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stringlengths 6
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stringlengths 11
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stringlengths 108
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Q23381 | MYLQLLKPTLLRCSTRPSSSGAYTRSPIDQKWAAMAKKAMKGREADTLTWNTPEGIPIKPLYLRSDRDCDAQRSVELPGQFPFTRGPYPTMYTQRPWTIRQYAGFSTVEESNKFYKENIKAGQQGLSVAFDLATHRGYDSDNPRVFGDVGMAGVAVDSVEDMRQLFDGINLEKMSVSMTMNGAVVPVLAMYVVAAEEAGVSRKLLAGTIQNDILKEFMVRNTYIYPPEPSMRIIGDIFAYTSREMPKFNSISISGYHMQEAGADAVLEMAFTIADGIQYCETGLNAGLTIDAFAPRLSFFWGISMNFYMEIAKMRAARRLWANLIKERFSPKSDKSMMLRTHSQTSGWSLTEQDPYNNIIRTTIEAMASVFGGTQSLHTNSFDEALGLPTKFSARIARNTQIIIQEESGICNVADPWGGSYMMESLTDEIYEKALAVIKEIDELGGMAKAVASGMTKLKIEEAAAKKQARIDAGKDVIVGVNKYRLDHEQQVEVLKIDNAKVREEQCAKLNHIRATRDAEKAQKALDAITEGARGNGNLMELAIEAARARCTVGEISDAMEKVFNRHAAVNRLVSGAYKSEFGETSEMSQVLERVKSFADRDGRQPRIMVAKMGQDGHDRGAKVIATGFADLGFDVDVGPLFQTPLEAAQQAVDADVHVIGASSLAAGHLTLIPQLIGELKKLGRPDILVVAGGVIPPQDYKELYDAGVALVFGPGTRLPACANQILEKLEANLPEAPGKAASR | Function: Involved, in man, in the degradation of several amino acids, odd-chain fatty acids and cholesterol via propionyl-CoA to the tricarboxylic acid cycle. MCM has different functions in other species (By similarity).
Catalytic Activity: (R)-methylmalonyl-CoA = succinyl-CoA
Sequence Mass (Da): 81683
Sequence Length: 744
Subcellular Location: Mitochondrion matrix
EC: 5.4.99.2
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P22033 | MLRAKNQLFLLSPHYLRQVKESSGSRLIQQRLLHQQQPLHPEWAALAKKQLKGKNPEDLIWHTPEGISIKPLYSKRDTMDLPEELPGVKPFTRGPYPTMYTFRPWTIRQYAGFSTVEESNKFYKDNIKAGQQGLSVAFDLATHRGYDSDNPRVRGDVGMAGVAIDTVEDTKILFDGIPLEKMSVSMTMNGAVIPVLANFIVTGEEQGVPKEKLTGTIQNDILKEFMVRNTYIFPPEPSMKIIADIFEYTAKHMPKFNSISISGYHMQEAGADAILELAYTLADGLEYSRTGLQAGLTIDEFAPRLSFFWGIGMNFYMEIAKMRAGRRLWAHLIEKMFQPKNSKSLLLRAHCQTSGWSLTEQDPYNNIVRTAIEAMAAVFGGTQSLHTNSFDEALGLPTVKSARIARNTQIIIQEESGIPKVADPWGGSYMMECLTNDVYDAALKLINEIEEMGGMAKAVAEGIPKLRIEECAARRQARIDSGSEVIVGVNKYQLEKEDAVEVLAIDNTSVRNRQIEKLKKIKSSRDQALAERCLAALTECAASGDGNILALAVDASRARCTVGEITDALKKVFGEHKANDRMVSGAYRQEFGESKEITSAIKRVHKFMEREGRRPRLLVAKMGQDGHDRGAKVIATGFADLGFDVDIGPLFQTPREVAQQAVDADVHAVGISTLAAGHKTLVPELIKELNSLGRPDILVMCGGVIPPQDYEFLFEVGVSNVFGPGTRIPKAAVQVLDDIEKCLEKKQQSV | Function: Catalyzes the reversible isomerization of methylmalonyl-CoA (MMCoA) (generated from branched-chain amino acid metabolism and degradation of dietary odd chain fatty acids and cholesterol) to succinyl-CoA (3-carboxypropionyl-CoA), a key intermediate of the tricarboxylic acid cycle.
Catalytic Activity: (R)-methylmalonyl-CoA = succinyl-CoA
Sequence Mass (Da): 83134
Sequence Length: 750
Subcellular Location: Mitochondrion matrix
EC: 5.4.99.2
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P65486 | MSIDVPERADLEQVRGRWRNAVAGVLSKSNRTDSAQLGDHPERLLDTQTADGFAIRALYTAFDELPEPPLPGQWPFVRGGDPLRDVHSGWKVAEAFPANGATADTNAAVLAALGEGVSALLIRVGESGVAPDRLTALLSGVYLNLAPVILDAGADYRPACDVMLALVAQLDPGQRDTLSIDLGADPLTASLRDRPAPPIEEVVAVASRAAGERGLRAITVDGPAFHNLGATAATELAATVAAAVAYLRVLTESGLVVSDALRQISFRLAADDDQFMTLAKMRALRQLWARVAEVVGDPGGGAAVVHAETSLPMMTQRDPWVNMLRCTLAAFGAGVGGADTVLVHPFDVAIPGGFPGTAAGFARRIARNTQLLLLEESHVGRVLDPAGGSWFVEELTDRLARRAWQRFQAIEARGGFVEAHDFLAGQIAECAARRADDIAHRRLAITGVNEYPNLGEPALPPGDPTSPVRRYAAGFEALRDRSDHHLARTGARPRVLLLPLGPLAEHNIRTTFATNLLASGGIEAIDPGTVDAGTVGNAVADAGSPSVAVICGTDARYRDEVADIVQAARAAGVSRVYLAGPEKALGDAAHRPDEFLTAKINVVQALSNLLTRLGA | Function: Catalyzes the isomerization of succinyl-CoA to methylmalonyl-CoA during synthesis of propionate from tricarboxylic acid-cycle intermediates.
Catalytic Activity: (R)-methylmalonyl-CoA = succinyl-CoA
Sequence Mass (Da): 64744
Sequence Length: 615
Pathway: Metabolic intermediate metabolism; propanoyl-CoA degradation; succinyl-CoA from propanoyl-CoA: step 3/3.
EC: 5.4.99.2
|
Q59676 | MAKEKEKLFSEFPPVSREAWIDKITADLKGVPFEKKLVWRTNEGFNVNPFYRREDIEDLKTTTSLPDEYPYVRSTRMHNEWLVRQDIVVGDNVAEANEKALDLLNKGVDSLGFYLKKVHINVDTLAALLKDIELTAVELNFNCCITRAADLLSAFSAYVKKVGADPNKCHGSVSYDPFKKQLVRGVSNPDWVKMTLPVMDAARELPAFRVLNVNAVNLSDAGAFITQELGYALAWGAELLDKLTDAGYKPEEIASRIKFNFGIGSNYFMEIAKFRAARWLWAQIVGSYGDQYKNETAKIHQHATTSMWNKTVFDAHVNLLRTQTETMSAAIAGVDSITVLPFDVTYQQSDDFSERIARNQQLLLKEECHFDKVIDPSAGSYYIETLTNSIGEEAWKLFLSVEDAGGFTQAAETASIQKAVNASNIKRHQSVATRREIFLGTNQFPNFTEVAGDKITLAQGEHDCNCVKSIEPLNFSRGASEFEALRLATEKSGKTPVVFMLTIGNLAMRLARSQFSSNFFGCAGYKLIDNLGFKSVEEGVDAALAAKADIVVLCSSDDEYAEYAPAAFDYLAGRAEFVVAGAPACMADLEAKGIRNYVHVKSNVLETLRAFNDKFGIR | Function: Catalyzes the isomerization of succinyl-CoA to methylmalonyl-CoA during synthesis of propionate from tricarboxylic acid-cycle intermediates.
Catalytic Activity: (R)-methylmalonyl-CoA = succinyl-CoA
Sequence Mass (Da): 68739
Sequence Length: 618
Pathway: Metabolic intermediate metabolism; propanoyl-CoA degradation; succinyl-CoA from propanoyl-CoA: step 3/3.
EC: 5.4.99.2
|
P11652 | MSSTDQGTNPADTDDLTPTTLSLAGDFPKATEEQWEREVEKVLNRGRPPEKQLTFAECLKRLTVHTVDGIDIVPMYRPKDAPKKLGYPGVAPFTRGTTVRNGDMDAWDVRALHEDPDEKFTRKAILEGLERGVTSLLLRVDPDAIAPEHLDEVLSDVLLEMTKVEVFSRYDQGAAAEALVSVYERSDKPAKDLALNLGLDPIAFAALQGTEPDLTVLGDWVRRLAKFSPDSRAVTIDANIYHNAGAGDVAELAWALATGAEYVRALVEQGFTATEAFDTINFRVTATHDQFLTIARLRALREAWARIGEVFGVDEDKRGARQNAITSWRDVTREDPYVNILRGSIATFSASVGGAESITTLPFTQALGLPEDDFPLRIARNTGIVLAEEVNIGRVNDPAGGSYYVESLTRSLADAAWKEFQEVEKLGGMSKAVMTEHVTKVLDACNAERAKRLANRKQPITAVSEFPMIGARSIETKPFPAAPARKGLAWHRDSEVFEQLMDRSTSVSERPKVFLACLGTRRDFGGREGFSSPVWHIAGIDTPQVEGGTTAEIVEAFKKSGAQVADLCSSAKVYAQQGLEVAKALKAAGAKALYLSGAFKEFGDDAAEAEKLIDGRLFMGMDVVDTLSSTLDILGVAK | Function: Catalyzes the isomerization of succinyl-CoA to methylmalonyl-CoA during synthesis of propionate from tricarboxylic acid-cycle intermediates.
Catalytic Activity: (R)-methylmalonyl-CoA = succinyl-CoA
Sequence Mass (Da): 69464
Sequence Length: 638
Pathway: Metabolic intermediate metabolism; propanoyl-CoA degradation; succinyl-CoA from propanoyl-CoA: step 3/3.
EC: 5.4.99.2
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Q05064 | MTVLPDDGLSLAAEFPDATHEQWHRLVEGVVRKSGKDVSGTAAEEALSTTLEDGLTTRPLYTARDAAPDAGFPGFAPFVRGSVPEGNTPGGWDVRQRYASADPARTNEAVLTDLENGVTSLWLTLGSAGLPVTGLERALDGVYLDLVPVALDAGSEAATAARELLRLYEAAGVADDAVRGTLGADPLGHEARTGEKSTSFAAVAELARLCGERYPGLRALTVDALPYHEAGASAAQELGASLATGVEYLRALHDKGLGVEKAFAQLEFRFAATADQFLTIAKLRAARRLWARVAEVSGVPAAGAQRQHAVTSPVMMTRRDPWVNMLRTTVACLGAGVGGADAVTVLPFDHELGLPDAFARRIARNTSTILLEESHLARVIDPAGGSWYVERLTDELAHAAWDFFKEIERADGQVAALRSGLVGDRIAATWAERRKKLARRREPITGVSEFPLLTERPVEREPAPAAPPGGLPRVRRDEAYEELRGRSDAHLEATGARPKVFIAALGPAAAHTARATFAANLFMAGGVEPVHDPVSVDAETAAEAFAASGATVACLCSSDVLYAEQAEAVARALKSAGALRVFLAGRGEFADIDEYVFAGCDAVAVLTSTLDRMGVA | Function: Catalyzes the isomerization of succinyl-CoA to methylmalonyl-CoA during synthesis of propionate from tricarboxylic acid-cycle intermediates. This conversion most likely represents an important source of building blocks for polyketide antibiotic biosynthesis. It is unable to catalyze the conversion of isobutyryl-CoA into N-butyryl-CoA.
Catalytic Activity: (R)-methylmalonyl-CoA = succinyl-CoA
Sequence Mass (Da): 65041
Sequence Length: 616
Pathway: Metabolic intermediate metabolism; propanoyl-CoA degradation; succinyl-CoA from propanoyl-CoA: step 3/3.
EC: 5.4.99.2
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Q59677 | MKPNYKDIDIKSAGFVAKDATRWAEEKGIVADWRTPEQIMVKPLYTKDDLEGMEHLDYVSGLPPFLRGPYSGMYPMRPWTIRQYAGFSTAEESNAFYRRNLASGQKGLSVAFDLATHRGYDADHSRVVGDVGKAGVSICSLEDMKVLFDGIPLSKMSVSMTMNGAVLPILAFYINAGLEQGAKLEEMAGTIQNDILKEFMVRNTYIYPPEFSMRIIADIFEYTSQNMPKFNSISISGYHMQEAGATADIEMAYTLADGMQYLKAGIDAGIDVDAFAPRLSFFWAIGVNHFMEIAKMRAARLLWAKIVKSFGAKNPKSLALRTHSQTSGWSLTEQDPFNNVGRTCIEAMAAALGHTQSLHTNALDEAIALPTDFSARIARNTQIYIQEETLVCKEIDPWGGSYYVESLTNELVHKAWTLIKEVQEMGGMAKAIETGLPKLRIEEAAARTQARIDSHQQVIVGVNKYRLPKEDPIDILEIDNTAVRKQQIERLNDLRSHRDEKAVQEALEAITKCVETKEGNLLDLAVKAAGLRASLGEISDACEKVVGRYKAVIRTISGVYSSESGEDKDFAHAKELAEKFAKKEGRQPRIMIAKMGQDGHDRGAKVVATGYADCGFDVDMGPLFQTPEEAARQAVENDVHVMGVSSLAAGHKTLIPQVIAELEKLGRPDILVTAGGVIPAQDYDFLYQAGVAAIFGPGTPVAYSAAKVLEILLEE | Function: Catalyzes the isomerization of succinyl-CoA to methylmalonyl-CoA during synthesis of propionate from tricarboxylic acid-cycle intermediates.
