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stringlengths 6
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E2RU97 | MAEAFTREDYVFMAQLNENAERYDEMVETMRKISGMEGELSDKERNLLSVAYKNVIGPRRAAWRIVSSIEAKEKGRQKPNAKRIEQIRVYRQKIEKELSDICNDILKLLQEQFVPRSTNADAKVFYYKMQGDYYRYLAEYSSGEDKEKIAGSALNAYNSAFEISQQLPPTHPIRLGLALNFSVFYYEILASPDRACELARKAFDAAITDLDKLTEESYKDSTLIMQLLRDNLNLWVTDSAGDDNAEEK | Function: Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner (By similarity). Binds with varying affinity to various synthetic phosphopeptides having a consensus binding motif RSX(pS/pT)XP, called mode-1, where X is any residue and pS/pT is a phosphorylated serine/threonine, and to synthetic phosphopeptides having a consensus binding motif Xp(S/T)X1-2-COOH, called mode-3, in which the phosphorylated residue occupies the penultimate C-terminal position in the target protein, but does not bind to their unphosphorylated counterparts . Binds to synthetic human RAF1 phosphopeptides, but not to their unphosphorylated forms. Binds to difopein, a polypeptide containing a phosphorylation-independent binding motif . Involved in encystation . Involved in cell proliferation. Required for actin and tubulin cytoskeletal organization. Regulates actin filament formation and nuclear size .
PTM: Phosphorylated constitutively throughout the life cycle. Phosphorylation is very high in trophozoites and encysting cells of 12 hours . Phosphorylated during excystation . Phosphorylation promotes its binding to various target proteins and is critical for encystation process. Phosphorylation modification is not influenced by polyglycylation modification .
Sequence Mass (Da): 28576
Sequence Length: 248
Subcellular Location: Cytoplasm
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Q00257 | MKMLSTKATCNSHGQDSSYFLGWEAYENNPFHHTSNPNGIIQMGLAENQLSFDLLESWLSKNPDAASFKRDGKSIFRELALFQDYHGLPAFKKALVEFMAEIRGNKVSFEANNIVLTAGATSANETLMFCLAEAGDAFLLPTPYYPGFDRDLKWRTGVEIVPIHCTSSNGFQITQSALEQAYKDAQTRNLRVKGVLVTNPSNPLGTTMNRDELNLVFDFITSKGIHLISDEIYSGTVFGSPGFVSAMEVLKERSSEDEEVWKRVHIVYSLSKDLGLPGFRVGAIYSNDDMVVAAATKMSSFGLVSSQTQYLLSAMLSDKKFTISYISENQKRLKQRQKMLVSGLQKAGINCLDSNAGLFCWVDMRHLLESDKFESELELWKKIVYEVGLNISPGSSCHCTEPGWFRVCFANMSESTLKLAVRRLKSFVTELRSTTTSNHRNHDNKICKNIKKNIFTKWVFRQSAQEANRKMQAER | Function: Catalyzes the formation of 1-aminocyclopropane-1-carboxylate, a direct precursor of ethylene in higher plants.
Catalytic Activity: S-adenosyl-L-methionine = 1-aminocyclopropane-1-carboxylate + H(+) + S-methyl-5'-thioadenosine
Sequence Mass (Da): 53481
Sequence Length: 475
Pathway: Alkene biosynthesis; ethylene biosynthesis via S-adenosyl-L-methionine; ethylene from S-adenosyl-L-methionine: step 1/2.
EC: 4.4.1.14
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Q7XQ85 | MAYQGIDLLSTKAAGDDHGENSSYFDGWKAYDTNPFDLRHNRGGVIQMGLAENQLSLDLIEEWSKNHPEASICTPEGVSQFKRIANFQDYHGLPEFRKAMAQFMGQVRGGKATFDPDRVVMSGGATGAQETLAFCLANPGEAFLVPTPYYPAFDRDCCWRSGIKLLPIECHSFNDFRLTKEALVSAYDGARRQGISVKGILITNPSNPLGTITDRDTLAMLATFATEHRVHLVCDEIYAGSVFATPEYVSIAEVIERDVPWCNRDLIHVVYSLSKDFGLPGFRVGIIYSYNDAVVAAARRMSSFGLVSSQTQYFLARMLSDEEFIGRFLQESKCRLVARHERFTSGLREVGIGCLRGNAGLFSWMDLRRMLREKTAEAELELWRVIVHQVKLNVSPGTSFHCREPGWFRVCHANMDDETMEVALGRIHDFVRQHQQRRVKAERWAANRQLRLSLPHHHHLSPAHLSSPLALLSPQSPMVRATS | Function: Catalyzes the formation of 1-aminocyclopropane-1-carboxylate, a direct precursor of ethylene in higher plants (Probable). Involved in defense response by producing ethylene after pathogen infection . Involved in several phosphate deficiency-induced adaptive responses, such as lateral root elongation .
Catalytic Activity: S-adenosyl-L-methionine = 1-aminocyclopropane-1-carboxylate + H(+) + S-methyl-5'-thioadenosine
Sequence Mass (Da): 54340
Sequence Length: 483
Pathway: Alkene biosynthesis; ethylene biosynthesis via S-adenosyl-L-methionine; ethylene from S-adenosyl-L-methionine: step 1/2.
EC: 4.4.1.14
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A0A0P0WIY3 | MVGRMLSSPEPTLSTMAMSAAHGEDSPYFAGWRAYDEDPYDPITNPQGVIQMGLAENQVSFDLLEEYMREHPEASDCGAGVRENALFQDYHGLKSFRKAMASFMETIRGGKARFDPDRVVLTAGATAANELLTFILADPGDALLVPTPYYPGFDRDLRWRTGVNIVPVSCDSAAGFQVTAGALRAAYDEAVAAGTRVRGVLITNPSNPLGTTAARGVLEGILDFVARHDMHLISDEIYSGSVFAAPDLVSVAELVDERRRARGGAADAEDIARRVHVVYSLSKDLGLPGFRVGVVYSYNDAVVAAARRMSSFTLVSSQTQRTLAAMLSDAAFAAAYVRSNRDRLRERHARAVAGLRRAGVACLRGANAGLFVWVDMRRLLGDGEATVAGELRLWRRVVAEAKLNISPGSSCHCREPGWFRVCFANMSLETLDVALHRLGCFIKKWEQEQHEN | Function: Catalyzes the formation of 1-aminocyclopropane-1-carboxylate, a direct precursor of ethylene in higher plants.
Catalytic Activity: S-adenosyl-L-methionine = 1-aminocyclopropane-1-carboxylate + H(+) + S-methyl-5'-thioadenosine
Sequence Mass (Da): 49322
Sequence Length: 452
Pathway: Alkene biosynthesis; ethylene biosynthesis via S-adenosyl-L-methionine; ethylene from S-adenosyl-L-methionine: step 1/2.
EC: 4.4.1.14
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P29535 | MDLETSEISNYKSSVVLSKLASNEQHGENSPYFDGWKAYDNDPFHLVNNLNGVIQMGLAENQLSVDLIEEWIKRNPKASICTNDGIESFRRIANFQDYHGLPEFTNAIAKFMEKTRGGKVKFDAKRVVMAGGATGANETLILCLADPGDAFLVPTPYYPGFNRDLRWRSGVQLLPISCKSCNNFKITIEAIEEAYEKGQQANVKIKGLILTNPCNPLGTILDRDTLKKISTFTNEHNIHLVCDEIYAATVFNSPKFVSIAEIINEDNCINKDLVHIVSSLSKDLGFPGFRVGIVYSFNDDVVNCARKMSSFGLVSTQTQHLLAFMLSDDEFVEEFLIESAKRLRERYEKFTRGLEEIGIKCLESNAGVYCWMDLRSLLKEATLDAEMSLWKLIINEVKLNVSPGSSFNCSEVGWFRVCFANIDDQTMEIALARIRMFMDAYNNVNKNGVMKNKHNGRGTTYDLTPQMGSTMKMLLA | Function: Catalyzes the formation of 1-aminocyclopropane-1-carboxylate, a direct precursor of ethylene in higher plants.
Catalytic Activity: S-adenosyl-L-methionine = 1-aminocyclopropane-1-carboxylate + H(+) + S-methyl-5'-thioadenosine
Sequence Mass (Da): 53537
Sequence Length: 476
Pathway: Alkene biosynthesis; ethylene biosynthesis via S-adenosyl-L-methionine; ethylene from S-adenosyl-L-methionine: step 1/2.
EC: 4.4.1.14
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Q37001 | MKQLSTKVTSNGHGQDSSYFLGWEEYEKNPYDEIKNPNGMIQMGLAENQLCFDLIESWLTKNPDAASLKRNGQSIFRELALFQDYHGMPEFKKAMAEFMEEIRGNRVTFDPKKIVLAAGSTSANETLMFCLAEPGDAFLLPTPYYPGFDRDLKWRTGAEIVPIHCSSSNGFQITESALQQAYQQAQKLDLKVKGVLVTNPSNPLGTALTRRELNLLVDFITSKNIHLISDEIYSGTMFGFEQFISVMDVLKDKKLEDTEVSKRVHVVYSLSKDLGLPGFRVGAIYSNDEMIVSAATKMSSFGLVSSQTQYLLSALLSDKKFTSQYLEENQKRLKSRQRRLVSGLESAGITCLRSNAGLFCWVDMRHLLDTNTFEAELDLWKKIVYNVKLNISPGSSCHCTEPGWFRVCFANMSEDTLDLALKRLKTFVESTDCGRMISRSSHERLKSLRKKTVSNWVFRVSWTDRVPDER | Function: 1-aminocyclopropane-1-carboxylate synthase (ACS) enzymes catalyze the conversion of S-adenosyl-L-methionine (SAM) into 1-aminocyclopropane-1-carboxylate (ACC), a direct precursor of ethylene.
PTM: May be processed at its C-terminus.
Catalytic Activity: S-adenosyl-L-methionine = 1-aminocyclopropane-1-carboxylate + H(+) + S-methyl-5'-thioadenosine
Sequence Mass (Da): 53313
Sequence Length: 470
Pathway: Alkene biosynthesis; ethylene biosynthesis via S-adenosyl-L-methionine; ethylene from S-adenosyl-L-methionine: step 1/2.
EC: 4.4.1.14
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A0A0P0UZP7 | MIMSGFHIGIYTSICLYIPLPHLEPWIISSHTPKNLNLLDCLLYCSVASYTAIAYKFCTARLIQSERTRENIMGGKLLPAAAFAGSAPPLSQVATSAAHGEDSPYFAGWKAYDEDPYHAVDNPDGVIQMGLAENQVSFDLLEAYLRDHPEAAGWSTGGAGAGSFRDNALFQDYHGLKSFRKAMASFMGKIRGGKARFDPDHIVLTAGATAANELLTFILANPGDALLIPTPYYPGFDRDLRWRTGVNIVPVRCDSANGFQVTVAALQAAYDEAAAVGMRARAVLITNPSNPLGTTVRRKMLDDILDFVSRNDIHLISDEIYSGSVFAAPDLVSVAELVEARGGDGIAGRVHIVYSLSKDLGLPGFRVGVVYSYNDAVVTAARRMSSFTLVSSQTQKTLAAMLSDEAFAGEYIRTNRRRLRERHEHVVAGLARAGVPCLRGNAGLFVWMDMRRLLLGGGGVGGELRLWEKLLRQAKLNISPGSSCHCSEAGWFRVCFANMSLDTLDLALHRISRFMDTWNGTKQQASCQQQEQQ | Function: Catalyzes the formation of 1-aminocyclopropane-1-carboxylate, a direct precursor of ethylene in higher plants.
Catalytic Activity: S-adenosyl-L-methionine = 1-aminocyclopropane-1-carboxylate + H(+) + S-methyl-5'-thioadenosine
Sequence Mass (Da): 58164
Sequence Length: 533
Pathway: Alkene biosynthesis; ethylene biosynthesis via S-adenosyl-L-methionine; ethylene from S-adenosyl-L-methionine: step 1/2.
EC: 4.4.1.14
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Q9SAR0 | MVAFATEKKQDLNLLSKIASGDGHGENSSYFDGWKAYEENPFHPIDRPDGVIQMGLAENQLCGDLMRKWVLKHPEASICTSEGVNQFSDIAIFQDYHGLPEFRQAVAKFMEKTRNNKVKFDPDRIVMSGGATGAHETVAFCLANPGDGFLVPTPYYPGFDRDLRWRTGVNLVPVTCHSSNGFKITVEALEAAYENARKSNIPVKGLLVTNPSNPLGTTLDRECLKSLVNFTNDKGIHLIADEIYAATTFGQSEFISVAEVIEEIEDCNRDLIHIVYSLSKDMGLPGLRVGIVYSYNDRVVQIARKMSSFGLVSSQTQHLIAKMLSDEEFVDEFIRESKLRLAARHAEITTGLDGLGIGWLKAKAGLFLWMDLRNLLKTATFDSETELWRVIVHQVKLNVSPGGSFHCHEPGWFRVCFANMDHKTMETALERIRVFTSQLEEETKPMAATTMMAKKKKKCWQSNLRLSFSDTRRFDDGFFSPHSPVPPSPLVRAQT | Function: 1-aminocyclopropane-1-carboxylate synthase (ACS) enzymes catalyze the conversion of S-adenosyl-L-methionine (SAM) into 1-aminocyclopropane-1-carboxylate (ACC), a direct precursor of ethylene. Involved in bacterial flagellin-induced ethylene production.
PTM: Phosphorylated on serine residue by MAP kinase (MPK6).
Catalytic Activity: S-adenosyl-L-methionine = 1-aminocyclopropane-1-carboxylate + H(+) + S-methyl-5'-thioadenosine
Sequence Mass (Da): 55524
Sequence Length: 495
Pathway: Alkene biosynthesis; ethylene biosynthesis via S-adenosyl-L-methionine; ethylene from S-adenosyl-L-methionine: step 1/2.
EC: 4.4.1.14
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Q9SNN8 | MRRSGNGGAAKKKKKRSASAASERRPRADGGMRIVVPLQGVVQGRGGLVLGSLIPCALFYFFQLYIKRNRASPPPPPGSPTAASAAAVSPIHRSLSRGLLAPRAALPAISARGASVRDDDSLYYAGLRRCAADPYHPVTNPSGIIQLGLAENYLSLDLVGRWMEEHAAEAASMAGGEDEDERELSIRGLAAYQPYDGILALKMALAGFMRQIMQGSVSFEPSQVVITSGATPAMEILSFCLADPGNAFLVPSPYYPGWDRDIKWRTGIELIPVPCRSTDNFNISITALEIAYNQAKKRGIKVRGVLISNPNNPTGSFVPKQTLHDLLEFAAEKNIHLISDEVFAGSTYGSGKFVSVAEVVDDLEDFDKGRVHIIYGLSKDLSLAGFRVGVIYSYNESIVTAAAKIARFSSVSTPTQRLLVAMLSDQKFISDYLKVNRERLRKMYHLFVDALDQVGIECYKSSGGFYCWADMSKFIRSYSEKGERKLWDRLLEEAKVNVTPGSSCHCIEPGWFRCCFTTLSEHDIPVLVQRLRTITDSHKPNH | Function: Catalyzes the formation of 1-aminocyclopropane-1-carboxylate, a direct precursor of ethylene in higher plants (By similarity). Required for the regulation of starch grain size in endosperm .
Catalytic Activity: S-adenosyl-L-methionine = 1-aminocyclopropane-1-carboxylate + H(+) + S-methyl-5'-thioadenosine
Sequence Mass (Da): 59475
Sequence Length: 542
Pathway: Alkene biosynthesis; ethylene biosynthesis via S-adenosyl-L-methionine; ethylene from S-adenosyl-L-methionine: step 1/2.
Subcellular Location: Plastid
EC: 4.4.1.14
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P27486 | MGSYKGVYDREILSKIATNDGHGENLEYFDGWKAYDRDPYHSTKNSNGVIQMGLAENQLCFDLVTEWLLKNPQASICTNEGVNKFMDIAIFQDYHGLPEFRSAVAKFMGKARDEKVIFNPDRIVMSGGASASETLLFCLANPGDAFLIPSPYYPAFNRDLRWRTGVNLIPFTCSSSNNFKITKEALQSAYEDALKKNIKVKGIIVTNPSNPLGTVLDKDTLKMLLTFVNAKNIHLVCDEIYATTVFNSPSFISVAEVIKDMPHVNQDLVHILYSLSKDMGMPGFRVGIIYSYNDRVVSTARRMSSFGLVSSQTQFMIAALLSDDDFVRRFLVESRDRLFRRHQHFTSELAKIGIGCLQGNAALFVWMDLRHLLDEATVERELKLWRVIINEVKINVSPGSSFLCSEPGWFRVCFANMDNATLDVALNRIRSFVTRGRVDNSTMTTTSARAAATTTTTTTTTTTTTTTTTTIKKKRGQMELRLSFNNRRFEDGLMSPHSILLSPHSPMPQSPLVKART | Function: Catalyzes the formation of 1-aminocyclopropane-1-carboxylate, a direct precursor of ethylene in higher plants.
Catalytic Activity: S-adenosyl-L-methionine = 1-aminocyclopropane-1-carboxylate + H(+) + S-methyl-5'-thioadenosine
Sequence Mass (Da): 58057
Sequence Length: 517
Pathway: Alkene biosynthesis; ethylene biosynthesis via S-adenosyl-L-methionine; ethylene from S-adenosyl-L-methionine: step 1/2.
EC: 4.4.1.14
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P37821 | MRMLSRNATFNSHGQDSSYFLGWQEYEKNPYHEVHNTNGIIQMGLAENQLCFDLLESWLAKNPEAAAFKKNGESIFAELALFQDYHGLPAFKKAMVDFMAEIRGNKVTFDPNHLVLTAGATSANETFIFCLADPGEAVLIPTPYYPGFDRDLKWRTGVEIVPIHCTSSNGFQITETALEEAYQEAEKRNLRVKGVLVTNPSNPLGTTMTRNELYLLLSFVEDKGIHLISDEIYSGTAFSSPSFISVMEVLKDRNCDENSEVWQRVHVVYSLSKDLGLPGFRVGAIYSNDDMVVAAATKMSSFGLVSSQTQHLLSAMLSDKKLTKNYIAENHKRLKQRQKKLVSGLQKSGISCLNGNAGLFCWVDMRHLLRSNTFEAEMELWKKIVYEVHLNISPGSSCHCTEPGWFRVCFANLPERTLDLAMQRLKAFVGEYYNVPEVNGGSQSSHLSHSRRQSLTKWVSRLSFDDRGPIPGR | Function: Catalyzes the formation of 1-aminocyclopropane-1-carboxylate, a direct precursor of ethylene in higher plants . Catalyzes also the conversion of L-vinylglycine (L-VG) to alpha-ketobutyrate and ammonia . Can use S-methylmethionine as substrate .
Catalytic Activity: S-adenosyl-L-methionine = 1-aminocyclopropane-1-carboxylate + H(+) + S-methyl-5'-thioadenosine
Sequence Mass (Da): 53251
Sequence Length: 473
Pathway: Alkene biosynthesis; ethylene biosynthesis via S-adenosyl-L-methionine; ethylene from S-adenosyl-L-methionine: step 1/2.
