ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
Q23381 | MYLQLLKPTLLRCSTRPSSSGAYTRSPIDQKWAAMAKKAMKGREADTLTWNTPEGIPIKPLYLRSDRDCDAQRSVELPGQFPFTRGPYPTMYTQRPWTIRQYAGFSTVEESNKFYKENIKAGQQGLSVAFDLATHRGYDSDNPRVFGDVGMAGVAVDSVEDMRQLFDGINLEKMSVSMTMNGAVVPVLAMYVVAAEEAGVSRKLLAGTIQNDILKEFMVRNTYIYPPEPSMRIIGDIFAYTSREMPKFNSISISGYHMQEAGADAVLEMAFTIADGIQYCETGLNAGLTIDAFAPRLSFFWGISMNFYMEIAKMRAARRL... | 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... |
P22033 | MLRAKNQLFLLSPHYLRQVKESSGSRLIQQRLLHQQQPLHPEWAALAKKQLKGKNPEDLIWHTPEGISIKPLYSKRDTMDLPEELPGVKPFTRGPYPTMYTFRPWTIRQYAGFSTVEESNKFYKDNIKAGQQGLSVAFDLATHRGYDSDNPRVRGDVGMAGVAIDTVEDTKILFDGIPLEKMSVSMTMNGAVIPVLANFIVTGEEQGVPKEKLTGTIQNDILKEFMVRNTYIFPPEPSMKIIADIFEYTAKHMPKFNSISISGYHMQEAGADAILELAYTLADGLEYSRTGLQAGLTIDEFAPRLSFFWGIGMNFYMEIA... | 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)-methy... |
P65486 | MSIDVPERADLEQVRGRWRNAVAGVLSKSNRTDSAQLGDHPERLLDTQTADGFAIRALYTAFDELPEPPLPGQWPFVRGGDPLRDVHSGWKVAEAFPANGATADTNAAVLAALGEGVSALLIRVGESGVAPDRLTALLSGVYLNLAPVILDAGADYRPACDVMLALVAQLDPGQRDTLSIDLGADPLTASLRDRPAPPIEEVVAVASRAAGERGLRAITVDGPAFHNLGATAATELAATVAAAVAYLRVLTESGLVVSDALRQISFRLAADDDQFMTLAKMRALRQLWARVAEVVGDPGGGAAVVHAETSLPMMTQRDPW... | 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 degrada... |
Q59676 | MAKEKEKLFSEFPPVSREAWIDKITADLKGVPFEKKLVWRTNEGFNVNPFYRREDIEDLKTTTSLPDEYPYVRSTRMHNEWLVRQDIVVGDNVAEANEKALDLLNKGVDSLGFYLKKVHINVDTLAALLKDIELTAVELNFNCCITRAADLLSAFSAYVKKVGADPNKCHGSVSYDPFKKQLVRGVSNPDWVKMTLPVMDAARELPAFRVLNVNAVNLSDAGAFITQELGYALAWGAELLDKLTDAGYKPEEIASRIKFNFGIGSNYFMEIAKFRAARWLWAQIVGSYGDQYKNETAKIHQHATTSMWNKTVFDAHVNLL... | 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 degrada... |
P11652 | MSSTDQGTNPADTDDLTPTTLSLAGDFPKATEEQWEREVEKVLNRGRPPEKQLTFAECLKRLTVHTVDGIDIVPMYRPKDAPKKLGYPGVAPFTRGTTVRNGDMDAWDVRALHEDPDEKFTRKAILEGLERGVTSLLLRVDPDAIAPEHLDEVLSDVLLEMTKVEVFSRYDQGAAAEALVSVYERSDKPAKDLALNLGLDPIAFAALQGTEPDLTVLGDWVRRLAKFSPDSRAVTIDANIYHNAGAGDVAELAWALATGAEYVRALVEQGFTATEAFDTINFRVTATHDQFLTIARLRALREAWARIGEVFGVDEDKRGA... | 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 degrada... |
Q05064 | MTVLPDDGLSLAAEFPDATHEQWHRLVEGVVRKSGKDVSGTAAEEALSTTLEDGLTTRPLYTARDAAPDAGFPGFAPFVRGSVPEGNTPGGWDVRQRYASADPARTNEAVLTDLENGVTSLWLTLGSAGLPVTGLERALDGVYLDLVPVALDAGSEAATAARELLRLYEAAGVADDAVRGTLGADPLGHEARTGEKSTSFAAVAELARLCGERYPGLRALTVDALPYHEAGASAAQELGASLATGVEYLRALHDKGLGVEKAFAQLEFRFAATADQFLTIAKLRAARRLWARVAEVSGVPAAGAQRQHAVTSPVMMTRRD... | 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 isobutyr... |