Catalytic Activity: (R)-methylmalonyl-CoA = succinyl-CoA
Sequence Mass (Da): 78703
Sequence Length: 715
EC: 5.4.99.2
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P11653 | MSTLPRFDSVDLGNAPVPADAARRFEELAAKAGTGEAWETAEQIPVGTLFNEDVYKDMDWLDTYAGIPPFVHGPYATMYAFRPWTIRQYAGFSTAKESNAFYRRNLAAGQKGLSVAFDLPTHRGYDSDNPRVAGDVGMAGVAIDSIYDMRELFAGIPLDQMSVSMTMNGAVLPILALYVVTAEEQGVKPEQLAGTIQNDILKEFMVRNTYIYPPQPSMRIISEIFAYTSANMPKWNSISISGYHMQEAGATADIEMAYTLADGVDYIRAGESVGLNVDQFAPRLSFFWGIGMNFFMEVAKLRAARMLWAKLVHQFGPKNPKSMSLRTHSQTSGWSLTAQDVYNNVVRTCIEAMAATQGHTQSLHTNSLDEAIALPTDFSARIARNTQLFLQQESGTTRVIDPWSGSAYVEELTWDLARKAWGHIQEVEKVGGMAKAIEKGIPKMRIEEAAARTQARIDSGRQPLIGVNKYRLEHEPPLDVLKVDNSTVLAEQKAKLVKLRAERDPEKVKAALDKITWAAGNPDDKDPDRNLLKLCIDAGRAMATVGEMSDALEKVFGRYTAQIRTISGVYSKEVKNTPEVEEARELVEEFEQAEGRRPRILLAKMGQDGHDRGQKVIATAYADLGFDVDVGPLFQTPEETARQAVEADVHVVGVSSLAGGHLTLVPALRKELDKLGRPDILITVGGVIPEQDFDELRKDGAVEIYTPGTVIPESAISLVKKLRASLDA | Function: Catalyzes the reversible conversion of succinyl-CoA to (R)-methylmalonyl-CoA through a radical mechanism . Is involved in the fermentation of pyruvate to propanoate that occurs in Propionibacteria (Probable).
Catalytic Activity: (R)-methylmalonyl-CoA = succinyl-CoA
Sequence Mass (Da): 80178
Sequence Length: 728
EC: 5.4.99.2
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Q7SB97 | MSLFGSSPPNDGSAALNPAKTANSSRSTLFDNEAPTTRSGSALFADDDHDSPWDMPTPRKQRSRADLIRNLLPSGDVPESYIETFDAVVRTENRSTNGRITAGGVARTLAAAKLGADDQARIMGIIAPASASATGAGGGGDGAHGGEANSSAAAAAAAVGLGDLGRNEFNVLLALIGLVQEGEVASLDGVDERRRNLPQPKLQGLVNENVQPMLPNLSELGAKPPQRPVTPPKAPTPSPPKQQQQQQHQPPTLRKVSMEYPEDPWNAPDLHKGHNHGPLEHSTGHNGAADVPRSVANDLNGNDAVSYSTSPEVTTTSSALPGRTTSTFTTSQPPSGPSSIHNVAESIQESNGAWNYFPGSSSGGGFGEPADNAITGPFGDSGGPGQSVSGSVGGSNPNRSIGHVRSGSNVEENILVTLMPEKEGVFMFQHHNYEVSSIRRGSKVVRRYSDFVWLLDCLHKRYPFRVLPLLPPKRVAFNGNHLSNDGAFIEKRRRGLARFLNALVRHPVLGQEQLVIMFLTVPTELSVWRKQATISVQDEFTGRTLPPGLEDSLPPTLEELFARTRVGVRRSAELYISTCTIMDRLIKRSEGVAADHARMAVSLISLTETSADTYATDHNDVPLLNDGLQAMGRHLRTAQTLMEDEAKAWEEGVLEDLKRQRDALVSLRDMFDRRDRLDKDNIPFLQRRIETNEAKLQALNAKPEGMVKPGEKERVVEAIIKDKESIVTQHNRSVFVKECIRDELRFFQNTQYNVSRLTQDWAQERVKYSEMLADNWRRLLDDLEGMPLGD | Function: Required for vacuolar protein sorting.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 86091
Sequence Length: 790
Domain: The PX domain binds phosphatidylinositol 3-phosphate which is necessary for peripheral membrane localization.
Subcellular Location: Cytoplasm
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O14120 | MGDNVFLEPDPWASSSNWGSPVKPLNYKTAIGNSSIPLQYRNYWDVFQANNVLLFPEEESYSDIFHVPQDVMKEFFTLIESSSNQPLRQIQFFVLLALVACYQLGVPSTLEQIFKQRNVLPILQRFNPELFNRSSDNETPLFPNNSPPASTTALNLSSNIVPSINESKILEQEDDDVSNKSLPHAQQSIIRSFPDIQKQPKGFFSYPSSTVSSIAPSTLEAGNLHSQQPPKFSVDSSVDDNAITPRKPFSKIPNRLSPSTQPLLSNSRHSSFRLASSSTSFPASLEMNVDIDLEPSGYFFYRHNNYIISDSSNTREVLRRYSDFFWLHSYLMKKYPFRRVPLIPLKKFHSKCFNSKQFFRTPPPGLSDFVNDLSHHPIFSNDEVVRVFFTEPNVFKNWRRENQKRIDQEIEQFLVVPQSQVPDASETVKERLLKLNMSTTTAINNQLNIFRIFEKMIFTLQHFHEDFLRLQNSFNCLLDSGLYHQVFTSTFAQNESKIMSMASGHFYNIDSLLHQQNDAVKHTFLLGLSKEIKILISLRLLIERISEVFSTDLTKVRHTISNDENLLRETANSDESGRNRTFLNRSSKKRAENSLKSKKELYLKNLNQRYQIAHELEQELSYLQDYVFSLGNPYVEYCKQHVKLEEESLKIWHTLESDFSRLET | Function: Required for vacuolar protein sorting.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 76861
Sequence Length: 664
Domain: The PX domain binds phosphatidylinositol 3-phosphate which is necessary for peripheral membrane localization.
Subcellular Location: Cytoplasm
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Q4PHC3 | MSRHHRPFTWGGAQPGASFSNPTSPTLEASTFGFEPSVPDIYRRAWILVTKDASAELFADTSDADIHLGLLHKLLTSAGGLGPGSAEQIVNSACKGSRCSRSDFYCALGLLHQMQQGEELDVHLVQQRLTMGSLSAPVLDLSDATLNPHSHHTFPPTAPSGPSRIDPRPSTFMREMSDPWNANSSGSYNGIDTRPAYNQYDAMPQQYDTLNSHDSALPAGFAGNVSSGSFERIKFNAGDDRRSHQLLAHNQGSSTDTFLAPDRTEARARQPNTRQERPFSYMSDTAETNAVDAAEDPAADLPEDQVTVRLRSELEGFIIKHNVYIVSSSLRKSQVTRRYSDWLWLAECLVKRYPFRCLPVLPPKRIAMPIAGRHLSADDLFIERRRRGLERFLRMLTCHPMLREDKLVEVFFTEPRPIAEWKSSAPALFLDEEGLIKTVDEAERMSIPEDLQLKLTQQRQAIPELLERWTAMVALFERIVKRNDAAAADYSRLNFSLLSVIETSARRWRPGSDNGKKTEEIMSTMASIFQDHSDTTSSRVSAVSLSTLEGMKAQRDLILSFRDLIGRIDRQLVDPIDMLKKRIEASQKRITTLAASANSNSASIQQEQATLSAQVKQDTQSIQKYLNRRIHAKKTVWEELIWFHHRFKAVEEDMQKFVRDETFFLSTLTRMWEATEMKMKMIR | Function: Required for vacuolar protein sorting.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 77206
Sequence Length: 683
Domain: The PX domain binds phosphatidylinositol 3-phosphate which is necessary for peripheral membrane localization.
Subcellular Location: Cytoplasm
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Q6CHY6 | MSLFSAATTAVERTGYGSRYDHIFDMFHPIDGRIPAVCYKRLLETINVSGEDKDRLATLAGSILEGGDGSGGILTSSFTRESWRAALLLANVAQDGLPFDDPSQLVNVDTLTPMDFSEEGERSSINFSASTTGRSQTPLFGDDLDDHSIQSSRSESIIHNNGHSRGHSALDWNPEEQEALQQSQLSQSQLSRSTTPPPLNPQALVPESESGVWTAPPRPDFAPNKADSVTLAIVPEREGMFLFRHVNYSISSVSGTDRITVIRRYSDFSWLQDYLLKKYCFRQVPLLPPKRLAVNGHYLSSDNYFLERRRRGLTRFINQVLRHPVLGQDEAVRTFVTLRNDISGWKKSVFNTAREEFNGRTIDPKFVQQWDEQQATALWAGLIVELDRSHDSVVQLCVLLDRVAKRQEAQAVDSAKIAYNLGAALPPSARVLYSVADDGCVQQITRGLSRASARIETDCQLQQDEARGSQVGVLEEAKKYREALGSMRELFDRLEKYGGNNIPLLEKRIQQNQGRVTLARQRKALMSEIEKLDRAIKMDTEMIAAHKNRTWLIRECITEEIGLFQKTQLQISKLLQEFCVDKIKYAELYSDNWGGLDNDVMDLPV | Function: Required for vacuolar protein sorting.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 68061
Sequence Length: 605
Domain: The PX domain binds phosphatidylinositol 3-phosphate which is necessary for peripheral membrane localization.
Subcellular Location: Cytoplasm
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P40959 | MDNYEGSDPWNTSSNAWTKDDDHVVSTTNSEPSLNGISGEFNTLNFSTPLDTNEEDTGFLPTNDVLEESIWDDSRNPLGATGMSQTPNIAANETVIDKNDARDQNIEESEADLLDWTNNVRKTYRPLDADIIIIEEIPEREGLLFKHANYLVKHLIALPSTSPSEERTVVRRYSDFLWLREILLKRYPFRMIPELPPKRIGSQNADQLFLKKRRIGLSRFINLVMKHPKLSNDDLVLTFLTVRTDLTSWRKQATYDTSNEFADKKISQEFMKMWKKEFAEQWNQAASCIDTSMELWYRITLLLERHEKRIMQMVHERNFFETLVDNFSEVTPKLYPVQQNDTILDINNNLSIIKKHLETTSSICKQETEEISGTLSPKFKIFTDILLSLRSLFERYKIMAANNVVELQRHVELNKEKLESMKGKPDVSGAEYDRIKKIIQKDRRSIIEQSNRAWLIRQCILEEFTIFQETQFLITRAFQDWAKLNSNHAGLKLNEWEKLVTSIMDMPISRE | Function: Required for vacuolar protein sorting.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 59657
Sequence Length: 511
Domain: The PX domain binds phosphatidylinositol 3-phosphate which is necessary for peripheral membrane localization.
Subcellular Location: Cytoplasm
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Q08542 | MDCVLRSYLLLAFGFLICLFLFCLVVFIWFVYKQILFRTTAQSNEARHNHSTVV | Function: Transports viral genome to neighboring plant cells directly through plasmosdesmata, without any budding. The movement protein allows efficient cell to cell propagation, by bypassing the host cell wall barrier. Two movement proteins, p6, Hsp70h and three structural proteins, CP, CPm, and P64 are essential for cell-cell movement. Also plays a role in virion formation. Together with CPm and p64, encapsidates the 5'-terminal portion of the viral genome (By similarity).
Location Topology: Single-pass type III membrane protein
Sequence Mass (Da): 6389
Sequence Length: 54
Subcellular Location: Host rough endoplasmic reticulum membrane
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O71191 | MDDFKQAILLLVVDFVFVIILLLVLTFVVPRLQQSSTINTGLRTV | Function: Transports viral genome to neighboring plant cells directly through plasmosdesmata, without any budding. The movement protein allows efficient cell to cell propagation, by bypassing the host cell wall barrier. Two movement proteins, p6, Hsp70h and three structural proteins, CP, CPm, and P64 are essential for cell-cell movement. Also plays a role in virion formation. Together with CPm and p64, encapsidates the 5'-terminal portion of the viral genome (By similarity).
Location Topology: Single-pass type III membrane protein
Sequence Mass (Da): 5090
Sequence Length: 45
Subcellular Location: Host rough endoplasmic reticulum membrane
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Q9HK44 | MNSRIMFIGGVPGVGKTSISGYIARNTDIDIVLSSDYLREFLRPFAPQESHLETSVYDAWKFYGDMSDDNIIRGYLDQARPIMGGINRVIARALANGEDLIIESLYFVPDMMDEMVLKNAFLAYVYIDDPDLHRSRLEDRINYTHRNSPGSRLAAHLKEYRTIMDYSMDMARGRGIGLYSTDDYALARQRLLDDFRKFVDRR | Function: Phosphorylates mevalonate 3-phosphate to form mevalonate 3,5-bisphosphate. Functions in an alternative mevalonate pathway, only present in extreme acidophiles of the Thermoplasmatales order, which passes through mevalonate 3-phosphate rather than mevalonate 5-phosphate.
Catalytic Activity: (R)-3-phosphomevalonate + ATP = (R)-3,5-bisphosphomevalonate + ADP + H(+)
Sequence Mass (Da): 23298
Sequence Length: 202
Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via mevalonate pathway.
EC: 2.7.1.186
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P21946 | MDSQLVNPPNAFNYIESHRDEYQLSHDLTEIILQFPSTAAQLTARLSRSCMKIDHCVIEYRQQVPINATGSVIVEIHDKRMTDNESLQASWTFPIRCNIDLHYFSASFFSLKDPIPWKLYYKVCDTNVHQRTHFAKFKGKLKLSTAKHSVDIPFRAPTVRILSKQFSEKDVDFSHVDYGKWERKPIRCASMSRIGLRGPIEIRPGESWASRSTIGTAQPDTDSEMENELHPYRHLNRLGTSLLDPGESASIVGDQRAEPNITMSMGQLNELVRTAVQECVNSNCQASQAKSLK | Function: Transports viral genome to neighboring plant cells directly through plasmosdesmata, without any budding. The movement protein allows efficient cell to cell propagation, by bypassing the host cell wall barrier. Begomovirus genome is shuttled out of nucleus by Nuclear shuttle protein (NSP) and the movement protein transports the DNA-NSP complex to cell plasmodesmata and facilitates further movement across the cell wall.