EC: 1.4.-.-
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P31531 | MGLMDVDQTQLLSKMVIGDGHGEASPYFDGWKAYDENPFHPKENPNGVIQMGLAENQLTSDLVEDWILNNPEASICTPEGINDFRAIANFQDYHGLPEFRNAVAKFMGRTRGNRVTFDPDRIVMSGGATGAHEVTTFCLADPGDAFLVPIPYYPGFDRDLRWRTGIKLVPVMCDSSNNFKLTKQALEDAYEKAKEDNIRVKGLLITNPSNPLGTVMDRNTLRTVMSFINEKRIHLVSDEIYSATVFSHPSFISIAEILEEDTDIECDRNLVHIVYSLSKDMGFPGFRVGIIYSYNDAVVHCARKMSSFGLVSTQTQYLLASMLNDDEFVESFLVESAKRLAQRHRVFTGGLAKVGIKCLQSNAGLFVWMDLRQLLKKPTLDSEMELWRVIIDEVKINVSPGSSFHCTEPGWFRVCYANMDDMAVQIALQRIRNFVLQNKEIMVPNKKHCWHSNLRLSLKTRRFDDIMMSPHSPIPQSPLVKATI | Function: Catalyzes the formation of 1-aminocyclopropane-1-carboxylate, a direct precursor of ethylene in higher plants.
Catalytic Activity: S-adenosyl-L-methionine = 1-aminocyclopropane-1-carboxylate + H(+) + S-methyl-5'-thioadenosine
Sequence Mass (Da): 54731
Sequence Length: 484
Pathway: Alkene biosynthesis; ethylene biosynthesis via S-adenosyl-L-methionine; ethylene from S-adenosyl-L-methionine: step 1/2.
EC: 4.4.1.14
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Q0D1U6 | MLPPALNIPKWLEANSHLLQPPVNNYCVYHPSSPATSGYTVMIVGGPNARTDYHINSTPEFFYQYRGSMLLRTVDRSVSPPAFQDIPIHEGSLFLLPANTPHCPVRFADTVGVVMEVPRAPDATDTMLWFCPNSACKQVVWEKRFVCTDLGTQVKEVVEEFSADLAKRTCAACGTVAESRYKEGELTQPPRFPPE | Function: Catalyzes the oxidative ring opening of 3-hydroxyanthranilate to 2-amino-3-carboxymuconate semialdehyde, which spontaneously cyclizes to quinolinate.
Catalytic Activity: 3-hydroxyanthranilate + O2 = (2Z,4Z)-2-amino-3-carboxymuconate 6-semialdehyde
Sequence Mass (Da): 21701
Sequence Length: 195
Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate from L-kynurenine: step 3/3.
Subcellular Location: Cytoplasm
EC: 1.13.11.6
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C1ERL1 | MSKTLQSFNLLKWIDENKELLKPPVNNKVIWQDSEFIAMILGGPNRRRDFHVDPSDEFFYQIKGECYVECITEEGKREVVTVKEGDVFMLPAMVPHSPHRVANTYGLVIERKRSQGELEDFVWFCDECNHEMHRVRVQLSDIEKQVKEAIHSFNSNKEIRACKNCGHIMPEEVEEWKCE | Cofactor: Binds 2 Fe(2+) ions per subunit.
Function: Catalyzes the oxidative ring opening of 3-hydroxyanthranilate to 2-amino-3-carboxymuconate semialdehyde, which spontaneously cyclizes to quinolinate.
Catalytic Activity: 3-hydroxyanthranilate + O2 = (2Z,4Z)-2-amino-3-carboxymuconate 6-semialdehyde
Sequence Mass (Da): 21057
Sequence Length: 179
Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate from L-kynurenine: step 3/3.
EC: 1.13.11.6
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Q39LI1 | MLKYGTPFNFSRWIDEHAHLLKPPVGNQQVWQDSDFIVTVVGGPNHRTDYHDDPFEEFFYQLRGNAYLHLWIDGKRERVDLKEGDMFLLPPHVRHSPQRPEAGSACLVIERQRPAGVVDGFEWYCDACGHLVHRVEVQLKSIVDDLPPLFDAFYASDTLRRCAHCGHMHPGKAT | Cofactor: Binds 2 Fe(2+) ions per subunit.
Function: Catalyzes the oxidative ring opening of 3-hydroxyanthranilate to 2-amino-3-carboxymuconate semialdehyde, which spontaneously cyclizes to quinolinate.
Catalytic Activity: 3-hydroxyanthranilate + O2 = (2Z,4Z)-2-amino-3-carboxymuconate 6-semialdehyde
Sequence Mass (Da): 20048
Sequence Length: 174
Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate from L-kynurenine: step 3/3.
EC: 1.13.11.6
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Q19341 | MSGVTAIEIPQWIQDNQEDFVPPVCNKCMFSDQLKVFYVGGPNQRKDFHLEEGEEFFFQRKGDMVLKVIEKGQVRDLVIKQGEMFMLPARVEHSPQRFSNSIGLVVERERKNTEFDCVRFLVGSSNITLFERWFYLTDVVKDLPPLIKEFYGSNEFKTGKPGKGTFACNAPYEARWTDLPVPINRKEFIYDHISEVKNGPVRIYGAPEYKTEVMLLGEGSYDLESGTVELLIWLQENTFAVVEESGFTYAMKSETMVRIKPNTKCLLNVKGGFAITIRMPA | Function: Catalyzes the oxidative ring opening of 3-hydroxyanthranilate to 2-amino-3-carboxymuconate semialdehyde, which spontaneously cyclizes to quinolinate.
Catalytic Activity: 3-hydroxyanthranilate + O2 = (2Z,4Z)-2-amino-3-carboxymuconate 6-semialdehyde
Sequence Mass (Da): 32227
Sequence Length: 281
Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate from L-kynurenine: step 3/3.
Subcellular Location: Cytoplasm
EC: 1.13.11.6
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Q59K86 | MVLGQPINIIKWIEENGDLLKPPVNNFCLHRGGFTIMIVGGPNERSDYHINQTPEYFYQFKGTMCLKVVDDGEFKDIFINEGDSFLLPPNVPHNPCRYENTIGIVVEQDRPAGVNDKVRWYCQKCQTVIHEVEFYLTDLGTQIKEAIVKFDADLDARTCKNCGTVNSSRRD | Function: Catalyzes the oxidative ring opening of 3-hydroxyanthranilate to 2-amino-3-carboxymuconate semialdehyde, which spontaneously cyclizes to quinolinate.
Catalytic Activity: 3-hydroxyanthranilate + O2 = (2Z,4Z)-2-amino-3-carboxymuconate 6-semialdehyde
Sequence Mass (Da): 19545
Sequence Length: 171
Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate from L-kynurenine: step 3/3.
Subcellular Location: Cytoplasm
EC: 1.13.11.6
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Q1LCS4 | MLTYGAPFNFPRWIDEHAHLLKPPVGNRQVWQDSDFIVTVVGGPNHRTDYHDDPLEEFFYQLRGNAYLNLWVDGRRERADLKEGDIFLLPPHVRHSPQRPEAGSACLVIERQRPAGMLDGFEWYCDACGHLVHRVEVQLKSIVTDLPPLFESFYASEDKRRCPHCGQVHPGRAA | Cofactor: Binds 2 Fe(2+) ions per subunit.
Function: Catalyzes the oxidative ring opening of 3-hydroxyanthranilate to 2-amino-3-carboxymuconate semialdehyde, which spontaneously cyclizes to quinolinate.
Catalytic Activity: 3-hydroxyanthranilate + O2 = (2Z,4Z)-2-amino-3-carboxymuconate 6-semialdehyde
Sequence Mass (Da): 20028
Sequence Length: 174
Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate from L-kynurenine: step 3/3.
EC: 1.13.11.6
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Q5U3F8 | MTNQSLHVNIDKWIAENETSFLPPVCNKLMFFYQLNIMYVGGPNVRKDYHIEEGEELFYQVRGDMVLKVIENGKHKDVHIREGEMFLLPARIPHSPQRQANTVGLVIERRRLSKETDGLRYFVANSTEVLFERWFYCENLGTQLVPIIKEFMDSKENETGKPDPANPIKPAPYPLNTMNVMTPFSFREWVEKQKPVLASGCPVDMFGEQFETETLLFGSGTSANKRRTDGWIWQLEGLSNVFMNGKEYSLTAGDCLLIFGETEYKWQRSQDCVALYVAQDPDRKRPY | Function: Catalyzes the oxidative ring opening of 3-hydroxyanthranilate to 2-amino-3-carboxymuconate semialdehyde, which spontaneously cyclizes to quinolinate.
Catalytic Activity: 3-hydroxyanthranilate + O2 = (2Z,4Z)-2-amino-3-carboxymuconate 6-semialdehyde
Sequence Mass (Da): 33239
Sequence Length: 287
Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate from L-kynurenine: step 3/3.
Subcellular Location: Cytoplasm
EC: 1.13.11.6
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Q54S02 | MLPPININKWIEENKSLLQPPVGAKLLYTDIDSTFVVMIVGGPNQRTDYHVNETDEFFYQFKGDMILKIVDKDGSFRDINIREGETFILPGNTPHSPQRYRDTIGLVIEKKRSSENIDKLLWFCDNKDCRKLLFSRSFHVDDLDLGKQLTPIINEFYGNEENRTCKHCNHISQKPTVNDYIQ | Function: Catalyzes the oxidative ring opening of 3-hydroxyanthranilate to 2-amino-3-carboxymuconate semialdehyde, which spontaneously cyclizes to quinolinate.
Catalytic Activity: 3-hydroxyanthranilate + O2 = (2Z,4Z)-2-amino-3-carboxymuconate 6-semialdehyde
Sequence Mass (Da): 21210
Sequence Length: 182
Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate from L-kynurenine: step 3/3.
Subcellular Location: Cytoplasm
EC: 1.13.11.6
|
P46952 | MERRLGVRAWVKENRGSFQPPVCNKLMHQEQLKVMFIGGPNTRKDYHIEEGEEVFYQLEGDMVLRVLEQGKHRDVVIRQGEIFLLPARVPHSPQRFANTVGLVVERRRLETELDGLRYYVGDTMDVLFEKWFYCKDLGTQLAPIIQEFFSSEQYRTGKPIPDQLLKEPPFPLSTRSIMEPMSLDAWLDSHHRELQAGTPLSLFGDTYETQVIAYGQGSSEGLRQNVDVWLWQLEGSSVVTMGGRRLSLAPDDSLLVLAGTSYAWERTQGSVALSVTQDPACKKPLG | Function: Catalyzes the oxidative ring opening of 3-hydroxyanthranilate to 2-amino-3-carboxymuconate semialdehyde, which spontaneously cyclizes to quinolinate.
Catalytic Activity: 3-hydroxyanthranilate + O2 = (2Z,4Z)-2-amino-3-carboxymuconate 6-semialdehyde
Sequence Mass (Da): 32556
Sequence Length: 286
Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate from L-kynurenine: step 3/3.
Subcellular Location: Cytoplasm
EC: 1.13.11.6
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P0CAR3 | MICYNHQSSEPPTTXTCSEGQ | Function: Binds to muscle nicotinic acetylcholine receptor (nAChR) and inhibit acetylcholine from binding to the receptor, thereby impairing neuromuscular transmission.
PTM: Contains 4 disulfide bonds.
Sequence Mass (Da): 2325
Sequence Length: 21
Subcellular Location: Secreted
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Q8WXA8 | MEGGWPARQSALLCLTVSLLLQGRGDAFTINCSGFDQHGVDPAVFQAVFDRKAFRPFTNYSIPTRVNISFTLSAILGVDAQLQLLTSFLWMDLVWDNPFINWNPKECVGINKLTVLAENLWLPDIFIVESMDVDQTPSGLTAYISSEGRIKYDKPMRVTSICNLDIFYFPFDQQNCTFTFSSFLYTVDSMLLGMDKEVWEITDTSRKVIQTQGEWELLGINKATPKMSMGNNLYDQIMFYVAIRRRPSLYIINLLVPSSFLVAIDALSFYLPAESENRAPFKITLLLGYNVFLLMMNDLLPASGTPLISVYFALCLSLMVVSLLETVFITYLLHVATTQPPPMPRWLHSLLLHCTSPGRCCPTAPQKGNKGLGLTLTHLPGPKEPGELAGKKLGPRETEPDGGSGWTKTQLMELWVQFSHAMDTLLFRLYLLFMASSILTVIVLWNT | Function: This is one of the several different receptors for 5-hydroxytryptamine (serotonin), a biogenic hormone that functions as a neurotransmitter, a hormone, and a mitogen. This receptor is a ligand-gated ion channel, which when activated causes fast, depolarizing responses. It is a cation-specific, but otherwise relatively nonselective, ion channel.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 50220
Sequence Length: 447
Subcellular Location: Cell membrane
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A5X5Y0 | MEGSWFHRKRFSFYLLLGFLLQGRGVTFTINCSGFGQHGADPTALNSVFNRKPFRPVTNISVPTQVNISFAMSAILDVNEQLHLLSSFLWLEMVWDNPFISWNPEECEGITKMSMAAKNLWLPDIFIIELMDVDKTPKGLTAYVSNEGRIRYKKPMKVDSICNLDIFYFPFDQQNCTLTFSSFLYTVDSMLLDMEKEVWEITDASRNILQTHGEWELLGLSKATAKLSRGGNLYDQIVFYVAIRRRPSLYVINLLVPSGFLVAIDALSFYLPVKSGNRVPFKITLLLGYNVFLLMMSDLLPTSGTPLIGVYFALCLSLMVGSLLETIFITHLLHVATTQPPPLPRWLHSLLLHCNSPGRCCPTAPQKENKGPGLTPTHLPGVKEPEVSAGQMPGPAEAELTGGSEWTRAQREHEAQKQHSVELWLQFSHAMDAMLFRLYLLFMASSIITVICLWNT | Function: This is one of the several different receptors for 5-hydroxytryptamine (serotonin), a biogenic hormone that functions as a neurotransmitter, a hormone, and a mitogen. This receptor is a ligand-gated ion channel, which when activated causes fast, depolarizing responses. It is a cation-specific, but otherwise relatively nonselective, ion channel.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 51438
Sequence Length: 456
Subcellular Location: Cell membrane
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O70528 | MDKLDANVSSKEGFGSVEKVVLLTFLSAVILMAILGNLLVMVAVCRDRQLRKIKTNYFIVSLAFADLLVSVLVMPFGAIELVQDIWVYGEMFCLVRTSLDVLLTTASIFHLCCISLDRYYAICCQPLVYRNKMTPLRIALMLGGCWVIPMFISFLPIMQGWNNIGIVDLIEKRKFNQNSNSTYCVFMVNKPYAITCSVVAFYIPFLLMVLAYYRIYVTAKEHARQIQVLQRAGAPAEGRPQPADQHSTHRMRTETKAAKTLCIIMGCFCLCWAPFFVTNIVDPFIDYTVPGQLWTAFLWLGYINSGLNPFLYAFLNKSFRRAFLIILCCDDERYRRPSILGQTVPCSTTTINGSTHVLRDTVECGGQWESQCHPAASSPLVAAQPIDT | Function: This is one of the several different receptors for 5-hydroxytryptamine (serotonin), a biogenic hormone that functions as a neurotransmitter, a hormone, and a mitogen. The activity of this receptor is mediated by G proteins that stimulate adenylate cyclase (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 43726
Sequence Length: 388
Subcellular Location: Cell membrane
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Q13639 | MDKLDANVSSEEGFGSVEKVVLLTFLSTVILMAILGNLLVMVAVCWDRQLRKIKTNYFIVSLAFADLLVSVLVMPFGAIELVQDIWIYGEVFCLVRTSLDVLLTTASIFHLCCISLDRYYAICCQPLVYRNKMTPLRIALMLGGCWVIPTFISFLPIMQGWNNIGIIDLIEKRKFNQNSNSTYCVFMVNKPYAITCSVVAFYIPFLLMVLAYYRIYVTAKEHAHQIQMLQRAGASSESRPQSADQHSTHRMRTETKAAKTLCIIMGCFCLCWAPFFVTNIVDPFIDYTVPGQVWTAFLWLGYINSGLNPFLYAFLNKSFRRAFLIILCCDDERYRRPSILGQTVPCSTTTINGSTHVLRDAVECGGQWESQCHPPATSPLVAAQPSDT | Function: This is one of the several different receptors for 5-hydroxytryptamine (serotonin), a biogenic hormone that functions as a neurotransmitter, a hormone, and a mitogen. The activity of this receptor is mediated by G proteins that stimulate adenylate cyclase.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 43761
Sequence Length: 388
Subcellular Location: Cell membrane
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P47898 | MDLPVNLTSFSLSTPSPLETNHSLGKDDLRPSSPLLSVFGVLILTLLGFLVAATFAWNLLVLATILRVRTFHRVPHNLVASMAVSDVLVAALVMPLSLVHELSGRRWQLGRRLCQLWIACDVLCCTASIWNVTAIALDRYWSITRHMEYTLRTRKCVSNVMIALTWALSAVISLAPLLFGWGETYSEGSEECQVSREPSYAVFSTVGAFYLPLCVVLFVYWKIYKAAKFRVGSRKTNSVSPISEAVEVKDSAKQPQMVFTVRHATVTFQPEGDTWREQKEQRAALMVGILIGVFVLCWIPFFLTELISPLCSCDIPAIWKSIFLWLGYSNSFFNPLIYTAFNKNYNSAFKNFFSRQH | Function: This is one of the several different receptors for 5-hydroxytryptamine (serotonin), a biogenic hormone that functions as a neurotransmitter, a hormone, and a mitogen. The activity of this receptor is mediated by G proteins.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 40255
Sequence Length: 357
Subcellular Location: Cell membrane
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P35364 | MDLPINLTSFSLSTPSTLEPNRSLDTEALRTSQSFLSAFRVLVLTLLGFLAAATFTWNLLVLATILRVRTFHRVPHNLVASMAISDVLVAVLVMPLSLVHELSGRRWQLGRRLCQLWIACDVLCCTASIWNVTAIALDRYWSITRHLEYTLRARKRVSNVMILLTWALSAVISLAPLLFGWGETYSELSEECQVSREPSYTVFSTVGAFYLPLCVVLFVYWKIYKAAKFRMGSRKTNSVSPIPEAVEVKDASQHPQMVFTVRHATVTFQTEGDTWREQKEQRAALMVGILIGVFVLCWFPFFVTELISPLCSWDIPALWKSIFLWLGYSNSFFNPLIYTAFNRSYSSAFKVFFSKQQ | Function: This is one of the several different receptors for 5-hydroxytryptamine (serotonin), a biogenic hormone that functions as a neurotransmitter, a hormone, and a mitogen. The activity of this receptor is mediated by G proteins.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 40673
Sequence Length: 357
Subcellular Location: Cell membrane
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P50406 | MVPEPGPTANSTPAWGAGPPSAPGGSGWVAAALCVVIALTAAANSLLIALICTQPALRNTSNFFLVSLFTSDLMVGLVVMPPAMLNALYGRWVLARGLCLLWTAFDVMCCSASILNLCLISLDRYLLILSPLRYKLRMTPLRALALVLGAWSLAALASFLPLLLGWHELGHARPPVPGQCRLLASLPFVLVASGLTFFLPSGAICFTYCRILLAARKQAVQVASLTTGMASQASETLQVPRTPRPGVESADSRRLATKHSRKALKASLTLGILLGMFFVTWLPFFVANIVQAVCDCISPGLFDVLTWLGYCNSTMNPIIYPLFMRDFKRALGRFLPCPRCPRERQASLASPSLRTSHSGPRPGLSLQQVLPLPLPPDSDSDSDAGSGGSSGLRLTAQLLLPGEATQDPPLPTRAAAAVNFFNIDPAEPELRPHPLGIPTN | Function: This is one of the several different receptors for 5-hydroxytryptamine (serotonin), a biogenic hormone that functions as a neurotransmitter, a hormone, and a mitogen. The activity of this receptor is mediated by G proteins that stimulate adenylate cyclase. It has a high affinity for tricyclic psychotropic drugs (By similarity). Controls pyramidal neurons migration during corticogenesis, through the regulation of CDK5 activity (By similarity). Is an activator of TOR signaling .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 46954
Sequence Length: 440
Subcellular Location: Cell membrane
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P31388 | MVPEPGPVNSSTPAWGPGPPPAPGGSGWVAAALCVVIVLTAAANSLLIVLICTQPALRNTSNFFLVSLFTSDLMVGLVVMPPAMLNALYGRWVLARGLCLLWTAFDVMCCSASILNLCLISLDRYLLILSPLRYKLRMTAPRALALILGAWSLAALASFLPLLLGWHELGKARTPAPGQCRLLASLPFVLVASGVTFFLPSGAICFTYCRILLAARKQAVQVASLTTGTAGQALETLQVPRTPRPGMESADSRRLATKHSRKALKASLTLGILLGMFFVTWLPFFVANIAQAVCDCISPGLFDVLTWLGYCNSTMNPIIYPLFMRDFKRALGRFLPCVHCPPEHRPALPPPPCGPLTAVPDQASACSRCCLCLCRQTQIQTPLQGAPRACSSQPSFCCLERPPGTPRHPPGPPLWSTSLSQTLWSLRYGRIHSVPP | Function: This is one of the several different receptors for 5-hydroxytryptamine (serotonin), a biogenic hormone that functions as a neurotransmitter, a hormone, and a mitogen. The activity of this receptor is mediated by G proteins that stimulate adenylate cyclase. It has a high affinity for tricyclic psychotropic drugs . Controls pyramidal neurons migration during corticogenesis, through the regulation of CDK5 activity (By similarity). Is an activator of TOR signaling (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 46923
Sequence Length: 436
Subcellular Location: Cell membrane
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P50407 | MMGVNSSGRPDLYGHLHSILLPGRGLPDWSPDGGADPGVSTWTPRLLSGVPEVAASPSPSWDGTWDNVSGCGEQINYGRAEKVVIGSILTLITLLTIAGNCLVVISVCFVKKLRQPSNYLIVSLALADLSVAVAVIPFVSVTDLIGGKWIFGHFFCNVFIAMDVMCCTASIMTLCVISIDRYLGITRPLTYPVRQNGKCMPKMILSVWLLSASITLPPLFGWAQNVNDDKVCLISQDFGYTIYSTAVAFYIPMSVMLFMYYRIYKAARKSAAKHKFPGFPRVQPESIISLNGMVKLQKEVEECANLSRLLKHERKNISIFKREQKAATTLGIIVGAFTVCWLPFFLLSTARPFICGTACSCIPLWVERTCLWLGYANSLINPFIYAFFNRDLRTTYRSLLQCQYRNINRKLSAAGMHEALKLAERPERPECVLQNSDYCRKKGHDS | Function: This is one of the several different receptors for 5-hydroxytryptamine (serotonin), a biogenic hormone that functions as a neurotransmitter, a hormone, and a mitogen. The activity of this receptor is mediated by G proteins that stimulate adenylate cyclase.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 49614
Sequence Length: 446
Subcellular Location: Cell membrane
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Q49700 | MSASVEIFSDSKTMVGAAGKRLASTIQSAVAARERALIVLTGGSSGIGLLRDLATRGQQIDWSRVHLFWGDERYVPKDDDERNEKQARVALLDHIDIPPSQVHPMPAGDGEFGNDLEAAALAYEQLLAAYAAPGYPTPNFDVHLMGMGPEGHINSLFPNTVAVRETSRMVVGVRNSPKPPPERITLTLNAIQRSREVWLMVSGTAKADAVAAAMGGAPSASIPAAGAVGLETTLWLLDEEAAAKIPG | Function: Hydrolysis of 6-phosphogluconolactone to 6-phosphogluconate.
