniProtKB:Q16531}. | null | null | FUNCTION: Protein, which is both involved in DNA repair and protein ubiquitination, as part of the UV-DDB complex and DCX (DDB1-CUL4-X-box) complexes, respectively. Core component of the UV-DDB complex (UV-damaged DNA-binding protein complex), a complex that recognizes UV-induced DNA damage and recruit proteins of the ... | Bos taurus (Bovine) |
A1A4K5 | ENPP2_BOVIN | MARRRSCQLHQVISLFTFAVGVNICLGVTANRIKRAEGWGEGPPTVLSDSPSINISGSCKGRCFELQEAGPPDCRCDNLCKSYSSCCLDFDELCLKTAGGWECTKDRCGEVRNEDHACHCSEDCLARGDCCTNYQVVCKGESHWVDDDCEEIKTPECPAGFVRPPLIIFSVDGFRASYMKKGSKVMPNIEKLRSCGTHSPYMRPVYPTKTFPNLYTLATGLYPESHGIVGNSMYDPVFDAHFNLRGREKFNHRWWGGQPLWITATKQGVIAGTFFWPVVIPHERRILTILQWLTLPDHERPSVYAFYSEQPDFSGHKYGP... | 3.1.4.39 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:Q13822}; Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:Q13822}; COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250|UniProtKB:Q13822}; Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250|UniProtKB:Q13822}; | chemotaxis [GO:0006935]; estrous cycle [GO:0044849]; immune response [GO:0006955]; phosphatidylcholine catabolic process [GO:0034638]; phospholipid catabolic process [GO:0009395]; sphingolipid catabolic process [GO:0030149] | extracellular space [GO:0005615] | alkylglycerophosphoethanolamine phosphodiesterase activity [GO:0047391]; calcium ion binding [GO:0005509]; lysophospholipase activity [GO:0004622]; nucleic acid binding [GO:0003676]; phosphodiesterase I activity [GO:0004528]; polysaccharide binding [GO:0030247]; scavenger receptor activity [GO:0005044]; zinc ion bindin... | PF01223;PF01663;PF01033; | 4.10.410.20;3.40.720.10;3.40.570.10; | Nucleotide pyrophosphatase/phosphodiesterase family | PTM: N-glycosylation, but not furin-cleavage, plays a critical role on secretion and on lysoPLD activity. {ECO:0000250|UniProtKB:Q9R1E6}.; PTM: The interdomain disulfide bond between Cys-414 and Cys-831 is essential for catalytic activity. {ECO:0000250|UniProtKB:Q9R1E6}. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12119361}. | CATALYTIC ACTIVITY: Reaction=1-O-alkyl-sn-glycero-3-phosphoethanolamine + H2O = 1-O-alkyl-sn-glycero-3-phosphate + ethanolamine + H(+); Xref=Rhea:RHEA:15965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57603, ChEBI:CHEBI:58014, ChEBI:CHEBI:76168; EC=3.1.4.39; Evidence={ECO:0000269|PubMed:12119361}; CATALYTIC ACTI... | null | null | null | null | FUNCTION: Hydrolyzes lysophospholipids to produce the signaling molecule lysophosphatidic acid (LPA) in extracellular fluids. Major substrate is lysophosphatidylcholine (PubMed:12119361). Can also act on sphingosylphosphorylcholine producing sphingosine-1-phosphate, a modulator of cell motility. Can hydrolyze, in vitro... | Bos taurus (Bovine) |
A1A4L1 | THEM4_BOVIN | MLRSCTAGLRSIWALRGRREGAPRLSMDLQPARRLFSTEKVIHKDWALPNPSWSKDLKLLFDQFMKKCEDGSWERLPSYKRRSTQESEDFKTYFLDPKLVEEERLSQAQLFTRGFEDGLGFEYVIFKNNDEKRTVCLFQGGPYLQGVPGLLHGGAMATMIDIALGSCTGGAVMTANLNINFKRPVPLCSVVVINSQLDKLEGRKLFLSCNVRSVDEKTLYSEATGLFIKLDPEKSST | 3.1.2.2 | null | fatty acid metabolic process [GO:0006631]; phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0043491]; regulation of mitochondrial membrane permeability involved in apoptotic process [GO:1902108] | cytosol [GO:0005829]; mitochondrial inner membrane [GO:0005743]; mitochondrial intermembrane space [GO:0005758]; mitochondrion [GO:0005739]; ruffle membrane [GO:0032587] | long-chain fatty acyl-CoA hydrolase activity [GO:0052816] | PF03061; | 3.10.129.10; | THEM4/THEM5 thioesterase family | PTM: Phosphorylated. {ECO:0000250|UniProtKB:Q5T1C6}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q5T1C6}. Cell projection, ruffle membrane {ECO:0000250|UniProtKB:Q5T1C6}. Cytoplasm {ECO:0000250|UniProtKB:Q5T1C6}. Mitochondrion {ECO:0000250|UniProtKB:Q5T1C6}. Mitochondrion inner membrane {ECO:0000250|UniProtKB:Q5T1C6}; Peripheral membrane protein {ECO:00002... | CATALYTIC ACTIVITY: Reaction=H2O + hexadecanoyl-CoA = CoA + H(+) + hexadecanoate; Xref=Rhea:RHEA:16645, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379; EC=3.1.2.2; Evidence={ECO:0000250|UniProtKB:Q5T1C6}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16646; Evidence=... | null | null | null | null | FUNCTION: Has acyl-CoA thioesterase activity towards medium and long-chain (C14 to C18) fatty acyl-CoA substrates, and probably plays a role in mitochondrial fatty acid metabolism (By similarity). Plays a role in the apoptotic process, possibly via its regulation of AKT1 activity (By similarity). {ECO:0000250|UniProtKB... | Bos taurus (Bovine) |
A1A4L8 | MOCS3_BOVIN | MAAREEVLALQAEVAQREEELSSLKQRLAAALSTGQESARSVPVSPLPPRAALSREEIRRYSRQLVLPELGMQGQLRLAAAAVLVVGCGGLGCPLAQYLAAAGVGRLGLVDYDVVEASNLARQVLHGEALAGQAKVFSAAAALRRLNSAVECVPYAQALTPATALDLVRRYDVVADCSDNAPTRYLVSDACVLAGRPLVSASALRFEGQLTVYHYGGGPCYRCVFPRPPPAETVTSCADGGVLGAVTGVLGCLQALEVLKTAAGLGPSYSGRLLLFDALRGDFRCIRLRRRRPDCAACGERPTVTDLQDYESFCGSSATD... | 2.7.7.80; 2.8.1.11 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|HAMAP-Rule:MF_03049}; Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_03049}; | Mo-molybdopterin cofactor biosynthetic process [GO:0006777]; protein urmylation [GO:0032447]; tRNA thio-modification [GO:0034227]; tRNA wobble position uridine thiolation [GO:0002143]; tRNA wobble uridine modification [GO:0002098] | cytoplasm [GO:0005737]; cytosol [GO:0005829] | ATP binding [GO:0005524]; metal ion binding [GO:0046872]; molybdopterin-synthase adenylyltransferase activity [GO:0061605]; molybdopterin-synthase sulfurtransferase activity [GO:0061604]; nucleotidyltransferase activity [GO:0016779]; sulfotransferase activity [GO:0008146]; sulfurtransferase activity [GO:0016783]; thios... | PF00581;PF00899; | 3.40.50.720;3.40.250.10; | HesA/MoeB/ThiF family, UBA4 subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03049}. | CATALYTIC ACTIVITY: Reaction=[molybdopterin-synthase sulfur-carrier protein]-C-terminal Gly-Gly + ATP + H(+) = [molybdopterin-synthase sulfur-carrier protein]-C-terminal Gly-Gly-AMP + diphosphate; Xref=Rhea:RHEA:43616, Rhea:RHEA-COMP:12159, Rhea:RHEA-COMP:12202, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ... | null | PATHWAY: tRNA modification; 5-methoxycarbonylmethyl-2-thiouridine-tRNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03049}.; PATHWAY: Cofactor biosynthesis; molybdopterin biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03049}. | null | null | FUNCTION: Plays a central role in 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of cytosolic tRNA(Lys), tRNA(Glu) and tRNA(Gln). Also essential during biosynthesis of the molybdenum cofactor. Acts by mediating the C-terminal thiocarboxylation of sulfur carriers URM1 and MOCS2A. Its N-terminus first activates URM... | Bos taurus (Bovine) |
A1A4N1 | S29A3_BOVIN | MAIISEDDFRHTSNSTYRTASSSLRADQEALLEKLLDRPPPSLQRPEDRFNGTYIIFFSLGIGGLLPWNFFVTAQEYWIFKLSNCSSPAAGEEPKDSDILNYFESYLAVASTVPSVLCLALNFLLVNRVPIRVRVLASLTVMLAIFIVMTVLVKVDTSSWTHSFFTITITCMAILSGTSTIFNSSVFGMTGSFPMRNSQALISGGAMGGTLSAVASLVDLAVASDVTDSTLAFFLTADIFLALCIGLYLLLPRLDYARYYMKPVWPTVFSGEEQLPQDSPSPTSVAPGSSDPQTPPLGPILKKTTGLGFCIIYLFFITSL... | null | null | adenosine transport [GO:0032238]; cytidine transport [GO:0015861]; dopamine transport [GO:0015872]; guanine transmembrane transport [GO:1903716]; inosine transport [GO:0035340]; norepinephrine transport [GO:0015874]; nucleobase transport [GO:0015851]; nucleoside transmembrane transport [GO:1901642]; nucleoside transpor... | Golgi apparatus [GO:0005794]; late endosome membrane [GO:0031902]; lysosomal membrane [GO:0005765]; mitochondrial membrane [GO:0031966]; plasma membrane [GO:0005886] | cytidine transmembrane transporter activity [GO:0015212]; guanine transmembrane transporter activity [GO:0015208]; monoamine transmembrane transporter activity [GO:0008504]; neurotransmitter transmembrane transporter activity [GO:0005326]; nucleobase transmembrane transporter activity [GO:0015205]; nucleoside transmemb... | PF01733; | null | SLC29A/ENT transporter (TC 2.A.57) family | null | SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000250|UniProtKB:Q9BZD2}; Multi-pass membrane protein {ECO:0000305}. Late endosome membrane {ECO:0000250|UniProtKB:Q9BZD2}; Multi-pass membrane protein {ECO:0000305}. Mitochondrion membrane {ECO:0000250|UniProtKB:Q9BZD2}; Multi-pass membrane protein {ECO:0000305}. Cell memb... | CATALYTIC ACTIVITY: Reaction=adenosine(in) = adenosine(out); Xref=Rhea:RHEA:75343, ChEBI:CHEBI:16335; Evidence={ECO:0000250|UniProtKB:Q9BZD2}; CATALYTIC ACTIVITY: Reaction=guanosine(in) = guanosine(out); Xref=Rhea:RHEA:75371, ChEBI:CHEBI:16750; Evidence={ECO:0000250|UniProtKB:Q9BZD2}; CATALYTIC ACTIVITY: Reaction=inosi... | null | null | null | null | FUNCTION: Uniporter that mediates the facilitative transport of nucleoside across lysosomal and mitochondrial membranes. Functions as a non-electrogenic Na(+)-independent transporter. Substrate transport is pH-dependent and enhanced under acidic condition, probably reflecting the location of the transporter in acidic i... | Bos taurus (Bovine) |
A1A4Q9 | NUD16_BOVIN | MAGMRRLELSEALHLGPGWRHACHALLYAPDPGLLFGRIPLRYAVLMQMRFDGRLGFPGGFVDLRDGSLEDGLNRELGEELGEAAGAFRVERADYRSSHAGSRPRVVAHFYTKLLTLEQLTAVEMGAPRARDHGLEVLGLVRVPLYTLRDGVGGLPAFLENTFIGNAREQLLEAVQNLGLLEPGSFARLKISTPP | 3.6.1.62; 3.6.1.64 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q96DE0}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:Q96DE0}; Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000250|UniProtKB:Q96DE0}; Note=Binds 3 or 4 divalent metal cations. Acts specifically on U8 snoRNA wit... | dITP catabolic process [GO:0035863]; mRNA catabolic process [GO:0006402]; NAD-cap decapping [GO:0110155]; negative regulation of rRNA processing [GO:2000233]; positive regulation of cell cycle process [GO:0090068]; sno(s)RNA catabolic process [GO:0016077] | cytoplasm [GO:0005737]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | 5'-(N(7)-methylguanosine 5'-triphospho)-[mRNA] hydrolase activity [GO:0140933]; chloride ion binding [GO:0031404]; cobalt ion binding [GO:0050897]; dIDP phosphatase activity [GO:0097383]; dITP diphosphatase activity [GO:0035870]; IDP phosphatase activity [GO:1990003]; magnesium ion binding [GO:0000287]; manganese ion b... | PF00293; | 3.90.79.10; | Nudix hydrolase family, NUDT16 subfamily | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q96DE0}. Nucleus, nucleolus {ECO:0000250|UniProtKB:Q6TEC1}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q6TEC1}. Cytoplasm {ECO:0000250|UniProtKB:Q96DE0}. Note=Localized predominantly in the cytoplasm. Localized in nucleolus, and in a minor proportion in distinct foc... | CATALYTIC ACTIVITY: Reaction=a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleoside in mRNA + H2O = a 5'-end phospho-ribonucleoside in mRNA + 2 H(+) + N(7)-methyl-GDP; Xref=Rhea:RHEA:67484, Rhea:RHEA-COMP:15692, Rhea:RHEA-COMP:17167, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:63714, ChEBI:CHEBI:138282, ChE... | null | null | null | null | FUNCTION: RNA-binding and decapping enzyme that catalyzes the cleavage of the cap structure of snoRNAs and mRNAs in a metal-dependent manner. Part of the U8 snoRNP complex that is required for the accumulation of mature 5.8S and 28S rRNA. Has diphosphatase activity and removes m7G and/or m227G caps from U8 snoRNA and l... | Bos taurus (Bovine) |