PTM: Phosphorylated in yeast.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 33342
Sequence Length: 293
Subcellular Location: Host cell membrane
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Q65387 | MALTTERVKLFFEWFLFFGAIFIAITILYILLVLLFEVPRYIKELVRCLVEYLTRRRVWMQRTQLTEATGDVEIGRGIVEDRRDQEPAVIPHVSQVIPSQPNRRDDQGRRGNAGPMF | Function: Transports viral genome to neighboring plant cells directly through plasmosdesmata, without any budding. The movement protein allows efficient cell to cell propagation, by bypassing the host cell wall barrier. Begomovirus genome is shuttled out of nucleus by Nuclear shuttle protein (NSP) and the movement protein transports the DNA-NSP complex to cell plasmodesmata and facilitates further movement across the cell wall. Acts as a suppressor of RNA-mediated gene silencing, also known as post-transcriptional gene silencing (PTGS), a mechanism of plant viral defense that limits the accumulation of viral RNAs.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 13739
Sequence Length: 117
Subcellular Location: Host cell membrane
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P0A1I5 | MIQSFLKQVSTKPELIILVLMVMIIAMLIIPLPTYLVDFLIGLNIVLAILVFMGSFYIERILSFSTFPSVLLITTLFRLALSISTSRLILVDADAGKIITTFGQFVIGDSLAVGFVIFSIVTVVQFIVITKGSERVAEVAARFSLDGMPGKQMSIDADLKAGIIDAAGAKERRSILERESQLYGSFDGAMKFIKGDAIAGIIIIFVNLIGGISVGMSQHGMSLSGALSTYTILTIGDGLVSQIPALLISISAGFIVTRVNGDSDNMGRNIMSQIFGNPFVLIVTSALALAIGMLPGFPFFVFFLIAVTLTALFYYKKVVEKEKSLSESDSSGYTGTFDIDNSHDSSLAMIENLDAISSETVPLILLFAENKINANDMEGLIERIRSQFFIDYGVRLPTILYRTSNELKVDDIVLLINEVRADSFNIYFDKVCITDENGDIDALGIPVVSTSYNERVISWVDVSYTENLTNIDAKIKSAQDEFYHQLSQALLNNINEIFGIQETKNMLDQFENRYPDLLKEVFRHVTIQRISEVLQRLLGENISVRNLKLIMESLALWAPREKDVITLVEHVRASLSRYICSKIAVSGEIKVVMLSGYIEDAIRKGIRQTSGGSFLNMDIEVSDEVMETLAHALRELRNAKKNFVLLVSVDIRRFVKRLIDNRFKSILVISYAEIDEAYTINVLKTI | Function: Necessary for the secretion of IPA invasins.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 76145
Sequence Length: 686
Subcellular Location: Cell inner membrane
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Q9LTF7 | MECKREEGKSYVKRGLWKPEEDMILKSYVETHGEGNWADISRRSGLKRGGKSCRLRWKNYLRPNIKRGSMSPQEQDLIIRMHKLLGNRWSLIAGRLPGRTDNEVKNYWNTHLNKKPNSRRQNAPESIVGATPFTDKPVMSTELRRSHGEGGEEESNTWMEETNHFGYDVHVGSPLPLISHYPDNTLVFDPCFSFTDFFPLL | Function: Transcription activation factor positively regulating trichomes development . Has a function nearly equivalent to that of GL1 and can complement gl1 mutants .
Sequence Mass (Da): 23292
Sequence Length: 201
Domain: The N-terminal domain is necessary and sufficient for dimer formation. The C-terminal domain is responsible for the transcription activation function.
Subcellular Location: Nucleus
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Q58DG1 | MGHRFLRGFLRVLLPPLPLRSPHLKLSLEPVAPSKRPRSHLMAPPRIGTHNGTFHCDEALACALLRLLPEYREAEIVRTRDPEKLAACDIVVDVGGEYDPQRHRYDHHQRSFTETMSSLSPGKPWQTKLSSAGLIYLHFGHKLLAQLLGTSEEDGMVGTLYDKMYENFVEEVDAVDNGISQWEEGEPRYLLTTTLSARVARLNPTWNQPNQDTEAGFKRAMDLVREEFLQRLDFYQNSWLPARTLVEEALAKRFQVDPSGEIIELEKGGCPWKEHLYQLELGLSPAGTIAFVIYTDQAGQWRVQCVPKEPHSFQSRLPLLEPWRGLRDEALDQISGIPGCIFVHASGFIGGHRTREGALSMARATLAQRPAPTPAPNPMVQ | Function: 3'-5' RNA exonuclease which cleaves in situ on specific transcripts in both nucleus and mitochondrion. Involved in regulating spatially segregated organellar RNA processing, acts as a coordinator of nucleo-mitochondrial crosstalk. In nucleolus, processes pre-ribosomal RNA involved in ribosome assembly and alters cytoplasmic translation. In mitochondrial matrix, processes 3'-termini of the mito-ribosomal and messenger RNAs and controls translation of mitochondrial proteins.
Sequence Mass (Da): 42967
Sequence Length: 381
Subcellular Location: Nucleus
EC: 3.1.-.-
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Q9HB07 | MGHRFLRGLLTLLLPPPPLYTRHRMLGPESVPPPKRSRSKLMAPPRIGTHNGTFHCDEALACALLRLLPEYRDAEIVRTRDPEKLASCDIVVDVGGEYDPRRHRYDHHQRSFTETMSSLSPGKPWQTKLSSAGLIYLHFGHKLLAQLLGTSEEDSMVGTLYDKMYENFVEEVDAVDNGISQWAEGEPRYALTTTLSARVARLNPTWNHPDQDTEAGFKRAMDLVQEEFLQRLDFYQHSWLPARALVEEALAQRFQVDPSGEIVELAKGACPWKEHLYHLESGLSPPVAIFFVIYTDQAGQWRIQCVPKEPHSFQSRLPLPEPWRGLRDEALDQVSGIPGCIFVHASGFTGGHHTREGALSMARATLAQRSYLPQIS | Function: 3'-5' RNA exonuclease which cleaves in situ on specific transcripts in both nucleus and mitochondrion. Involved in regulating spatially segregated organellar RNA processing, acts as a coordinator of nucleo-mitochondrial crosstalk . In nucleolus, processes pre-ribosomal RNA involved in ribosome assembly and alters cytoplasmic translation. In mitochondrial matrix, processes 3'-termini of the mito-ribosomal and messenger RNAs and controls translation of mitochondrial proteins (Probable).
Sequence Mass (Da): 42477
Sequence Length: 376
Subcellular Location: Nucleus
EC: 3.1.-.-
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Q9JK81 | MGRRFLRGILTLPLRSVLQAQHRMLGSEQDPPAKRPRNNLMAPPRIGTHNGTFHCDEALACALLRLLPEYANAEIVRTRDPEKLASCDIVVDVGGEYNPQSHRYDHHQRTFTETMSSLCPGKPWQTKLSSAGLVYLHFGRKLLAQLLGTSEEDSVVDTIYDKMYENFVEEVDAVDNGISQWAEGEPRYAMTTTLSARVARLNPTWNQPNQDTEAGFRRAMDLVQEEFLQRLNFYQHSWLPARALVEEALAQRFKVDSSGEIVELAKGGCPWKEHLYHLESELSPKVAITFVIYTDQAGQWRVQCVPKEPHSFQSRLPLPEPWRGLRDKALDQVSGIPGCIFVHASGFIGGHHTREGALNMARATLAQRPAPVPLANAVVQ | Function: 3'-5' RNA exonuclease which cleaves in situ on specific transcripts in both nucleus and mitochondrion. Involved in regulating spatially segregated organellar RNA processing, acts as a coordinator of nucleo-mitochondrial crosstalk . In nucleolus, processes pre-ribosomal RNA involved in ribosome assembly and alters cytoplasmic translation. In mitochondrial matrix, processes 3'-termini of the mito-ribosomal and messenger RNAs and controls translation of mitochondrial proteins .
Sequence Mass (Da): 42723
Sequence Length: 380
Subcellular Location: Nucleus
EC: 3.1.-.-
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P81271 | RSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAANAIPKLRNWQWWRLFTK | Function: Muscle contraction.
Sequence Mass (Da): 7864
Sequence Length: 65
Domain: The rodlike tail sequence is highly repetitive, showing cycles of a 28-residue repeat pattern composed of 4 heptapeptides, characteristic for alpha-helical coiled coils.
Subcellular Location: Melanosome
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D2BRP0 | MNSPGLRKPTIWRPLLLLFPLLALLLSMSSPRLPDEVMLHITPLHQGMTLPDGFYIYQRLNERGIAIKSITPENNSIIVRLSSPEQSGAAKEILSIALPNTVVIAQRTHGTIRVARS | Function: Modulates the activity of the EnvZ/OmpR two-component regulatory system, probably by directly modulating EnvZ enzymatic activity and increasing stability of phosphorylated OmpR.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 12974
Sequence Length: 117
Subcellular Location: Cell inner membrane
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P42615 | MQIPRMSLRQLAWSGAVLLLVGTLLLAWSAVRQQESTLAIRAVHQGTTMPDGFSIWHHLDAHGIPFKSITPKNDTLLITFDSSDQSAAAKAVLDRTLPHGYIIAQQDNNSQAMQWLTRLRDNSHRFG | Function: Modulates the activity of the EnvZ/OmpR two-component regulatory system, probably by directly modulating EnvZ enzymatic activity and increasing stability of phosphorylated OmpR. Links the two-component systems CpxA/CpxR and EnvZ/OmpR.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 14172
Sequence Length: 127
Domain: Interacts with EnvZ through its soluble periplasmic region.
Subcellular Location: Cell inner membrane
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C5BH44 | MNQANSQPFTRRQGWKRILGLLLFIVAALTVVILPQLGHKEVSLQIRATHNGLATPDGFFVYQKLDENGVSITSITQDREGLVIRLAHPEQRTLALQVLQRELPPGYSIADKILHRSLFYKSERPAAATLSYSAGHNR | Function: Modulates the activity of the EnvZ/OmpR two-component regulatory system, probably by directly modulating EnvZ enzymatic activity and increasing stability of phosphorylated OmpR.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 15456
Sequence Length: 138
Subcellular Location: Cell inner membrane
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D4I1C3 | MTTASIKKRDPRRRLLPWLIVAFVALIGLAMIPALFRHDSTLQIRASRQGVSLPDGFYVYQTLSAQGIHIQSITPEQDSLVIRFDSPEQSYAAERVLRKLFAQSFDIAHQPGPGAASWINRISLLPQFVG | Function: Modulates the activity of the EnvZ/OmpR two-component regulatory system, probably by directly modulating EnvZ enzymatic activity and increasing stability of phosphorylated OmpR.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 14544
Sequence Length: 130
Subcellular Location: Cell inner membrane
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D8MMF7 | MLALLRPYLSTRVLCVLVVCFSALMLVAFIPTLFRNDTALQIRASRQGTTLPDGFYVYQRLNAEGIRIKSITPDNDSLVIRFDTEEQSMAAEKVLHQLLPYGFDIGQMDPSGSSQLMNRLSLRKQSVG | Function: Modulates the activity of the EnvZ/OmpR two-component regulatory system, probably by directly modulating EnvZ enzymatic activity and increasing stability of phosphorylated OmpR.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 14354
Sequence Length: 128
Subcellular Location: Cell inner membrane
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F2EUZ7 | MKPLHAFPKRWLPWLIGGAFALVAISMMPSLMRHENVVQIRVSHAGAPMPDGFYLYQQLSAQGIRIKSITPSGDALIIHFDNEEQSLAAQKVLRRLLPDGFIVAQHDQAAHLSLA | Function: Modulates the activity of the EnvZ/OmpR two-component regulatory system, probably by directly modulating EnvZ enzymatic activity and increasing stability of phosphorylated OmpR.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 12764
Sequence Length: 115
Subcellular Location: Cell inner membrane
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C6DKE3 | MSIRWLFPKLTPRKVARILILLALPIIALTQSQSLRHSQDDAMLHIKPYDGAALPDGFYVYQRLNEKGIAIKSITPEQDSLIVRLASPEQSIAARDVLRLSLPKVTITAQQATTPTPFWQQKLTQKQSKLG | Function: Modulates the activity of the EnvZ/OmpR two-component regulatory system, probably by directly modulating EnvZ enzymatic activity and increasing stability of phosphorylated OmpR.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 14714
Sequence Length: 131
Subcellular Location: Cell inner membrane
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E8XVS9 | MNRRLLKRSFIWPLLLMLLAAATMIGLAVSRLPAPTSALQIRPARAGVALPDGFYVYQRLSQRGIHIKSITPLNDALVVQLDTASQRKLAETVLQDILPAGFVIQYYEPQHATAWGAKLDRERLKFG | Function: Modulates the activity of the EnvZ/OmpR two-component regulatory system, probably by directly modulating EnvZ enzymatic activity and increasing stability of phosphorylated OmpR.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 14180
Sequence Length: 127
Subcellular Location: Cell inner membrane
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A8GJY0 | MIKRPRWQYVLLIALALLALATLLVPCMVRTESELRIRAGQQGLSLPDGFYVYQRLDQRGIRIKSITPEGDGLVIRLDSPEQQLLAREALQNILPPGYIIALSESPVPTHWVREFARAPLNLG | Function: Modulates the activity of the EnvZ/OmpR two-component regulatory system, probably by directly modulating EnvZ enzymatic activity and increasing stability of phosphorylated OmpR.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 13855
Sequence Length: 123
Subcellular Location: Cell inner membrane
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A4THL5 | MINFRGRFGRPLWHYLVLPVVLLLLAVILLTPMIVQTESTLKIRPNQQGLSLPDGFYLYQHLNGRGIHIKSIIPENDSLVVSLEFPEQQMQAIEVLQDVLPAGYAIVASESKKRHRLLPVFRSNQQNLG | Function: Modulates the activity of the EnvZ/OmpR two-component regulatory system, probably by directly modulating EnvZ enzymatic activity and increasing stability of phosphorylated OmpR.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 14667
Sequence Length: 129
Subcellular Location: Cell inner membrane
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Q147X3 | MAEVPPGPSSLLPPPAPPAPAAVEPRCPFPAGAALACCSEDEEDDEEHEGGGSRSPAGGESATVAAKGHPCLRCPQPPQEQQQLNGLISPELRHLRAAASLKSKVLSVAEVAATTATPDGGPRATATKGAGVHSGERPPHSLSSNARTAVPSPVEAAAASDPAAARNGLAEGTEQEEEEEDEQVRLLSSSLTADCSLRSPSGREVEPGEDRTIRYVRYESELQMPDIMRLITKDLSEPYSIYTYRYFIHNWPQLCFLAMVGEECVGAIVCKLDMHKKMFRRGYIAMLAVDSKYRRNGIGTNLVKKAIYAMVEGDCDEVVLETEITNKSALKLYENLGFVRDKRLFRYYLNGVDALRLKLWLR | Function: Catalytic subunit of the N-terminal acetyltransferase C (NatC) complex. Catalyzes acetylation of the N-terminal methionine residues of peptides beginning with Met-Leu-Ala and Met-Leu-Gly. Necessary for the lysosomal localization and function of ARL8B sugeesting that ARL8B is a NatC substrate.