Q59677 | MKPNYKDIDIKSAGFVAKDATRWAEEKGIVADWRTPEQIMVKPLYTKDDLEGMEHLDYVSGLPPFLRGPYSGMYPMRPWTIRQYAGFSTAEESNAFYRRNLASGQKGLSVAFDLATHRGYDADHSRVVGDVGKAGVSICSLEDMKVLFDGIPLSKMSVSMTMNGAVLPILAFYINAGLEQGAKLEEMAGTIQNDILKEFMVRNTYIYPPEFSMRIIADIFEYTSQNMPKFNSISISGYHMQEAGATADIEMAYTLADGMQYLKAGIDAGIDVDAFAPRLSFFWAIGVNHFMEIAKMRAARLLWAKIVKSFGAKNPKSLAL... | 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
|
P11653 | MSTLPRFDSVDLGNAPVPADAARRFEELAAKAGTGEAWETAEQIPVGTLFNEDVYKDMDWLDTYAGIPPFVHGPYATMYAFRPWTIRQYAGFSTAKESNAFYRRNLAAGQKGLSVAFDLPTHRGYDSDNPRVAGDVGMAGVAIDSIYDMRELFAGIPLDQMSVSMTMNGAVLPILALYVVTAEEQGVKPEQLAGTIQNDILKEFMVRNTYIYPPQPSMRIISEIFAYTSANMPKWNSISISGYHMQEAGATADIEMAYTLADGVDYIRAGESVGLNVDQFAPRLSFFWGIGMNFFMEVAKLRAARMLWAKLVHQFGPKNP... | 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: 7... |
Q7SB97 | MSLFGSSPPNDGSAALNPAKTANSSRSTLFDNEAPTTRSGSALFADDDHDSPWDMPTPRKQRSRADLIRNLLPSGDVPESYIETFDAVVRTENRSTNGRITAGGVARTLAAAKLGADDQARIMGIIAPASASATGAGGGGDGAHGGEANSSAAAAAAAVGLGDLGRNEFNVLLALIGLVQEGEVASLDGVDERRRNLPQPKLQGLVNENVQPMLPNLSELGAKPPQRPVTPPKAPTPSPPKQQQQQQHQPPTLRKVSMEYPEDPWNAPDLHKGHNHGPLEHSTGHNGAADVPRSVANDLNGNDAVSYSTSPEVTTTSSAL... | 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
|
O14120 | MGDNVFLEPDPWASSSNWGSPVKPLNYKTAIGNSSIPLQYRNYWDVFQANNVLLFPEEESYSDIFHVPQDVMKEFFTLIESSSNQPLRQIQFFVLLALVACYQLGVPSTLEQIFKQRNVLPILQRFNPELFNRSSDNETPLFPNNSPPASTTALNLSSNIVPSINESKILEQEDDDVSNKSLPHAQQSIIRSFPDIQKQPKGFFSYPSSTVSSIAPSTLEAGNLHSQQPPKFSVDSSVDDNAITPRKPFSKIPNRLSPSTQPLLSNSRHSSFRLASSSTSFPASLEMNVDIDLEPSGYFFYRHNNYIISDSSNTREVLRR... | 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
|
Q4PHC3 | MSRHHRPFTWGGAQPGASFSNPTSPTLEASTFGFEPSVPDIYRRAWILVTKDASAELFADTSDADIHLGLLHKLLTSAGGLGPGSAEQIVNSACKGSRCSRSDFYCALGLLHQMQQGEELDVHLVQQRLTMGSLSAPVLDLSDATLNPHSHHTFPPTAPSGPSRIDPRPSTFMREMSDPWNANSSGSYNGIDTRPAYNQYDAMPQQYDTLNSHDSALPAGFAGNVSSGSFERIKFNAGDDRRSHQLLAHNQGSSTDTFLAPDRTEARARQPNTRQERPFSYMSDTAETNAVDAAEDPAADLPEDQVTVRLRSELEGFIIK... | 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
|
Q6CHY6 | MSLFSAATTAVERTGYGSRYDHIFDMFHPIDGRIPAVCYKRLLETINVSGEDKDRLATLAGSILEGGDGSGGILTSSFTRESWRAALLLANVAQDGLPFDDPSQLVNVDTLTPMDFSEEGERSSINFSASTTGRSQTPLFGDDLDDHSIQSSRSESIIHNNGHSRGHSALDWNPEEQEALQQSQLSQSQLSRSTTPPPLNPQALVPESESGVWTAPPRPDFAPNKADSVTLAIVPEREGMFLFRHVNYSISSVSGTDRITVIRRYSDFSWLQDYLLKKYCFRQVPLLPPKRLAVNGHYLSSDNYFLERRRRGLTRFINQV... | 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
|