A1A4R9 | AP2A_BOVIN | MLWKLTDNIKYEDCEDRHDGASNGTARLPQLGTVGQSPYTSAPPLSHTPNADFQPPYFPPPYQPIYPQSQDPYSHVNDPYSLNPLHAQPQPQHPGWPGQRQSQESGLLHTHRGLPHQLSGLDPRRDYRRHEDLLHGPHGLGSGLGDLPIHSLPHAIEDVPHVEDPGINIPDQTVIKKGPVSLSKSNSNAVSAIPINKDNLFGGVVNPNEVFCSVPGRLSLLSSTSKYKVTVAEVQRRLSPPECLNASLLGGVLRRAKSKNGGRSLREKLDKIGLNLPAGRRKAANVTLLTSLVEGEAVHLARDFGYVCETEFPAKAVAEF... | null | null | bone morphogenesis [GO:0060349]; cellular response to iron ion [GO:0071281]; embryonic cranial skeleton morphogenesis [GO:0048701]; embryonic forelimb morphogenesis [GO:0035115]; eyelid development in camera-type eye [GO:0061029]; inner ear morphogenesis [GO:0042472]; kidney development [GO:0001822]; negative regulatio... | nucleus [GO:0005634] | DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; DNA-binding transcription repressor activity, RNA polymerase II-specific [GO:0001227]; RNA polymerase II cis-regulatory region sequence-specific DNA ... | PF03299; | null | AP-2 family | PTM: Sumoylated on Lys-10; which inhibits transcriptional activity. {ECO:0000305}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. | null | null | null | null | null | FUNCTION: Sequence-specific DNA-binding protein that interacts with inducible viral and cellular enhancer elements to regulate transcription of selected genes. AP-2 factors bind to the consensus sequence 5'-GCCNNNGGC-3' and activate genes involved in a large spectrum of important biological functions including proper e... | Bos taurus (Bovine) |
A1A4S6 | RHG10_HUMAN | MGLQPLEFSDCYLDSPWFRERIRAHEAELERTNKFIKELIKDGKNLIAATKSLSVAQRKFAHSLRDFKFEFIGDAVTDDERCIDASLREFSNFLKNLEEQREIMALSVTETLIKPLEKFRKEQLGAVKEEKKKFDKETEKNYSLIDKHLNLSAKKKDSHLQEADIQVEQNRQHFYELSLEYVCKLQEIQERKKFEFVEPMLSFFQGMFTFYHQGHELAKDFNHYKMELQINIQNTRNRFEGTRSEVEELMNKIRQNPKDHKRASQFTAEGYLYVQEKRPAPFGSSWVKHYCMYRKAAKKFNMIPFEHRSGGKLGDGEVFF... | null | null | cytoskeleton organization [GO:0007010]; negative regulation of apoptotic process [GO:0043066]; regulation of small GTPase mediated signal transduction [GO:0051056]; signal transduction [GO:0007165] | cytosol [GO:0005829]; endosome membrane [GO:0010008]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886] | GTPase activator activity [GO:0005096] | PF16746;PF00169;PF00620;PF14604; | 1.20.1270.60;2.30.29.30;1.10.555.10;2.30.30.40; | null | PTM: Phosphorylated. Phosphorylated in vitro by constitutive active PKN3. {ECO:0000269|PubMed:11432776}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Cell membrane {ECO:0000250}. Endosome membrane {ECO:0000269|PubMed:32344433}. Note=Association to cell membrane is dependent on PH domain. Colocalized with MICAL1, RAB8A, RAB8B and RAB10 on endosomal tubules (PubMed:32344433). {... | null | null | null | null | null | FUNCTION: GTPase-activating protein that catalyzes the conversion of active GTP-bound Rho GTPases to their inactive GDP-bound form, thus suppressing various Rho GTPase-mediated cellular processes (PubMed:11432776). Also converts Cdc42 to an inactive GDP-bound state (PubMed:11432776). Essential for PTKB2 regulation of c... | Homo sapiens (Human) |
A1A4Y4 | IRGM_HUMAN | MEAMNVEKASADGNLPEVISNIKETLKIVSRTPVNITMAGDSGNGMSTFISALRNTGHEGKASPPTELVKATQRCASYFSSHFSNVVLWDLPGTGSATTTLENYLMEMQFNRYDFIMVASAQFSMNHVMLAKTAEDMGKKFYIVWTKLDMDLSTGALPEVQLLQIRENVLENLQKERVCEY | 3.6.5.- | null | autophagosome assembly [GO:0000045]; autophagosome maturation [GO:0097352]; CAMKK-AMPK signaling cascade [GO:0061762]; cellular response to interferon-beta [GO:0035458]; cellular response to lipopolysaccharide [GO:0071222]; cellular response to virus [GO:0098586]; defense response [GO:0006952]; defense response to bact... | autophagosome membrane [GO:0000421]; cell projection [GO:0042995]; cytosol [GO:0005829]; endoplasmic reticulum membrane [GO:0005789]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; late endosome membrane [GO:0031902]; lysosomal membrane [GO:0005765]; mitochondrial membrane [GO:0031966]; mitochondrion [GO:00... | BH3 domain binding [GO:0051434]; CARD domain binding [GO:0050700]; cardiolipin binding [GO:1901612]; G protein activity [GO:0003925]; GTP binding [GO:0005525]; GTPase activity [GO:0003924]; protein kinase binding [GO:0019901]; protein serine/threonine kinase activator activity [GO:0043539]; protein-macromolecule adapto... | PF05049; | 3.40.50.300; | TRAFAC class dynamin-like GTPase superfamily, IRG family | PTM: Ubiquitinated via 'Lys-63'-linked polyubiquitination in a NOD2-dependent process. 'Lys-63'-linked polyubiquitination is required for interactions with the core autophagy factors. {ECO:0000269|PubMed:25891078}. | SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000269|PubMed:28389568}. Cell membrane {ECO:0000250|UniProtKB:Q60766}. Cytoplasmic vesicle, phagosome membrane {ECO:0000250|UniProtKB:Q60766}. Cytoplasmic vesicle, autophagosome membrane {ECO:0000269|PubMed:29420192}. Lysosome membrane {ECO:0000250|UniProtKB:Q60766}.... | CATALYTIC ACTIVITY: Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; Evidence={ECO:0000269|PubMed:29420192, ECO:0000269|PubMed:30612879}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670; Evidence=... | null | null | null | null | FUNCTION: Immunity-related GTPase that plays important roles in innate immunity and inflammatory response (PubMed:16888103, PubMed:19165925, PubMed:25891078). Acts as a dynamin-like protein that binds to intracellular membranes and promotes remodeling and trafficking of those membranes (By similarity). Required for cle... | Homo sapiens (Human) |