Catalytic Activity: acetyl-CoA + N-terminal L-methionyl-L-leucyl-[protein] = CoA + H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-leucyl-[protein]
Sequence Mass (Da): 39320
Sequence Length: 362
Subcellular Location: Cytoplasm
EC: 2.3.1.256
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Q8CES0 | MAEVPPGPSSLLPPPAPAAPAAAELRCPFPAGAALACCSEDEEDDEEHEGGCGSPAGGEAATSAKARSCLRCPQLPPEQQQQQLNGLIGPELRHLRAAATLKSKVLSAAEAAAPDGASKVTATKGAEGHPGERPPHSVPNNARTALPGRSEAAAAAAGAASDPAAARNGLVEGTEQQEEEEMDEQVRLLSSSLTTGCSLRSSQGREAEPGEDRTIRYVRYESELQMPDIMRLITKDLSEPYSIYTYRYFIHNWPQLCFLAMVGEECVGAIVCKLDMHKKMFRRGYIAMLAVDSKYRRNGIGTNLVKKAIYAMVEGDCDEVVLETEITNKSALKLYENLGFVRDKRLFRYYLNGVDALRLKLWLR | Function: Catalytic subunit of the N-terminal acetyltransferase C (NatC) complex. Catalyzes acetylation of the N-terminal methionine residues of peptides beginning with Met-Leu-Ala and Met-Leu-Gly. Necessary for the lysosomal localization and function of ARL8B sugeesting that ARL8B is a NatC substrate.
Catalytic Activity: acetyl-CoA + N-terminal L-methionyl-L-leucyl-[protein] = CoA + H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-leucyl-[protein]
Sequence Mass (Da): 39433
Sequence Length: 364
Subcellular Location: Cytoplasm
EC: 2.3.1.256
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O74311 | MVTIVPYSHQYLKDICQLIQKDLSEPYSKYVYRYFVHQWPEFSFVALDNDRFIGAVICKQDVHRGTTLRGYIAMLAIVKEYRGQGIATKLTQASLDVMKNRGAQEIVLETEVDNEAAMSFYERLGFCRYKRLYRYYLNGTDAFRYILYPN | Function: Catalytic component of the NatC N-terminal acetyltransferase.
Catalytic Activity: acetyl-CoA + N-terminal L-methionyl-L-leucyl-[protein] = CoA + H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-leucyl-[protein]
Sequence Mass (Da): 17699
Sequence Length: 150
Subcellular Location: Cytoplasm
EC: 2.3.1.256
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Q0IHH1 | MADAPSGPSVLSHYPGAGLAGEQQREEERHKGCHHHQLNGLISPDLRHLKAVSSLKNKLLEQKTRKDSGLVQPQGRTDTRAPNGLERLQGEEEKLSACLASCSLRGDGEALGNHVSQGENDDTIRYVRYESELQMADIMRLITRDLSEPYSIYTYRYFIHNWPQLCFLAMVGEECVGAIVCKLDMHKKMFRRGYIAMLAVDSKYRRKGIGTHLVKKAIYAMVEGDCDEVVLETEITNKSALKLYENLGFVRDKRLFRYYLNGVDALRLKLWLR | Function: Catalytic subunit of the N-terminal acetyltransferase C (NatC) complex. Catalyzes acetylation of the N-terminal methionine residues of peptides beginning with Met-Leu-Ala and Met-Leu-Gly. Necessary for the lysosomal localization and function of ARL8B sugeesting that ARL8B is a NatC substrate.
Catalytic Activity: acetyl-CoA + N-terminal L-methionyl-L-leucyl-[protein] = CoA + H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-leucyl-[protein]
Sequence Mass (Da): 31074
Sequence Length: 273
Subcellular Location: Cytoplasm
EC: 2.3.1.256
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Q03503 | MEIVYKPLDIRNEEQFASIKKLIDADLSEPYSIYVYRYFLNQWPELTYIAVDNKSGTPNIPIGCIVCKMDPHRNVRLRGYIGMLAVESTYRGHGIAKKLVEIAIDKMQREHCDEIMLETEVENSAALNLYEGMGFIRMKRMFRYYLNEGDAFKLILPLTEKSCTRSTFLMHGRLAT | Function: Catalytic component of the NatC N-terminal acetyltransferase, which catalyzes acetylation of the N-terminus Met of L-A virus GAG protein and possibly GRH1.
Catalytic Activity: acetyl-CoA + N-terminal L-methionyl-L-leucyl-[protein] = CoA + H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-leucyl-[protein]
Sequence Mass (Da): 20457
Sequence Length: 176
Subcellular Location: Cytoplasm
EC: 2.3.1.256
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Q5E9A1 | MPGEATDTVPATEQELPQPQAETGSGTESDSDESVPELEEQDSTQATTQQAQLAAAAEIDEEPVSKAKQSRSEKKARKAMSKLGLRQVTGVTRVTIRKSKNILFVITKPDVYKSPASDTYIVFGEAKIEDLSQQAQLAAAEKFKVQGEAVSNIQENTQTPTVQEESEEEEVDETGVEVKDIELVMSQANVSRAKAVRALKNNSNDIVNAIMELTM | Function: Prevents inappropriate targeting of non-secretory polypeptides to the endoplasmic reticulum (ER). Binds to nascent polypeptide chains as they emerge from the ribosome and blocks their interaction with the signal recognition particle (SRP), which normally targets nascent secretory peptides to the ER. Also reduces the inherent affinity of ribosomes for protein translocation sites in the ER membrane (M sites). May act as a specific coactivator for JUN, binding to DNA and stabilizing the interaction of JUN homodimers with target gene promoters.
PTM: Phosphorylation of Ser-43 by ILK during cell adhesion may promote nuclear localization. Phosphorylation of Thr-159 by GSK3B may promote proteasome mediated degradation.
Sequence Mass (Da): 23370
Sequence Length: 215
Domain: The positively charged inner surface of the NAC-A/B domain is crucial for NACA localization in the nucleus and DNA-binding. This region is blocked from binding nucleic acids in the heterodimeric complex by a helix region in the beta-subunit, it also displays much higher affinity for RNA than DNA (By similarity).
Subcellular Location: Cytoplasm
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Q6QN10 | MPGEATETVPATEQELPQPQAETGSGTESDSDESVPELEGQDSTQATTQQAQLAAAAEIDEEPVSKAKQSRSEKKARKAMSKLGLRQVTGVTRVTIRKSKNILFVITKPDVYKSPASDTYIVFGEAKIEDLSQQAQLAAAEKFKVQGEAVSNIQENTQTPTVQEESEEEEVDETGVEVKDIEWVMSQANVSRAKAVRALKNNSNNIVNAIMELTM | Function: Prevents inappropriate targeting of non-secretory polypeptides to the endoplasmic reticulum (ER). Binds to nascent polypeptide chains as they emerge from the ribosome and blocks their interaction with the signal recognition particle (SRP), which normally targets nascent secretory peptides to the ER. Also reduces the inherent affinity of ribosomes for protein translocation sites in the ER membrane (M sites). May act as a specific coactivator for JUN, binding to DNA and stabilizing the interaction of JUN homodimers with target gene promoters (By similarity).
PTM: Phosphorylation of Ser-43 by ILK during cell adhesion may promote nuclear localization. Phosphorylation of Thr-159 by GSK3B may promote proteasome mediated degradation.
Sequence Mass (Da): 23384
Sequence Length: 215
Domain: The positively charged inner surface of the NAC-A/B domain is crucial for NACA localization in the nucleus and DNA-binding. This region is blocked from binding nucleic acids in the heterodimeric complex by a helix region in the beta-subunit, it also displays much higher affinity for RNA than DNA (By similarity).
Subcellular Location: Cytoplasm
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Q9K105 | MQTAARRSFDYDMPLIQTPTSACQIRQAWAKVADTPDRETADRLKDEIKALLKEKNAVLVAHYYVDPLIQDLALETGGCVGDSLEMARFGAEHEAGTLVVAGVRFMGESAKILCPEKTVLMPDLEAECSLDLGCPEEAFSAFCDQHPDRTVVVYANTSAAVKARADWVVTSSVALEIVSYLKSRGEKLIWGPDRHLGDYICRETGADMLLWQGSCIVHNEFKGQELAALKAEHPEAVVLVHPESPQSVIELGDVVGSTSKLLKAAVSRPEKKFIVATDLGILHEMQKQAPDKQFIAAPTAGNGGSCKSCAFCPWMAMNSLGGIKYALTSGRNEILLDRKLGEAAKLPLQRMLDFAAGLKKKDVFNGMGPA | Cofactor: Binds 1 [4Fe-4S] cluster per subunit.
Function: Catalyzes the condensation of iminoaspartate with dihydroxyacetone phosphate to form quinolinate.
Catalytic Activity: dihydroxyacetone phosphate + iminosuccinate = H(+) + 2 H2O + phosphate + quinolinate
Sequence Mass (Da): 40164
Sequence Length: 370
Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate from iminoaspartate: step 1/1.
Subcellular Location: Cytoplasm
EC: 2.5.1.72
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Q7S936 | MKFTLLSTAVALLTSTAVALPTSSSSAGSLLNERSYVNASSTATTCPYSRRSPAYCAGTAQNRTLSATYICGDSRLGPVVLPQFFLPLDPILDIYDRFGGLCPGAFLEKWFNQTGSGWWDYPPQNGFSVDDEGNIIAANLTLQTGTFVDRFGSEYGSFLAPAAAPYLQRSLPPSNLNGDAKFPWNYHVYSVIKPFAVLAGPIAPWFGQPGQGVQYQTYENVATLIADGYLKAEDPQRLVPRNY | Function: Conidial surface nicotinamide adenine dinucleotide glycohydrolase that cleave NAD(+) and NADP(+) but not their reduced counterparts, NADH and NADPH . Lacks both ADP-ribosyl cyclase and base exchange activity and does not mediate synthesis of calcium messengers cADPR or NAADP . Its function is correlated with aerial hyphae formation and conidiogenesis, but its physiological role is still obscure . Is able to ADP-ribosylate itself for self-inactivation .
PTM: N-glycosylated.
Catalytic Activity: H2O + NAD(+) = ADP-D-ribose + H(+) + nicotinamide
Sequence Mass (Da): 26378
Sequence Length: 243
Subcellular Location: Secreted
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Q2QTL0 | MDVSSLAAAAPSLVAPPLHHKPHLAFPPHHPSPARGSIGVRCAHSPSPHPLRPSAATADEEVSLPPSLRVSRLAEEFRVSPDAADRARRLLARAAALPRLGEADRVAANRVMGCVAQVWLVGRCDGAGRMRFAADSDSELSRGYCACLVSALDGARPEEVLDVDPADLAPLGGAAAGTGARSRASTWHNVLIGMQKRARAAIAAREGRPAGEPFPSLIIGRDGAIRAQGTYAEAQAMFLSPNESKTSELVKSLREKKIGIVAHFYMDPEVQGILTASKKHWPHIHISDSLVMADSAVKMAEAGCEYITVLGVDFMSENVRAILDQAGYSKVGVYRMSSDQIGCSLADAASSSAYTHFLKEASRSPPSLHVIYINTSLETKAHAHELVPTITCTSSNVVATILQAFAQIPGLNVWYGPDSYMGANIADLFQRMAVMSDEEIAEVHPSHNKKSINALLPRLHYYQDGNCIVHDMFGHEVVDKIKEQYCDAFLTAHFEVPGEMFSLSMEAKTRGMGVVGSTQNILDFIKNHLMEALDRNIDDHLQFVLGTESGMITSIVAAVRELFDSYKTSQQSANIEVEIVFPVSSDAVSNTSVNGSHHLDSSTVTDLDNVSVVPGVSSGEGCSIHGGCASCPYMKMNSLRSLLKVCHQLPDRDNRLVAYQASRFNAKTPLGKLVAEVGCEPILHMRHFQATKRLPDKLVHHVIHGKGEPTS | Cofactor: Binds 1 [4Fe-4S] cluster per subunit.
Function: Catalyzes the condensation of iminoaspartate with dihydroxyacetone phosphate to form quinolinate.
Catalytic Activity: dihydroxyacetone phosphate + iminosuccinate = H(+) + 2 H2O + phosphate + quinolinate
Sequence Mass (Da): 76683
Sequence Length: 711
Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate from iminoaspartate: step 1/1.
Subcellular Location: Plastid
EC: 2.5.1.72
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Q7N6S3 | MNQYIDFNSTIYPFPPKPAFLSKDEKKHYREKIKRLLKQQDAVMVAHYYTDPEIQALAEETGGCVADSLEMARFGNNHPASTLLVAGVRFMGETAKILNPEKRVLMPTLEAECSLDLGCPEKEFTQFCDDHPDRTVVVYANTSAAVKARADWVVTSSIAVELIDYLDSQGKKIIWAPDRHLGNYVRKQTGADILCWQGACIVHDEFKTQALIRVKGLHPDAAVLVHPESPQAVIDLADAVGSTSQLIKSAQSLPHQKLIVATDKGIFYKMQQACPEKQLFAAPTAGEGASCRSCAHCPWMAMNGLQAIVQGLEQGGGQHEILVEKELREKALVPLNRMLDFAAQLK | Cofactor: Binds 1 [4Fe-4S] cluster per subunit.
Function: Catalyzes the condensation of iminoaspartate with dihydroxyacetone phosphate to form quinolinate.
Catalytic Activity: dihydroxyacetone phosphate + iminosuccinate = H(+) + 2 H2O + phosphate + quinolinate
Sequence Mass (Da): 38243
Sequence Length: 346
Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate from iminoaspartate: step 1/1.
Subcellular Location: Cytoplasm
EC: 2.5.1.72
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Q7V7S6 | MVRMTAVCTAKTVSPVPSTRKELKGAIAELRKKLNAVILAHYYQDPEIQDIADFIGDSLELSRRAASTNADVIVFCGVHFMAETAKILSPEKIVLLPDLEAGCSLADDCPADEFAAFRDKHPDHIVVSYINCTAAVKAQSDLICTSSNAVELVNQLPKDQPILFAPDQNLGRWVQKQSGRKLTIWPGRCMVHETFSEEALLKLKIMHPEAKVIAHPECLENLLELADYIGSTSKLLEFTEISSCTKFIVLTEPGILHQMKLKNPKKEFMDVPGIDGCSCNECPYMRLNTLEKLWSCLSTMKPSIEIEEGVRQKAFIPIQRMLNMKETQEASEH | Cofactor: Binds 1 [4Fe-4S] cluster per subunit.
Function: Catalyzes the condensation of iminoaspartate with dihydroxyacetone phosphate to form quinolinate.
Catalytic Activity: dihydroxyacetone phosphate + iminosuccinate = H(+) + 2 H2O + phosphate + quinolinate
Sequence Mass (Da): 37173
Sequence Length: 333
Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate from iminoaspartate: step 1/1.
Subcellular Location: Cytoplasm
EC: 2.5.1.72
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A8FFF0 | MKKIGLFGGTFDPPHNGHLLMANEVRFQVGLDEIWFIPNHKPPHKTDRKRADSRHRVKMVEAAIESNPHFRLELIEMEREGPSYTVDTVELLKKRHPEDEFFFMIGADMVEYLPKWHRIDDLLQMITFIGMKRPGYTGSTTYSLLFADVPAFDVSSTLIRQRIMQEKPVDYLLPKAVERYIKEHHLYES | Function: Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
Catalytic Activity: ATP + H(+) + nicotinate beta-D-ribonucleotide = deamido-NAD(+) + diphosphate
Sequence Mass (Da): 22197
Sequence Length: 189
Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; deamido-NAD(+) from nicotinate D-ribonucleotide: step 1/1.