P40959 | MDNYEGSDPWNTSSNAWTKDDDHVVSTTNSEPSLNGISGEFNTLNFSTPLDTNEEDTGFLPTNDVLEESIWDDSRNPLGATGMSQTPNIAANETVIDKNDARDQNIEESEADLLDWTNNVRKTYRPLDADIIIIEEIPEREGLLFKHANYLVKHLIALPSTSPSEERTVVRRYSDFLWLREILLKRYPFRMIPELPPKRIGSQNADQLFLKKRRIGLSRFINLVMKHPKLSNDDLVLTFLTVRTDLTSWRKQATYDTSNEFADKKISQEFMKMWKKEFAEQWNQAASCIDTSMELWYRITLLLERHEKRIMQMVHERNFF... | 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 ... |
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 ... |
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-phosphomevalo... |
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 prot... |
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 prot... |
P0A1I5 | MIQSFLKQVSTKPELIILVLMVMIIAMLIIPLPTYLVDFLIGLNIVLAILVFMGSFYIERILSFSTFPSVLLITTLFRLALSISTSRLILVDADAGKIITTFGQFVIGDSLAVGFVIFSIVTVVQFIVITKGSERVAEVAARFSLDGMPGKQMSIDADLKAGIIDAAGAKERRSILERESQLYGSFDGAMKFIKGDAIAGIIIIFVNLIGGISVGMSQHGMSLSGALSTYTILTIGDGLVSQIPALLISISAGFIVTRVNGDSDNMGRNIMSQIFGNPFVLIVTSALALAIGMLPGFPFFVFFLIAVTLTALFYYKKVVE... | 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 ... |
Q58DG1 | MGHRFLRGFLRVLLPPLPLRSPHLKLSLEPVAPSKRPRSHLMAPPRIGTHNGTFHCDEALACALLRLLPEYREAEIVRTRDPEKLAACDIVVDVGGEYDPQRHRYDHHQRSFTETMSSLSPGKPWQTKLSSAGLIYLHFGHKLLAQLLGTSEEDGMVGTLYDKMYENFVEEVDAVDNGISQWEEGEPRYLLTTTLSARVARLNPTWNQPNQDTEAGFKRAMDLVREEFLQRLDFYQNSWLPARTLVEEALAKRFQVDPSGEIIELEKGGCPWKEHLYQLELGLSPAGTIAFVIYTDQAGQWRVQCVPKEPHSFQSRLPLL... | 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 alt... |
Q9HB07 | MGHRFLRGLLTLLLPPPPLYTRHRMLGPESVPPPKRSRSKLMAPPRIGTHNGTFHCDEALACALLRLLPEYRDAEIVRTRDPEKLASCDIVVDVGGEYDPRRHRYDHHQRSFTETMSSLSPGKPWQTKLSSAGLIYLHFGHKLLAQLLGTSEEDSMVGTLYDKMYENFVEEVDAVDNGISQWAEGEPRYALTTTLSARVARLNPTWNHPDQDTEAGFKRAMDLVQEEFLQRLDFYQHSWLPARALVEEALAQRFQVDPSGEIVELAKGACPWKEHLYHLESGLSPPVAIFFVIYTDQAGQWRIQCVPKEPHSFQSRLPLP... | 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 al... |
Q9JK81 | MGRRFLRGILTLPLRSVLQAQHRMLGSEQDPPAKRPRNNLMAPPRIGTHNGTFHCDEALACALLRLLPEYANAEIVRTRDPEKLASCDIVVDVGGEYNPQSHRYDHHQRTFTETMSSLCPGKPWQTKLSSAGLVYLHFGRKLLAQLLGTSEEDSVVDTIYDKMYENFVEEVDAVDNGISQWAEGEPRYAMTTTLSARVARLNPTWNQPNQDTEAGFRRAMDLVQEEFLQRLNFYQHSWLPARALVEEALAQRFKVDSSGEIVELAKGGCPWKEHLYHLESELSPKVAITFVIYTDQAGQWRVQCVPKEPHSFQSRLPLPE... | 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 al... |
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 memb... |
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
S... |
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 memb... |
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 memb... |
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 memb... |
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 memb... |