A1A519 | F170A_HUMAN | MKRRQKRKHLENEESQETAEKGGGMSKSQEDALQPGSTRVAKGWSQGVGEVTSTSEYCSCVSSSRKLIHSGIQRIHRDSPQPQSPLAQVQERGETPPRSQHVSLSSYSSYKTCVSSLCVNKEERGMKIYYMQVQMNKGVAVSWETEETLESLEKQPRMEEVTLSEVVRVGTPPSDVSTRNLLSDSEPSGEEKEHEERTESDSLPGSPTVEDTPRAKTPDWLVTMENGFRCMACCRVFTTMEALQEHVQFGIREGFSCHVFHLTMAQLTGNMESESTQDEQEEENGNEKEEEEKPEAKEEEGQPTEEDLGLRRSWSQCPGC... | null | null | fertilization [GO:0009566]; positive regulation of DNA-templated transcription [GO:0045893]; transcription by RNA polymerase II [GO:0006366] | nucleus [GO:0005634] | DNA binding [GO:0003677]; metal ion binding [GO:0046872] | PF17734; | null | FAM170 family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20162441}. | null | null | null | null | null | FUNCTION: Acts as a nuclear transcription factor that positively regulates the expression of heat shock genes. Binds to heat shock promoter elements (HSE). {ECO:0000269|PubMed:20162441}. | Homo sapiens (Human) |
A1A546 | ISX_MOUSE | MAGPTIHRDMEKSSGYCEAPENLGLSFSIEAILKKPTERRSLPRPQSICKEDSRQTTIPGSKLERPPQDQPQEEKKNKRRVRTTFTTEQLQELEKLFHFTHYPDIHVRSQLASRINLPEARVQIWFQNQRAKWRKQEKSGNLSAPQQPGEAGLALPSNMDVSGPVLTPTAMTTLVPPTECCLLSQTQLPSSWFPTQIPLVPWHPWDLQPLPGPLTQHPCVPTFMFPPLHPKWGSICATST | null | null | negative regulation of intestinal absorption [GO:1904479]; regulation of transcription by RNA polymerase II [GO:0006357]; regulation of vitamin A metabolic process [GO:1901738] | nucleus [GO:0005634] | DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; DNA-binding transcription repressor activity, RNA polymerase II-specific [GO:0001227]; RNA polymerase II transcription regulatory region sequence-specific DNA binding [GO:0000977]; sequence-specific DNA binding [GO:0043565] | PF00046; | 1.10.10.60; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108}. | null | null | null | null | null | FUNCTION: Transcription factor that regulates gene expression in intestine. May participate in vitamin A metabolism most likely by regulating BCO1 expression in the intestine. {ECO:0000269|PubMed:16971476, ECO:0000269|PubMed:18093975}. | Mus musculus (Mouse) |
A1A547 | PGRP3_MOUSE | MLVSWDHPKMLPRLLGFLALSLLACGNPTIVSRKEWGASSLTCRVPLSLPVPYLIIEQVTRMQCQDQITCSQVVRVLQSQYVHNKGWCDIAFNFLVGDDGKVYEGVGWYVQGLHTQGYNNVSLGIAFFGSKIGSPSPAALSATEDLIFFAIQNGYLSPKYIQPFLLKEETCLVPQHSEIPKKACPNITPRSAWEARETHCPQMNLPAKFVIIIHTAGKSCNESADCLVRVRDTQSFHIDNQDFCDIAYHFLVGQDGEVYEGVGWNIEGSHTYGYNDIALGIAFMGNFVEKPPNEASLKAAQSLIQCAVAKGYLTSNYLLM... | null | null | antimicrobial humoral immune response mediated by antimicrobial peptide [GO:0061844]; biological process involved in interaction with host [GO:0051701]; defense response to Gram-positive bacterium [GO:0050830]; detection of bacterium [GO:0016045]; innate immune response [GO:0045087]; killing of cells of another organis... | extracellular region [GO:0005576]; protein-containing complex [GO:0032991] | N-acetylmuramoyl-L-alanine amidase activity [GO:0008745]; peptidoglycan binding [GO:0042834]; peptidoglycan immune receptor activity [GO:0016019]; protein heterodimerization activity [GO:0046982]; zinc ion binding [GO:0008270] | PF01510; | 3.40.80.10; | N-acetylmuramoyl-L-alanine amidase 2 family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000250}. | null | null | null | null | null | FUNCTION: Pattern receptor that binds to murein peptidoglycans (PGN) of Gram-positive bacteria. Has bactericidal activity towards Gram-positive bacteria. May kill Gram-positive bacteria by interfering with peptidoglycan biosynthesis. Binds also to Gram-negative bacteria, and has bacteriostatic activity towards Gram-neg... | Mus musculus (Mouse) |
A1A5B4 | ANO9_HUMAN | MQGEESLRILVEPEGDSFPLMEISTCETEASEQWDYVLVAQRHTQRDPRQARQQQFLEELRRKGFHIKVIRDQKQVFFGIRADNSVFGLYRTLLLEPEGPAPHAELAAPTTIPVTTSLRIRIVNFVVMNNKTSAGETFEDLMKDGVFEARFPLHKGEGRLKKTWARWRHMFREQPVDEIRNYFGEKVALYFVWLGWYTYMLVPAALTGLLVFLSGFSLFEASQISKEICEAHDILMCPLGDHSRRYQRLSETCTFAKLTHLFDNDGTVVFAIFMALWATVFLEIWKRQRARVVLHWDLYVWDEEQEEMALQLINCPDYKL... | null | null | calcium activated galactosylceramide scrambling [GO:0061591]; calcium activated phosphatidylcholine scrambling [GO:0061590]; calcium activated phosphatidylserine scrambling [GO:0061589]; chloride transmembrane transport [GO:1902476]; establishment of localization in cell [GO:0051649]; lipid metabolic process [GO:000662... | plasma membrane [GO:0005886] | chloride channel activity [GO:0005254]; chloride channel inhibitor activity [GO:0019869]; intracellular calcium activated chloride channel activity [GO:0005229]; phospholipid scramblase activity [GO:0017128] | PF04547; | null | Anoctamin family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20056604, ECO:0000269|PubMed:22946059}; Multi-pass membrane protein {ECO:0000269|PubMed:20056604, ECO:0000269|PubMed:22946059}. Note=Shows predominantly an intracellular localization with a weak expression in the cell membrane. | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-L-serine(in) = a 1,2-diacyl-sn-glycero-3-phospho-L-serine(out); Xref=Rhea:RHEA:38663, ChEBI:CHEBI:57262; Evidence={ECO:0000250|UniProtKB:P86044}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38664; Evidence={ECO:0000250|UniProtKB:P86044}; CATALYTIC ... | null | null | null | null | FUNCTION: Has calcium-dependent phospholipid scramblase activity; scrambles phosphatidylserine, phosphatidylcholine and galactosylceramide (By similarity). Does not exhibit calcium-activated chloride channel (CaCC) activity (PubMed:22178883). Can inhibit the activity of ANO1 (PubMed:20056604, PubMed:22946059). {ECO:000... | Homo sapiens (Human) |