Catalytic Activity: 6-phospho-D-glucono-1,5-lactone + H2O = 6-phospho-D-gluconate + H(+)
Sequence Mass (Da): 26161
Sequence Length: 247
Pathway: Carbohydrate degradation; pentose phosphate pathway; D-ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step 2/3.
EC: 3.1.1.31
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P63336 | MFVWHEYENAAEAAQSLADAVADALQGALDEKGGAVLAVSGGRSPIAFFNALSQKDLDWKNVGITLADERIVPTVHADSNTGLVREYLLKNKAEAAMWIPMVEDGKTETELHPDAVVDYALKHYKQPDVLVLGMGNDGHTASIFPKAPQFQTAIDGSAGVALVHTTPVTAPHERVSMTLDAIAHTGHVFLAIRGEEKKAVFDQAAQGENREYPINLVLNHQGVNCHVFYAE | Function: Hydrolysis of 6-phosphogluconolactone to 6-phosphogluconate.
Catalytic Activity: 6-phospho-D-glucono-1,5-lactone + H2O = 6-phospho-D-gluconate + H(+)
Sequence Mass (Da): 24980
Sequence Length: 231
Pathway: Carbohydrate degradation; pentose phosphate pathway; D-ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step 2/3.
EC: 3.1.1.31
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Q7N6R1 | MKQVVYTASPNSCQIHVWSLNNEGELSLIQTVDVPGEVQPMVVSPDRKHLYVGIRPQFSIVTYQIGSRGELAQQGISSIPGSPTHISTDKQGRFLFSASYSYNNLSVSLIDDQGIVGEPVQVIAGLQAPHSANIDWDNKQLLVPCLKEDRVRIFEMAKEGYLTEKRAEEITTAMGAGPRHMAFHPNQQVIYCINELDSTVDVYRKWEKYRTVQTVDSLPADLAGVRWSADIHITPDGRHLYTSERTSSLISHFVISQDGSNLTLAGHYKTEIQPRGFAIDHSGKYLIASGQKSDHISVSSIDKYTGKLTELTRYPVGKGPMWVTVLAL | Function: Catalyzes the hydrolysis of 6-phosphogluconolactone to 6-phosphogluconate.
Catalytic Activity: 6-phospho-D-glucono-1,5-lactone + H2O = 6-phospho-D-gluconate + H(+)
Sequence Mass (Da): 36427
Sequence Length: 328
Pathway: Carbohydrate degradation; pentose phosphate pathway; D-ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step 2/3.
EC: 3.1.1.31
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Q9X2N2 | MAISELKLPAGVGLQVWGSAAEQARGLAAEVAGRLRSALAEQGQALLVVSGGRSPVAFLEALSEEPLDWSRITVSLADERWVPESHADSNAGLVRRHLLRGEAAKARFIGLYQPAASLEEAAELADHHLHELPLPIDVLVLGMGDDGHTASLFPNSPGLDLAMDPQGTRRCLPMWAPSVPHQRLTLPRAVLAAAKVQLLAIQGQSKLATLNAALAVEDERRMPVRAFLRAPLTIHWYP | Function: Hydrolysis of 6-phosphogluconolactone to 6-phosphogluconate.
Catalytic Activity: 6-phospho-D-glucono-1,5-lactone + H2O = 6-phospho-D-gluconate + H(+)
Sequence Mass (Da): 25571
Sequence Length: 238
Pathway: Carbohydrate degradation; pentose phosphate pathway; D-ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step 2/3.
EC: 3.1.1.31
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P85971 | MAAPAPGLISVFSSPQELGASLAQLVAQRAASCLEGNRGRFALGLSGGSLVSMLARDLPAATAPAGPASFARWTLGFCDERLVPFDHAESTYGLYRTHLLSKLPIPDSQVLTIDPALPVEDAAEDYARKLRQAFQGDTVPVFDLLILGVGPDGHTCSLFPGHPLLQEREKIVAPIGDSPKPPPQRVTLTLPVLNAAQSVIFVATGEGKAAVLKRILEDQESALPAAMVQPRTGALCWFLDEAAARLLSVPFEKHSTL | Function: Hydrolysis of 6-phosphogluconolactone to 6-phosphogluconate.
Catalytic Activity: 6-phospho-D-glucono-1,5-lactone + H2O = 6-phospho-D-gluconate + H(+)
Sequence Mass (Da): 27234
Sequence Length: 257
Pathway: Carbohydrate degradation; pentose phosphate pathway; D-ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step 2/3.
Subcellular Location: Cytoplasm
EC: 3.1.1.31
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Q9Z3S1 | MSANMHIFENPSALAEALADDVGARLAAAIAARGTASLAVSGGSTPKAFFRSLSRRELDWSKVTVTLVDERFVPPENDRSNHRLVADNLLKDGAAEARFVPLYQAAETAEAAAAIASGRTASLGAPLDVVVLGMGTDGHTASFFPGGTRLEEALDPTTPRGVITMEAEGAGEPRLTFTFSSLQDAGYLVLHIEGSGKKEVLAQAEASGDEAEMPIRAMLRRAASPLQIYWAP | Function: Hydrolysis of 6-phosphogluconolactone to 6-phosphogluconate.
Catalytic Activity: 6-phospho-D-glucono-1,5-lactone + H2O = 6-phospho-D-gluconate + H(+)
Sequence Mass (Da): 24408
Sequence Length: 232
Pathway: Carbohydrate degradation; pentose phosphate pathway; D-ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step 2/3.
EC: 3.1.1.31
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Q6AZW2 | MTATITLSTGQRMPTVGLGTWKSAPGQVKQAVLAALDCGYRHIDCAAAYSNEREVGEALTERLGPGKSLRRDDIFVTSKLWNTKHHPDDVEEACRRSLSDLRLSYLDLYLIHWPMAFGRGDELIPRHPDGTIQYDDTHYRDTWAAMEKLVDQGLAKAIGLSNFNAKQIDDILSIAKHKPVVNQVECHPYLVQAELVSHCWSRNLTVTAYSPLGSPDRPWVTPGEALLLDDPRVVGIAKSYNKTPAQVIIRWHIQRGVVCIPKSVTPSRIKQNIEVFDFKLSDEDMRLIESFNRNERFIIPTVIKDGQKIWRDAKHPHFPFIEPY | Function: Catalyzes the NADPH-dependent reduction of a wide variety of carbonyl-containing compounds to their corresponding alcohols. Displays enzymatic activity towards endogenous metabolites such as aromatic and aliphatic aldehydes, ketones, monosaccharides and bile acids. Acts as an aldehyde-detoxification enzyme (By similarity). Displays no reductase activity towards retinoids (By similarity).
Catalytic Activity: a primary alcohol + NADP(+) = an aldehyde + H(+) + NADPH
Sequence Mass (Da): 36762
Sequence Length: 324
Subcellular Location: Cytoplasm
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P02763 | MALSWVLTVLSLLPLLEAQIPLCANLVPVPITNATLDRITGKWFYIASAFRNEEYNKSVQEIQATFFYFTPNKTEDTIFLREYQTRQDQCIYNTTYLNVQRENGTISRYVGGQEHFAHLLILRDTKTYMLAFDVNDEKNWGLSVYADKPETTKEQLGEFYEALDCLRIPKSDVVYTDWKKDKCEPLEKQHEKERKQEEGES | Function: Functions as transport protein in the blood stream. Binds various ligands in the interior of its beta-barrel domain. Also binds synthetic drugs and influences their distribution and availability in the body. Appears to function in modulating the activity of the immune system during the acute-phase reaction.
PTM: N-glycosylated. N-glycan heterogeneity at Asn-33: Hex5HexNAc4 (minor), Hex6HexNAc5 (major) and dHex1Hex6HexNAc5 (minor).
Sequence Mass (Da): 23540
Sequence Length: 201
Domain: Contains a beta-barrel that binds various ligands in its interior.
Subcellular Location: Secreted
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Q7Z1N0 | NNGGRAYIVLSIPNLAHYQLITGFKETLKNKGHPELMDKVGHDFSGNDNIDQVEKAYKKAGVTGHVWQSDGITNCIASFIRGLDRAKKAVANRDSSNGFINKVYYWTVDKYATTREALDAGVDGIMTNYPDVVANVLSESAYKAKFRIATYDDNPWETFKN | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Dermonecrotic toxins cleave the phosphodiester linkage between the phosphate and headgroup of certain phospholipids (sphingolipid and lysolipid substrates), forming an alcohol (often choline) and a cyclic phosphate (By similarity). This toxin acts on sphingomyelin (SM) (By similarity). It may also act on ceramide phosphoethanolamine (CPE), lysophosphatidylcholine (LPC) and lysophosphatidylethanolamine (LPE), but not on lysophosphatidylserine (LPS), and lysophosphatidylglycerol (LPG) (By similarity). It acts by transphosphatidylation, releasing exclusively cyclic phosphate products as second products (By similarity). Induces dermonecrosis, hemolysis, increased vascular permeability, edema, inflammatory response, and platelet aggregation (By similarity).
PTM: Contains 2 disulfide bonds.
Catalytic Activity: an N-(acyl)-sphingosylphosphocholine = an N-(acyl)-sphingosyl-1,3-cyclic phosphate + choline
Sequence Mass (Da): 17957
Sequence Length: 161
Subcellular Location: Secreted
EC: 4.6.1.-
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P69502 | ADNRRPIWVMGHMVNSLAQIDEFVNLGANSIETDVSFDRNCQVLVVFDLKTGHRWQFGGITNKVLNEAAYK | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the hydrolysis of sphingomyelin (By similarity). May also act on other phosphatidyl esters (By similarity).
PTM: Contains 2 disulfide bonds.
Catalytic Activity: an N-(acyl)-sphingosylphosphocholine = an N-(acyl)-sphingosyl-1,3-cyclic phosphate + choline
Sequence Mass (Da): 8051
Sequence Length: 71
Subcellular Location: Secreted
EC: 4.6.1.-
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P0C2T2 | MTDVSRKIRAWGRRLMIGTAAAVVLPGLVGLAGGAATAGAFSRPGLPVEYLQVPSPSMGRDIKVQFQSGGNNSPAVYLLDGLRAQDDYNGWDINTPAFEWYYQSGLSIVMPVGGQSSFYSDWYSPACGKAGCQTYKWETFLTSELPQWLSANRAVKPTGSAAIGLSMAGSSAMILAAYHPQQFIYAGSLSALLDPSQGMGPSLIGLAMGDAGGYKAADMWGPSSDPAWERNDPTQQIPKLVANNTRLWVYCGNGTPNELGGANIPAEFLENFVRSSNLKFQDAYNAAGGHNAVFNFPPNGTHSWEYWGAQLNAMKGDLQSSLGAG | Function: The antigen 85 proteins (FbpA, FbpB, FbpC) are responsible for the high affinity of mycobacteria for fibronectin, a large adhesive glycoprotein, which facilitates the attachment of Mycobacteria to murine alveolar macrophages (AMs) . They also help to maintain the integrity of the cell wall by catalyzing the transfer of mycolic acids to cell wall arabinogalactan and through the synthesis of alpha,alpha-trehalose dimycolate (TDM, cord factor). They catalyze the transfer of a mycoloyl residue from one molecule of alpha,alpha-trehalose monomycolate (TMM) to another TMM, leading to the formation of TDM (By similarity).
Catalytic Activity: 2 alpha,alpha'-trehalose 6-mycolate = alpha,alpha'-trehalose 6,6'-bismycolate + alpha,alpha-trehalose
Sequence Mass (Da): 34581
Sequence Length: 325
Subcellular Location: Secreted
EC: 2.3.1.122
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Q8N5Z0 | MNYARFITAASAARNPSPIRTMTDILSRGPKSMISLAGGLPNPNMFPFKTAVITVENGKTIQFGEEMMKRALQYSPSAGIPELLSWLKQLQIKLHNPPTIHYPPSQGQMDLCVTSGSQQGLCKVFEMIINPGDNVLLDEPAYSGTLQSLHPLGCNIINVASDESGIVPDSLRDILSRWKPEDAKNPQKNTPKFLYTVPNGNNPTGNSLTSERKKEIYELARKYDFLIIEDDPYYFLQFNKFRVPTFLSMDVDGRVIRADSFSKIISSGLRIGFLTGPKPLIERVILHIQVSTLHPSTFNQLMISQLLHEWGEEGFMAHVDRVIDFYSNQKDAILAAADKWLTGLAEWHVPAAGMFLWIKVKGINDVKELIEEKAVKMGVLMLPGNAFYVDSSAPSPYLRASFSSASPEQMDVAFQVLAQLIKESL | Function: Transaminase with broad substrate specificity. Has transaminase activity towards aminoadipate, kynurenine, methionine and glutamate. Shows activity also towards tryptophan, aspartate and hydroxykynurenine. Accepts a variety of oxo-acids as amino-group acceptors, with a preference for 2-oxoglutarate, 2-oxocaproic acid, phenylpyruvate and alpha-oxo-gamma-methiol butyric acid. Can also use glyoxylate as amino-group acceptor (in vitro).
Catalytic Activity: 2-oxoglutarate + glycine = glyoxylate + L-glutamate
Sequence Mass (Da): 47352
Sequence Length: 425
Pathway: Amino-acid degradation; L-lysine degradation via saccharopine pathway; glutaryl-CoA from L-lysine: step 4/6.
Subcellular Location: Mitochondrion
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Q9WVM8 | MNYSRFLTATSLARKPSPIRTTADILSKAPKTLISLAPGSPNPSMFPFKSAAFTVENGSTIRFEDDLIKRALQYSPSYGIPELLSWLKQFQVKLHNPPTVNYPPNQGQMDLCITSGCQDGLCKAFEMLINPGDTILVNEPLFPGTLYAMKPLGCNIINVPSDEHGIIPEGLKKILSQWKPEDSKDPTKKTPKFLYTVPNGNNPTGNSLTGDRKKEIYELARKYDFLIIEDDPYYFLQFSKPWEPTFLSMDVDGRVIRADTFSKTVSSGLRVGFMTGPKTLIQNIVLHTQVSSVHACTLSQLMILQLLHQWGEEGFLAHIDRTIDFYKNQRDSILAAADKWLRGLAEWHVPKAGMFLWIKVKGISDTKQLIEEKAIEREVLLVPGNGFFIDGSAPTSFFRASFSLATPAQMDTAFQRLAQLIKESL | Function: Transaminase with broad substrate specificity. Has transaminase activity towards aminoadipate, kynurenine, methionine and glutamate. Shows activity also towards tryptophan, aspartate and hydroxykynurenine. Accepts a variety of oxo-acids as amino-group acceptors, with a preference for 2-oxoglutarate, 2-oxocaproic acid, phenylpyruvate and alpha-oxo-gamma-methiol butyric acid. Can also use glyoxylate as amino-group acceptor (in vitro) (By similarity).
Catalytic Activity: 2-oxoglutarate + L-kynurenine = H2O + kynurenate + L-glutamate
Sequence Mass (Da): 47598
Sequence Length: 425
Pathway: Amino-acid degradation; L-lysine degradation via saccharopine pathway; glutaryl-CoA from L-lysine: step 4/6.
Subcellular Location: Mitochondrion
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Q64602 | MNYSRFLTATSLARKTSPIRATVEIMSRAPKDIISLAPGSPNPKVFPFKSAVFTVENGSTIRFEGEMFQRALQYSSSYGIPELLSWLKQLQIKLHNPPTVNYSPNEGQMDLCITSGCQDGLCKVFEMLINPGDTVLVNEPLYSGALFAMKPLGCNFISVPSDDCGIIPEGLKKVLSQWKPEDSKDPTKRTPKFLYTIPNGNNPTGNSLTGDRKKEIYELARKYDFLIIEDDPYYFLQFTKPWEPTFLSMDVDGRVIRADSLSKVISSGLRVGFITGPKSLIQRIVLHTQISSLHPCTLSQLMISELLYQWGEEGFLAHVDRAIDFYKNQRDFILAAADKWLRGLAEWHVPKAGMFLWIKVNGISDAKKLIEEKAIEREILLVPGNSFFVDNSAPSSFFRASFSQVTPAQMDLVFQRLAQLIKDVS | Function: Transaminase with broad substrate specificity. Has transaminase activity towards aminoadipate, kynurenine, methionine and glutamate. Shows activity also towards tryptophan, aspartate and hydroxykynurenine. Accepts a variety of oxo-acids as amino-group acceptors, with a preference for 2-oxoglutarate, 2-oxocaproic acid, phenylpyruvate and alpha-oxo-gamma-methiol butyric acid. Can also use glyoxylate as amino-group acceptor (in vitro).