EC: 2.7.7.18
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P54455 | MKKIGIFGGTFDPPHNGHLLMANEVLYQAGLDEIWFMPNQIPPHKQNEDYTDSFHRVEMLKLAIQSNPSFKLELVEMEREGPSYTFDTVSLLKQRYPNDQLFFIIGADMIEYLPKWYKLDELLNLIQFIGVKRPGFHVETPYPLLFADVPEFEVSSTMIRERFKSKKPTDYLIPDKVKKYVEENGLYES | Function: Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
Catalytic Activity: ATP + H(+) + nicotinate beta-D-ribonucleotide = deamido-NAD(+) + diphosphate
Sequence Mass (Da): 22157
Sequence Length: 189
Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; deamido-NAD(+) from nicotinate D-ribonucleotide: step 1/1.
EC: 2.7.7.18
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Q8A675 | MRMAESNKLKTGIFSGSFNPVHIGHLALANYLCEYEELDEVWFMVSPQNPLKAGTELWPDDLRLRLVELATEEYPRFRSSDFEFHLPRPSYSVHTLEKLHETYPERDFYLIIGSDNWARFDRWYQSERIIKENRILIYPRPGFPVNENGLPETVRLVHSPTFEISSTFIRQALDEKKDVRYFLHPKVWEYIREYIRQSITDN | Function: Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
Catalytic Activity: ATP + H(+) + nicotinate beta-D-ribonucleotide = deamido-NAD(+) + diphosphate
Sequence Mass (Da): 24160
Sequence Length: 202
Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; deamido-NAD(+) from nicotinate D-ribonucleotide: step 1/1.
EC: 2.7.7.18
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Q1LTM7 | MAKRLLTAFYGGTFDPIHHGHLQPVIALAQLVNLKQVILLPNHIPLHRPLPKATPQQRLRMTRLAIADTPGKLFVIDERELRRNTPSWTVETFKVLRSEYGPMAPLGLIIGQDSLLTLPQWHRSQELFELCHILVCARPGYQYGIAGYKNNNWMEYRFTDDPSALNYQPAGLVYCAETPELAISASDIRGRVHAILPYYDLLTHSVHAYINKQGLYR | Function: Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
Catalytic Activity: ATP + H(+) + nicotinate beta-D-ribonucleotide = deamido-NAD(+) + diphosphate
Sequence Mass (Da): 24750
Sequence Length: 217
Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; deamido-NAD(+) from nicotinate D-ribonucleotide: step 1/1.
EC: 2.7.7.18
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Q2KYV6 | MKRIGLLGGSFDPIHVAHVTLAQSALAHLQLDEVQLVPAANPWQRAPLAATAQDRLAMINAAITGLPGLAVNTSEIQRGGATYTVDTILALPQDARYTWILGADQLANFCTWRDWETIVRHVDLAVATRPGSTLQAAPELAQALLEAGRSLRELPFTPMPVSASEIRQRLAQGQNTEGLLPEGVARHIAEHGLYRPA | Function: Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
Catalytic Activity: ATP + H(+) + nicotinate beta-D-ribonucleotide = deamido-NAD(+) + diphosphate
Sequence Mass (Da): 21230
Sequence Length: 197
Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; deamido-NAD(+) from nicotinate D-ribonucleotide: step 1/1.
EC: 2.7.7.18
|
O51723 | MRIAILGGTYNPVHIGHIFLAKEIEYLLNIDRVIFIPTCNPAHKLIDENVSVSNRIDMLKLALENEDKMFIDDCDIINGGITYTVDTISCVKKKYKNDKLFLIIGDDLFQNFDSWKDPQSIVSSVELVVAHRIYKERLKSSFKHIYIDNKIIPISSSEIRNRIVNGLPVSYLLPFGVLKYIKDNNLYVKKVNV | Function: Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
Catalytic Activity: ATP + H(+) + nicotinate beta-D-ribonucleotide = deamido-NAD(+) + diphosphate
Sequence Mass (Da): 22174
Sequence Length: 193
Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; deamido-NAD(+) from nicotinate D-ribonucleotide: step 1/1.
EC: 2.7.7.18
|
Q89X84 | MRVGLLGGSFNPPHQAHRAISQFALKRLQLDRVWWLVTPGNPLKENGTLHELGARMQAARDVANDPRIEVSCLESVIRTRYTIDTINTLRRRLRGLRFVWIMGADNLAQFHRWQDWRRIAGQVPIAVIDRPPQSFRALASPAAKALSRYRLPENEAALLADRPAPAWVFLTGLKLNLSSTGLRNPDGSWKGTK | Function: Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
Catalytic Activity: ATP + H(+) + nicotinate beta-D-ribonucleotide = deamido-NAD(+) + diphosphate
Sequence Mass (Da): 21803
Sequence Length: 193
Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; deamido-NAD(+) from nicotinate D-ribonucleotide: step 1/1.
EC: 2.7.7.18
|
P57090 | MKKIGLFGGTFDPIHNGHLHIARAFADEIGLDAVVFLPTGGPYHKDAASASAADRLAMVELATAEDARFAVSDCDIVREGATYTFDTVQIFRQQFPSAQLWWLMGSDSLMKLHTWKKWQMLVRETNIAVAMRQGDSLHQTPRELHAWLGKSLQDGSVRILSAPMHNVSSTEIRRNLAGQGVSDGIPPAAARYIREHGLYEK | Function: Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
Catalytic Activity: ATP + H(+) + nicotinate beta-D-ribonucleotide = deamido-NAD(+) + diphosphate
Sequence Mass (Da): 22269
Sequence Length: 201
Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; deamido-NAD(+) from nicotinate D-ribonucleotide: step 1/1.
EC: 2.7.7.18
|
A6Q541 | MKIAIFGGSFDPPHKGHIAIVKRALEELDIDYVIIVPTYLNPFKTSFQASPSLRLRWLRKIFLPYNRVKICDYEVRKGRPTYAIETVEFLRRKYAPKKLYYIIGSDNLPTLHKWHKYQKLSHLVQFVVATRKGYKVPKKYKMIEVHEDISSTELRIHPKKRYLPPIVAEEIIRFYRS | Function: Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
Catalytic Activity: ATP + H(+) + nicotinate beta-D-ribonucleotide = deamido-NAD(+) + diphosphate
Sequence Mass (Da): 21062
Sequence Length: 177
Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; deamido-NAD(+) from nicotinate D-ribonucleotide: step 1/1.
EC: 2.7.7.18
|
Q8YM77 | MQHLAVFGGTFDPIHWGHLLIAEAALQQIPIEKVIWVPSLNPPHKKASAFRHRLAMLQLATQDNPAFTVSSVEKNRSGVSYAINTLTDLSVCFPNTHWYWIVGLDTFQTLPRWYRGQELAPMCDWLIAPRLVGGENIAQSELICKQVKQQLRKQSDTIHWHLLHIPLVGVSSSLIRKLYRIGKSIRYLVPEDVRSYIAAHKLYSEDSE | Function: Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
Catalytic Activity: ATP + H(+) + nicotinate beta-D-ribonucleotide = deamido-NAD(+) + diphosphate
Sequence Mass (Da): 23745
Sequence Length: 208
Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; deamido-NAD(+) from nicotinate D-ribonucleotide: step 1/1.
EC: 2.7.7.18
|
B1ZVV8 | MKIGFLGGSFDPVHFGHLIAAQDAFEQFRLDRLILVPAAQAPLKPNDVQSSPEDRFAMLRAAVEWDQRFEVSDVELRRGGTSYTIDSARYFRKQFPRDELYWIIGGDQLPQLHLWRDVSELGQLVDFIFLERPGFPIKARVDIPGLRLHRCDGHLLAISSTELRDRVKRNLSLDYFVPHKAIVYIREKHLYRPSQ | Function: Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
Catalytic Activity: ATP + H(+) + nicotinate beta-D-ribonucleotide = deamido-NAD(+) + diphosphate
Sequence Mass (Da): 22643
Sequence Length: 195
Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; deamido-NAD(+) from nicotinate D-ribonucleotide: step 1/1.
EC: 2.7.7.18
|
A6L8D1 | MGLKTGIYSGSFNPIHIGHLALANWLCEFEGLDEVWFVVTPHNPLKKKDDLLDDSLRLEMAQAAIDGYPKFRVCDIEFYLPKPSYSIDTLRTLSRNYPNRDFYFIMGADNWQLFPRWKEHEKILQDYKLLIYPRLGFDISIPAIYPNVKKVDAPLMEISSTFIRNAYQADKDIRFFLPEGVRPYYYKI | Function: Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
Catalytic Activity: ATP + H(+) + nicotinate beta-D-ribonucleotide = deamido-NAD(+) + diphosphate
Sequence Mass (Da): 22113
Sequence Length: 188
Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; deamido-NAD(+) from nicotinate D-ribonucleotide: step 1/1.
EC: 2.7.7.18
|
A7HT64 | MARRELLTPGLKVGLLGGSFNPAHEGHLHVTRMCLRALGLDRVWWLVSPQNPLKSDAGMASFDRRLASAEKMARDPRICVSDIEARLGTRYTVDTLAALTSRFPQIRFVWLMGADNLIQLPHWARWRDIVQTVPIAVYPRPGFTLKARLSPAATALRDVTLDATDAALLPLLTAPALAFLDGPESSQSATSIRERGGWSLR | Function: Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
Catalytic Activity: ATP + H(+) + nicotinate beta-D-ribonucleotide = deamido-NAD(+) + diphosphate
Sequence Mass (Da): 22176
Sequence Length: 201
Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; deamido-NAD(+) from nicotinate D-ribonucleotide: step 1/1.
EC: 2.7.7.18
|
B4SH35 | MHLALFGATFDPPHNGHLALCLFARELLGIDKLIVSVSNNPFKPESGRADVHRMRMAELLTQEINLTGAFSEVSGWELEKKQPSYTVDLLRYLRTLYPADKLTLLVGEDSFREFSKWKESETFCSLSDVVVFRRVSTQSESTPRPEIIPCEACISFVNFACDISSTLVRSVVASGRSISTLVPPSVHRYIMEYGLYAGEEHHATSIPEPKPRES | Function: Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
Catalytic Activity: ATP + H(+) + nicotinate beta-D-ribonucleotide = deamido-NAD(+) + diphosphate
Sequence Mass (Da): 24007
Sequence Length: 214
Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; deamido-NAD(+) from nicotinate D-ribonucleotide: step 1/1.
EC: 2.7.7.18
|
A1AV35 | MKIGLMGGTFNPIHMAHLRIAEEARELCGLDRVLFIPVADPPHKPLAGEVPFHQRCQMVRLAIAGNRAFELSEIEGQRPGKSYSIDTIGTFREQHPQAELYFIIGSDSFLELGLWRRYADILRSCNLIVVERPGRQVNDPLSALPVDIRGELRYTPASRSLEHVGGTRVHFFAGCLLDISSSEIRRLAATGRSITYLVPPQVEAYIKEQRIYSECP | Function: Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
Catalytic Activity: ATP + H(+) + nicotinate beta-D-ribonucleotide = deamido-NAD(+) + diphosphate
Sequence Mass (Da): 24268
Sequence Length: 216
Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; deamido-NAD(+) from nicotinate D-ribonucleotide: step 1/1.
EC: 2.7.7.18
|
Q4FP43 | MVKPENNLNQKKTKIGILGGTFDPAHKGHLEISKQAKKILELKNIIWAITKQNPFKNTSKTDLKNRIKFAKKIIGKNNFIKVKFYEEKVLSNKTIDLINYLNKDKKFEIYFIMGADNLINFHKWYKWKSIIKKCNLLVFDRQGYKAKSLKSVTYNGVNKNRLSFINFKKVNISSSQLRKI | Function: Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
Catalytic Activity: ATP + H(+) + nicotinate beta-D-ribonucleotide = deamido-NAD(+) + diphosphate
Sequence Mass (Da): 21099
Sequence Length: 180
Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; deamido-NAD(+) from nicotinate D-ribonucleotide: step 1/1.
EC: 2.7.7.18
|
A9BK06 | MLMLFGGSFNPPHIGHRIIAEIAYDEFNPDRFLIVPSKNPPHKSIDFIANFDKRYSWCERVFFEHYFEVSDIENKLPSPSYTIRTIEYLSNFDKNINLLIGEDSLKNFHKWYKWEEILKKVKLVVYPRYFEEKNSYSVDFDYVKLESPIVEISSTYIRQRIKKGKTVKGLIDDKIFEEVLKEYS | Function: Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
Catalytic Activity: ATP + H(+) + nicotinate beta-D-ribonucleotide = deamido-NAD(+) + diphosphate
Sequence Mass (Da): 22010
Sequence Length: 184
Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; deamido-NAD(+) from nicotinate D-ribonucleotide: step 1/1.
EC: 2.7.7.18
|
A6L0W0 | MEKSKIKTGIFGGSFNPIHMGHLALANYLCEYNGLDEIWFLVSPHNPLKQQTDLWDDNLRLELVKLAIADYPKFRASDFEFHLSRPSYTIHTLDALHKAYPNREFTLIIGADNWLLFPRWYKAEEILKNHHVMIYPRPNFTIDPTTLPPSVQLADTPLLEVSSTFIRQALAEGRDIRYFLHPAVYERLKK | Function: Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
Catalytic Activity: ATP + H(+) + nicotinate beta-D-ribonucleotide = deamido-NAD(+) + diphosphate
Sequence Mass (Da): 22152
Sequence Length: 190
Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; deamido-NAD(+) from nicotinate D-ribonucleotide: step 1/1.
EC: 2.7.7.18
|
B2RMD0 | MLTGLFFGSFNPMHIGHLALANYLTEYTPIRQLWFVPSPLNPLKNTQELLPYDLRCELIEQAIRKDIRFQVLRIEELLPSPHYTIRTLRALSMLYPHHRFALLIGADNWQSFDRWKDHHRLMAKYELIIYPRFGYEVNDTTLPTGCRYIHDAPRIEISSTQIRTSILEGKDLRYWLPLPESQDVIASALQSCLSPKR | Function: Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
Catalytic Activity: ATP + H(+) + nicotinate beta-D-ribonucleotide = deamido-NAD(+) + diphosphate
Sequence Mass (Da): 23150
Sequence Length: 197
Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; deamido-NAD(+) from nicotinate D-ribonucleotide: step 1/1.