A1A5C7 | S22AN_HUMAN | MAIDRRREAAGGGPGRQPAPAEENGSLPPGDAAASAPLGGRAGPGGGAEIQPLPPLHPGGGPHPSCCSAAAAPSLLLLDYDGSVLPFLGGLGGGYQKTLVLLTWIPALFIGFSQFSDSFLLDQPNFWCRGAGKGTELAGVTTTGRGGDMGNWTSLPTTPFATAPWEAAGNRSNSSGADGGDTPPLPSPPDKGDNASNCDCRAWDYGIRAGLVQNVVSKWDLVCDNAWKVHIAKFSLLVGLIFGYLITGCIADWVGRRPVLLFSIIFILIFGLTVALSVNVTMFSTLRFFEGFCLAGIILTLYALRIELCPPGKRFMITMV... | null | null | monoatomic ion transport [GO:0006811] | plasma membrane [GO:0005886] | transmembrane transporter activity [GO:0022857] | PF00083; | 1.20.1250.20; | Major facilitator (TC 2.A.1) superfamily, Organic cation transporter (TC 2.A.1.19) family | null | SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. | null | null | null | null | null | null | Homo sapiens (Human) |
A1A5H8 | YES_DANRE | MGCVKSKEDKGPTQKYRPDPTNPTPGSHMGLYGPDPTQMGQSPALKGPTNNYNSRSSGLTPFGGSSSVITPFGGASSSFSTVAVNNPFPGVVTGGVTFFVALYDYEARTSDDLSFSKGDRFQIINNTEGDWWEARSINTGQKGYIPSNYVAPADSIQAEEWYFGKMGRKDAERLLLLPGNQRGTFLVRESETTKGAYSLSIRDWDEMKGDNVKHYKIRKLDSGGYYITTRAQFDTLQKLVKHYTEHADGLCYRLTTVCPTVKPQTQGLAKDAWEIPRESLRLELKLGQGCFGEVWMGTWNGTTKVAIKTLKPGTMSPEAF... | 2.7.10.2 | null | adherens junction maintenance [GO:0034334]; cell differentiation [GO:0030154]; convergent extension involved in gastrulation [GO:0060027]; innate immune response [GO:0045087]; phosphorylation [GO:0016310]; transmembrane receptor protein tyrosine kinase signaling pathway [GO:0007169] | centrosome [GO:0005813]; cytosol [GO:0005829]; extrinsic component of cytoplasmic side of plasma membrane [GO:0031234] | ATP binding [GO:0005524]; non-membrane spanning protein tyrosine kinase activity [GO:0004715]; protein tyrosine kinase activity [GO:0004713]; signaling receptor binding [GO:0005102] | PF07714;PF00017;PF00018; | 3.30.505.10;2.30.30.40;1.10.510.10; | Protein kinase superfamily, Tyr protein kinase family, SRC subfamily | PTM: Autophosphorylation at Tyr-429 maintains enzyme activity. {ECO:0000250}.; PTM: Palmitoylation at Cys-3 promotes membrane localization. {ECO:0000250}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15572145}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Cytoplasm, cytosol {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.2; Evidence={ECO:0000255|PROSITE-ProRule:PRU100... | null | null | null | null | FUNCTION: Non-receptor protein tyrosine kinase that is involved in the regulation of cell growth and survival, apoptosis, cell-cell adhesion, cytoskeleton remodeling, differentiation, G2/M progression and cytokinesis (By similarity). Required for convergent extension cell movements during gastrulation, acting with fyna... | Danio rerio (Zebrafish) (Brachydanio rerio) |
A1A5K2 | CLA1B_XENLA | MEQGMDYWLGQIQQKDVGKRLQVGPDLIEYLLDRQKSIDLEQDQTLLDRMVDGLATSWVNSSNYKVALLGMDILSALVTRLQDRFRTQIGTVLPSLMDRLGDAKDSVRDQDQNLLIKIMEQASNPQYMWERMFSGFKHKNFRTREGVCLCLIATLNVYGANSLTLSKIVPHICNLLGDPNSQVRDAAINCLVEIYRHVGERVRADLSKKGLPQSRLNVIFTKFDEVQKSGTMILSTTDKNFDDEDSVDGNRPSSASSSASSKAPQTARRGVSLGTGRRPGTSSAAPKTGGTAKEGAGALDEEDFIRAFEDAPTVQIYSSR... | null | null | cell division [GO:0051301]; establishment of mitotic spindle localization [GO:0040001]; microtubule anchoring [GO:0034453]; microtubule nucleation [GO:0007020]; microtubule organizing center organization [GO:0031023]; mitotic spindle assembly [GO:0090307]; regulation of microtubule polymerization or depolymerization [G... | basal cortex [GO:0045180]; centrosome [GO:0005813]; cytoplasmic microtubule [GO:0005881]; Golgi apparatus [GO:0005794]; kinetochore [GO:0000776]; mitotic spindle [GO:0072686]; spindle microtubule [GO:0005876] | kinetochore binding [GO:0043515]; microtubule binding [GO:0008017] | PF12348;PF21041; | 1.25.10.10; | CLASP family | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:16390996}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:16390996}. Chromosome, centromere, kinetochore {ECO:0000269|PubMed:16390996}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:16390996}. Golgi apparatu... | null | null | null | null | null | FUNCTION: Microtubule plus-end tracking protein that promotes the stabilization of dynamic microtubules during anaphase. Plays a crucial role in chromatin-induced microtubule formation. May also act at microtubule minus ends. May be involved in the nucleation of noncentrosomal microtubules originating from the trans-Go... | Xenopus laevis (African clawed frog) |
A1A5Q0 | LMOD2_RAT | MSTFGYRRGLSKYESIDEDELLASLTAEELKELERELEDIEPDRNLPVGLRQKSLTEKTPTGNFSREALMAYWEKESQKLLEKERLGECGKLAEEDKEESEEELIFTESNSEVSEEVCTEEEEESTEEEEEEEEEDSEEEEVTTEVTKHINGTVSHNGVNPDNSKPKTFKSQIENINLTNGNSGGTQRNTESPAAIHPCGNPTVIEDALEKIKNNDPDTTEVNLNNIENITTQTLSRFAEALKENTVVKTFSLANTHADDAAAIAIAEMLKVNEHITSVNVESNFITGKGILAIMRALQHNTVLTELRFHNQRHIMGSQV... | null | null | actin filament organization [GO:0007015]; actin filament polymerization [GO:0030041]; actin nucleation [GO:0045010]; muscle contraction [GO:0006936]; myofibril assembly [GO:0030239]; pointed-end actin filament capping [GO:0051694]; positive regulation of actin filament polymerization [GO:0030838]; sarcomere organizatio... | actin filament [GO:0005884]; cardiac myofibril [GO:0097512]; cytoskeleton [GO:0005856]; M band [GO:0031430]; myofibril [GO:0030016]; sarcomere [GO:0030017]; striated muscle thin filament [GO:0005865] | actin binding [GO:0003779]; actin monomer binding [GO:0003785]; tropomyosin binding [GO:0005523] | PF03250; | 3.80.10.10; | Tropomodulin family | null | SUBCELLULAR LOCATION: Cytoplasm, myofibril, sarcomere {ECO:0000269|PubMed:18403713, ECO:0000269|PubMed:20685966}. Cytoplasm, myofibril {ECO:0000269|PubMed:20685966}. Cytoplasm, myofibril, sarcomere, M line {ECO:0000269|PubMed:18403713}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:18403713}. Note=Colocalizes with actin ... | null | null | null | null | null | FUNCTION: Mediates nucleation of actin filaments and thereby promotes actin polymerization (PubMed:18403713). Plays a role in the regulation of actin filament length (By similarity). Required for normal sarcomere organization in the heart, and for normal heart function (PubMed:18403713). {ECO:0000250|UniProtKB:Q6P5Q4, ... | Rattus norvegicus (Rat) |