PTM: The N-terminus is blocked.
Catalytic Activity: 2-oxoglutarate + L-kynurenine = H2O + kynurenate + L-glutamate
Sequence Mass (Da): 47784
Sequence Length: 425
Pathway: Amino-acid degradation; L-lysine degradation via saccharopine pathway; glutaryl-CoA from L-lysine: step 4/6.
Subcellular Location: Mitochondrion
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P29806 | MDTTQVTLIHQILAAADERNLPLWIGGGWAIDARLGRVTRKHDDIDLTFPGERRGELEAMVEMLGGRVTEELDYGFLAEIGDELLDCEPAWWADEAYEIAEAPQGSCPEAAEGVIAGRPVRCNSWEAIIWDYFYYADEVPPVDWPTKHIESYRLACTSLGAEKVEVLRAAFRSRYAA | Cofactor: Binds 2 Mg(2+).
Function: Mediates bacterial resistance to kanamycin, gentamicin, dibekacin, sisomicin, neomycin and tobramycin by adenylating the 2''-hydroxyl group of these antibiotics.
Catalytic Activity: nucleoside triphosphate + gentamicin = diphosphate + 2''-nucleotidylgentamicin.
Sequence Mass (Da): 19861
Sequence Length: 177
EC: 2.7.7.46
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P0AE04 | MDTTQVTLIHKILAAADERNLPLWIGGGWAIDARLGRVTRKHDDIDLTFPGERRGELEAIVEMLGGRVMEELDYGFLAEIGDELLDCEPAWWADEAYEIAEAPQGSCPEAAEGVIAGRPVRCNSWEAIIWDYFYYADEVPPVDWPTKHIESYRLACTSLGAEKVEVLRAAFRSRYAA | Cofactor: Binds 2 Mg(2+).
Function: Mediates bacterial resistance to kanamycin, gentamicin and tobramycin by adenylating the 2''-hydroxyl group of these antibiotics.
Catalytic Activity: nucleoside triphosphate + gentamicin = diphosphate + 2''-nucleotidylgentamicin.
Sequence Mass (Da): 19873
Sequence Length: 177
EC: 2.7.7.46
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I0DFJ0 | MSENLQLSAEEMRQLGYQAVDLIIDHMNHLKSKPVSETIDSDILRNKLTESIPENGSDPKELLHFLNRNVFNQITHVDHPHFLAFVPGPNNYVGVVADFLASGFNVFPTAWIAGAGAEQIELTTINWLKSMLGFPDSAEGLFVSGGSMANLTALTVARQAKLNNDIENAVVYFSDQTHFSVDRALKVLGFKHHQICRIETDEHLRISVSALKKQIKEDRTKGKKPFCVIANAGTTNCGAVDSLNELADLCNDEDVWLHADGSYGAPAILSEKGSAMLQGIHRADSLTLDPHKWLFQPYDVGCVLIRNSQYLSKTFRMMPEYIKDSETNVEGEINFGECGIELSRRFRALKVWLSFKVFGVAAFRQAIDHGIMLAEQVEAFLGKAKDWEVVTPAQLGIVTFRYIPSELASTDTINEINKKLVKEITHRGFAMLSTTELKEKVVIRLCSINPRTTTEEMLQIMMKIKALAEEVSISYPCVAE | Function: Involved in bacillamide C biosynthesis (Probable). Catalyzes the decarboxylation of L-tryptophan to tryptamine . The tryptamine obtained is then probably incorporated into the bacillamide C peptide, which is derived from the amino acids alanine, cysteine and tryptophan through nonribosomal peptide synthetase (NRPS) biosynthesis strategy (Probable). L-tryptophan is the best substrate, but the enzyme displays broad substrate specificity for various aromatic amino acids in vitro and it can also catalyze the decarboxylation of L-phenylalanine, 5-hydroxy-L-tryptophan (L-HTP) and L-DOPA, with lower efficiency . Exhibits weak activity with L-tyrosine .
Catalytic Activity: H(+) + L-tryptophan = CO2 + tryptamine
Sequence Mass (Da): 53548
Sequence Length: 480
EC: 4.1.1.28
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Q93YB2 | MDIPIPTRQLFINGDWKAPVLNKRIPVINPATQNIIGDIPAATKEDVDVAVAAAKTALTRNKGADWATASGAVRARYLRAIAAKVTEKKPELAKLESIDCGKPLDEAAWDIDDVAGCFEYYADLAEKLDARQKAPVSLPMDTFKSHVLREPIGVVGLITPWNYPMLMATWKVAPALAAGCAAILKPSELASLTCLELGEICKEVGLPPGVLNILTGLGPEAGAPLATHPDVDKVAFTGSSATGSKIMTAAAQLVKPVSLELGGKSPLVVFEDVDLDKAAEWAIFGCFWTNGQICSATSRLILHESIATEFLNRIVKWIKNIKISDPLEEGCRLGPVVSEGQYEKILKFVSNAKSEGATILTGGSRPEHLKKGFFIEPTIITDVTTNMQIWREEVFGPVLCVKTFSTEEEAIDLANDTVYGLGAAVISNDLERCERVTKAFKAGIVWVNCSQPCFTQAPWGGVKRSGFGRELGEWGLDNYLSVKQVTQYISEEPWGWYQPPAKL | Function: Dehydrogenase that catalyzes the oxidation of several aminoaldehydes . Metabolizes and detoxifies aldehyde products of polyamine degradation to non-toxic amino acids (Probable). Catalyzes the oxidation of 3-aminopropanal to beta-alanine . Catalyzes the oxidation of 4-aminobutanal to 4-aminobutanoate . Catalyzes the oxidation of 4-guanidinobutanal to 4-guanidinobutanoate .
Catalytic Activity: 3-aminopropanal + H2O + NAD(+) = beta-alanine + 2 H(+) + NADH
Sequence Mass (Da): 54496
Sequence Length: 503
Pathway: Amine and polyamine biosynthesis; betaine biosynthesis via choline pathway; betaine from betaine aldehyde: step 1/1.
Subcellular Location: Peroxisome
EC: 1.2.1.-
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P17585 | MRSEQEMMDIFLDFALNDERIRLVTLEGSRTNRNIPPDNFQDYDISYFVTDVESFKENDQWLEIFGKRIMMQKPEDMELFPPELGNWFSYIILFEDGNKLDLTLIPIREAEDYFANNDGLVKVLLDKDSFINYKVTPNDRQYWIKRPTAREFDDCCNEFWMVSTYVVKGLARNEILFAIDHLNEIVRPNLLRMMAWHIASQKGYSFSMGKNYKFMKRYLSNKEWEELMSTYSVNGYQEMWKSLFTCYALFRKYSKAVSEGLAYKYPDYDEGITKYTEGIYCSVK | Function: Mediates bacterial resistance to streptomycin . Adenylates streptomycin on the O-6 residue . Adenylates streptidine on the O-6 residue . Does not act on spectinomycin, neomycin-B or kanamycin . Specific for ATP and GTP nucleotides incorporating a purine ring. No reaction with CTP or UTP .
Catalytic Activity: ATP + streptomycin = 6-O-adenylylstreptomycin + diphosphate
Sequence Mass (Da): 33908
Sequence Length: 284
Subcellular Location: Cytoplasm
EC: 2.7.7.-
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P0DTV9 | MRSEKEVYDIVLNFAKTDKRIRMVTLEGSRTNTNIPPDDFQDFDITFFVTDMDSFTSDDKWLDIFGERLILQKPEDMELFPAVEKGFSYLMLFTDDVKIDLTLLPLELIDEYFTWDKLVKLLLDKDNRIVKPPIPTDIDYHLQKPTQRMFDDCCNEFWNTTTYVVKGLCRKEILFAIDHMNDIVRKELLRMISWLIGIKQGFHFSLGKNYKFMKQYVPEELWERLMSTYNMDSYPHMWESFEQCMALFREVSSEVACQLDYQYPLYDEKISNYVIRQKKKYGIEDDNK | Function: Mediates bacterial resistance to streptomycin, is probably a streptomycin 6-adenylyltransferase.
Catalytic Activity: ATP + streptomycin = 6-O-adenylylstreptomycin + diphosphate
Sequence Mass (Da): 34552
Sequence Length: 288
EC: 2.7.7.-
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P12055 | MRTEKEILNLVSEFAYQRSNVKIIALEGSRTNENIKKDKFQDYDFAFFVSDIEYFTHEESWLSLFGELLFIQKPEDMELFPPDLDYGYSYIMYFKDGIKMDITLINLKDLNRYFSDSDGLVKILVDKDNLVTQEIVPDDSNYWLKKPTEREFYDCCNEFWSVSTYVAKGVFRREILFALDHFNNILRPELLRMISWYIGFNRGFDFSLGKNYKFINKYLTDKEFNMLLATFEMNGYRKTYQSFKLCCELFKYYSNKVSCLGNYNYPNYEKNIENFIRNNYEN | Function: Required for streptomycin resistance . Adenylates streptomycin on the O-6 residue (By similarity).
Catalytic Activity: ATP + streptomycin = 6-O-adenylylstreptomycin + diphosphate
Sequence Mass (Da): 33962
Sequence Length: 282
EC: 2.7.7.-
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Q01752 | MNIWAPAPEPPTKLGRHRQLAPGCGLHVSPIQLGAMSIGDKWHPYGMGTMDKEASFKLLDAFYNAGGNFIDTANVYQDETSEEFIGEWMEARGNRDQMVVATKYSLVYKRGASFEEIPQKTQYVGNSLKSMHISVHDSLRKLRTSYIDIFYVHFWDYTCTIEEVMNGLHNLVAQGKVLYLGVSDTPAWVVSKANNYARMAGKTPFVIYEGEWNITMRDMERDIIPMCIHEGMAIAPWNVLCAGKIRTDAEEERRLKSGEGGRTLLQFDGWLRNETERKVSKALEKVAEEIGAKSITSVAIAYLMQKFPYVFPIVGGRKVEHLYANLEALDISLSPEQMQFLNDTVPFNKGFPYLLFGDGSDYNIVHKAAGHYDKWPAQQAIRPQK | PTM: The N-terminus is blocked.
Catalytic Activity: an aromatic primary alcohol + NADP(+) = an aromatic aldehyde + H(+) + NADPH
Sequence Mass (Da): 43563
Sequence Length: 385
EC: 1.1.1.91
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Q988D4 | MDMAADIASDHFISRRVDIGRITLNVREKGSGPLMLFFHGITSNSAVFEPLMIRLSDRFTTIAVDQRGHGLSDKPETGYEANDYADDIAGLIRTLARGHAILVGHSLGARNSVTAAAKYPDLVRSVVAIDFTPYIETEALDALEARVNAGSQLFEDIKAVEAYLAGRYPNIPADAIRIRAESGYQPVDGGLRPLASSAAMAQTARGLRSDLVPAYRDVTKPVLIVRGESSKLVSAAALAKTSRLRPDLPVVVVPGADHYVNEVSPEITLKAITNFIDA | Function: Catalyzes the final reaction in the degradation of vitamin B6 from (E)-2-(acetamidomethylene)succinate (E-2AMS) to produce succinic semialdehyde, acetate, ammonia and carbon dioxide.
Catalytic Activity: 2-(acetamidomethylene)succinate + H(+) + 2 H2O = acetate + CO2 + NH4(+) + succinate semialdehyde
Sequence Mass (Da): 29896
Sequence Length: 278
Pathway: Cofactor degradation; B6 vitamer degradation.
EC: 3.5.1.29
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D9XDR8 | MAKMSTTHEEIALAGPDGIPAVDLRDLIDAQLYMPFPFERNPHASEAAAGVDHWLSTWGLTDDPAVAAMISCTRPAELAAFNGPDMDSGLLQIAANQIAYQFVFDDRAEDIGRHSPGRLLPMLSESVAILRDGQPPTTPLGAALADLHRQVQERCTPAQAARWAWNSREYVHGLLYEAVAQAHPAPVESGLCRSIRSLIAGVEPFYPLCEAAQRCELAPEELHHPAMRRLSRLSADAAVWIPDLFSAVKEQRAGGMINLALAYRRTHRCSLPAAVTLAVRHINSTIREFEDLYGEVRPELSPSGIGYVEGMAGWIRGCYFWSRTVPRYADTLTAPAGL | Cofactor: Binds 3 Mg(2+) ions per subunit.
Function: Catalyzes the conversion of (2E,6E)-farnesyl diphosphate (FPP) to yield the bicyclic sesquiterpene (1R,6S,7S)-(-)-alpha-amorphene via a probable 1,6-cyclization, which could involve the abstraction of the pyrophosphate from FPP to yield a (R)-bisabolyl cation . The only accepted substrate is (2E,6E)-farnesyl diphosphate (FPP) .
Catalytic Activity: (2E,6E)-farnesyl diphosphate = (-)-alpha-amorphene + diphosphate
Sequence Mass (Da): 37003
Sequence Length: 338
Domain: The Asp-Asp-Xaa-Xaa-Glu (DDXXE) motif is important for the catalytic activity, presumably through binding to Mg(2+).
Pathway: Secondary metabolite biosynthesis; terpenoid biosynthesis.
EC: 4.2.3.162
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D9J100 | MPMRIERDLHMATGNGETSYTKNSRIQEKVMFQIKPVLEEATRAAYSALLPQTMVVADLGCSSGPNTLRFVSEVIGIIARHCKEHDRRHDYPQLQFFLNDLPGNDFNNLFLLIQQFNKSMARNHKGEAAEALPPCYISGLPGSFYTRIFPSESVHLFHSLFSVHWHSQASEQLKDTKNKCLDIYITKNMPPSMVKLFQQQFEKDFSLFLKLRYEELVSGGQMVLTFIGRKHEDVFTGESNHLYGLLAQSLKSLVDEGLVEKEKLESFYLPIYSPSVGEVEAIVKQVGLFNMNHVKVFEINWDPYGDSEGDDVHDSIRSGENVAKCLRAVMEPLVASQFGEHILDKLFKEYARRVAKHLENEKTKHAILVLSIEKAIIHV | Function: Methyltransferase involved in the biosynthesis of methyl anthranilate in response to stresses. Utilizes anthranilic acid as substrate. Produces exclusively the O-methyl ester. Can also use benzoic acid as substrate. Low activity with salicylic acid.
Catalytic Activity: anthranilate + S-adenosyl-L-methionine = O-methyl anthranilate + S-adenosyl-L-homocysteine
Sequence Mass (Da): 43220
Sequence Length: 379
EC: 2.1.1.277
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K9NBS6 | MTEQNLHWLSATEMAASVASNNLSPNEIAEAMIQRVDAVNPSINAIVQFDREQVTRDAAELSRQQEAGEKLGPLHGVPFTIKDLTAVDGLPTTFGMKPMADNIATGNAVVVDRLRGAGGLFLGKTNTPESGYYGGTDNHLYGPTHNPWKLGNSAGGSSGGASAAVAAGLGPLAEGSDGAGSVRIPSALCGVVGLKPTTGVIPQTILAGRFYNWAYHGPITRTVADNALMLDIMAGPDNADPLSIERAETSYVEASKGDVKGLRVAWSPNLGLGHVDPEVLAVCLDALAAFEELGAQITEATPQWGNPSESMWSGIWVPGFASEYDLLDWENQRGEVDDYLIEIMHEAERLTGVDVGRADAFRGDMWDTWTTFMNDYDVLVSPTLASATFPLRQFAPSWLEGASLREQLLDWLFTYPYNMLNNPAITVPAGFTADGRPVGLQIAARHRRDALVLRTAANFEAVRPWADKKPADSLVVA | Function: Amidase with broad substrate specificity, catalyzing the hydrolysis of a wide range of N-substituted amides, and, to a lesser extent, the hydrolysis of non-substituted amides. Acid para-nitroanilides (4'-nitroacetanilide, Gly-pNA, Ala-pNA, Leu-pNA) are the best substrates for this enzyme. N-substituted acrylamides (isopropyl acrylamide, N,N-dimethyl-aminopropyl acrylamide, and methylene-bis-acrylamide), N-acetyl derivatives of glycine, alanine and leucine, and aliphatic amides (acetamide, acrylamide, isobutyramide, n-butyramide, and valeramide) can also be used as substrates but with less efficiency.
Catalytic Activity: a monocarboxylic acid amide + H2O = a monocarboxylate + NH4(+)
Sequence Mass (Da): 51076
Sequence Length: 477
EC: 3.5.1.13
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Q42400 | MKSFNTEGHNHSTAESGDAYTVSDPTKNVDEDGREKRTGTWLTASAHIITAVIGSGVLSLAWAIAQLGWIAGTSILLIFSFITYFTSTMLADCYRAPDPVTGKRNYTYMDVVRSYLGGRKVQLCGVAQYGNLIGVTVGYTITASISLVAVGKSNCFHDKGHTADCTISNYPYMAVFGIIQVILSQIPNFHKLSFLSIMAAVMSFTYATIGIGLAIATVAGGKVGKTSMTGTAVGVDVTAAQKIWRSFQAVGDIAFAYAYATVLIEIQDTLRSSPAENKAMKRASLVGVSTTTFFYILCGCIGYAAFGNNAPGDFLTDFGFFEPFWLIDFANACIAVHLIGAYQVFAQPIFQFVEKKCNRNYPDNKFITSEYSVNVPFLGKFNISLFRLVWRTAYVVITTVVAMIFPFFNAILGLIGAASFWPLTVYFPVEMHIAQTKIKKYSARWIALKTMCYVCLIVSLLAAAGSIAGLISSVKTYKPFRTMHE | Function: Amino acid-proton symporter. Stereospecific transporter with a broad specificity for histidine, glutamate and neutral amino acids. Reduced affinities for asparagine and valine. Involved in amino acid uptake from the apoplastic cavity into the embryo cells for storage protein accumulation and in root amino acid uptake.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 52895
Sequence Length: 485
Subcellular Location: Cell membrane
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P37898 | MSREVLPNNVTPLHYDITLEPNFRAFTFEGSLKIDLQINDHSINSVQINYLEIDFHSARIEGVNAIEVNKNENQQKATLVFPNGTFENLGPSAKLEIIFSGILNDQMAGFYRAKYTDKVTGETKYMATTQMEATDARRAFPCFDEPNLKATFAVTLVSESFLTHLSNMDVRNETIKEGKKYTTFNTTPKMSTYLVAFIVADLRYVESNNFRIPVRVYSTPGDEKFGQFAANLAARTLRFFEDTFNIEYPLPKMDMVAVHEFSAGAMENWGLVTYRVIDLLLDIENSSLDRIQRVAEVIQHELAHQWFGNLVTMDWWEGLWLNEGFATWMSWYSCNKFQPEWKVWEQYVTDNLQRALNLDSLRSSHPIEVPVNNADEINQIFDAISYSKGSSLLRMISKWLGEETFIKGVSQYLNKFKYGNAKTGDLWDALADASGKDVCSVMNIWTKRVGFPVLSVKEHKNKITLTQHRYLSTGDVKEEEDTTIYPILLALKDSTGIDNTLVLNEKSATFELKNEEFFKINGDQSGIFITSYSDERWAKLSKQANLLSVEDRVGLVADAKALSASGYTSTTNFLNLISNWKNEDSFVVWEQIINSLSALKSTWVFEPEDILNALDKFTLDLVLNKLSELGWNIGEDDSFAIQRLKVTLFSAACTSGNEKMQSIAVEMFEEYANGNKQAIPALFKAVVFNTVARLGGENNYEKIFNIYQNPVSSEEKIIALRALGRFEDKELLERTLSYLLDGTVLNQDFYIPMQGIRVHKKGIERLWAWMQEHWDEIAKRLQPGSPVLGGVLTLGLTNFTSFEALEKISAFYSRKVTKGFDQTLAQALDTIRSKAQWVSRDREIVATYLREHEYDQ | Cofactor: Binds 1 zinc ion per subunit.