EC: 2.7.7.18
|
Q8KEX2 | MKPQNLHFDYGLVEAILVPFIRNEIRKFGFGSVVLGLSGGIDSAVVCELAVRALGVENVLALMMPYKTSSQESLDHAELMVDRLGIRYEIMPVTEVVDAFFATRPDASRLRRGNVMARSRMLCLYDVSARDGCLVLGTSNKTELMLGYGTMFGDMASAVNPIGDLYKTQIFGLARHLGIPAPLIDKPPSADLWEGQSDEADLGFSYEEVDQLLYMMLEERMDRDAILAEGIDSAFYQRVRSMVVRNQYKRMMPVIAKLSSRTPGIDFRYARDWQEVR | Function: Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses ammonia as a nitrogen source.
Catalytic Activity: ATP + deamido-NAD(+) + NH4(+) = AMP + diphosphate + H(+) + NAD(+)
Sequence Mass (Da): 31125
Sequence Length: 277
Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from deamido-NAD(+) (ammonia route): step 1/1.
EC: 6.3.1.5
|
B5Y8Q4 | MNTAMEETQRIEQFLRKALVSERKHGYLIGVSGGLDSAVVLKLLVQAVGKENVLGLILPDRDTEKKSTTLARSLLEQEKVPYKVISMTPLLRHLGVYKDMPLFLLPTRGLKESIVRRFYNDYTKKLNKPVFFAQWEEPPTQLPYFYEGIAYYRIKHRVRMATLYYYAEKNDYLLVGCTNLSERLIGFYVKYGDDVCDVAPIAHLYKTEVRQLSEYLSVPEDIRNRPPSPDLIPGITDEYSLGINYETLDQILAGLEEGKTAEDLKQLFPADIVELVINQVKFTQKLEGKPYMLKRA | Function: Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses ammonia as a nitrogen source.
Catalytic Activity: ATP + deamido-NAD(+) + NH4(+) = AMP + diphosphate + H(+) + NAD(+)
Sequence Mass (Da): 34067
Sequence Length: 296
Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from deamido-NAD(+) (ammonia route): step 1/1.
EC: 6.3.1.5
|
Q8NMN7 | MTNTQTEIINELKVSPAIDVAKEVEFRVQFLVDYLRASHTKGFVLGISGGQDSTLAGRLTQLAVERIRAEENSTDYVFYAVRLPYAIQADEDDAQVALEFIAPDKSVTVNVKDATDATEATVAAALELPELTDFNRGNIKARQRMVAQYAIAGQLGLLVIGTDHAAENVTGFFTKFGDGAADLLPLAGLSKRQGAAILEHLGAPSSTWTKVPTADLEEDRPALPDEEALGVSYADIDNYLENKPDVSEKAQQRIEHLWKVGQHKRHLPATPQENWWR | Function: Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses ammonia as a nitrogen source.
Catalytic Activity: ATP + deamido-NAD(+) + NH4(+) = AMP + diphosphate + H(+) + NAD(+)
Sequence Mass (Da): 30426
Sequence Length: 277
Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from deamido-NAD(+) (ammonia route): step 1/1.
EC: 6.3.1.5
|
Q9RYV5 | MTPSPLPLSPLRSHIIRELHVQPDIDPGAEVERRVAFLCDYLQSTPTKGFVLGISGGQDSTLAGRLCQLAVERRRSQGHGATFLAVRLPYGVQADEADAQQALDFIQADREVTVNIKEAADASVAAAQAALGSEVRDFVRGNVKARERMVAQYALAGQENLLVVGTDHAAEALTGFYTKYGDGGVDLTPLSGLTKRQGAQLLAHLGAPEGTWRKVPTADLEDDRPGLPDEVALGVTYAQIDAYLEGREVSDEAAARLERLFLNSRHKRALPVTPFDGWWQPGEQKQS | Function: Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses ammonia as a nitrogen source.
Catalytic Activity: ATP + deamido-NAD(+) + NH4(+) = AMP + diphosphate + H(+) + NAD(+)
Sequence Mass (Da): 31077
Sequence Length: 287
Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from deamido-NAD(+) (ammonia route): step 1/1.
EC: 6.3.1.5
|
Q54ML1 | MKTVTLATCNLNQWAMDFKGNLERIIESINIAKSKGAKYRLGPELEICGYGCEDHFLEQDTMLHCWQSLAVILKDPELTKDILVDVGMPVLHKDVRYNCRVILLNQKIYLIQPKKAMAMDGNYREGRWFTPWIKPRVVETFYLPRIISQITGQDECQIGDAIISTLDTAISSETCEELFTPNSPHIQMGLDGVEIFTNGSGSHHQLRKLDTRVDLIRSATSKSGGIYLYSNQQGCDGSRLYYDGSCMIMINGDCVSQGSQFSLVDIEVITATVDLEDVRSVRASFMARCAQANLTKEFPRVRCPIQLTHIDYCHPPDRVIHINYNTPAEEIGFGPACWLWDYLRRSGLSGYFLPLSGGADSAATAAIIGIMCQLVILDVSKGNKQVLKDAQRITNSPEDYIPTDSREFASRLFFTAYLGSKNSSKETRDRAMEIAKDIGSVHKEVDIDDISQSFNDAFSQITKKQPQFRAHGGTPRENLALQNVQARTRMVLSYHLASLLLWEQGRPGSLLVLGSANCDESLRGYMTKYDCSSADINPIGGMSKIDLRSFIEWAGKFRDMKSILSVLTATPTAELEPITENYTQSDEIDMGMTYEELSIFGKLRKVNRCGPVSMFERLVADWAHLEPSVVAEKVKRFFYYYAINRHKLTTLTPSYHAEGYSPDDNRYDHRQFLYNSKWDVQFETIDKIVLRLSQRPQLKNTVNCPNQASLTQQ | Catalytic Activity: ATP + deamido-NAD(+) + H2O + L-glutamine = AMP + diphosphate + H(+) + L-glutamate + NAD(+)
Sequence Mass (Da): 80583
Sequence Length: 713
Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from deamido-NAD(+) (L-Gln route): step 1/1.
EC: 6.3.5.1
|
Q9VYA0 | MGRKVTVAVSTLNQWALDFEGNMVRILQSILEAKDMGASYRTGPELEVCGYSCEDHFREPDTFLHSWEVLLEVMMSPMCENMLVDVGMPVMHRNVAYNCRVAFFNRQILLIRPKMAMCDDGNYRESRWFTAWTKALQTEEYVLPRMIAQHTGQQTVPFGDAVIATRDTCLGYEICEELWNVRSKHIEMSLAGVELIVNSSGSYMELRKAHITSDLIRNASFKAGGAYLFSNLRGCDGQRVYFNGCSAIALNGEILARSQQFALQDVEVTLATIDLEEIRAYRVSLRSRCTAAASAAEYPRIHCDFEMSTHSDIFKTSTPPLNWPMHTPEEEIALGPACWLWDYLRRSGQGGFFLPLSGGVDSSSSATIVHSMCRQIVQAVQQGDAQVLHDIRQLLADSDYTPDNAAGLCNRLLVTCYMGSVNSSKETRRRAAQLANQLGSYHIEISIDSAVNALLSIFNAVTGLTPRFRTQGGCARQNLALQNMQSRIRMVLAYIFAQLTLWVRNRPGGLLVLGSANVDESLRGYLTKYDCSSADINPIGGISKMDLRRFLTYAKDKFNLPVLESIIDAPPTAELEPLQENGELQQTDEADMGMTYAELSQFGRLRKQSFCGPYSMFCHLVATWKSDLSPKEVAEKVKHFFLCYAINRHKMTVLTPSVHAESYSPDDNRFDHRPFLYRPNWSWQFKAIDDEAEKLQPIYTPSSAQLRPSSEDLLISTQRSSHLDDSKHSSPLSSASASASIDVGISTAAVPLPGAAAPGGLSKKPSGYSKVHVNVLGKIKDRTGIPV | Function: Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses L-glutamine as a nitrogen source (By similarity). Because of its role in energy metabolism, involved in the modulation of aged-related cardiac function, mobility, and lifespan .
Catalytic Activity: ATP + deamido-NAD(+) + H2O + L-glutamine = AMP + diphosphate + H(+) + L-glutamate + NAD(+)
Sequence Mass (Da): 87615
Sequence Length: 787
Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from deamido-NAD(+) (L-Gln route): step 1/1.
EC: 6.3.5.1
|
Q3JP04 | MKIGHQFHTVALVGRSNTPGIAEPLASLAACIAKRGFEVVFEADTAQAIGSAGYPALTPAEIGARADVAVVLGGDGTMLGMGRQLAPYKTPLIGINHGRLGFITDIPASDMREVVPMMLAGSYEREERTLLEARIVRNGEPIYHALAFNDVVVNRSGFSGMAELRVSVDGRFMYNQRSDGLIVATPTGSTAYALSSQGPILHPQLQGIVLVPIAPHALSNRPIVLPDDSKIAIQIIGGRDVNVNFDMQSFTALELNDTIEVRRSKHTVPFLHPVGYSYYATLRKKLHWNEHPSSEDDDDA | Function: Involved in the regulation of the intracellular balance of NAD and NADP, and is a key enzyme in the biosynthesis of NADP. Catalyzes specifically the phosphorylation on 2'-hydroxyl of the adenosine moiety of NAD to yield NADP.
Catalytic Activity: ATP + NAD(+) = ADP + H(+) + NADP(+)
Sequence Mass (Da): 32424
Sequence Length: 300
Subcellular Location: Cytoplasm
EC: 2.7.1.23
|
Q8RAC3 | MKKVGVIPNINKDKDLEVTKSVVNWLLDHGSEPYLNEIVAARIGYEKHGKKANEIYSKSDFLIALGGDGTILNVARLCAPFGTPILAVNLGHLGFLTEIDASELFPSLEKIYKGEYAIEKRMMLEANVVKNDMEVINFRALNDIVITRGAFSRMARIKAYVNDNYVDTYLADGVIVATPTGSTAYSLSAGGPIVYPTVEVIIITPICPHTLYSRSIVVSPDDVIRLEIAEENQDLMITTDGQQGYKIDYRDVIYIKKSNEYTNLIKVKNSNFFDLLRDKLTER | Function: Involved in the regulation of the intracellular balance of NAD and NADP, and is a key enzyme in the biosynthesis of NADP. Catalyzes specifically the phosphorylation on 2'-hydroxyl of the adenosine moiety of NAD to yield NADP.
Catalytic Activity: ATP + NAD(+) = ADP + H(+) + NADP(+)
Sequence Mass (Da): 31617
Sequence Length: 283
Subcellular Location: Cytoplasm
EC: 2.7.1.23
|
A4XKP6 | MIVGVFANFQKELSKEILDKIVSVLKNEKIDWVLMNEKNKDSVKVNFLITIGGDGTLLNVVEKVAKENLPVLGINCGRVGYLTEEVADNIHFAIKKIIDNDYFIEERHLVEAHFKDKIFYALNDICLARSTFNIIDLSLYIDEVFAQEYRSDGIIIATATGSTAYSLSAGGPIVEPQLGVMVVTPICPHSLSSRSLVLGDDRVVKIKSESDEVLVVSDGRVADTLKKGEYLECKISSKKLKLVRLKKKNFYEVLREKIKE | Function: Involved in the regulation of the intracellular balance of NAD and NADP, and is a key enzyme in the biosynthesis of NADP. Catalyzes specifically the phosphorylation on 2'-hydroxyl of the adenosine moiety of NAD to yield NADP.
Catalytic Activity: ATP + NAD(+) = ADP + H(+) + NADP(+)
Sequence Mass (Da): 29141
Sequence Length: 260
Subcellular Location: Cytoplasm
EC: 2.7.1.23
|
Q9PHM6 | MQNKIDYKNIKKIGLVTRPNVSLDKEILKLQSILSIYKVELVLLKESSEILDLPKYGLDDLFKISDFVISLGGDGTLISLCRKACEYDKAVLGIHAGHLGFLTDFKVDEAENFFQAFFQGEFRIEKPYLLSIFLEDRQGKILEKLAFNDVVISKNNQASMAHIEVFRKEKKFNEYFGDGLIVATPAGSTAYNLSANGPIVYTLAQAFILTPVCSHSLTQRPIVLPKGFEIEIMAKDCMLCIDGQENYKMNDFKSIKVGLSDKNVALIHPKNRDYFQILKEKLHWGN | Function: Involved in the regulation of the intracellular balance of NAD and NADP, and is a key enzyme in the biosynthesis of NADP. Catalyzes specifically the phosphorylation on 2'-hydroxyl of the adenosine moiety of NAD to yield NADP.
Catalytic Activity: ATP + NAD(+) = ADP + H(+) + NADP(+)
Sequence Mass (Da): 32382
Sequence Length: 286
Subcellular Location: Cytoplasm
EC: 2.7.1.23
|
B9KFZ4 | MKKCINIEKIQKIGLFCRLNTNLNKQIDFLRAIFLQKNIELVLLEQEKINLKDLQELDFLISLGGDGTLLSLCRQAYQAKKPILGINAGNLGFLTALSFNEAESFFKDFFKNDFKIEKAKMLQITLYKKNKIIKKFAFNDAVFSRDNALMANVEVFFENKLFNAYYGDGLIIASSSGSTAYNISAGGPIVHPWSEIFVLTPVCSHSLTQRPIVLPYGFELELKVEHCLLYLDGQEVVDPKEYDKILIGLSKKELSFIHKKNRDYFQVLKEKLNWGK | Function: Involved in the regulation of the intracellular balance of NAD and NADP, and is a key enzyme in the biosynthesis of NADP. Catalyzes specifically the phosphorylation on 2'-hydroxyl of the adenosine moiety of NAD to yield NADP.
Catalytic Activity: ATP + NAD(+) = ADP + H(+) + NADP(+)
Sequence Mass (Da): 31594
Sequence Length: 276
Subcellular Location: Cytoplasm
EC: 2.7.1.23
|
Q3AAN2 | MNKDKKLGPILLEKIMEKARDYDFLLKNRYLVSGECGIVEIAEIDEKTEKIDLVLVLGGDGTILCATRYFAPKAIPILGINLGQLGYLSELDPQEIDFGLQKIRAGEYLVEDRTMLEARVRRANQEVAVFYGLNDGVLTKGAFARIINFAVFVDEQYITEYAADGVIVATPTGSTAYSLSAGGAILDPEVKAFIITPICPHTLAARSLVVADDKEIRIVVKTALESSMLTVDGQQGFGIKPGDEIIIKKAPYQAKFIKLKNRSFYQLLREKMREANRYHD | Function: Involved in the regulation of the intracellular balance of NAD and NADP, and is a key enzyme in the biosynthesis of NADP. Catalyzes specifically the phosphorylation on 2'-hydroxyl of the adenosine moiety of NAD to yield NADP.