A1A5Q5 | KDM4D_RAT | MKTKSTCAQNPNCSIMIFRPTKEEFNDFDKYIAYMESQGAHRAGLAKVIPPKEWRARQSYDNISNILIATPLQQVVSGQAGVFTQYHKKKKAMTVGQYRHLANSKKYQTPPHLDFEDLERKYWKNRLYESPIYGADVSGSLFDGKTQQWNVGHLGTIQDLLEQECGIVIEGVNTPYLYFGMWKTSFAWHTEDMDLYSINYLHFGQPKTWYAVPPEHGRRLELLAKELFPGSSQGCQAFLRHKVALISPTVLKENGIPFGRITQEAGEFMVTFPYGYHAGFNHGFNCAEAINFATPRWIDYGKVASQCSCGEARVSFSMDA... | 1.14.11.66 | COFACTOR: Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000250}; Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000250}; | cellular response to ionizing radiation [GO:0071479]; chromatin remodeling [GO:0006338]; DNA damage response [GO:0006974]; double-strand break repair via homologous recombination [GO:0000724]; inflammatory response [GO:0006954]; positive regulation of double-strand break repair via nonhomologous end joining [GO:2001034... | chromatin [GO:0000785]; nucleus [GO:0005634]; pericentric heterochromatin [GO:0005721]; site of double-strand break [GO:0035861] | chromatin DNA binding [GO:0031490]; damaged DNA binding [GO:0003684]; histone demethylase activity [GO:0032452]; histone H3K9 demethylase activity [GO:0032454]; histone H3K9me2/H3K9me3 demethylase activity [GO:0140684]; metal ion binding [GO:0046872] | PF02373;PF02375; | 2.60.120.650; | JHDM3 histone demethylase family | PTM: Ubiquitinated via 'Lys-63'-linked ubiquitin chains. Deubiquitinated by USP14 with the help of TRIM14 leading to stabilization. {ECO:0000250|UniProtKB:Q6B0I6}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00537}. | CATALYTIC ACTIVITY: Reaction=2 2-oxoglutarate + N(6),N(6),N(6)-trimethyl-L-lysyl(9)-[histone H3] + 2 O2 = 2 CO2 + 2 formaldehyde + N(6)-methyl-L-lysyl(9)-[histone H3] + 2 succinate; Xref=Rhea:RHEA:60200, Rhea:RHEA-COMP:15538, Rhea:RHEA-COMP:15542, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:168... | null | null | null | null | FUNCTION: Histone demethylase that specifically demethylates 'Lys-9' of histone H3, thereby playing a central role in histone code. Does not demethylate histone H3 'Lys-4', H3 'Lys-27', H3 'Lys-36' nor H4 'Lys-20'. Demethylates both di- and trimethylated H3 'Lys-9' residue, while it has no activity on monomethylated re... | Rattus norvegicus (Rat) |
A1A5R1 | RFOX2_RAT | MAEGGQAQQQPPQLGPGAAARGMKRESEVELPVPGAGADGPEPGLSKRPRTEEAADEGMQGNQEPTTTPDAMVQPFTTIPFPPPPQNGIPTEYGVPHTQDYAGQTSEHNLTLYGSSQPHGEQSSNSPSNQNGSLTQTEGGAQTDGQQSQTQSSENSESKSTPKRLHVSNIPFRFRDPDLRQMFGQFGKILDVEIIFNERGSKGFGFVTFENSADADRAREKLHGTVVEGRKIEVNNATARVMTNKKMVTPYANGWKLSPVVGAVYGPELYAASSFQADVSLGNEAAVPLSGRGGINTYIPLISLPLVPGFPYPTAATTAA... | null | null | cellular response to angiotensin [GO:1904385]; cellular response to endothelin [GO:1990859]; cellular response to hydrogen peroxide [GO:0070301]; cellular response to retinoic acid [GO:0071300]; dendrite morphogenesis [GO:0048813]; heart development [GO:0007507]; intracellular estrogen receptor signaling pathway [GO:00... | cytoplasm [GO:0005737]; nucleus [GO:0005634] | DNA-binding transcription factor binding [GO:0140297]; mRNA binding [GO:0003729]; RNA binding [GO:0003723]; single-stranded RNA binding [GO:0003727]; transcription corepressor activity [GO:0003714] | PF12414;PF00076; | 3.30.70.330; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. | null | null | null | null | null | FUNCTION: RNA-binding protein that regulates alternative splicing events by binding to 5'-UGCAUGU-3' elements. Prevents binding of U2AF2 to the 3'-splice site. Regulates alternative splicing of tissue-specific exons and of differentially spliced exons during erythropoiesis. Seems to act as a coregulatory factor of ER-a... | Rattus norvegicus (Rat) |
A1A696 | OHK3_ORYSJ | MDEMSCGGGGGGARWKRARVAGMGEGKAGGGGGAAFLGLERVGMVVRMLPVPEKVSARARVVRGSLVAHFRGWRVVRETWWWVLLLWILAGSLGSFYLFLFMNAQSLDKRRDSLASMCDERARMLQDQFNVSMNHLQALAILVSTFHHSKTPSAIDQMTFARYAERTAFERPLTSGVAYAVRVTHGEREQFERQQGWAIKKMYSSSNKKQSSPGPGPGDAAVAEIREPAEEYAPVIFAQDAYKHVISFDMLSGNEDRDNILRARKSGKGVLTAPFKLLNNRLGVILTYTVYKYELPAYARPHERIQAAIGYLGGIFDIQA... | 2.7.13.3 | null | cellular response to abscisic acid stimulus [GO:0071215]; cellular response to cold [GO:0070417]; cellular response to phosphate starvation [GO:0016036]; cellular response to sucrose stimulus [GO:0071329]; cytokinin-activated signaling pathway [GO:0009736]; defense response to bacterium [GO:0042742]; leaf senescence [G... | plasma membrane [GO:0005886] | phosphorelay sensor kinase activity [GO:0000155]; protein histidine kinase binding [GO:0043424] | PF03924;PF02518;PF00512;PF00072; | 1.10.287.130;3.40.50.2300;6.10.250.1190;3.30.450.350;3.30.565.10; | null | PTM: Activation probably requires a transfer of a phosphate group between a His in the transmitter domain and an Asp of the receiver domain. {ECO:0000305}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.; EC=2.7.13.3; Evidence={ECO:0000305}; | null | null | null | null | FUNCTION: Cytokinin receptor related to bacterial two-component regulators. Functions as a histidine kinase and transmits the stress signal to a downstream MAPK cascade. {ECO:0000250|UniProtKB:A1A698}. | Oryza sativa subsp. japonica (Rice) |