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 memb... |
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 memb... |
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 memb... |
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 memb... |
Q147X3 | MAEVPPGPSSLLPPPAPPAPAAVEPRCPFPAGAALACCSEDEEDDEEHEGGGSRSPAGGESATVAAKGHPCLRCPQPPQEQQQLNGLISPELRHLRAAASLKSKVLSVAEVAATTATPDGGPRATATKGAGVHSGERPPHSLSSNARTAVPSPVEAAAASDPAAARNGLAEGTEQEEEEEDEQVRLLSSSLTADCSLRSPSGREVEPGEDRTIRYVRYESELQMPDIMRLITKDLSEPYSIYTYRYFIHNWPQLCFLAMVGEECVGAIVCKLDMHKKMFRRGYIAMLAVDSKYRRNGIGTNLVKKAIYAMVEGDCDEVVL... | 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 Activi... |
Q8CES0 | MAEVPPGPSSLLPPPAPAAPAAAELRCPFPAGAALACCSEDEEDDEEHEGGCGSPAGGEAATSAKARSCLRCPQLPPEQQQQQLNGLIGPELRHLRAAATLKSKVLSAAEAAAPDGASKVTATKGAEGHPGERPPHSVPNNARTALPGRSEAAAAAAGAASDPAAARNGLVEGTEQQEEEEMDEQVRLLSSSLTTGCSLRSSQGREAEPGEDRTIRYVRYESELQMPDIMRLITKDLSEPYSIYTYRYFIHNWPQLCFLAMVGEECVGAIVCKLDMHKKMFRRGYIAMLAVDSKYRRNGIGTNLVKKAIYAMVEGDCDEV... | 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 Activi... |
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
|
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 Activi... |
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]
Sequen... |
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 redu... |
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 redu... |
Q9K105 | MQTAARRSFDYDMPLIQTPTSACQIRQAWAKVADTPDRETADRLKDEIKALLKEKNAVLVAHYYVDPLIQDLALETGGCVGDSLEMARFGAEHEAGTLVVAGVRFMGESAKILCPEKTVLMPDLEAECSLDLGCPEEAFSAFCDQHPDRTVVVYANTSAAVKARADWVVTSSVALEIVSYLKSRGEKLIWGPDRHLGDYICRETGADMLLWQGSCIVHNEFKGQELAALKAEHPEAVVLVHPESPQSVIELGDVVGSTSKLLKAAVSRPEKKFIVATDLGILHEMQKQAPDKQFIAAPTAGNGGSCKSCAFCPWMAMNSL... | 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: Cof... |
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 ... |
Q2QTL0 | MDVSSLAAAAPSLVAPPLHHKPHLAFPPHHPSPARGSIGVRCAHSPSPHPLRPSAATADEEVSLPPSLRVSRLAEEFRVSPDAADRARRLLARAAALPRLGEADRVAANRVMGCVAQVWLVGRCDGAGRMRFAADSDSELSRGYCACLVSALDGARPEEVLDVDPADLAPLGGAAAGTGARSRASTWHNVLIGMQKRARAAIAAREGRPAGEPFPSLIIGRDGAIRAQGTYAEAQAMFLSPNESKTSELVKSLREKKIGIVAHFYMDPEVQGILTASKKHWPHIHISDSLVMADSAVKMAEAGCEYITVLGVDFMSENVR... | 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: Cof... |
Q7N6S3 | MNQYIDFNSTIYPFPPKPAFLSKDEKKHYREKIKRLLKQQDAVMVAHYYTDPEIQALAEETGGCVADSLEMARFGNNHPASTLLVAGVRFMGETAKILNPEKRVLMPTLEAECSLDLGCPEKEFTQFCDDHPDRTVVVYANTSAAVKARADWVVTSSIAVELIDYLDSQGKKIIWAPDRHLGNYVRKQTGADILCWQGACIVHDEFKTQALIRVKGLHPDAAVLVHPESPQAVIDLADAVGSTSQLIKSAQSLPHQKLIVATDKGIFYKMQQACPEKQLFAAPTAGEGASCRSCAHCPWMAMNGLQAIVQGLEQGGGQHE... | 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: Cof... |