Catalytic Activity: ATP + NAD(+) = ADP + H(+) + NADP(+)
Sequence Mass (Da): 31111
Sequence Length: 280
Subcellular Location: Cytoplasm
EC: 2.7.1.23
|
Q87YK2 | MEQFRNIGIIGRLGSVQVLDTVRRLKRFLLDRHLHVILEETIAEVLPGHGLQTSSRKMLGEVCDMVIVVGGDGSLLGAARALARHNVPVLGINRGSLGFLTDIRPDELEVKCAEVLDGHYLVENRFLLQAEVRRHGEAIGQGDALNDVVLHPGKSTRMIEFEIYIDGQFVCSQKADGLIVATPTGSTAYALSAGGPIMHPKLDAIVIVPMYPHTLSGRPIVVDGNSELKIVVSKDMTIYPQVSCDGQNHFTCAPGDTITVSKKPQKLRLIHPLDHNYYEVCRTKLGWGSRLGGGGD | Function: Involved in the regulation of the intracellular balance of NAD and NADP, and is a key enzyme in the biosynthesis of NADP. Catalyzes specifically the phosphorylation on 2'-hydroxyl of the adenosine moiety of NAD to yield NADP.
Catalytic Activity: ATP + NAD(+) = ADP + H(+) + NADP(+)
Sequence Mass (Da): 32255
Sequence Length: 296
Subcellular Location: Cytoplasm
EC: 2.7.1.23
|
Q4FRP5 | MPHLHESELFHAIKNPAFRRIGLMGRARTRSVTQSIGQIAQIINDMNLTLIMDVQTANLPTLNLTEIERVKIVKRSLIGEICDLVIVVGGDGSILHAAEALARYRVPVLGVNRGRLGFLADVKPDEAAFKLRQVLMGNYQLDHRFLLTMEIREGRKIIHEDMALNDVVLHAGKSVHMIDFQMKIDGHDVYRQHSDGLIVATPTGSTAYALSGGGPIIHPSMDAICLVPMHPHTLSSRPIVVSGTSEICIRIHEDNRTQPMVSADGKPSTPLDQEQRLYIRKHPDKLTLLHPPGFDFYEACRTKLHWNVHAEEFSLDVDDDIMDDE | Function: Involved in the regulation of the intracellular balance of NAD and NADP, and is a key enzyme in the biosynthesis of NADP. Catalyzes specifically the phosphorylation on 2'-hydroxyl of the adenosine moiety of NAD to yield NADP.
Catalytic Activity: ATP + NAD(+) = ADP + H(+) + NADP(+)
Sequence Mass (Da): 36371
Sequence Length: 325
Subcellular Location: Cytoplasm
EC: 2.7.1.23
|
Q57961 | MRGFIIGRFQPFHKGHLEVIKKIAEEVDEIIIGIGSAQKSHTLENPFTAGERILMITQSLKDYDLTYYPIPIKDIEFNSIWVSYVESLTPPFDIVYSGNPLVRVLFEERGYEVKRPEMFNRKEYSGTEIRRRMLNGEKWEHLVPKAVVDVIKEIKGVERLRKLAQTDK | Catalytic Activity: ATP + beta-nicotinamide D-ribonucleotide + H(+) = diphosphate + NAD(+)
Sequence Mass (Da): 19610
Sequence Length: 168
Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from nicotinamide D-ribonucleotide: step 1/1.
Subcellular Location: Cytoplasm
EC: 2.7.7.1
|
A2SS82 | MRRGLYVGRFQPFHNGHKAVIDGLAEEVDELIIGIGSADISHDIRHPFTAGERVLMITRALNGLKIPFYVIPLEDVKRNALWVAHVKSMVPPFDTVYTSNPLVIQLFKEAGIPVLSPPMYLRESLSGTAVRKKMYHGEAWEEYVPKEVVSVVGEIHGIERMQQISKSD | Catalytic Activity: ATP + beta-nicotinamide D-ribonucleotide + H(+) = diphosphate + NAD(+)
Sequence Mass (Da): 18905
Sequence Length: 168
Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from nicotinamide D-ribonucleotide: step 1/1.
Subcellular Location: Cytoplasm
EC: 2.7.7.1
|
A3CVW1 | MSRGFYIGRFQPYHNGHQSVLERIARTADEIVIGVGSAQVSHTVANPFTAGERVLMLTRSLEDLDCPFYVIPIEDVQRNALWVAHVRSMTPPFDTVYSSNPLVMQLFAEAGVDVQSPDMYERLTHSGTVIRQRMLGGEPWEHLVPPAVVDVIREIHGVERLQRIAGSD | Catalytic Activity: ATP + beta-nicotinamide D-ribonucleotide + H(+) = diphosphate + NAD(+)
Sequence Mass (Da): 18837
Sequence Length: 168
Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from nicotinamide D-ribonucleotide: step 1/1.
Subcellular Location: Cytoplasm
EC: 2.7.7.1
|
Q9UXN8 | MRRAFYIGRFQPFHLGHYSLIKDIARDADEVVIGIGSAQKSHEPKNPFTAGERVMMIKHALEDAGIKHYAIPLEDLQRNAVWVSHIISMTPPFDVVYSNNPLVVRLFQESGILVEQPPMYQREGYSGSEIRKRMLRGEDWKSLVPAAVIDVIDEIDGVNRLKSVSKSDKDYRD | Catalytic Activity: ATP + beta-nicotinamide D-ribonucleotide + H(+) = diphosphate + NAD(+)
Sequence Mass (Da): 19738
Sequence Length: 173
Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from nicotinamide D-ribonucleotide: step 1/1.
Subcellular Location: Cytoplasm
EC: 2.7.7.1
|
Q6L2T8 | MRAFIVGRFQPFHNGHMEILKRILHENDSVIIGIGSAQFSHTLKDPFTAGERHLMISSALEESGVYNYYLVPIEDVNSNPLWVSHVESLTPPFQRVYTNNPLVKRLFYEKGYEVLSMDLLNRKEWSGTSIRNKMIRGENWKKDVPPAVARVIDEIDGVSRIRDLSESDE | Catalytic Activity: ATP + beta-nicotinamide D-ribonucleotide + H(+) = diphosphate + NAD(+)
Sequence Mass (Da): 19459
Sequence Length: 169
Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from nicotinamide D-ribonucleotide: step 1/1.
Subcellular Location: Cytoplasm
EC: 2.7.7.1
|
Q97MK9 | MKIVTVNDYDEMSKFAAKIIASQIILKENSVLGLATGGTPLGMYKELINLYNKENLNFSKVQTFNLDEYYGVSDDNPQSYHYYMKNNFFKFTNIKNENINILDGTTSDIENECKSYDNKILSSGGIDIQVLGIGENGHIGFNEPDINFEAKTHLVKLDEKTIEANSRFFNSKNEVPTSALSMGIKTIMQSKKILLLANGEKKAEAIFKMVNGKISPEVPASILQLHNDTTIIIDKAAAKML | Function: Catalyzes the reversible isomerization-deamination of glucosamine 6-phosphate (GlcN6P) to form fructose 6-phosphate (Fru6P) and ammonium ion.
Catalytic Activity: alpha-D-glucosamine 6-phosphate + H2O = beta-D-fructose 6-phosphate + NH4(+)
Sequence Mass (Da): 26905
Sequence Length: 241
Pathway: Amino-sugar metabolism; N-acetylneuraminate degradation; D-fructose 6-phosphate from N-acetylneuraminate: step 5/5.
EC: 3.5.99.6
|
A0PYW1 | MKILSFKDYNELSKEASKIVLNQVISKPNSVLGLATGSTPLGMYKNLIVAYQNKNIDFSKIKTFNLDEYYGLSKHNNQSYYHYMMENLFNHINIDINNINIPNGTASDILKECSDYEDKIKNYNGIDLQILGIGVNGHIGFNEPSTYFEPSTHVVTLDKKTIESNSRFFSSKEEVPTKAISMGIKTIMNAKKIILLANGKNKADAIFKTVNGKIDPNIPASILQLHNDVTLILDKDAASKL | Function: Catalyzes the reversible isomerization-deamination of glucosamine 6-phosphate (GlcN6P) to form fructose 6-phosphate (Fru6P) and ammonium ion.
Catalytic Activity: alpha-D-glucosamine 6-phosphate + H2O = beta-D-fructose 6-phosphate + NH4(+)
Sequence Mass (Da): 26955
Sequence Length: 241
Pathway: Amino-sugar metabolism; N-acetylneuraminate degradation; D-fructose 6-phosphate from N-acetylneuraminate: step 5/5.
EC: 3.5.99.6
|
Q0TML8 | MRLIVTKNYEEMSKVAAKEMAEDIKRNPEIVLGLATGGTPVGMYKELIRMYNEGELDFSKVTSINLDEYVGLSGDHDQSYRYFMNTNLFNHINIDKNNTFVPNGLAENVEEECMAYDARIQDMGGIDLQLLGLGANGHIGFNEPGEALSVGTHLTDLKESTIEANARFFDSIDDVPRKAITMGLGGIMKAKKIMVIASGEGKAEVVKAMMSGKITTEIPATMLQMHRDVILIVDEDAAKLLK | Function: Catalyzes the reversible isomerization-deamination of glucosamine 6-phosphate (GlcN6P) to form fructose 6-phosphate (Fru6P) and ammonium ion.
Catalytic Activity: alpha-D-glucosamine 6-phosphate + H2O = beta-D-fructose 6-phosphate + NH4(+)
Sequence Mass (Da): 26653
Sequence Length: 242
Pathway: Amino-sugar metabolism; N-acetylneuraminate degradation; D-fructose 6-phosphate from N-acetylneuraminate: step 5/5.
EC: 3.5.99.6
|
A1JQE8 | MRLIPLKNTTEVGKWAARYIVNRINAFKPTADRPFVLGLPTGGTPMEAYKHLVALYKAGEVSFKNVVTFNMDEYVGLPQEHPESYYTFMHSNFFDHVDIPAENINLLNGNAPDIDEECRRYEEKIKSYGKIHLFMGGVGVDGHIAFNEPASSLASRTRIKTLTEETREANSRFFGGDANLVPKYALTVGVGTLLDAEEVMILVTGRGKAQALQAAVEGSINHMWTISCLQLHAKAIMVCDEPSTMELKVKTVKYFSELEAENIKNL | Function: Catalyzes the reversible isomerization-deamination of glucosamine 6-phosphate (GlcN6P) to form fructose 6-phosphate (Fru6P) and ammonium ion.
Catalytic Activity: alpha-D-glucosamine 6-phosphate + H2O = beta-D-fructose 6-phosphate + NH4(+)
Sequence Mass (Da): 29662
Sequence Length: 266
Pathway: Amino-sugar metabolism; N-acetylneuraminate degradation; D-fructose 6-phosphate from N-acetylneuraminate: step 5/5.
EC: 3.5.99.6
|
Q5FA94 | MTVPHIPRGPVMADIAAFRLTEEEKQRLLDPAIGGIILFRRNFQNIEQLKTLTAEIKALRTPELIIAVDHEGGRVQRFIEGFTRLPAMNVLGQIWDKDGASAAETAAGQVGRVLATELSACGIDLSFTPVLDLDWGNCAVIGNRSFHRNPEAVARLALALQKGLAKGGMKSCGKHFPGHGFVEGDSHLVLPEDGRSLDELEAADLAPFRIMSREGMAAVMPAHVVYPQVDTKPAGFSEIWLKQILRRDIGFKGVIFSDDLTMEGACGAGGIKERARISFEAGCDIVLVCNRPDLVDELRDGFTIPDNQDLAGRWQYMENSLGHEAVQAVMQTMGFQAAQAFVAGLASPQDTAGGVKVGEAF | Function: Plays a role in peptidoglycan recycling by cleaving the terminal beta-1,4-linked N-acetylglucosamine (GlcNAc) from peptide-linked peptidoglycan fragments, giving rise to free GlcNAc, anhydro-N-acetylmuramic acid and anhydro-N-acetylmuramic acid-linked peptides.
Catalytic Activity: Hydrolysis of terminal non-reducing N-acetyl-D-hexosamine residues in N-acetyl-beta-D-hexosaminides.
Sequence Mass (Da): 39033
Sequence Length: 361
Pathway: Cell wall biogenesis; peptidoglycan recycling.
Subcellular Location: Cytoplasm
EC: 3.2.1.52
|
Q82SJ8 | MSLGPLMLDIAGTELTETDRVRLSHPLVGGVILFARNYASPAQLAGLTAEIHALRYPSLLIAVDQEGGRVQRFRDGFARLPPMRVLGEICDRNPDRAHHLASQAGYVLAAELKACGVDLSFTPVLDLDYGQSCVIGDRAFHREPQVVADLACALMNGLQSAGMAAVGKHFPGHGAIRADTHVETAIDTRSYTDIEKEDLIPFRRMIDAGLSGIMAAHVIYPAIDQHSAGFSSRWLQRILRHDLGFEGCIFSDDLGMQAARNYGSITRRAEQALQAGCDMVLVCNDADAADELLGSLHWEFSAASLARVECMRGQHMIHSMAQLHEMERFLQAADEISKIDPAGISVSL | Function: Plays a role in peptidoglycan recycling by cleaving the terminal beta-1,4-linked N-acetylglucosamine (GlcNAc) from peptide-linked peptidoglycan fragments, giving rise to free GlcNAc, anhydro-N-acetylmuramic acid and anhydro-N-acetylmuramic acid-linked peptides.
Catalytic Activity: Hydrolysis of terminal non-reducing N-acetyl-D-hexosamine residues in N-acetyl-beta-D-hexosaminides.
Sequence Mass (Da): 37871
Sequence Length: 348
Pathway: Cell wall biogenesis; peptidoglycan recycling.
Subcellular Location: Cytoplasm
EC: 3.2.1.52
|
B4EVE7 | MGPVMLDVEGYELDNEEREILKHPLVGGLILFTRNFHDAEQLNELVRQIRDASHERLVIAVDQEGGRVQRFRDGFTRLPAAQSYAALNERYQASRLAQEAGWLMASEMIAMDIDISFAPVLDLGHDCIAIGERSFHECPEIAMDMAESFIKGMRSAGMKSTGKHFPGHGAVRADSHKETPRDERSLNDIRQRDMAIFKDFIQRQLLDAIMPAHVIYSQIDERPASGSPYWLKSILREQLGFQGVIFSDDLSMEGAAIMGSYAQRAQRSLDAGCDMLLVCNNRKGAVSVLDNLSFVKAERISALYHHRGRYTLSELQASDRWKKANQMLTQLQEQWQERA | Function: Plays a role in peptidoglycan recycling by cleaving the terminal beta-1,4-linked N-acetylglucosamine (GlcNAc) from peptide-linked peptidoglycan fragments, giving rise to free GlcNAc, anhydro-N-acetylmuramic acid and anhydro-N-acetylmuramic acid-linked peptides.
Catalytic Activity: Hydrolysis of terminal non-reducing N-acetyl-D-hexosamine residues in N-acetyl-beta-D-hexosaminides.