A1A698 | OHK4_ORYSJ | MGVGGGGGGGGGEAAAAVAVEGDEAGKGRRWWRVKVKLSTVAVVAWVLASAALWAGLHWRFRRAALHKAEEALVCMCEERARMLQDQFAVSVNHVHALAILVATFHYDKHPPALDQDTFAVYAARTSFERPLLSGVAYAQRVVHADRESFERQQGWIIKTMKHEPSPAQDEYAPVIYSQETISYIEGLDVMSGEEDRENILRARATGKAVLTRPFRLMSNHLGVVLTFPVYLVDLPNDTAVEDRVAATAGYLGGAFDVESLVENLLRQLAGNQELVVNVYDVTNHSNPLVMYGSEVPLGIPSPSHTYTLDFGDPLRKHQM... | 2.7.13.3 | null | cytokinin-activated signaling pathway [GO:0009736]; protein phosphorylation [GO:0006468] | plasma membrane [GO:0005886] | cytokine binding [GO:0019955]; phosphorelay sensor kinase activity [GO:0000155]; protein histidine kinase activity [GO:0004673] | PF03924;PF02518;PF00512;PF00072; | 1.10.287.130;3.40.50.2300;6.10.250.1190;3.30.450.350;3.30.565.10; | null | PTM: Activation probably requires a transfer of a phosphate group between a His in the transmitter domain and an Asp of the receiver domain. {ECO:0000305}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.; EC=2.7.13.3; Evidence={ECO:0000305}; | null | null | null | null | FUNCTION: Cytokinin receptor related to bacterial two-component regulators. Functions as a histidine kinase and transmits the stress signal to a downstream MAPK cascade. {ECO:0000269|PubMed:22642989}. | Oryza sativa subsp. japonica (Rice) |
A1A699 | OHK6_ORYSJ | MGKPEARSGWRNAAAAAWVLVAVACAAYMHWHLRRETMDRAEERLVSMCEERARMLQEQFGVTVNHVHALAILISTFHFEKFPSAIDQDTFAKYTARTSFERPLLNGVAYAQRIFHHEREMFENQQGWIMKTMKRQAAPPQDEYAPVIFSQDTVSYLARIDMMSGEEDRENILRARATGKAVLTNPFRLLGSNHLGVVLTFAVYRPGLAADASVEERVEATAGYLGGAFDVESLVENLLSKLAGNQDIVVNVYDVTNASEPMAMYGPQSPDGKVSLFHVSTLDFGDPFRAHEMRCRYRQKPPLPWSAITNPLGTFVIWML... | 2.7.13.3 | null | cytokinin-activated signaling pathway [GO:0009736]; protein phosphorylation [GO:0006468] | plasma membrane [GO:0005886] | cytokine binding [GO:0019955]; phosphorelay sensor kinase activity [GO:0000155]; protein histidine kinase activity [GO:0004673] | PF03924;PF02518;PF00512;PF00072; | 1.10.287.130;3.40.50.2300;6.10.250.1190;3.30.450.350;3.30.565.10; | null | PTM: Activation probably requires a transfer of a phosphate group between a His in the transmitter domain and an Asp of the receiver domain. {ECO:0000305}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.; EC=2.7.13.3; Evidence={ECO:0000305}; | null | null | null | null | FUNCTION: Cytokinin receptor related to bacterial two-component regulators. Functions as a histidine kinase and transmits the stress signal to a downstream MAPK cascade. {ECO:0000269|PubMed:22642989}. | Oryza sativa subsp. japonica (Rice) |
A1A6H3 | RBSK_ARATH | MMKGISSVSQSINYNPYIEFNRPQLQISTVNPNPAQSRFSRPRSLRVLSLSADPSANRNPKSAVDAHAPPLVVVGSANADIYVEIERLPKEGETISAKTGQTLAGGKGANQAACGAKLMYPTYFVGRLGEDAHGKLIAEALGDDGCGVHLDYVRSVNNEPTGHAVVMLQSDGQNSIIIVGGANMKAWPEIMSDDDLEIVRNAGIVLLQREIPDSINIQVAKAVKKAGVPVILDVGGMDTPIPNELLDSIDILSPNETELSRLTGMPTETFEQISQAVAKCHKLGVKQVLVKLGSKGSALFIQGEKPIQQSIIPAAQVVDT... | 2.7.1.15 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_03215}; Note=Requires a divalent cation, most likely magnesium in vivo, as an electrophilic catalyst to aid phosphoryl group transfer. It is the chelate of the metal and the nucleotide that is the actual substrate. {ECO:0000255|HAMAP-Rul... | D-ribose catabolic process [GO:0019303]; nucleoside metabolic process [GO:0009116] | chloroplast [GO:0009507]; chloroplast nucleoid [GO:0042644]; chloroplast stroma [GO:0009570]; cytosol [GO:0005829]; nucleus [GO:0005634]; plastid nucleoid [GO:0042646] | ATP binding [GO:0005524]; metal ion binding [GO:0046872]; ribokinase activity [GO:0004747] | PF00294; | 3.40.1190.20; | Carbohydrate kinase PfkB family, Ribokinase subfamily | null | SUBCELLULAR LOCATION: Plastid, chloroplast stroma, chloroplast nucleoid {ECO:0000269|PubMed:27601466}. | CATALYTIC ACTIVITY: Reaction=ATP + D-ribose = ADP + D-ribose 5-phosphate + H(+); Xref=Rhea:RHEA:13697, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:47013, ChEBI:CHEBI:78346, ChEBI:CHEBI:456216; EC=2.7.1.15; Evidence={ECO:0000255|HAMAP-Rule:MF_03215, ECO:0000269|PubMed:27601466}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=150 uM for D-ribose {ECO:0000269|PubMed:27601466}; KM=45 uM for ATP {ECO:0000269|PubMed:27601466}; Note=kcat is 2 sec(-1). {ECO:0000269|PubMed:27601466}; | PATHWAY: Carbohydrate metabolism; D-ribose degradation; D-ribose 5-phosphate from beta-D-ribopyranose: step 2/2. {ECO:0000255|HAMAP-Rule:MF_03215}. | null | null | FUNCTION: Catalyzes the phosphorylation of ribose at O-5 in a reaction requiring ATP and magnesium. The resulting D-ribose-5-phosphate can then be used either for sythesis of nucleotides, histidine, and tryptophan, or as a component of the pentose phosphate pathway (By similarity) (PubMed:27601466). Can also use xylose... | Arabidopsis thaliana (Mouse-ear cress) |
A1A6M1 | PTAC5_ARATH | MASSSLPLSLPFPLRSLTSTTRSLPFQCSPLFFSIPSSIVCFSTQNPDREEVRWLREEQRWIREEQRWIREEQRWIRERESLLQEISDLQLRIQSLESRNSQLGNSIPDTISNIAALLQVLKEKNRISESGLSATPMVLESTREQIVEEVEEEEKRVIIAEEKVRVSEPVKKIKRRILKVGSEGDDVQALQEALLKLGFYSGEEDMEFSSFSSGTASAVKTWQASLGVREDGVMTAELLQRLFMDEDVETDKDEASTMKKEEAGNGAVFTSVTQVPEKKQSIVKDQSDREVDVTQNRVFLLGENRWEDPSRLIGRNKPVD... | 5.3.4.1 | null | chloroplast organization [GO:0009658]; plastid transcription [GO:0042793]; regulation of DNA-templated transcription [GO:0006355]; response to heat [GO:0009408]; response to light stimulus [GO:0009416] | chloroplast [GO:0009507]; chloroplast envelope [GO:0009941]; chloroplast nucleoid [GO:0042644]; chloroplast thylakoid [GO:0009534]; chloroplast thylakoid membrane [GO:0009535]; cytosol [GO:0005829] | metal ion binding [GO:0046872]; protein disulfide isomerase activity [GO:0003756] | PF01471; | 1.10.101.10; | null | null | SUBCELLULAR LOCATION: Plastid, chloroplast stroma, chloroplast nucleoid {ECO:0000269|PubMed:23922206}. | CATALYTIC ACTIVITY: Reaction=Catalyzes the rearrangement of -S-S- bonds in proteins.; EC=5.3.4.1; Evidence={ECO:0000269|PubMed:23922206}; | null | null | null | null | FUNCTION: Exhibits zinc-dependent disulfide isomerase activity. Required for seedling and chloroplast development under heat stress, probably by maintaining plastid-encoded RNA polymerase (PEP)-dependent transcription. {ECO:0000269|PubMed:23922206}. | Arabidopsis thaliana (Mouse-ear cress) |