Function: Positive effector of glycogen accumulation. May be involved in nutrient-sensing.
Sequence Mass (Da): 97663
Sequence Length: 856
EC: 3.4.11.-
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Q38967 | MGETAAANNHRHHHHHGHQVFDVASHDFVPPQPAFKCFDDDGRLKRTGTVWTASAHIITAVIGSGVLSLAWAIAQLGWIAGPAVMLLFSLVTLYSSTLLSDCYRTGDAVSGKRNYTYMDAVRSILGGFKFKICGLIQYLNLFGIAIGYTIAASISMMAIKRSNCFHKSGGKDPCHMSSNPYMIVFGVAEILLSQVPDFDQIWWISIVAAVMSFTYSAIGLALGIVQVAANGVFKGSLTGISIGTVTQTQKIWRTFQALGDIAFAYSYSVVLIEIQDTVRSPPAESKTMKKATKISIAVTTIFYMLCGSMGYAAFGDAAPGNLLTGFGFYNPFWLLDIANAAIVVHLVGAYQVFAQPIFAFIEKSVAERYPDNDFLSKEFEIRIPGFKSPYKVNVFRMVYRSGFVVTTTVISMLMPFFNDVVGILGALGFWPLTVYFPVEMYIKQRKVEKWSTRWVCLQMLSVACLVISVVAGVGSIAGVMLDLKVYKPFKSTY | Function: Amino acid-proton symporter. Stereospecific transporter with a broad specificity for histidine, arginine, glutamate and neutral amino acids, favoring small amino acids such as alanine, asparagine and glutamine. Accepts also large aromatic residues such as in phenlalanine or tyrosine. Has a much higher affinity for basic amino acids as compared with AAP1. May function in xylem-to-phloem transfer and in uptake of amino acids assimilated in the green silique tissue.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 54147
Sequence Length: 493
Subcellular Location: Cell membrane
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P00508 | MALLQSRLLLSAPRRAAATARASSWWSHVEMGPPDPILGVTEAFKRDTNSKKMNLGVGAYRDDNGKSYVLNCVRKAEAMIAAKKMDKEYLPIAGLADFTRASAELALGENSEAFKSGRYVTVQGISGTGSLRVGANFLQRFFKFSRDVYLPKPSWGNHTPIFRDAGLQLQAYRYYDPKTCSLDFTGAMEDISKIPEKSIILLHACAHNPTGVDPRQEQWKELASVVKKRNLLAYFDMAYQGFASGDINRDAWALRHFIEQGIDVVLSQSYAKNMGLYGERAGAFTVICRDAEEAKRVESQLKILIRPMYSNPPMNGARIASLILNTPELRKEWLVEVKGMADRIISMRTQLVSNLKKEGSSHNWQHITDQIGMFCFTGLKPEQVERLTKEFSIYMTKDGRISVAGVASSNVGYLAHAIHQVTK | Function: Catalyzes the irreversible transamination of the L-tryptophan metabolite L-kynurenine to form kynurenic acid (KA). As a member of the malate-aspartate shuttle, it has a key role in the intracellular NAD(H) redox balance. Is important for metabolite exchange between mitochondria and cytosol, and for amino acid metabolism.
Catalytic Activity: 2-oxoglutarate + L-aspartate = L-glutamate + oxaloacetate
Sequence Mass (Da): 47241
Sequence Length: 423
Subcellular Location: Mitochondrion matrix
EC: 2.6.1.1
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Q55F21 | MIRSARLISNIKFGQKNIRQFSTNTNWWANVQKGPEDPILGVSIAYNKDTSPSKINLGVGAYRDENGKPYVLDCVKKADKKIYEANVDHEYAPIVGVAAFNQLAAQLALGEECKHIKEKRIATVQSISGTGALRIAADFFARFLKGKTAYVPNPTWGNHNVIFNDAGIPVKSYGYYNPATCGLNFEAMTKDIAAAPEGSIILLHACAHNPTGVDPTAEQWKKISEICKERGHFVLFDFAYQGFASGSPEKDAAAVRMFVEDGHNIALCQSFAKNFGLYGERIGAFSILTETSDQALNVESQLKILIRPMYSNPPVYGARLVQAILKDKELTNEWRSEVKGMADRIINMREQLVKYLKKHGSTRDWSHITTQIGMFCFTGLTPEQVDRLANEYHIYLTRNGRISIAGINSTNVEYLAKAMAAVTKDN | Function: Plays a key role in amino acid metabolism. Important for metabolite exchange between mitochondria and cytosol (By similarity).
Catalytic Activity: 2-oxoglutarate + L-aspartate = L-glutamate + oxaloacetate
Sequence Mass (Da): 47285
Sequence Length: 426
Subcellular Location: Mitochondrion matrix
EC: 2.6.1.1
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P26563 | SSLLSIPSLSLQYNDKLKVGGNSLRFSKEQSNTFSNAKSSCRISMVAAVNVSRFEGIPMAPPDPILGVSEAFRADTSDAKLNLGVGAYRTEELQPYVLKVVNKAENLMLERGQNKEYLAIEGLAAFNKATAELLLGADNPAIKQQRVATVQGLSGTGSLRLGAALIERYFPGAKVLISAPTWGNHKNIFNDARVPWSEYRYYDPKTVGLDFEGMIEDIKAAPEGTFVLLHGCAHNPTGIDPTPEQWEKIADVIQEKNHIPFFDVAYQGFASGSLDEDAASVRLFVARGLEVLVAQSYSKNLGLYAERIGAINVISSSPESAARVKSQLKRIARPMYSNPPVHGARIVADIVGNPALFDEWKVEMEMMAGRIKNVRQQLYDSISSKDKSGKDWSFILKQIGMFSYTGLNKNQSDNMTNKWHVYMTKDGRISLAGLSLAKCEYLADAIIDSFHYVS | Function: Important for the metabolism of amino acids and Krebs-cycle related organic acids. In plants, it is involved in nitrogen metabolism and in aspects of carbon and energy metabolism.
Catalytic Activity: 2-oxoglutarate + L-aspartate = L-glutamate + oxaloacetate
Sequence Mass (Da): 49916
Sequence Length: 454
Subcellular Location: Mitochondrion matrix
EC: 2.6.1.1
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P00507 | MALLHSGRVLSGMAAAFHPGLAAAASARASSWWTHVEMGPPDPILGVTEAFKRDTNSKKMNLGVGAYRDDNGKPYVLPSVRKAEAQIAGKNLDKEYLPIGGLADFCKASAELALGENSEVLKSGRFVTVQTISGTGALRVGASFLQRFFKFSRDVFLPKPSWGNHTPIFRDAGMQLQGYRYYDPKTCGFDFSGALEDISKIPEQSVLLLHACAHNPTGVDPRPEQWKEMAAVVKKKNLFAFFDMAYQGFASGDGDKDAWAVRHFIEQGINVCLCQSYAKNMGLYGERVGAFTVVCKDAEEAKRVESQLKILIRPLYSNPPLNGARIAATILTSPDLRKQWLQEVKGMADRIISMRTQLVSNLKKEGSSHNWQHITDQIGMFCFTGLKPEQVERLTKEFSVYMTKDGRISVAGVTSGNVGYLAHAIHQVTK | Function: Catalyzes the irreversible transamination of the L-tryptophan metabolite L-kynurenine to form kynurenic acid (KA). As a member of the malate-aspartate shuttle, it has a key role in the intracellular NAD(H) redox balance. Is important for metabolite exchange between mitochondria and cytosol, and for amino acid metabolism. Facilitates cellular uptake of long-chain free fatty acids (By similarity).
Catalytic Activity: 2-oxoglutarate + L-aspartate = L-glutamate + oxaloacetate
Sequence Mass (Da): 47314
Sequence Length: 430
Subcellular Location: Mitochondrion matrix
EC: 2.6.1.1
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O94320 | MLARNLRCLHPNTFASLKTNVSYHGVKCLASQSKRGFKVWADVPMGPPDPIFGITEAYKKDGDVKKMNLGAGTYRDDAGKPYVLPSVRQAETELLSQKLDKEYAPITGIPSFRVQATKLAYGDVYESIKDRLVSAQSISGTGALCIAANFLASFYPSKTIYVSDPTWGNHKNVFSRAGLTVKSYKYYDPATRGLDIKGMLSDLTSAPDGSIILLHACAHNPTGVDPTKAQWDDILKTMQKKNHFALLDMAYQGFASGDFARDAYATRLFASSNVPMLLCQSFAKNMGLYGERAGCFSILANDAEEAARIESQTKILIRALYSNPPVNGARIANHILSNPALREQWAGEVVGMSERLKSMRKALRNILEKDLKNKHSWKHITDQIGMFCYTGLNPQQVDVLAKQYHIYLTKNGRISISGLNTSNVRYFAEAINAVTSN | Function: Plays a key role in amino acid metabolism. Important for metabolite exchange between mitochondria and cytosol (By similarity).
Catalytic Activity: 2-oxoglutarate + L-aspartate = L-glutamate + oxaloacetate
Sequence Mass (Da): 48243
Sequence Length: 437
Subcellular Location: Mitochondrion matrix
EC: 2.6.1.1
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Q01802 | MLRTRLTNCSLWRPYYTSSLSRVPRAPPDKVLGLSEHFKKVKNVNKIDLTVGIYKDGWGKVTTFPSVAKAQKLIESHLELNKNLSYLPITGSKEFQENVMKFLFKESCPQFGPFYLAHDRISFVQTLSGTGALAVAAKFLALFISRDIWIPDPSWANHKNIFQNNGFENIYRYSYYKDGQIDIDGWIEQLKTFAYNNQQENNKNPPCIILHACCHNPTGLDPTKEQWEKIIDTIYELKMVPIVDMAYQGLESGNLLKDAYLLRLCLNVNKYPNWSNGIFLCQSFAKNMGLYGERVGSLSVITPATANNGKFNPLQQKNSLQQNIDSQLKKIVRGMYSSPPGYGSRVVNVVLSDFKLKQQWFKDVDFMVQRLHHVRQEMFDRLGWPDLVNFAQQHGMFYYTRFSPKQVEILRNNYFVYLTGDGRLSLSGVNDSNVDYLCESLEAVSKMDKLA | Function: Plays a key role in amino acid metabolism. Important for metabolite exchange between mitochondria and cytosol (By similarity).
Catalytic Activity: 2-oxoglutarate + L-aspartate = L-glutamate + oxaloacetate
Sequence Mass (Da): 51795
Sequence Length: 451
Subcellular Location: Mitochondrion matrix
EC: 2.6.1.1
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O66728 | MVCPKVVILSEGADLDSLSAAYGVLKLYPDAYLLKPKHLSKKAGEVFKKYRDKFRVIEDLPDCFELVLVDTHFLPEGLPRERIKRIIVYDHHPIGDVKEFEGKIEKVGAATTLVVEEIKEKGIDINPRDATLLAFGIYEDTGNFTYEGTTPRDALALAFLLEKGANLREIREVVMETYTPEQIEAVGKIVQSIEKVFINGRQISFATAVLERYQPDINTLLYEIKDLKESDAFFVIIEAEGKTYVFGRSQSEDVDVGEILSHFGGGGHREAGAVKLENVSAERIKELIKAFLKRKYVKLKVRDIMNTPPFVLEEHVSVKDALTELSERGIANAPVINREGKLVGIISKKALLKLVKLYPDEPIELFVNRDFYTLSPDAPVWEAEEILTKFGQKLIPVVEDGTVVGVVTRLDILQAVKEDLEKLKEKRRKIKVPENIEEIAREVGQIAKEMGLRAYIVGGVVRDILLGKEVWDVDFVVEGNAIELAKELARRHGVNVHPFPEFGTAHLKIGKLKLEFATARRETYPRPGAYPKVEPASLKEDLIRRDFTINAMAISVNLEDYGTLIDYFGGLRDLKDKVIRVLHPVSFIEDPVRILRALRFAGRLNFKLSRSTEKLLKQAVNLGLLKEAPRGRLINEIKLALREDRFLEILELYRKYRVLEEIIEGFQWNEKVLQKLYALRKVVDWHALEFSEERIDYGWLYLLILISNLDYERGKHFLEEMSAPSWVRETYKFMKFKLGSLKEELKKAKENYEVYRLLKPLHTSVLLLLMLEEELKEKIKLYLEKLRKVKLPKEKIEELKKQGLKGKELGERIEELKREIMNKI | Function: tRNA nucleotidyltransferase involved in the synthesis of the tRNA CCA terminus. Adds the terminal adenosine residue to tRNA . Can incorporate CMP into tRNA ending with C74C75 (tRNACC), with very weak efficiency .
Catalytic Activity: a tRNA with a 3' CC end + ATP = a tRNA with a 3' CCA end + diphosphate
Sequence Mass (Da): 94658
Sequence Length: 824
Domain: Adopts a seahorse-like shape and consists of four domains: head, neck, body, and tail.
EC: 2.7.7.-
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Q9RV39 | MFRRRPPLPPFPPGAALVGGAVRDWLRGVRSADYDWAHPDPAAGARALAALVGGAAFPLDEERGYWRVTAGEVQHDFVPLPPNLEDDLRRRDFTVNAIALREGRRLVDPLGGQQDLKRRVLRMVSEDNLRADPLRAWRAARFVTTLSFTLEPQTEQAVRQVAADLKAGRLPFPAWERVRDELHALLRSPDAARGILTLEALGLLDLTLPELREGQGLTQGGFHHLDVFEHGVEALHQLLTRRPDADLLLRWATLLHDVGKPRTFARDPDTGRRSFHGHDRVGAELTTQILTRLKLPGADVKRAAALVKAHMVQLPADDAQARRFVHRRRELLPDLLSLMLADREAARGPSSSELGRFAYMLAMERVLAALEEQPAAPPPLLSGKEVMALLGLTPGPRVGEVLRALAEARALGEVGTPQEARAFVQRWAEETPGS | Function: tRNA nucleotidyltransferase involved in the synthesis of the tRNA CCA terminus. Adds the terminal adenosine residue to tRNA.
Catalytic Activity: a tRNA with a 3' CC end + ATP = a tRNA with a 3' CCA end + diphosphate
Sequence Mass (Da): 47988
Sequence Length: 434
EC: 2.7.7.-
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Q74CU0 | MDVITTHVNADFDCLGAMVAASKLYPDALMVFSGSQEKSMRDLFLKTTGYALPFTRLRDVDFSDITRLVLVDCQHTSRIGRFAEVARRPGVEVHIYDHHPGSSGDIRPSGGEIRDCGSSTTILTRKLMEQGIEVTAVEATLMMLGIYEDTGNLTFPSTTPEDYAAASWLLERGANLNIVSDFVSQELTAEQVALLNDLLKSLRSTPVNGVDIAVAHATLDHYVGDIAVLAHMMRDMQNLDAIFLVVGMGERVYLVARSRIAEVDAGAVMRVFGGGGHATAAAATVRDQTVIQVLGRLNRLLPELVNPVRTAADLMSSPVITLPLATTITEAREILTRYNVNAMPVMDGERMAGIISRRIVEKALYHGLGNLPVDEYMHTEFLRAAPDTPINAIQDYIVGQHRRLVPVFSGERLVGVITRTDLLRYMYTGTQRNAEPVYDLGSENLPVRRREVVHLMNRHLPRPTVAMLRDLGKVGDELELPVYAVGGFVRDLLLGAENDDIDVSVEGDGILFAETVANRVGCRVKSHAKFGTAVIVFPDGLKVDVASTRLEYYETPGALPTVERSSLKMDLYRRDFTINTLAVKLNAEGFGTLIDYFGAYRDLQEKTIRVLHNLSFVEDPTRVFRAIRFEQRLGFPISRHTENLIKNAVKMGFLDKLGGRRLLNELVLILREREPVKAILRMSGLGLLRFIHPDLVLAPNTLQVLDEVKKVITWFDLLYLGEKVETWVVYFLALTSSLPDEGFWGTCTRLSVSEHYREKLIDMRVHGEQVLEVMTRKAARREDVRRSDIYFWLRGLSPEVLLYIMAKTRSDEVRRYVSLYVTQLRGIVTHITGDDLKTLGIPSGPRYREILDRVLTARLNGEAATRDDEMRIAVRLADSA | Function: tRNA nucleotidyltransferase involved in the synthesis of the tRNA CCA terminus. Adds the terminal adenosine residue to tRNA.
Catalytic Activity: a tRNA with a 3' CC end + ATP = a tRNA with a 3' CCA end + diphosphate
Sequence Mass (Da): 98394
Sequence Length: 880
EC: 2.7.7.-
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Q9K8X1 | MSEEHQESYHSDNLIDLMNHTLTNDHLQLLKKLGEMAAKLRMNLFLVGGTVRDMLRGVPGGDLDLVIEGDALAFSQNVANVLGGKVKHHEPFATATWVGAENLKLDIVSARAESYAKPGALPTIRHSHITDDLARRDFSINAMAIHLHPASYGQLVDPFHGRHDLTNGLIRILHSQSFIDDPTRLLRGVRFVSRFNYRFEQKTANLALATQPALTNALANVSPERIVHELKLLCHETDPVSSFSKLEDLHVWQALLGLTFSSSSATHLSRLQEEQNGEPLHWFQAIATVGFLEDNWKASLVPFAITAMEQRFLQNIEDIQKRLTNMTRFSTDYLHKQLYQVPEEPLRFYALSSGEEMQKVLDLYLHQRKQLQPLLTGHDLMELGMKPSPLFKECLLLHECEQLKGTIENKQDALQFAREFFNHKQPL | Function: tRNA nucleotidyltransferase involved in the synthesis of the tRNA CCA terminus. Adds the terminal adenosine residue to tRNA.
Catalytic Activity: a tRNA with a 3' CC end + ATP = a tRNA with a 3' CCA end + diphosphate
Sequence Mass (Da): 48501
Sequence Length: 427
EC: 2.7.7.-
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P74081 | MDLILCHQTADFDVLGAAVGLAKLHPGSRIVLTGGSHPTVRQFLALHRNEFPLIELRSVNPDKIRSLYIVDNQQGDRLGKAADWLTLPHLRQVAIYDHHLNSPRDIEADIWELEAVGASTTLIVEKLQRADISLSMVEASVMALGIHVDTGSLTFTQTTVRDVKALAWLMEQGANLRLIAEYADPGFPPPLQFLFAEAMQNLHKEMVRGYWLGSVLLTTENFVPGLSHLTERLLSLTECDALLLGHVYDKGKDKTKNDEQREKTGVISNQRFSLIGRTRIPDTDLTQLLEPYGGGGHAQAAAVNLRDVEPTTVMAEIYQALQRQIPKPLLARDFMSSPVRTIRPHTTIEQAQRVLFRYGHSGLTVVNQEEKLVGIISRRDLDLALHHGFSHAPVKGYMTRNVKTIAPDTPLPRIEAIMVADDVGRLPVMDQEKLVGIVTRTDVLRQLLQDKQEQSGRFGAPRSGSLRDRPTTPNQNFGQGSLLQLLKTHLPPATWQLLTTAAQQAQTRGWHLYLVGGAVRDLWLRHSQGAEKHQNITFQDIDLVVDGFHATADVGAGVELAQALQGDYPGARLSVHGEFQTAALLWHKDPQLDTLWVDIATARTEFYPYPAANPEVEASSIRQDLYRRDFTINALSIRLTNPNPGKLLDFFGGMNDLQSQQVRVLHANSFIEDPTRIYRAVRFVVRLGFELEPQTETYIRYAIASGVYERWRLTEHPTPALTTRLKAELSIILKAPYWKGALTLLADLDALKCLHAELKLTEQLWWQVRYLSRWLRWFDPERNLEHWLLRLGILLGALPPQEREKIAAGLQLPKATIDGLTNLETIETAIAKGLNSPASPKSSPKSSVIYQTLKDYDRFSLFLVAARGNKLLRKQIWFYFSQLCQVSPFLTGHDLKALGYKPGPQFKQILTDLLNACLDGELGDRQQEEAWLRTHYPLPNKV | Function: tRNA nucleotidyltransferase involved in the synthesis of the tRNA CCA terminus. Adds the terminal adenosine residue to tRNA . Acts as a nucleotidyltransferase and not a poly(A) polymerase .