Q7V7S6 | MVRMTAVCTAKTVSPVPSTRKELKGAIAELRKKLNAVILAHYYQDPEIQDIADFIGDSLELSRRAASTNADVIVFCGVHFMAETAKILSPEKIVLLPDLEAGCSLADDCPADEFAAFRDKHPDHIVVSYINCTAAVKAQSDLICTSSNAVELVNQLPKDQPILFAPDQNLGRWVQKQSGRKLTIWPGRCMVHETFSEEALLKLKIMHPEAKVIAHPECLENLLELADYIGSTSKLLEFTEISSCTKFIVLTEPGILHQMKLKNPKKEFMDVPGIDGCSCNECPYMRLNTLEKLWSCLSTMKPSIEIEEGVRQKAFIPIQR... | 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: Cof... |
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(+) biosynt... |
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(+) biosynt... |
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(+) biosynt... |
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(+) biosynt... |
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(+) biosynt... |
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(+) biosynt... |
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(+) biosynt... |
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(+) biosynt... |
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(+) biosynt... |
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(+) biosynt... |
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(+) biosynt... |
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(+) biosynt... |
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(+) biosynt... |
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(+) biosynt... |
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(+) biosynt... |
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(+) biosynt... |
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(+) biosynt... |
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(+) biosynt... |
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(+) biosynt... |
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... |
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... |
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... |
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... |