A1ACB2 | HCHA_ECOK1 | MTVQKSKNPQVDIAEDNAFFPSEYSLSQYTSPVSDLDGVDYPKPYRGKHKILVIAADERYLPTDNGKLFSTGNHPIETLLPLYHLHAAGFEFEVATISGLMTKFEYWAMPHKDEKVMPFFEQHKSLFRNPKKLADVVASLNADSEYAAIFVPGGHGALIGLPESEDVAAALQWAIENDRFVISLCHGPAAFLALRHGDNPLNGYSICAFPDAADKQTPEIGYMPGHLTWYFGEELKKMGMNIINDDITGRVHKDRKVLTGDSPFAANALGKLAAQEMLAAYAG | 3.1.2.-; 3.5.1.-; 3.5.1.124 | null | DNA repair [GO:0006281]; methylglyoxal catabolic process to D-lactate via S-lactoyl-glutathione [GO:0019243]; protein repair [GO:0030091] | cytoplasm [GO:0005737] | glyoxalase III activity [GO:0019172]; protein deglycase activity [GO:0036524]; thiolester hydrolase activity [GO:0016790]; zinc ion binding [GO:0008270] | null | 3.40.50.880; | Peptidase C56 family, HchA subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01046}. | CATALYTIC ACTIVITY: Reaction=H2O + N(omega)-(1-hydroxy-2-oxopropyl)-L-arginyl-[protein] = H(+) + L-arginyl-[protein] + lactate; Xref=Rhea:RHEA:49548, Rhea:RHEA-COMP:10532, Rhea:RHEA-COMP:12428, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:29965, ChEBI:CHEBI:131708; EC=3.5.1.124; Evidence={ECO:00... | null | null | null | null | FUNCTION: Protein and nucleotide deglycase that catalyzes the deglycation of the Maillard adducts formed between amino groups of proteins or nucleotides and reactive carbonyl groups of glyoxals. Thus, functions as a protein deglycase that repairs methylglyoxal- and glyoxal-glycated proteins, and releases repaired prote... | Escherichia coli O1:K1 / APEC |
A1B198 | HPBD_PARDP | MKIAEIHVYAHDLPVKDGPYTIASSTVWSLQTTLVKIVADSGLAGWGETCPVGPTYAPSHALGARAALAEMAPGLIGANPLQPLVLRRRMDGLLCGHNYAKAAIDIAAYDLMGKHYGVRVADLLGGVAAERVPSYYATGIGQPDEIARIAAEKVAEGFPRLQIKIGGRPVEIDIETVRKVWERIRGTGTRLAVDGNRSLPSRDALRLSRECPEIPFVLEQPCNTLEEIAAIRGRVQHGIYLDESGEDLSTVIRAAGQGLCDGFGMKLTRIGGLQQMAAFRDICEARALPHSCDDAWGGDIIAAACTHIGATVQPRLNEGV... | 5.1.1.22 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:24520058}; Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000269|PubMed:24520058}; | amino-acid betaine catabolic process [GO:0006579] | null | metal ion binding [GO:0046872]; racemase activity, acting on amino acids and derivatives [GO:0036361]; racemase and epimerase activity, acting on amino acids and derivatives [GO:0016855] | PF13378;PF02746; | 3.20.20.120;3.30.390.10; | Mandelate racemase/muconate lactonizing enzyme family | null | null | CATALYTIC ACTIVITY: Reaction=trans-4-hydroxy-L-proline betaine = cis-4-hydroxy-D-proline betaine; Xref=Rhea:RHEA:47544, ChEBI:CHEBI:85533, ChEBI:CHEBI:85534; EC=5.1.1.22; Evidence={ECO:0000269|PubMed:24056934, ECO:0000269|PubMed:24520058}; CATALYTIC ACTIVITY: Reaction=L-proline betaine = D-proline betaine; Xref=Rhea:RH... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=64 mM for trans-4-hydroxy-L-proline betaine {ECO:0000269|PubMed:24056934}; KM=34 mM for L-proline betaine {ECO:0000269|PubMed:24056934}; KM=7.3 mM for D-proline betaine {ECO:0000269|PubMed:24520058}; Note=kcat is 110 sec(-1) with trans-4-hydroxy-L-proline betaine a... | null | null | null | FUNCTION: Catalyzes the 2-epimerization of trans-4-hydroxy-L-proline betaine (tHyp-B) to cis-4-hydroxy-D-proline betaine (cHyp-B). Is involved in a catabolic pathway that degrades tHyp-B to alpha-ketoglutarate. This pathway would permit the utilization of tHyp-B as a carbon and nitrogen source in the absence of osmotic... | Paracoccus denitrificans (strain Pd 1222) |
A1B2F3 | AZTC_PARDP | MKDWLFRIATCSIMTFSSLAAAQAEPLDVVATFSIIGDFAAKVGGDRIRLNVLVGPDSDTHVYEPRPADAIALAGADVVLTNGLEFEGFLTRLIAASGTDAAVATLTDGVETMEEPGGGHYHYIDGKAVFHAGAHDPHAWQAVPNAKVYVQNIAAAFCAADAEGCAAYQANAARYIGELDALDTEIRAAIAALPQDRRTVVVAHNAFRYFEAAYGVHFLSPQGVSTESEAAAADVAGLIREIRARNASAIFAENISDTRLLEQIAREAGLPLAGTLYSDALSGPDGPASNYIAMMRHNAGAIAAALAAR | null | null | cell adhesion [GO:0007155]; zinc ion transport [GO:0006829] | periplasmic space [GO:0042597] | zinc ion binding [GO:0008270] | PF01297; | 3.40.50.1980; | Bacterial solute-binding protein 9 family | null | SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:25787075}. | null | null | null | null | null | FUNCTION: Part of the ATP-binding cassette (ABC) transport system AztABCD involved in zinc import (PubMed:25787075, PubMed:26468286, PubMed:30353723, PubMed:32781785, PubMed:35128285). Binds zinc with high affinity and specificity and delivers it to the membrane permease for translocation into the cytoplasm (PubMed:257... | Paracoccus denitrificans (strain Pd 1222) |
A1B2F4 | AZTD_PARDP | MLRHLAGASALALTLAGAGFAQDHDHDHEDVTLYRVFVGDHEKGQVTAFDLAEPDHRWTFPTTGQVKLYSVAGGAVVAAVQSDADTVQFIRSGISFHDHGDHRDIEVGDPAAIDASLTGPRPFHLVEHDGKVVLNYDQGGYAEILDGHALAEGKAEPGRFPQARAHHGFVAPLGGNWLSTVASDEKVEGDASVPRLGLQAFDAEGNPAGNLATCTGIHGEAFSGAYLAAGCKEGVLTVKAGANGSEYKLLPYPADLPQGVTTGTLLGSTGIQVFLGNYGPDGLVVIDPVDEPHYRYIKLPFRRVDFALDPAKPSTGYVLT... | null | null | null | periplasmic space [GO:0042597] | zinc chaperone activity [GO:0140827]; zinc ion binding [GO:0008270] | null | null | null | null | SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:26468286, ECO:0000269|PubMed:31428696}. | null | null | null | null | null | FUNCTION: Acts as a zinc chaperone in the AztABCD zinc transport system (PubMed:26468286, PubMed:30353723, PubMed:31428696, PubMed:32781785). Directly transfers one zinc cation to the solute binding protein AztC; the transfer occurs without the formation of a stable interaction (PubMed:26468286, PubMed:31428696, PubMed... | Paracoccus denitrificans (strain Pd 1222) |
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