Catalytic Activity: a tRNA with a 3' CC end + ATP = a tRNA with a 3' CCA end + diphosphate
Sequence Mass (Da): 105906
Sequence Length: 942
EC: 2.7.7.-
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Q9SZR9 | MDNQEVSMDVETPIAKTNDDRSLPFSIFKKANNPVTLKFENLVYTVKLKDSQGCFGKNDKTEERTILKGLTGIVKPGEILAMLGPSGSGKTSLLTALGGRVGEGKGKLTGNISYNNKPLSKAVKRTTGFVTQDDALYPNLTVTETLVFTALLRLPNSFKKQEKIKQAKAVMTELGLDRCKDTIIGGPFLRGVSGGERKRVSIGQEILINPSLLFLDEPTSGLDSTTAQRIVSILWELARGGRTVVTTIHQPSSRLFYMFDKLLLLSEGNPVYFGLGSNAMDYFASVGYSPLVERINPSDFLLDIANGVGSDESQRPEAMKAALVAFYKTNLLDSVINEVKGQDDLCNKPRESSRVATNTYGDWPTTWWQQFCVLLKRGLKQRRHDSFSGMKVAQIFIVSFLCGLLWWQTKISRLQDQIGLLFFISSFWAFFPLFQQIFTFPQERAMLQKERSSGMYRLSPYFLSRVVGDLPMELILPTCFLVITYWMAGLNHNLANFFVTLLVLLVHVLVSGGLGLALGALVMDQKSATTLGSVIMLTFLLAGGYYVQHVPVFISWIKYVSIGYYTYKLLILGQYTANELYPCGDNGKLRCHVGDFEGIKHIGFNSGLVSALALTAMLVVYRVIAYIALTRIGKTKSG | Function: Together with ABCG31, involved in pollen coat deposition of steryl glycosides required for pollen fitness . Together with ABCG11 and ABCG14, required for vascular development by regulating lipid/sterol homeostasis .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 70753
Sequence Length: 638
Subcellular Location: Cell membrane
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A0A384JQG4 | MSNSILNLGSFACLLSLGSIVLWYTISAVLAWYPLRKIPAPSFLATFSYLWLAKTTYSGKQYWIQRDLHKKYGPLVRIGPTDIITDDPEIIKKISSARSSHRRGDWYLTGRFNPYYDNMFTMLEPGPHAKAKARTAAAYSGRDMPDLEVGVNAQLQTLIGLMRSKYASNTVKPHQPLLDLGQVSCFFTMDVITRLAFGEEFGYLKEETDQYGFLGEVRELWPRMSTSADTPWIRKFLFSPPFLKVLGPKPTDKTGFGALMAVAEHHVGKRFAPDAKKKEDMLGSFIRHGLNQQECEVEGLFMIVAGTESTASAIRSTLVHVMTCPRVYQKLKTEINLAVEEGKVSSPIKLEEAKLLPFLQAVIYEGIRMRPPLLGLFPKIVPDGGEEFHGMFIPAGTAICMNTSSLLRSTALFGDDAEVYRPERFMELEKSKRGEMERNVELAFGYGQYMCVGKTVAFMELNKSIFEILRAFDLQLLSPAKPCDVLSYGIFLESNMLVKVTESEGTEYK | Function: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of abscisic acid (ABA), a phytohormone that acts antagonistically toward salicylic acid (SA), jasmonic acid (JA) and ethylene (ETH) signaling, to impede plant defense responses . The first step of the pathway catalyzes the reaction from farnesyl diphosphate to alpha-ionylideneethane performed by the alpha-ionylideneethane synthase aba3 via a three-step reaction mechanism involving 2 neutral intermediates, beta-farnesene and allofarnesene . The cytochrome P450 monooxygenase aba1 might then be involved in the conversion of alpha-ionylideneethane to alpha-ionylideneacetic acid (Probable). Alpha-ionylideneacetic acid is further converted to abscisic acid in 2 steps involving the cytochrome P450 monooxygenase aba2 and the short-chain dehydrogenase/reductase aba4, via the intermediates 1'-deoxy-ABA or 1',4'-trans-diol-ABA, depending on the order of action of these 2 enzymes (Probable). Aba2 is responsible for the hydroxylation of carbon atom C-1' and aba4 might be involved in the oxidation of the C-4' carbon atom .
Sequence Mass (Da): 57218
Sequence Length: 509
Pathway: Hormone biosynthesis.
EC: 1.-.-.-
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G4N2Y3 | MMLQQVADALATHWLSGILAIATVYLATSYIIDYRRLRAFPGPPLGSFSYLWLAYNALQGRQGSIFYEVMKRYRVPEHSFVRIGPNDLMTDSPEVVRHMSSARSTYLRSSWYRTSKLDPSGDSLLSIMDTAHHDALKAKAGRGYAGRDNRNLESDIDDQLRRLIGLLERKYLSGGGDASSFRPVDMATTMQYFTLDSITKLAYSSAFGFLDLDTDVYGYIKAIRDAAPPIIVCSEWPLAGRIFFSPPFLKMFGPTPKDKSGVGKLMGTLRQVVASRFGPDAKDQPDMLGSFVRNGLSQHQCEQEVILQIVAGSDTTATALRGTLLQLCSTPMVYLKLQKEIDEAVRSGMVGEGVISQETARKLPYLQAVIYEGLRLNPPFTGALMKEVPPGGDEIDGVFIPAGVRIGVSAKGIQMRQDVYGHDVDVFRPERWTECDEQRRMRMAANTELVFGYGRWMCAGKNVAFMELNKVYFELLRRFDFQVVDTKTPVKEESFNVMFSKDMFMKVTKRVL | Function: Cytochrome P450 monooxygenase involved in the biosynthesis of abscisic acid (ABA), a phytohormone that acts antagonistically toward salicylic acid (SA), jasmonic acid (JA) and ethylene (ETH) signaling, to impede plant defense responses . During pathogen-host interaction, ABA plays a dual role in disease severity by increasing plant susceptibility and accelerating pathogenesis in the fungus itself . The first step of the pathway catalyzes the reaction from farnesyl diphosphate to alpha-ionylideneethane performed by the alpha-ionylideneethane synthase ABA3 via a three-step reaction mechanism involving 2 neutral intermediates, beta-farnesene and allofarnesene (By similarity). The cytochrome P450 monooxygenase ABA1 might then be involved in the conversion of alpha-ionylideneethane to alpha-ionylideneacetic acid (By similarity). Alpha-ionylideneacetic acid is further converted to abscisic acid in 2 steps involving the cytochrome P450 monooxygenase ABA2 and the short-chain dehydrogenase/reductase ABA4, via the intermediates 1'-deoxy-ABA or 1',4'-trans-diol-ABA, depending on the order of action of these 2 enzymes (By similarity). ABA2 is responsible for the hydroxylation of carbon atom C-1' and ABA4 might be involved in the oxidation of the C-4' carbon atom (By similarity).
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 57458
Sequence Length: 512
Pathway: Hormone biosynthesis.
Subcellular Location: Membrane
EC: 1.-.-.-
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Q9C826 | MSTNTESSSYSSLPSQRLLGKVALITGGATGIGESIVRLFHKHGAKVCIVDLQDDLGGEVCKSLLRGESKETAFFIHGDVRVEDDISNAVDFAVKNFGTLDILINNAGLCGAPCPDIRNYSLSEFEMTFDVNVKGAFLSMKHAARVMIPEKKGSIVSLCSVGGVVGGVGPHSYVGSKHAVLGLTRSVAAELGQHGIRVNCVSPYAVATKLALAHLPEEERTEDAFVGFRNFAAANANLKGVELTVDDVANAVLFLASDDSRYISGDNLMIDGGFTCTNHSFKVFR | Function: Involved in the biosynthesis of abscisic acid . Catalyzes the conversion of xanthoxin to abscisic aldehyde .
Catalytic Activity: 2-cis,4-trans-xanthoxin + NAD(+) = 2-cis-(+)-abscisic aldehyde + H(+) + NADH
Sequence Mass (Da): 30272
Sequence Length: 285
Subcellular Location: Cytoplasm
EC: 1.1.1.288
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A0A384JQH2 | MLLSIKDLSEKYIMLLDVKDLSTLKTTVAVLVTVALIAQVLWKIFFHPLSAFPGPWFNRISEIPGSWVIATGKQHSYYRKLHEKYGPVVRVAPNELSFIGDRAWDDIYGVQKKGPNFEKSPIFIGAVSPLDGQTGISLAPNEAHTRQRRALAHVFSNTALLQQEEIMRSHVDKLVGQLKKTIAENRPINFSNWYTYTTFDMMGDLCFAEPFGCLDQGGATEWSTSVINVFKSAAWDQSIRRVAGVNTWLQKLMVKLLIPSKAANWRKVHFQNSREKTLRRLADGNREHKDFIYHILKNKEAKNSLSETEIILNMVLLISAGTETTASLLTGWTYFICTHPEVYKRLTDEIRGRFNSEQDITWETVKDLPYLHATLSEALRLYSPAPANQQRIVPPGGSVIDGHFVPGKTTVAVAPWAAINSSLNFKDPQKFIPERWLGDERFVNDKLNASQPFSLGPRGCIGKNLSFFEMRLITSRLLWNFDVSLVTTGEHGETNKLWDMDGAGKYMKVYQTWNKPDMWVMLKEVPR | Function: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of abscisic acid (ABA), a phytohormone that acts antagonistically toward salicylic acid (SA), jasmonic acid (JA) and ethylene (ETH) signaling, to impede plant defense responses . The first step of the pathway catalyzes the reaction from farnesyl diphosphate to alpha-ionylideneethane performed by the alpha-ionylideneethane synthase aba3 via a three-step reaction mechanism involving 2 neutral intermediates, beta-farnesene and allofarnesene . The cytochrome P450 monooxygenase aba1 might then be involved in the conversion of alpha-ionylideneethane to alpha-ionylideneacetic acid (Probable). Alpha-ionylideneacetic acid is further converted to abscisic acid in 2 steps involving the cytochrome P450 monooxygenase aba2 and the short-chain dehydrogenase/reductase aba4, via the intermediates 1'-deoxy-ABA or 1',4'-trans-diol-ABA, depending on the order of action of these 2 enzymes (Probable). Aba2 is responsible for the hydroxylation of carbon atom C-1' and aba4 might be involved in the oxidation of the C-4' carbon atom .
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 59910
Sequence Length: 527
Pathway: Hormone biosynthesis.
Subcellular Location: Membrane
EC: 1.-.-.-
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Q96375 | MYASSARDGIPGKWCNARRKQLPLLISKDFPAELYHSLPCKSLENGHIKKVKGVKATLAEAPATPTEKSNSEVPQKKLKVLVAGGGIGGLVFALAGKKRGFDVLVFERDISAIRGEGQYRGPIQIQSNALAALEAIDMDVAEEIMNAGCITGQRINGLVDGISGNWYCKFDTFTPAVERGLPVTRVISRMTLQQILARLQGEDVIMNESHVVNFADDGETVTVNPELCQQYTGDLLVGADGIRSKVRTNLFGPSELTYSGYTCYTGIADFVPADIDTAGYRVFLGHKQYFVSSDVGGGKMQWYAFHNEPAGGVDAPNGKKERLLKIFGGWCDNVIDLSVATDEDAILRRDIYDRPPTFSWGKGRVTLLGDSVHAMQPNLGQGGCMAIEDSYQLALELEKAWSRSAESGSPMDVISSLRSYESARKLRVGVIHGLARMAAIMASAYKAYLGVGLGPLSFITKFRIPHPGRVGGRFFIDLGMPLMLSWVLGGNGEKLEGRIQHCRLSEKANDQLRNWFEDDDALERATDAEWLLLPAGNSNAALETLVLSRDENMPCTIGSVSHANIPGKSVVIPLSQVSDMHARISYNGGAFLGTAFRSDHGTWFIDNEGRRYRVSPNFPMRFHSSDVIVFGSDKAAFRIKAMKFAPKTAAKEDRQAVGAA | Function: Converts zeaxanthin into antheraxanthin and subsequently violaxanthin. Acts also on beta-cryptoxanthin. Involved in the epoxidation of zeaxanthin.
Catalytic Activity: all-trans-zeaxanthin + 4 H(+) + 2 O2 + 4 reduced [2Fe-2S]-[ferredoxin] = all-trans-violaxanthin + 2 H2O + 4 oxidized [2Fe-2S]-[ferredoxin]
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 71952
Sequence Length: 660
Pathway: Plant hormone biosynthesis; abscisate biosynthesis.
Subcellular Location: Plastid
EC: 1.14.15.21
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G4N2X2 | MYGTNLLETMGKPTAGHLGMAVTFTILVAFTIHVLRMRFFHPLRRYPGPWLNSITQIPAAWALLRARQPKAYRELHEKYGPIVRVAPNELSFINVEAWDDIYGFLKSTPNFEKSPVFIGAVSPLNGQTGISLANNEEHTRQRRALAAPFTNRALLQQQDILRVHVDKLITALRAKARNKESVNMGEWYTYTTFDIIGDICFAEPFGCLDGGESNEWARAIINIFKAATWDQAIRRVAGTGTLLHKALVKIIIPAEAAQWRTIHFSNSKAKTLARLADPDRQHPDLIKHILDSEDSRAALSPTEIILNMVLFISAGSETTANTMTGWTYFMLRHPEARARATAEVRAAFASPRDIKWETVRALPYLNATLEEALRLFSPAPSNQPRVVPACGAVVAGCPLPSGTTVSVAPWAAVFSARNFADPERFAPERWLDEGGADPRYAADRRGASQPFSTGPRGCMGKNLAYFELRLVLAHLLWHFDLEPTDSAAGRECMRRWEQTDMDTYQTWMKPDLWVDLKEAQR | Function: Cytochrome P450 monooxygenase involved in the biosynthesis of abscisic acid (ABA), a phytohormone that acts antagonistically toward salicylic acid (SA), jasmonic acid (JA) and ethylene (ETH) signaling, to impede plant defense responses . During pathogen-host interaction, ABA plays a dual role in disease severity by increasing plant susceptibility and accelerating pathogenesis in the fungus itself . The first step of the pathway catalyzes the reaction from farnesyl diphosphate to alpha-ionylideneethane performed by the alpha-ionylideneethane synthase ABA3 via a three-step reaction mechanism involving 2 neutral intermediates, beta-farnesene and allofarnesene (By similarity). The cytochrome P450 monooxygenase ABA1 might then be involved in the conversion of alpha-ionylideneethane to alpha-ionylideneacetic acid (By similarity). Alpha-ionylideneacetic acid is further converted to abscisic acid in 2 steps involving the cytochrome P450 monooxygenase ABA2 and the short-chain dehydrogenase/reductase ABA4, via the intermediates 1'-deoxy-ABA or 1',4'-trans-diol-ABA, depending on the order of action of these 2 enzymes (By similarity). ABA2 is responsible for the hydroxylation of carbon atom C-1' and ABA4 might be involved in the oxidation of the C-4' carbon atom (By similarity).
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 58440
Sequence Length: 521
Pathway: Hormone biosynthesis.
Subcellular Location: Membrane
EC: 1.-.-.-
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A0A384JQC9 | MQQVITQTLVDDRFIQISDSKKSEGLATDSTKRQSQEQPIHDKDPIKAATAAMAATPLVKEHQDTWYYPPDIANDLQSINLPAELKGEIFACAWEYTRCVIPNYTNWNRYVAFMRIIIMGIIAEFRGEMVDVTASNNLLGYDLDATLAALFEGTPGHKEMAREYKTFLLITADKASERRDGELFRRYVNALAQSPRHWFRMRDCDALARFTIASALACNDLDDIWFTEDQFEILTEIGDTLYDAVAFYKHRAEGETNSTFAYMPEDLRIKAYSECREILWALDAAWARNPKLANVINFVRFFGGPIHMMMRRYRFVEENLTIGKSETDKVVDQTRKNFKLWNRVDANKRSVLNTQRYKALIARSEELMFPGLAEFLEMGGDGICDKCKYRESYGAELSHQFGGVELCSECRLSWRKYLECFVERATKVFPELKTHFEVPV | Function: Alpha-ionylideneethane synthase; part of the gene cluster that mediates the biosynthesis of abscisic acid (ABA), a phytohormone that acts antagonistically toward salicylic acid (SA), jasmonic acid (JA) and ethylene (ETH) signaling, to impede plant defense responses . The first step of the pathway catalyzes the reaction from farnesyl diphosphate to alpha-ionylideneethane performed by the alpha-ionylideneethane synthase aba3 via a three-step reaction mechanism involving 2 neutral intermediates, beta-farnesene and allofarnesene . The cytochrome P450 monooxygenase aba1 might then be involved in the conversion of alpha-ionylideneethane to alpha-ionylideneacetic acid (Probable). Alpha-ionylideneacetic acid is further converted to abscisic acid in 2 steps involving the cytochrome P450 monooxygenase aba2 and the short-chain dehydrogenase/reductase aba4, via the intermediates 1'-deoxy-ABA or 1',4'-trans-diol-ABA, depending on the order of action of these 2 enzymes (Probable). Aba2 is responsible for the hydroxylation of carbon atom C-1' and aba4 might be involved in the oxidation of the C-4' carbon atom .
Sequence Mass (Da): 50777
Sequence Length: 440
Pathway: Hormone biosynthesis.
EC: 4.2.3.-
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Q694B7 | MKPQFRNTVERMYRDTFFYNFNNRPILSRRNTVWLCYEVKTRGPSMPTWDAKIFRGQVYSKAKYHPEMRFLHWFRKWRQLHRDQEYEVTWYVSWSPCTGCANSVATFLAEDPKVTLTIFVARLYYFWKPDYQEALRVLCQKRGSPHATMKIMNYNEFQHCWNKFVRGRREPFEPWENLPKHYTLLHATLGELLRHLMDPGTFTSNFYNKPWVSGQHETYLCYKVERLHNGTWVPLNQHRGFLRNQAPDIHGFPKGRHAELCFLDLIPFWKLDGQQYRVTCFTSWSPCFSCAQEMAKFISNNEHVSLCIFAARIYDDQGRCQEGLRTLHRDGAKIAMMNYSEFEYCWDTFVDRQGRPFQPWDGLDEHSQDLSGRLRAILQNQGN | Function: DNA deaminase (cytidine deaminase) which acts as an inhibitor of retrovirus replication and retrotransposon mobility. After the penetration of retroviral nucleocapsids into target cells of infection and the initiation of reverse transcription, it can induce the conversion of cytosine to uracil in the minus-sense single-strand viral DNA, leading to G-to-A hypermutations in the subsequent plus-strand viral DNA. The resultant detrimental levels of mutations in the proviral genome, along with a deamination-independent mechanism that works prior to the proviral integration, together exert efficient antiretroviral effects in infected target cells. Selectively targets single-stranded DNA and does not deaminate double-stranded DNA or single- or double-stranded RNA (By similarity).
Catalytic Activity: a 2'-deoxycytidine in single-stranded DNA + H(+) + H2O = a 2'-deoxyuridine in single-stranded DNA + NH4(+)
Sequence Mass (Da): 45904
Sequence Length: 383
Domain: The CMP/dCMP deaminase domain 1 mediates RNA binding, RNA-dependent oligomerization and virion incorporation whereas the CMP/dCMP deaminase domain 2 confers deoxycytidine deaminase activity and substrate sequence specificity.