Q54ML1 | MKTVTLATCNLNQWAMDFKGNLERIIESINIAKSKGAKYRLGPELEICGYGCEDHFLEQDTMLHCWQSLAVILKDPELTKDILVDVGMPVLHKDVRYNCRVILLNQKIYLIQPKKAMAMDGNYREGRWFTPWIKPRVVETFYLPRIISQITGQDECQIGDAIISTLDTAISSETCEELFTPNSPHIQMGLDGVEIFTNGSGSHHQLRKLDTRVDLIRSATSKSGGIYLYSNQQGCDGSRLYYDGSCMIMINGDCVSQGSQFSLVDIEVITATVDLEDVRSVRASFMARCAQANLTKEFPRVRCPIQLTHIDYCHPPDRVI... | 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 | MGRKVTVAVSTLNQWALDFEGNMVRILQSILEAKDMGASYRTGPELEVCGYSCEDHFREPDTFLHSWEVLLEVMMSPMCENMLVDVGMPVMHRNVAYNCRVAFFNRQILLIRPKMAMCDDGNYRESRWFTAWTKALQTEEYVLPRMIAQHTGQQTVPFGDAVIATRDTCLGYEICEELWNVRSKHIEMSLAGVELIVNSSGSYMELRKAHITSDLIRNASFKAGGAYLFSNLRGCDGQRVYFNGCSAIALNGEILARSQQFALQDVEVTLATIDLEEIRAYRVSLRSRCTAAASAAEYPRIHCDFEMSTHSDIFKTSTPP... | 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 ... |
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
Se... |
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
Se... |
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
Se... |
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
Se... |
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
Se... |
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
Se... |
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
Se... |
Q4FRP5 | MPHLHESELFHAIKNPAFRRIGLMGRARTRSVTQSIGQIAQIINDMNLTLIMDVQTANLPTLNLTEIERVKIVKRSLIGEICDLVIVVGGDGSILHAAEALARYRVPVLGVNRGRLGFLADVKPDEAAFKLRQVLMGNYQLDHRFLLTMEIREGRKIIHEDMALNDVVLHAGKSVHMIDFQMKIDGHDVYRQHSDGLIVATPTGSTAYALSGGGPIIHPSMDAICLVPMHPHTLSSRPIVVSGTSEICIRIHEDNRTQPMVSADGKPSTPLDQEQRLYIRKHPDKLTLLHPPGFDFYEACRTKLHWNVHAEEFSLDVDDD... | 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
Se... |
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 met... |
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 met... |
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 met... |
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 met... |
Q5FA94 | MTVPHIPRGPVMADIAAFRLTEEEKQRLLDPAIGGIILFRRNFQNIEQLKTLTAEIKALRTPELIIAVDHEGGRVQRFIEGFTRLPAMNVLGQIWDKDGASAAETAAGQVGRVLATELSACGIDLSFTPVLDLDWGNCAVIGNRSFHRNPEAVARLALALQKGLAKGGMKSCGKHFPGHGFVEGDSHLVLPEDGRSLDELEAADLAPFRIMSREGMAAVMPAHVVYPQVDTKPAGFSEIWLKQILRRDIGFKGVIFSDDLTMEGACGAGGIKERARISFEAGCDIVLVCNRPDLVDELRDGFTIPDNQDLAGRWQYMENS... | 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-r... |
Q82SJ8 | MSLGPLMLDIAGTELTETDRVRLSHPLVGGVILFARNYASPAQLAGLTAEIHALRYPSLLIAVDQEGGRVQRFRDGFARLPPMRVLGEICDRNPDRAHHLASQAGYVLAAELKACGVDLSFTPVLDLDYGQSCVIGDRAFHREPQVVADLACALMNGLQSAGMAAVGKHFPGHGAIRADTHVETAIDTRSYTDIEKEDLIPFRRMIDAGLSGIMAAHVIYPAIDQHSAGFSSRWLQRILRHDLGFEGCIFSDDLGMQAARNYGSITRRAEQALQAGCDMVLVCNDADAADELLGSLHWEFSAASLARVECMRGQHMIHSM... | 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-r... |