Sequence Mass (Da): 38399
Sequence Length: 339
Pathway: Cell wall biogenesis; peptidoglycan recycling.
Subcellular Location: Cytoplasm
EC: 3.2.1.52
|
B7UYS5 | MQGSLMLDIGGTWLTAEDRQILRHPEVGGLIIFARNIEHPAQVRELCAAIRAIRPDLLLAVDQEGGRVQRLRQGFVRLPAMRAIADNPNAEELAEHCGWLMATEVQAVGLDLSFAPVLDLDHQRSAVVGSRAFEGDPERAALLAGAFIRGMHAAGMAATGKHFPGHGWAEADSHVAIPEDARSLEEIRRSDLVPFARLAGQLDALMPAHVIYPQVDPQPAGFSRRWLQEILRGELKFDGVIFSDDLSMAGAHVVGDAASRIEAALAAGCDMGLVCNDRASAELALAALQRLKVTPPSRLQRMRGKGYANTDYRQQPRWLEALSALRAAQLID | Function: Plays a role in peptidoglycan recycling by cleaving the terminal beta-1,4-linked N-acetylglucosamine (GlcNAc) from peptide-linked peptidoglycan fragments, giving rise to free GlcNAc, anhydro-N-acetylmuramic acid and anhydro-N-acetylmuramic acid-linked peptides.
Catalytic Activity: Hydrolysis of terminal non-reducing N-acetyl-D-hexosamine residues in N-acetyl-beta-D-hexosaminides.
Sequence Mass (Da): 36101
Sequence Length: 332
Pathway: Cell wall biogenesis; peptidoglycan recycling.
Subcellular Location: Cytoplasm
EC: 3.2.1.52
|
A1SW90 | MRPVILDVEGYELDSEEKEILAHPLVAGIILFTRNYYDIEQLKALVKDIRRYAGNELLIAVDHEGGRVQRFRDDFTRLPSAGSLIEKNDMKTACELAFSSAWVMASELIACDIDFSFAPVLDLNGISNVIQNRAFSSSITETVTLAEAYINGMKSAGMVSTGKHFPGHGSVEADSHTALPVDSRSELEIFTKDIKPFENLIKKGALDAVMPSHVVYSQCDLQPAGFSSYWLDDVLRTRLGFKGVVISDDLSMHGASFVGNHLSRAESAIQAGCDLILACNDRSGAVSILDNLKVKPTAQYHAVNQLRSTKNKFILPLNKNPIWIKNKQMLMQLSEQF | Function: Plays a role in peptidoglycan recycling by cleaving the terminal beta-1,4-linked N-acetylglucosamine (GlcNAc) from peptide-linked peptidoglycan fragments, giving rise to free GlcNAc, anhydro-N-acetylmuramic acid and anhydro-N-acetylmuramic acid-linked peptides.
Catalytic Activity: Hydrolysis of terminal non-reducing N-acetyl-D-hexosamine residues in N-acetyl-beta-D-hexosaminides.
Sequence Mass (Da): 37284
Sequence Length: 337
Pathway: Cell wall biogenesis; peptidoglycan recycling.
Subcellular Location: Cytoplasm
EC: 3.2.1.52
|
Q8RDN5 | MNKILESIRGKLIVSCQALEDEPLHSSFIMGRMAYAAYSGGAAGIRANTVEDIKEIKKNVSLPIIGIIKKVYNNSDVYITPTIKEVEDLINEGVQIIAIDATKRERPDRKDLKNFIAEIKEKYPNQLFMADISSVDEALYAEKIGFDIVGTTLVGYTDYTKNYKALEELKKVVKVVKIPVIAEGNIDTPLKAKKALEIGAFAVVVGGAITRPQQITKKFVDEMK | Function: Converts N-acetylmannosamine-6-phosphate (ManNAc-6-P) to N-acetylglucosamine-6-phosphate (GlcNAc-6-P).
Catalytic Activity: an N-acyl-D-glucosamine 6-phosphate = an N-acyl-D-mannosamine 6-phosphate
Sequence Mass (Da): 24823
Sequence Length: 224
Pathway: Amino-sugar metabolism; N-acetylneuraminate degradation; D-fructose 6-phosphate from N-acetylneuraminate: step 3/5.
EC: 5.1.3.9
|
Q7VKN0 | MSKLSHSEVLIMIQGGLVVSCQPVDDGPMDQPAIVAAMAQAAIVGGAVGVRIEGVQNLKATRPMVTAPIIAIVKRDLPESAVRITPFLADIDQLAAAGADIIAVDGTDRERPVAVVAALERIHAQGCLAMADCSTLAEGLYCQQLGFDIIGSTMSGYTGGELPVEPDYQLVKDLKSAGCYVMAEGRYNSPALAKSAMQMGADCVTVGSALTRLEHMVSWFAVAVQSAKE | Function: Converts N-acetylmannosamine-6-phosphate (ManNAc-6-P) to N-acetylglucosamine-6-phosphate (GlcNAc-6-P).
Catalytic Activity: an N-acyl-D-glucosamine 6-phosphate = an N-acyl-D-mannosamine 6-phosphate
Sequence Mass (Da): 23904
Sequence Length: 229
Pathway: Amino-sugar metabolism; N-acetylneuraminate degradation; D-fructose 6-phosphate from N-acetylneuraminate: step 3/5.
EC: 5.1.3.9
|
P71340 | MSKLSYQEVLSQIQYGLISSCQPVDDGPMDKPEIVSAMAQASVMGGRSGLRIEGVDNLKATRPFVNVPIIGIVKRDLPDSPVRITPFLQDIEDLANAGADIIAVDGTSRPRPVDIESAVKKIHEMGCLAMADCSNLEEGLYCKALGFDIVGSTMSGYTGGAVPEEPDYQLVKDLKSAGCFVMAEGRYNTPELAKVAIEIGADCVTVGSALTRLEHIVSWFANSVKSAR | Function: Converts N-acetylmannosamine-6-phosphate (ManNAc-6-P) to N-acetylglucosamine-6-phosphate (GlcNAc-6-P).
Catalytic Activity: an N-acyl-D-glucosamine 6-phosphate = an N-acyl-D-mannosamine 6-phosphate
Sequence Mass (Da): 24353
Sequence Length: 228
Pathway: Amino-sugar metabolism; N-acetylneuraminate degradation; D-fructose 6-phosphate from N-acetylneuraminate: step 3/5.
EC: 5.1.3.9
|
Q71VW2 | MGNSVMEKIKGGLVVSCQALEDEPLHSAFIMSKMALAAVQGGAVGIRANTAKDIRAIQSEIDVPIIGIYKKDYDDSDVFITPTLEEVREICETGVEIVAMDATTRKRPHNEDLKDILNAIRKEFPNTLFMADTGSIEDVYYADSLGFDLIGTTLYGYTEETANKNISDDDFSHLKEVLKSTKRPVIAEGKIDSPSKARQVLTLGCYAVVVGGAVTRPQEITTRFTNEIKKI | Function: Converts N-acetylmannosamine-6-phosphate (ManNAc-6-P) to N-acetylglucosamine-6-phosphate (GlcNAc-6-P).
Catalytic Activity: an N-acyl-D-glucosamine 6-phosphate = an N-acyl-D-mannosamine 6-phosphate
Sequence Mass (Da): 25352
Sequence Length: 231
Pathway: Amino-sugar metabolism; N-acetylneuraminate degradation; D-fructose 6-phosphate from N-acetylneuraminate: step 3/5.
EC: 5.1.3.9
|
P39185 | MKISRRDFIKQTAITATASVAGVTLPAGAANFVTDSEVTKLKWSKAPCRFCGTGCGVTVAVKDNKVVATQGDPQAEVNKGLNCVKGYFLSKIMYGQDRLTRPLMRMKNGKYDKNGDFAPVTWDQAFDEMERQFKRVLKEKGPTAVGMFGSGQWTVWEGYAAAKLYKAGFRSNNIDPNARHCMASAAAGFMRTFGMDEPMGCYDDFEAADAFVLWGSNMAEMHPILWTRVTDRRLSHPKTRVVVLSTFTHRCFDLADIGIIFKPQTDLAMLNYIANYIIRNNKVNKDFVNKHTVFKEGVTDIGYGLRPDHPLQKAAKNASDPGAAKVITFDEFAKFVSKYDADYVSKLSAVPKAKLDQLAELYADPNIKVMSLWTMGFNQHTRGTWANNMVYNLHLLTGKIATPGNSPFSLTGQPSACGTAREVGTFSHRLPADMVVTNPKHREEAERIWKLPPGTIPDKPGYDAVLQNRMLKDGKLNAYWVQVNNNMQAAANLMEEGLPGYRNPANFIVVSDAYPTVTALAADLVLPSAMWVEKEGAYGNAERRTQFWHQLVDAPGEARSDLWQLVEFAKRFKVEEVWPPELIAKKPEYKGKTLYDVLYRNGQVDKFPLKDVNAEYHNAEAKAFGFYLQKGLFEEYATFGRGHGHDLAPFDAYHEARGLRWPVVNGKETRWRYREGSDPYVKAGTGFQFYGNPDGKAVIFALPYEPPAESPDKEYPYWLVTGRVLEHWHSGSMTRRVPELYRSFPNAVVFMHPEDAKALGLRRGVEVEVVSRRGRMRSRIETRGRDAPPRGLVFVPWFDASQLINKVTLDATCPISLQTDFKKCAVKIVKV | Cofactor: Binds 1 [4Fe-4S] cluster.
Function: Catalytic subunit of the periplasmic nitrate reductase complex NapAB. Receives electrons from NapB and catalyzes the reduction of nitrate to nitrite.
PTM: Predicted to be exported by the Tat system (By similarity). The position of the signal peptide cleavage has been experimentally proven .
Catalytic Activity: 2 Fe(II)-[cytochrome] + 2 H(+) + nitrate = 2 Fe(III)-[cytochrome] + H2O + nitrite
Sequence Mass (Da): 93346
Sequence Length: 831
Subcellular Location: Periplasm
EC: 1.9.6.1
|
P81186 | MSTSRRDFLKYFAMSAAVAAASGAGFGSLALAADNRPEKWVKGVCRYCGTGCGVLVGVKDGKAVAIQGDPNNHNAGLLCLKGSLLIPVLNSKERVTQPLVRRHKGGKLEPVSWDEALDLMASRFRSSIDMYGPNSVAWYGSGQCLTEESYVANKIFKGGFGTNNVDGNPRLCMASAVGGYVTSFGKDEPMGTYADIDQATCFFIIGSNTSEAHPVLFRRIARRKQVEPGVKIIVADPRRTNTSRIADMHVAFRPGTDLAFMHSMAWVIINEELDNPRFWQRYVNFMDAEGKPSDFEGYKAFLENYRPEKVAEICRVPVEQIYGAARAFAESAATMSLWCMGINQRVQGVFANNLIHNLHLITGQICRPGATSFSLTGQPNACGGVRDGGALSHLLPAGRAIPNAKHRAEMEKLWGLPEGRIAPEPGYHTVALFEALGRGDVKCMIICETNPAHTLPNLNKVHKAMSHPESFIVCIEAFPDAVTLEYADLVLPPAFWCERDGVYGCGERRYSLTEKAVDPPGQCRPTVNTLVEFARRAGVDPQLVNFRNAEDVWNEWRMVSKGTTYDFWGMTRERLRKESGLIWPCPSEDHPGTSLRYVRGQDPCVPADHPDRFFFYGKPDGRAVIWMRPAKGAAEEPDAEYPLYLTSMRVIDHWHTATMTGKVPELQKANPIAFVEINEEDAARTGIKHGDSVIVETRRDAMELPARVSDVCRPGLIAVPFFDPKKLVNKLFLDATDPVSREPEYKICAARVRKA | Cofactor: Binds 1 [4Fe-4S] cluster.
Function: Catalytic subunit of the periplasmic nitrate reductase complex NapAB. Receives electrons from NapB and catalyzes the reduction of nitrate to nitrite.
PTM: Predicted to be exported by the Tat system (By similarity). The position of the signal peptide cleavage has been experimentally proven .
Catalytic Activity: 2 Fe(II)-[cytochrome] + 2 H(+) + nitrate = 2 Fe(III)-[cytochrome] + H2O + nitrite
Sequence Mass (Da): 83497
Sequence Length: 755
Subcellular Location: Periplasm
EC: 1.9.6.1
|
Q06457 | MTETRTTCPYCGVGCGVIASRAPHGQVSVRGDEQHPANFGRLCVKGAALGETVGLEGRMLFPEVDGERATWPQALAAAGSRLREIIDRHGPQAVAFYASGQLLTEDYYAANKLMKGFIGAANIDTNSRLCMSSAVTGYKRALGADVVPCSYEDVENSDLVVLVGSNAAWAHPVLYQRLAQAKRDNPQMRVVVIDPRRTATCDIADRHLALAPGSDGGLFVGLLNAIAASGAISDDFNDAQRALTIAQDWDLDKVAQFCGLPRQQIADFYREFIAAPRAITLYTMGINQSASGSDKCNAIINVHLACGKYGRPGCGPFSLTGQPNAMGGREVGGLATMLAAHMNFEPDDLRRLARFWGSERLAQTPGLTGVELFAAIGRGEVKAVWIMGTNPVVSLPDSHAVSEALARCPLVIISDVVADTDTGRFAHIRFPALAWGEKSGTVTNSERRISRQRAFMPPPGEARADWWIVARVAEALGFGSAFAWQHPHEVFSEHAALSGYENDGQRAFDIGGLADLSREAWDALEPVRWPVSRSEAAWSVHKGWHRDGKLRMVPVAPQPTRATTDAFYPLILNSGRIRDQWHTMTRTGAVPRLMQHINEPVVEVAPADAQRYHLLEGELARVRSPKGVMVAKVTIGDGQRPGSLFVPMHWNNQFARQGRVNNLLAAVTDPHSGQPESKQTAVAIATWLPAWKGELFSRQPVPLPASLHWRRRAAQGIIHLSLAGDTRSRDWLVEWCQRQGWQMQVAEGGKVWNLLAWRAGELMLGWWSDASEPAIDADWIHAAFRVPPQNAARRHALLSGRKGGVEMPRGRIICSCFSVGERAIGEAIAGGCRTPGALGGKLKCGTNCGSCIPELKALLAAKLAQA | Cofactor: Binds 1 [4Fe-4S] cluster.
Function: Nitrate reductase is a key enzyme involved in the first step of nitrate assimilation in plants, fungi and bacteria.
Sequence Mass (Da): 93897
Sequence Length: 866
Pathway: Nitrogen metabolism; nitrate reduction (denitrification); dinitrogen from nitrate: step 1/4.
EC: 1.7.-.-
|
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