Subcellular Location: Cytoplasm
EC: 3.5.4.38
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Q694C0 | MNPQFRNMVDGMDPHKFSYNFKNRPILSRRNTVWLCYEVKTKGPSRPPLDAKIFRGQVYFELKNHPEMRFFHWFSKWRKLHRDQECEVTWYMSWSPCTKCTRNVATFLAEDPKVTLTIFVARLYYFWDPDYQEALRSLCQERDGPRANMKIMNYDEFQHCWNKFVYSQRELFEPWNNLPKYYIVLHIILGEILRHSMDPLTFTSNFNNEPCVEGRHETYLCYKVERLHNDTWVLLNQRRGFLCNQAPAIHGFPEGRHAELCFLDVIPFWKLDGKQRYRVTCFTSWSPCFRCAQEMAKFISNNQHVSLCIFAARIYDDQGRCKEGLRTLDEAEAKISIMTYDEFQHCWDTFVDHQGRPFLPWIRLHEHSEALSGRLRAILLNQGN | Function: DNA deaminase (cytidine deaminase) which acts as an inhibitor of retrovirus replication and retrotransposon mobility. After the penetration of retroviral nucleocapsids into target cells of infection and the initiation of reverse transcription, it can induce the conversion of cytosine to uracil in the minus-sense single-strand viral DNA, leading to G-to-A hypermutations in the subsequent plus-strand viral DNA. The resultant detrimental levels of mutations in the proviral genome, along with a deamination-independent mechanism that works prior to the proviral integration, together exert efficient antiretroviral effects in infected target cells. Selectively targets single-stranded DNA and does not deaminate double-stranded DNA or single- or double-stranded RNA (By similarity).
Catalytic Activity: a 2'-deoxycytidine in single-stranded DNA + H(+) + H2O = a 2'-deoxyuridine in single-stranded DNA + NH4(+)
Sequence Mass (Da): 46078
Sequence Length: 384
Domain: The CMP/dCMP deaminase domain 1 mediates RNA binding, RNA-dependent oligomerization and virion incorporation whereas the CMP/dCMP deaminase domain 2 confers deoxycytidine deaminase activity and substrate sequence specificity.
Subcellular Location: Cytoplasm
EC: 3.5.4.38
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Q694B9 | MKPQTRNTVVRMDPDTFFYDFYNRPILSDRNTVWLCYEVKMKTNDRSRPPLVAKILEGQVHFDPEHHAEMYFLSWFRGNLLQACKSSQITWFVSWNPCLNCVAKVAEFLAEHPNVTLTVSTARIYCYWKKDWRRALRKLCQTGARVKIMNYKEFAYCWENFVYKERKPFRYWDKFSGNYRFLRCKLQEILRHLMDPGTFTYNFTNDPSVLGRHQTYLCYEAEHLHSGTWVPLHQHRGFILNEASNNLSFPEGRHAELCLLDLISFWKLDPAQTYRVTCFISWSPCFSCAQEVAEFLHENPHVNLRIFAARIYDYRPGYEEGLLRLSWAGAPISMMKYSGFSHCWDTFVDHQGRSFKPWKGLNEHSQALSGRLQAILQIMGN | Function: DNA deaminase (cytidine deaminase) which acts as an inhibitor of retrovirus replication and retrotransposon mobility. After the penetration of retroviral nucleocapsids into target cells of infection and the initiation of reverse transcription, it can induce the conversion of cytosine to uracil in the minus-sense single-strand viral DNA, leading to G-to-A hypermutations in the subsequent plus-strand viral DNA. The resultant detrimental levels of mutations in the proviral genome, along with a deamination-independent mechanism that works prior to the proviral integration, together exert efficient antiretroviral effects in infected target cells. Selectively targets single-stranded DNA and does not deaminate double-stranded DNA or single- or double-stranded RNA (By similarity).
Catalytic Activity: a 2'-deoxycytidine in single-stranded DNA + H(+) + H2O = a 2'-deoxyuridine in single-stranded DNA + NH4(+)
Sequence Mass (Da): 45133
Sequence Length: 381
Domain: The CMP/dCMP deaminase domain 1 mediates RNA binding, RNA-dependent oligomerization and virion incorporation whereas the CMP/dCMP deaminase domain 2 confers deoxycytidine deaminase activity and substrate sequence specificity.
Subcellular Location: Cytoplasm
EC: 3.5.4.38
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A9QA56 | MNPLQEVIFCRQFGNQHRVPKPYYRRKTYLCYQLKLPEGTLIHKDCLRNKKKRHAEMCFIDKIKALTRDTSQRFEIICYITWSPCPFCAEELVAFVKDNPHLSLRIFASRLYVHWRWKYQQGLRHLHASGIPVAVMSLPEFEDCWRNFVDHQDRSFQPWPNLDQYSKSIKRRLGKILTPLNDLRNDFRNLKLE | Function: DNA deaminase (cytidine deaminase) which acts as an inhibitor of retrovirus replication and retrotransposon mobility via deaminase-dependent and -independent mechanisms. Selectively targets single-stranded DNA and does not deaminate double-stranded DNA or single- or double-stranded RNA (By similarity). Exhibits single-stranded DNA deaminase activity (in vitro) . Incorporates into the released virions of the virion infectivity factor (vif)-deficient feline immunodeficiency virus (FIV) and suppresses FIV infectivity, probably in a deaminase-dependent manner (in vitro) . Induces G-to-A hypermutations in vif-deficient FIV (in vitro) . The APOBEC3H/APOBEC3Z3 haplotype 5 exhibits antiviral activity against vif-proficient FIV, strains Petaluma, C36 and Shizuoka (in vitro) . Does not exhibit inhibitory activity against feline leukemia virus (FeLV), feline endogenous retrovirus (RD-114 virus) or a long interspersed nuclear element-1 (LINE-1) retrotransposon (in vitro) .
Catalytic Activity: a 2'-deoxycytidine in single-stranded DNA + H(+) + H2O = a 2'-deoxyuridine in single-stranded DNA + NH4(+)
Sequence Mass (Da): 23297
Sequence Length: 193
Subcellular Location: Cytoplasm
EC: 3.5.4.38
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Q6NTF7 | MALLTAETFRLQFNNKRRLRRPYYPRKALLCYQLTPQNGSTPTRGYFENKKKCHAEICFINEIKSMGLDETQCYQVTCYLTWSPCSSCAWELVDFIKAHDHLNLGIFASRLYYHWCKPQQKGLRLLCGSQVPVEVMGFPEFADCWENFVDHEKPLSFNPYKMLEELDKNSRAIKRRLERIKIPGVRAQGRYMDILCDAEV | Function: DNA deaminase (cytidine deaminase) which acts as an inhibitor of retrovirus replication and retrotransposon mobility via deaminase-dependent and -independent mechanisms. The A3H-var/haplotype 2 exhibits antiviral activity against vif-deficient HIV-1. After the penetration of retroviral nucleocapsids into target cells of infection and the initiation of reverse transcription, it can induce the conversion of cytosine to uracil in the minus-sense single-strand viral DNA, leading to G-to-A hypermutations in the subsequent plus-strand viral DNA. The resultant detrimental levels of mutations in the proviral genome, along with a deamination-independent mechanism that works prior to the proviral integration, together exert efficient antiretroviral effects in infected target cells. Selectively targets single-stranded DNA and does not deaminate double-stranded DNA or single- or double-stranded RNA. Exhibits antiviral activity also against T-cell leukemia virus type 1 (HTLV-1) and may inhibit the mobility of LTR and non-LTR retrotransposons.
Catalytic Activity: a 2'-deoxycytidine in single-stranded DNA + H(+) + H2O = a 2'-deoxyuridine in single-stranded DNA + NH4(+)
Sequence Mass (Da): 23532
Sequence Length: 200
Subcellular Location: Nucleus
EC: 3.5.4.38
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Q19Q52 | MALLTAKTFSLQFNNKRRVNKPYYPRKALLCYQLTPQNGSTPTRGHLKNKKKDHAEIRFINKIKSMGLDETQCYQVTCYLTWSPCPSCAGELVDFIKAHRHLNLRIFASRLYYHWRPNYQEGLLLLCGSQVPVEVMGLPEFTDCWENFVDHKEPPSFNPSEKLEELDKNSQAIKRRLERIKSRSVDVLENGLRSLQLGPVTPSSSIRNSR | Function: DNA deaminase (cytidine deaminase) which acts as an inhibitor of retrovirus replication and retrotransposon mobility via deaminase-dependent and -independent mechanisms. Exhibits antiviral activity against vif-deficient HIV-1. After the penetration of retroviral nucleocapsids into target cells of infection and the initiation of reverse transcription, it can induce the conversion of cytosine to uracil in the minus-sense single-strand viral DNA, leading to G-to-A hypermutations in the subsequent plus-strand viral DNA. The resultant detrimental levels of mutations in the proviral genome, along with a deamination-independent mechanism that works prior to the proviral integration, together exert efficient antiretroviral effects in infected target cells. Selectively targets single-stranded DNA and does not deaminate double-stranded DNA or single- or double-stranded RNA.
Catalytic Activity: a 2'-deoxycytidine in single-stranded DNA + H(+) + H2O = a 2'-deoxyuridine in single-stranded DNA + NH4(+)
Sequence Mass (Da): 24327
Sequence Length: 210
Subcellular Location: Cytoplasm
EC: 3.5.4.38
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Q5ZIN0 | MRKRNESVTVEHERAAAAPAPLDKGCSLRHSLRLPAADTGMKRPLGRRHGLWFRLRRLIIWLLGVYIAIPFLVKLCPAIQAKLVFLNFVRVPYFIDLKRPQDQGLNHTCNYYLQPEEDVTIGVWHTVPAALWKNARGKDQLWFEDALGSSHPVILYLHGNAGTRGGDHRVELYKVLSSLGYHVVTFDYRGWGDSVGSPSERGMTYDALHVFDWIKARSGDNPVYIWGHSLGTGVATNLVRRLCERETPPEALILESPFTNIREEARSHPFSVIYRYFPGFDWFFLDPITTSGIKFANDENVKYISCSLLILHAEDDPVVPFHLGKKLYNIAATSRSFRDYKVQFVPFHTDLGYRHKYIYRSPELPRILREFLGIPEHEHHH | Function: Lysophosphatidylserine (LPS) lipase that mediates the hydrolysis of lysophosphatidylserine, a class of signaling lipids that regulates immunological and neurological processes (By similarity). Represents a major lysophosphatidylserine lipase in the brain, thereby playing a key role in the central nervous system (By similarity). Also able to hydrolyze oxidized phosphatidylserine; oxidized phosphatidylserine is produced in response to severe inflammatory stress and constitutes a proapoptotic 'eat me' signal. Also has monoacylglycerol (MAG) lipase activity: hydrolyzes 2-arachidonoylglycerol (2-AG), thereby acting as a regulator of endocannabinoid signaling pathways. Has a strong preference for very-long-chain lipid substrates; substrate specificity is likely due to improved catalysis and not improved substrate binding (By similarity).
Catalytic Activity: 1-(9Z-octadecenoyl)-sn-glycero-3-phospho-L-serine + H2O = (9Z)-octadecenoate + H(+) + sn-glycero-3-phospho-L-serine
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 43855
Sequence Length: 381
Subcellular Location: Endoplasmic reticulum membrane
EC: 3.1.-.-
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Q8N2K0 | MRKRTEPVALEHERCAAAGSSSSGSAAAALDADCRLKQNLRLTGPAAAEPRCAADAGMKRALGRRKGVWLRLRKILFCVLGLYIAIPFLIKLCPGIQAKLIFLNFVRVPYFIDLKKPQDQGLNHTCNYYLQPEEDVTIGVWHTVPAVWWKNAQGKDQMWYEDALASSHPIILYLHGNAGTRGGDHRVELYKVLSSLGYHVVTFDYRGWGDSVGTPSERGMTYDALHVFDWIKARSGDNPVYIWGHSLGTGVATNLVRRLCERETPPDALILESPFTNIREEAKSHPFSVIYRYFPGFDWFFLDPITSSGIKFANDENVKHISCPLLILHAEDDPVVPFQLGRKLYSIAAPARSFRDFKVQFVPFHSDLGYRHKYIYKSPELPRILREFLGKSEPEHQH | Function: Lysophosphatidylserine (LPS) lipase that mediates the hydrolysis of lysophosphatidylserine, a class of signaling lipids that regulates immunological and neurological processes . Represents a major lysophosphatidylserine lipase in the brain, thereby playing a key role in the central nervous system (By similarity). Also able to hydrolyze oxidized phosphatidylserine; oxidized phosphatidylserine is produced in response to severe inflammatory stress and constitutes a proapoptotic 'eat me' signal . Also has monoacylglycerol (MAG) lipase activity: hydrolyzes 2-arachidonoylglycerol (2-AG), thereby acting as a regulator of endocannabinoid signaling pathways . Has a strong preference for very-long-chain lipid substrates; substrate specificity is likely due to improved catalysis and not improved substrate binding .
PTM: Glycosylated; glycosylation is required for optimal activity.
Location Topology: Single-pass membrane protein
Catalytic Activity: 1-(9Z-octadecenoyl)-sn-glycero-3-phospho-L-serine + H2O = (9Z)-octadecenoate + H(+) + sn-glycero-3-phospho-L-serine
Sequence Mass (Da): 45097
Sequence Length: 398
Subcellular Location: Endoplasmic reticulum membrane
EC: 3.1.-.-
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Q99LR1 | MRKRTEPVTLEHERCAASGSSSSGSAAAALDADCSLKQNLRLAGKGTAEPHSASDAGMKRALGRRKSLWFRLRKILLCVLGFYIAIPFLVKLCPGIQAKLIFLNFVRVPYFIDLKKPQDQGLNHTCNYYLQPEDDVTIGVWHTIPSVWWKNAQGKDQMWYEDALASNHAIILYLHGNAGTRGGDHRVELYKVLSSLGYHVVTFDYRGWGDSVGTPSERGMTYDALHVFDWIKARSGDNPVYIWGHSLGTGVATNLVRRLCERETPPDALILESPFTNIREEAKSHPFSVIYRYFPGFDWFFLDPITSSGIKFANDENMKHISCPLLILHAEDDPVVPFHLGRKLYNIAAPSRSFRDFKVQFIPFHSDLGYRHKYIYKSPELPRILREFLGKSEPERQH | Function: Lysophosphatidylserine (LPS) lipase that mediates the hydrolysis of lysophosphatidylserine, a class of signaling lipids that regulates immunological and neurological processes . Represents a major lysophosphatidylserine lipase in the brain, thereby playing a key role in the central nervous system . Also able to hydrolyze oxidized phosphatidylserine; oxidized phosphatidylserine is produced in response to severe inflammatory stress and constitutes a proapoptotic 'eat me' signal . Also has monoacylglycerol (MAG) lipase activity: hydrolyzes 2-arachidonoylglycerol (2-AG), thereby acting as a regulator of endocannabinoid signaling pathways . Has a strong preference for very-long-chain lipid substrates; substrate specificity is likely due to improved catalysis and not improved substrate binding .
PTM: Glycosylated.
Location Topology: Single-pass membrane protein
Catalytic Activity: 1-(9Z-octadecenoyl)-sn-glycero-3-phospho-L-serine + H2O = (9Z)-octadecenoate + H(+) + sn-glycero-3-phospho-L-serine
Sequence Mass (Da): 45270
Sequence Length: 398
Subcellular Location: Endoplasmic reticulum membrane
EC: 3.1.1.-
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B4F753 | MRKRAEPVPPEHESFGRAPLDRECSIKQKLRIPGTKGHYPHDSDCDSKGMKRFGRRYGLWSRLRMFLIFLLGLYIAIPFLVKICPAIQTQLVFLNLVRFPYFIDLKRPEDQGLNHTCNFYLQPEEDVSIGVWHTVPAVLWKDAQGKDLEWYEEVLSTSYPVILYLHGNAGTRGGDHRVQLYKVLSSMGYHVISFDYRGWGDSVGSPSESGMTYDALHVFDWIKARSGDNPVYIWGHSLGTGVATNLVRRLCERETPPDSLILESPFTNIREEAKSHPFSVIYRYFPGFDWFFLDPITASGIKFANDDNVKYISCPLLILHAEDDPVIPFHLGKKLYNIAAPARSLRDYKVQFVPFHKDLGYRHKYIYRSPELRQILRDFLGNTEQQ | Function: Lysophosphatidylserine (LPS) lipase that mediates the hydrolysis of lysophosphatidylserine, a class of signaling lipids that regulates immunological and neurological processes (By similarity). Represents a major lysophosphatidylserine lipase in the brain, thereby playing a key role in the central nervous system (By similarity). Also able to hydrolyze oxidized phosphatidylserine; oxidized phosphatidylserine is produced in response to severe inflammatory stress and constitutes a proapoptotic 'eat me' signal. Also has monoacylglycerol (MAG) lipase activity: hydrolyzes 2-arachidonoylglycerol (2-AG), thereby acting as a regulator of endocannabinoid signaling pathways. Has a strong preference for very-long-chain lipid substrates; substrate specificity is likely due to improved catalysis and not improved substrate binding (By similarity).
Catalytic Activity: 1-(9Z-octadecenoyl)-sn-glycero-3-phospho-L-serine + H2O = (9Z)-octadecenoate + H(+) + sn-glycero-3-phospho-L-serine
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 44608
Sequence Length: 386
Subcellular Location: Endoplasmic reticulum membrane
EC: 3.1.-.-
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Q96IU4 | MAASVEQREGTIQVQGQALFFREALPGSGQARFSVLLLHGIRFSSETWQNLGTLHRLAQAGYRAVAIDLPGLGHSKEAAAPAPIGELAPGSFLAAVVDALELGPPVVISPSLSGMYSLPFLTAPGSQLPGFVPVAPICTDKINAANYASVKTPALIVYGDQDPMGQTSFEHLKQLPNHRVLIMKGAGHPCYLDKPEEWHTGLLDFLQGLQ | Function: Acts as an atypical protein-lysine deacetylase in vitro . Catalyzes the deacetylation of lysine residues using CoA as substrate, generating acetyl-CoA and the free amine of protein-lysine residues . Additional experiments are however required to confirm the protein-lysine deacetylase activity in vivo (Probable). Has hydrolase activity towards various surrogate p-nitrophenyl (pNp) substrates, such as pNp-butyrate, pNp-acetate and pNp-octanoate in vitro, with a strong preference for pNp-acetate . May activate transcription .
Catalytic Activity: acetyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-acetyl-L-lysyl-[protein]
Sequence Mass (Da): 22346
Sequence Length: 210
Subcellular Location: Cytoplasm
EC: 2.3.1.-
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Q1JPD2 | MAKLLSCVLGPRLYKIYRERDSERAPSSVPGTPTSVTNPHSSSWDTYYQPRALEKHADSILALASVFWSISYYSSPFAFFYLYRKGYLSLSKVVPFSHYAGTLLLLLAGVACLRGIGRWTNPQYRQFITILEATHRNHSAENKRQLANYNFDFRSWPVDFHWEEPSSRKESRGGPSRRGVALLRPEPLHRGTADTFLNRVKKLPCQITSYLVAHTLGRRMLYPGSVYLLQKALMPVLLQGQARLVEECHGRRAKLLACDGNEIDTMFVDRRGTAEPQGQKLVICCEGNAGFYEVGCVSTPLEAGYSVLGWNHPGFAGSTGVPFPQNEANAMDVVVQFAIHRLGFQPEDIILYAWSIGGFTATWAAMSYPDISAVILDASFDDLVPLALKVMPDSWRGLVTRTVRQHLNLNNAEQLCRYQGPVLLIRRTRDEIITTTVPEDIMSNRGNDLLLKFLQHRYPRVMAEEGLRVVRQWLEASSQLEEASIYSRWEVEEDWCLSVLRSYQAEHGPEFPWSVGEDMSADGRRQLALFLAQKHLNNFEATHCTPLPAQNFQMPWHL | Function: Phosphatidylserine (PS) lipase that mediates the hydrolysis of phosphatidylserine to generate lysophosphatidylserine (LPS). LPS constitutes a class of signaling lipids that regulates immunological and neurological processes (By similarity). Has no activity towards diacylglycerol, triacylglycerol or lysophosphatidylserine lipase (By similarity). Also has monoacylglycerol lipase activity, with preference for 1-(9Z,12Z-octadecadienoyl)-glycerol (1-LG) and 2-glyceryl-15-deoxy-Delta(12,14)-prostaglandin J2 (15d-PGJ(2)-G) (By similarity).