B4EVE7 | MGPVMLDVEGYELDNEEREILKHPLVGGLILFTRNFHDAEQLNELVRQIRDASHERLVIAVDQEGGRVQRFRDGFTRLPAAQSYAALNERYQASRLAQEAGWLMASEMIAMDIDISFAPVLDLGHDCIAIGERSFHECPEIAMDMAESFIKGMRSAGMKSTGKHFPGHGAVRADSHKETPRDERSLNDIRQRDMAIFKDFIQRQLLDAIMPAHVIYSQIDERPASGSPYWLKSILREQLGFQGVIFSDDLSMEGAAIMGSYAQRAQRSLDAGCDMLLVCNNRKGAVSVLDNLSFVKAERISALYHHRGRYTLSELQASDR... | 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-r... |
B7UYS5 | MQGSLMLDIGGTWLTAEDRQILRHPEVGGLIIFARNIEHPAQVRELCAAIRAIRPDLLLAVDQEGGRVQRLRQGFVRLPAMRAIADNPNAEELAEHCGWLMATEVQAVGLDLSFAPVLDLDHQRSAVVGSRAFEGDPERAALLAGAFIRGMHAAGMAATGKHFPGHGWAEADSHVAIPEDARSLEEIRRSDLVPFARLAGQLDALMPAHVIYPQVDPQPAGFSRRWLQEILRGELKFDGVIFSDDLSMAGAHVVGDAASRIEAALAAGCDMGLVCNDRASAELALAALQRLKVTPPSRLQRMRGKGYANTDYRQQPRWLE... | 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-r... |
A1SW90 | MRPVILDVEGYELDSEEKEILAHPLVAGIILFTRNYYDIEQLKALVKDIRRYAGNELLIAVDHEGGRVQRFRDDFTRLPSAGSLIEKNDMKTACELAFSSAWVMASELIACDIDFSFAPVLDLNGISNVIQNRAFSSSITETVTLAEAYINGMKSAGMVSTGKHFPGHGSVEADSHTALPVDSRSELEIFTKDIKPFENLIKKGALDAVMPSHVVYSQCDLQPAGFSSYWLDDVLRTRLGFKGVVISDDLSMHGASFVGNHLSRAESAIQAGCDLILACNDRSGAVSILDNLKVKPTAQYHAVNQLRSTKNKFILPLNKN... | 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-r... |
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; ... |
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; ... |
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; ... |
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; ... |
P39185 | MKISRRDFIKQTAITATASVAGVTLPAGAANFVTDSEVTKLKWSKAPCRFCGTGCGVTVAVKDNKVVATQGDPQAEVNKGLNCVKGYFLSKIMYGQDRLTRPLMRMKNGKYDKNGDFAPVTWDQAFDEMERQFKRVLKEKGPTAVGMFGSGQWTVWEGYAAAKLYKAGFRSNNIDPNARHCMASAAAGFMRTFGMDEPMGCYDDFEAADAFVLWGSNMAEMHPILWTRVTDRRLSHPKTRVVVLSTFTHRCFDLADIGIIFKPQTDLAMLNYIANYIIRNNKVNKDFVNKHTVFKEGVTDIGYGLRPDHPLQKAAKNASD... | 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 experi... |
P81186 | MSTSRRDFLKYFAMSAAVAAASGAGFGSLALAADNRPEKWVKGVCRYCGTGCGVLVGVKDGKAVAIQGDPNNHNAGLLCLKGSLLIPVLNSKERVTQPLVRRHKGGKLEPVSWDEALDLMASRFRSSIDMYGPNSVAWYGSGQCLTEESYVANKIFKGGFGTNNVDGNPRLCMASAVGGYVTSFGKDEPMGTYADIDQATCFFIIGSNTSEAHPVLFRRIARRKQVEPGVKIIVADPRRTNTSRIADMHVAFRPGTDLAFMHSMAWVIINEELDNPRFWQRYVNFMDAEGKPSDFEGYKAFLENYRPEKVAEICRVPVEQ... | 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 experi... |
Q06457 | MTETRTTCPYCGVGCGVIASRAPHGQVSVRGDEQHPANFGRLCVKGAALGETVGLEGRMLFPEVDGERATWPQALAAAGSRLREIIDRHGPQAVAFYASGQLLTEDYYAANKLMKGFIGAANIDTNSRLCMSSAVTGYKRALGADVVPCSYEDVENSDLVVLVGSNAAWAHPVLYQRLAQAKRDNPQMRVVVIDPRRTATCDIADRHLALAPGSDGGLFVGLLNAIAASGAISDDFNDAQRALTIAQDWDLDKVAQFCGLPRQQIADFYREFIAAPRAITLYTMGINQSASGSDKCNAIINVHLACGKYGRPGCGPFSLT... | 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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