Catalytic Activity: 1-heptadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphoserine + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + 1-heptadecanoyl-sn-glycero-3-phosphoserine + H(+)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 63304
Sequence Length: 558
Subcellular Location: Membrane
EC: 3.1.-.-
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O95870 | MAKLLSCVLGPRLYKIYRERDSERAPASVPETPTAVTAPHSSSWDTYYQPRALEKHADSILALASVFWSISYYSSPFAFFYLYRKGYLSLSKVVPFSHYAGTLLLLLAGVACLRGIGRWTNPQYRQFITILEATHRNQSSENKRQLANYNFDFRSWPVDFHWEEPSSRKESRGGPSRRGVALLRPEPLHRGTADTLLNRVKKLPCQITSYLVAHTLGRRMLYPGSVYLLQKALMPVLLQGQARLVEECNGRRAKLLACDGNEIDTMFVDRRGTAEPQGQKLVICCEGNAGFYEVGCVSTPLEAGYSVLGWNHPGFAGSTGVPFPQNEANAMDVVVQFAIHRLGFQPQDIIIYAWSIGGFTATWAAMSYPDVSAMILDASFDDLVPLALKVMPDSWRGLVTRTVRQHLNLNNAEQLCRYQGPVLLIRRTKDEIITTTVPEDIMSNRGNDLLLKLLQHRYPRVMAEEGLRVVRQWLEASSQLEEASIYSRWEVEEDWCLSVLRSYQAEHGPDFPWSVGEDMSADGRRQLALFLARKHLHNFEATHCTPLPAQNFQMPWHL | Function: Phosphatidylserine (PS) lipase that mediates the hydrolysis of phosphatidylserine to generate lysophosphatidylserine (LPS) (By similarity). LPS constitutes a class of signaling lipids that regulates immunological and neurological processes (By similarity). Has no activity towards diacylglycerol, triacylglycerol or lysophosphatidylserine lipase . Also has monoacylglycerol lipase activity, with preference for 1-(9Z,12Z-octadecadienoyl)-glycerol (1-LG) and 2-glyceryl-15-deoxy-Delta(12,14)-prostaglandin J2 (15d-PGJ(2)-G) .
Catalytic Activity: 1-heptadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphoserine + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + 1-heptadecanoyl-sn-glycero-3-phosphoserine + H(+)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 63243
Sequence Length: 558
Subcellular Location: Membrane
EC: 3.1.-.-
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Q8IZP0 | MAELQMLLEEEIPSGKRALIESYQNLTRVADYCENNYIQATDKRKALEETKAYTTQSLASVAYQINALANNVLQLLDIQASQLRRMESSINHISQTVDIHKEKVARREIGILTTNKNTSRTHKIIAPANMERPVRYIRKPIDYTVLDDVGHGVKWLKAKHGNNQPARTGTLSRTNPPTQKPPSPPMSGRGTLGRNTPYKTLEPVKPPTVPNDYMTSPARLGSQHSPGRTASLNQRPRTHSGSSGGSGSRENSGSSSIGIPIAVPTPSPPTIGPENISVPPPSGAPPAPPLAPLLPVSTVIAAPGSAPGSQYGTMTRQISRHNSTTSSTSSGGYRRTPSVTAQFSAQPHVNGGPLYSQNSISIAPPPPPMPQLTPQIPLTGFVARVQENIADSPTPPPPPPPDDIPMFDDSPPPPPPPPVDYEDEEAAVVQYNDPYADGDPAWAPKNYIEKVVAIYDYTKDKDDELSFMEGAIIYVIKKNDDGWYEGVCNRVTGLFPGNYVESIMHYTD | Function: May act in negative regulation of cell growth and transformation by interacting with nonreceptor tyrosine kinases ABL1 and/or ABL2. May play a role in regulation of EGF-induced Erk pathway activation. Involved in cytoskeletal reorganization and EGFR signaling. Together with EPS8 participates in transduction of signals from Ras to Rac. In vitro, a trimeric complex of ABI1, EPS8 and SOS1 exhibits Rac specific guanine nucleotide exchange factor (GEF) activity and ABI1 seems to act as an adapter in the complex. Regulates ABL1/c-Abl-mediated phosphorylation of ENAH. Recruits WASF1 to lamellipodia and there seems to regulate WASF1 protein level. In brain, seems to regulate the dendritic outgrowth and branching as well as to determine the shape and number of synaptic contacts of developing neurons.
PTM: Phosphorylated on tyrosine residues after serum stimulation or induction by v-Abl. Seems to be phosphorylated at Tyr-53 by ABL1, required for nuclear but not for synaptic localization.
Sequence Mass (Da): 55081
Sequence Length: 508
Domain: The t-SNARE coiled-coil homology domain is necessary and sufficient for interaction with STX1A.
Subcellular Location: Cytoplasm
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Q9NYB9 | MAELQMLLEEEIPGGRRALFDSYTNLERVADYCENNYIQSADKQRALEETKAYTTQSLASVAYLINTLANNVLQMLDIQASQLRRMESSINHISQTVDIHKEKVARREIGILTTNKNTSRTHKIIAPANLERPVRYIRKPIDYTILDDIGHGVKWLLRFKVSTQNMKMGGLPRTTPPTQKPPSPPMSGKGTLGRHSPYRTLEPVRPPVVPNDYVPSPTRNMAPSQQSPVRTASVNQRNRTYSSSGSSGGSHPSSRSSSRENSGSGSVGVPIAVPTPSPPSVFPAPAGSAGTPPLPATSASAPAPLVPATVPSSTAPNAAAGGAPNLADGFTSPTPPVVSSTPPTGHPVQFYSMNRPASRHTPPTIGGSLPYRRPPSITSQTSLQNQMNGGPFYSQNPVSDTPPPPPPVEEPVFDESPPPPPPPEDYEEEEAAVVEYSDPYAEEDPPWAPRSYLEKVVAIYDYTKDKEDELSFQEGAIIYVIKKNDDGWYEGVMNGVTGLFPGNYVESIMHYSE | Function: Regulator of actin cytoskeleton dynamics underlying cell motility and adhesion. Functions as a component of the WAVE complex, which activates actin nucleating machinery Arp2/3 to drive lamellipodia formation . Acts as regulator and substrate of nonreceptor tyrosine kinases ABL1 and ABL2 involved in processes linked to cell growth and differentiation. Positively regulates ABL1-mediated phosphorylation of ENAH, which is required for proper polymerization of nucleated actin filaments at the leading edge . Contributes to the regulation of actin assembly at the tips of neuron projections. In particular, controls dendritic spine morphogenesis and may promote dendritic spine specification toward large mushroom-type spines known as repositories of memory in the brain (By similarity). In hippocampal neurons, may mediate actin-dependent BDNF-NTRK2 early endocytic trafficking that triggers dendrite outgrowth (By similarity). Participates in ocular lens morphogenesis, likely by regulating lamellipodia-driven adherens junction formation at the epithelial cell-secondary lens fiber interface (By similarity). Also required for nascent adherens junction assembly in epithelial cells .
PTM: Phosphorylated by ABL1.
Sequence Mass (Da): 55663
Sequence Length: 513
Domain: The SH3 domain is critical for binding to ABL1 and ABL2.
Subcellular Location: Cytoplasm
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P62484 | MAELQMLLEEEIPGGRRALFDSYTNLERVADYCENNYIQSPDKQRALEETKAYTTQSLASVAYLINTLANNVLQMLDIQASQLRRMESSINHISQTVDIHKEKVARREIGILTTNKNTSRTHKIIAPANLERPVRYIRKPIDYTILDDIGHGVKVSTQNMKMGGLPRTTPPTQKPPSPPMSGKGTLGRHSPYRTLEPVRPPVVPNDYVPSPTRNMAPSQQSPVRTASVNQRNRTYSSSGSSGGSHPSSRSSSRENSGSGSVGVPIAVPTPSPPSVFPGHPVQFYSMNRPASRHTPPTIGGSLPYRRPPSITSQTSLQNQMNGGPFYNQNPVSDTPPPPPPVEEPVFDESPPPPPPPEDYEEEEAAVVEYSDPYAEEDPPWAPRAYLEKVVAIYDYTKDKEDELSFQEGAIIYVIKKNDDGWYEGVMNGVTGLFPGNYVESIMHYSE | Function: Regulator of actin cytoskeleton dynamics underlying cell motility and adhesion. Functions as a component of the WAVE complex, which activates actin nucleating machinery Arp2/3 to drive lamellipodia formation (By similarity). Acts as regulator and substrate of nonreceptor tyrosine kinases ABL1 and ABL2 involved in processes linked to cell growth and differentiation. Positively regulates ABL1-mediated phosphorylation of ENAH, which is required for proper polymerization of nucleated actin filaments at the leading edge (By similarity). Contributes to the regulation of actin assembly at the tips of neuron projections. In particular, controls dendritic spine morphogenesis and may promote dendritic spine specification toward large mushroom-type spines known as repositories of memory in the brain . In hippocampal neurons, may mediate actin-dependent BDNF-NTRK2 early endocytic trafficking that triggers dendrite outgrowth . Participates in ocular lens morphogenesis, likely by regulating lamellipodia-driven adherens junction formation at the epithelial cell-secondary lens fiber interface . Also required for nascent adherens junction assembly in epithelial cells (By similarity).
PTM: Phosphorylated by ABL1.
Sequence Mass (Da): 49387
Sequence Length: 446
Domain: The SH3 domain is critical for binding to ABL1 and ABL2.
Subcellular Location: Cell projection
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Q01593 | MKSLHVAANAGDLAEDCGILGGDADDTVLMDGIDEVGREIWLDDHGGDNNHVHGHQDDDLIVHHDPSIFYGDLPTLPDFPCMSSSSSSSTSPAPVNAIVSSASSSSAASSSTSSAASWAILRSDGEDPTPNQNQYASGNCDDSSGALQSTASMEIPLDSSQGFGCGEGGGDCIDMMETFGYMDLLDSNEFFDTSAIFSQDDDTQNPNLMDQTLERQEDQVVVPMMENNSGGDMQMMNSSLEQDDDLAAVFLEWLKNNKETVSAEDLRKVKIKKATIESAARRLGGGKEAMKQLLKLILEWVQTNHLQRRRTTTTTTNLSYQQSFQQDPFQNPNPNNNNLIPPSDQTCFSPSTWVPPPPQQQAFVSDPGFGYMPAPNYPPQPEFLPLLESPPSWPPPPQSGPMPHQQFPMPPTSQYNQFGDPTGFNGYNMNPYQYPYVPAGQMRDQRLLRLCSSATKEARKKRMARQRRFLSHHHRHNNNNNNNNNNQQNQTQIGETCAAVAPQLNPVATTATGGTWMYWPNVPAVPPQLPPVMETQLPTMDRAGSASAMPRQQVVPDRRQGWKPEKNLRFLLQKVLKQSDVGNLGRIVLPKKEAETHLPELEARDGISLAMEDIGTSRVWNMRYRFWPNNKSRMYLLENTGDFVKTNGLQEGDFIVIYSDVKCGKYLIRGVKVRQPSGQKPEAPPSSAATKRQNKSQRNINNNSPSANVVVASPTSQTVK | Function: Participates in abscisic acid-regulated gene expression during seed development. Regulates the transcription of SGR1 and SGR2 that are involved in leaf and embryo degreening.
PTM: Ubiquitinated by AIP2. Ubiquitination probably leads to its subsequent degradation, thus negatively regulating ABA signaling.
Sequence Mass (Da): 79500
Sequence Length: 720
Subcellular Location: Nucleus
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Q640U0 | MADTKPLHQTRFEAAVSVIQSLPKNGSFQPSNEMMLKFYSFYKQATLGPCNTPRPGFWDPVGRYKWDAWNSLGDMSKEDAMIAYVDEMKKILETMPVTEKVEELLQVIGPFYEIVEDKKHGRGSGVTSELGSVLTSTPNGKAVNGKAESSDSGAESDEEQAATKEVREEDEEEESEHSEQEDKDVEQQPGHEKPAESIVNGLTRNHRELVTEEPTPLPSKCLSEPGDKVAIPDTHSPVNDPEADREEDCTEDIAAMQHLTSDSDSEIFCDSMEQFGQDEADHSLLLQDAMLNGDITETSAGGELKDGGEDGKQSGHGAQRKTWSEKSEHFGSRRERPSRMQPGGDGSRSGQIGSGGDGDRWGSDRGPNGSLNEQIAVVLMRLQEDMQNVLQRLHSLEVQTASQAQFLLRESNNQPMEKKPSRWPFGISPGTLALAVVWPFVVHWLMHVFLQKRRRKQT | Function: Acyl-CoA binding protein which acts as the peroxisome receptor for pexophagy but is dispensable for aggrephagy and nonselective autophagy. Binds medium- and long-chain acyl-CoA esters (By similarity).
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 50881
Sequence Length: 458
Subcellular Location: Peroxisome membrane
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Q96GR2 | MPRNSGAGYGCPHGDPSMLDSRETPQESRQDMIVRTTQEKLKTSSLTDRQPLSKESLNHALELSVPEKVNNAQWDAPEEALWTTRADGRVRLRIDPSCPQLPYTVHRMFYEALDKYGDLIALGFKRQDKWEHISYSQYYLLARRAAKGFLKLGLKQAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAYDCCANVIMVDTQKQLEKILKIWKQLPHLKAVVIYKEPPPNKMANVYTMEEFMELGNEVPEEALDAIIDTQQPNQCCVLVYTSGTTGNPKGVMLSQDNITWTARYGSQAGDIRPAEVQQEVVVSYLPLSHIAAQIYDLWTGIQWGAQVCFAEPDALKGSLVNTLREVEPTSHMGVPRVWEKIMERIQEVAAQSGFIRRKMLLWAMSVTLEQNLTCPGSDLKPFTTRLADYLVLAKVRQALGFAKCQKNFYGAAPMMAETQHFFLGLNIRLYAGYGLSETSGPHFMSSPYNYRLYSSGKLVPGCRVKLVNQDAEGIGEICLWGRTIFMGYLNMEDKTCEAIDEEGWLHTGDAGRLDADGFLYITGRLKELIITAGGENVPPVPIEEAVKMELPIISNAMLIGDQRKFLSMLLTLKCTLDPDTSDQTDNLTEQAMEFCQRVGSRATTVSEIIEKKDEAVYQAIEEGIRRVNMNAAARPYHIQKWAILERDFSISGGELGPTMKLKRLTVLEKYKGIIDSFYQEQKM | Function: Catalyzes the conversion of fatty acids such as long-chain and very long-chain fatty acids to their active form acyl-CoAs for both synthesis of cellular lipids, and degradation via beta-oxidation . Can activate diverse saturated, monosaturated and polyunsaturated fatty acids .
Catalytic Activity: a long-chain fatty acid + ATP + CoA = a long-chain fatty acyl-CoA + AMP + diphosphate
Sequence Mass (Da): 81290
Sequence Length: 724
Subcellular Location: Cytoplasm
EC: 6.2.1.3
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Q4R4P9 | MPRNSGAGYGCPHGDPSMLDSRETPQESRQDMTVGTTQEKLKTSSLTDRQPLSKESLNHALKLSVPEKVNNAQWDAPEEALWTTRADGRVRLRIDPSCPQLPYTVHRMFYEALDKYGDFSALGFKCQDKWEHISYSQYYLLARRAAKGFLKLGLERAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAYDCCANVIMVDTQKQLEKILKVWKQLPHLKAVVIYKEPPPNKMANVYTMEEFMELGNEVPEEALDAIIDTQQPNQCCVLVYTSGTTGNPKGVMLSQDNITWTARYGSQAGDIRPAEVQQEVVVSYLPLSHIAAQIYDLWTGIQWGAQVCFAEPDALKGSLVNTLREVEPTSHMGVPRVWEKIMERIQEVAAQSGFIRRKMLLWAMSVTLEQNLTCPGSDLKPFTTRLADYLVLAKVRQALGFAKCQKNFYGAAPMTAETQHFFLGLNIRLYAGYGLSETSGPHFMSSPCNYRLYSSGKLVPGCRVKLVNQDTEGIGEICLWGRTIFMGYLNMEDKTCEAIDEEGWLHTGDAGRLDADGFLYITGRLKELIITAGGENVPPVPIEEAVKMELPIISNAMLIGTDQRKFLSMLLTLKCTLDPDTSDPTDNLTEQAVEFCQRVGSRATTVSEIVGKDEAVYQAIEEGIRRVNMNAAARPYHIQKWAILERDFSISGGELGPTMKLKRLTVLEKYKDIIDSFYREQKM | Function: Catalyzes the conversion of fatty acids such as long-chain and very long-chain fatty acids to their active form acyl-CoAs for both synthesis of cellular lipids, and degradation via beta-oxidation. Can activate diverse saturated, monosaturated and polyunsaturated fatty acids.
Catalytic Activity: a long-chain fatty acid + ATP + CoA = a long-chain fatty acyl-CoA + AMP + diphosphate
Sequence Mass (Da): 80998
Sequence Length: 724
Subcellular Location: Cytoplasm
EC: 6.2.1.3
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Q5ZKR7 | MLCESEARSTLADPVPMAYLSVDAQGSSEVSLDDITINSSAGTVEVCSMKPADDPKTERSQMNKTGLASSSRPASNVWTTQQDGEVKLRMDEEGMGSEAPKTVHEVFQEAVSKYGDYYALASKKNGQWVKLTYKMYYDKCWKAAKSFLKLVLERFHGVCILGFNSPEWFIADIGAIFAGGLAVGIYTTNSPEACHYVAENCSANILVVENHTQACRKSLEIEHKLPHMKAIIQYGEELKEKRPNQYSWREFLDLGEDIPDSQLREIIESQKPNQCCTLIYTSGTTGQPKGVMLSHDNLTWTSIAAGRSLMLLEATEKQELVVSYLPLSHVAAQMIDIWLPVTFGGQVFFAQPDALKGTLVDTLREVRPTAFLGVPRVWEKIEEKMKSVGAKSSTLRRKVASWAKGVGLQTNLKWMNGHSEVPMNFRLARQLVYKKVRKAIGLDRCTKCFTGAAPISRETLEFFLSLNIPVFELYGMSESSGPHTVSIPQAFRLTSCGKEMAGCRTLIHKPDADGIGEICFAGRHIFMGYLNMEEKTKEAIDKDGWLHSGDLGKCDKDGFIYITGRIKELIITAGGENVPPVPIEDAVKEACPIISNAMLVGDKAKFLAMLLTLKCIINTESGEPGDDLTAEAIEYCQKLGSKATKVSEIISSKDKAVYAAIQAAVSEVNKRAVSNAQKIQKWVVLEKDFSVGGGELGPTMKLKRPVVAQKYKDLIDEFYADANTPTTTEERTSAVMWGGRKLPLVHSIVSLGSLQQIQRVLQK | Function: Mediates activation of long-chain fatty acids for both synthesis of cellular lipids, and degradation via beta-oxidation.
Catalytic Activity: a long-chain fatty acid + ATP + CoA = a long-chain fatty acyl-CoA + AMP + diphosphate
Sequence Mass (Da): 84207
Sequence Length: 763
Subcellular Location: Cytoplasm
EC: 6.2.1.3
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Heavily deduplicated version of SwissProt (Novembe 2023) with dense natural language protein descriptions.
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