ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
Q9H2H0 | MHHRNDSQRLGKAGCPPEPSLQMANTNFLSTLSPEHCRPLAGECMNKLKCGAAEAEIMNLPERVGTFSAIPALGGISLPPGVIVMTALHSPAAASAAVTDSAFQIANLADCPQNHSSSSSSSSGGAGGANPAKKKRKRCGVCVPCKRLINCGVCSSCRNRKTGHQICKFRKCEELKKKPGTSLERTPVPSAEAFRWFF | Function: Acts as a negative regulator of the Wnt signaling pathway via its interaction with DVL1 (By similarity). Binds preferentially to DNA containing cytidine-phosphate-guanosine (CpG) dinucleotides over CpH (H=A, T, and C), hemimethylated-CpG and hemimethylated-hydroxymethyl-CpG .
Sequence Mass (Da): 20978
Sequenc... |
Q800L6 | MHRNDSQRLGKPGGAPESLQMANNNFLSTLSPEHCRPLAGECMNKLKCGAAEAEIMNLPERVGTFSAIPALGGISLPPGVIVMTALHSPAAASAAVTDSAFQIANLADCPQNNSSGAGGNPAKKKRKRCGVCVPCKRLINCGVCSSCRNRKTGHQICKFRKCEELKKKPGTSLEVRGDDSFFPCLASSLIPPFSPPFQCFLSPFKMHHSFSESPSRL | Function: Acts as a negative regulator of the Wnt signaling pathway required for anterior neural structure formation . Ectopic expression induces ventralization. Binds preferentially to DNA containing cytidine-phosphate-guanosine (CpG) dinucleotides over CpH (H=A, T, and C), hemimethylated-CpG and hemimethylated-hydrox... |
Q0VFP6 | MHRNDSQRLGKPGGAPESLQMANNNFLSTLSPEHCRPLAGECMNKLKCGAAEAEIMNLPERVGTFSAIPALGGISLPPGVIVMTALHSPAAASAAVTDSAFQIANLADCPQNNSSGAGGNPAKKKRKRCGVCVPCKRLINCGVCSSCRNRKTGHQICKFRKCEELKKKPGTSLERTPVPSAEAFRWFF | Function: Acts as a negative regulator of the Wnt signaling pathway required for anterior neural structure formation (By similarity). Binds preferentially to DNA containing cytidine-phosphate-guanosine (CpG) dinucleotides over CpH (H=A, T, and C), hemimethylated-CpG and hemimethylated-hydroxymethyl-CpG (By similarity).... |
Q7LFL8 | MSSLGGGSQDAGGSSSSSTNGSGGSGSSGPKAGAADKSAVVAAAAPASVADDTPPPERRNKSGIISEPLNKSLRRSRPLSHYSSFGSSGGSGGGSMMGGESADKATAAAAAASLLANGHDLAAAMAVDKSNPTSKHKSGAVASLLSKAERATELAAEGQLTLQQFAQSTEMLKRVVQEHLPLMSEAGAGLPDMEAVAGAEALNGQSDFPYLGAFPINPGLFIMTPAGVFLAESALHMAGLAEYPMQGELASAISSGKKKRKRCGMCAPCRRRINCEQCSSCRNRKTGHQICKFRKCEELKKKPSAALEKVMLPTGAAFRW... | Function: May indirectly participate in activation of the NF-kappa-B and MAPK pathways. Acts as a mediator of BMP4-mediated modulation of canonical Wnt signaling activity in neural stem cells (By similarity). Required for DNA damage-induced ATM phosphorylation, p53 activation and cell cycle arrest. Involved in myelopoi... |
A3CRP6 | MREKYLLHCPGCGRLFPDNYTLDCPLGCNALLRTVYAEHRLTLRDLPGIFRYSSWLPIEGHLRIDAGPVSYASEGLARELGLSNLTVTFSGYWPERGGRMETCSFKELEAQPTVLRLGEKGAGVLQISSAGNTGRAFCQVSALTGAPVVVVVPASAADRLWTTVPAPNVCLITVEGDYSDSIAFGREVCSLPGIVPEGGAKNVARRDGMGTVMLDAALFAGRLPDAYFQAIGSGTGGIAAWEAAERLVADGRFGSRLPTLHLSQNLPFVPMVRAWEAGRREIVPEVDMPDAEASIVRVSADVLTNRHPPWEVRGGVYDAL... | Function: Specifically catalyzes the beta-elimination of phosphate from L-phosphoserine and the beta-addition of sulfite to the dehydroalanine intermediate to produce L-cysteate.
Catalytic Activity: H(+) + O-phospho-L-serine + sulfite = L-cysteate + phosphate
Sequence Mass (Da): 46100
Sequence Length: 430
Pathway: Cofa... |
A0B6Z6 | MGEYTLRCAGCGNLLIGGAASCPLDGGLPRADYIERRFNPRKLPGIWSFIDWLPVDGWNRSTGASSVTYRSSGLAAELGLDSLYISFSGYWPERGALMRTCSFKELEAAPTMQMLRDRKAGETLVVASAGNTARAFAEVCSITDQPLILFVPVSSLDRIWTTVEPGRVLVVGVKGDYADAIKLADVLSSRSGFRAEGGARNIARRDGMGTVLLDHVRRFNSLPNHYFQAIGSGTGGIAVWEASMRIIEDGRFGERLPRLHLAQNTPCAPVYNMWHGMGSEESDFDAYGCPEGMHDDVLFNRNPPYAVPGGVRDAVISSGE... | Function: Specifically catalyzes the beta-elimination of phosphate from L-phosphoserine and the beta-addition of sulfite to the dehydroalanine intermediate to produce L-cysteate.
Catalytic Activity: H(+) + O-phospho-L-serine + sulfite = L-cysteate + phosphate
Sequence Mass (Da): 44863
Sequence Length: 415
Pathway: Cofa... |
O31215 | MSAEKTENLSWIDKRFPLSETWRNHLSEYYAPKNLNFWSFFGSLAILTLVIQIVTGVWLAMSYKPDAGLAFASVEYIMRDVDWGWLIRYMHSTGASMFFIVIYLHMFRGLLWGSYRKPRELLWMIGVVIYLVMMATAFFGYLLPWGQMSYWGAQVIVNLFAAVPVVGEDLSVWVRGDFVISDATLNRFFAFHFLLPFLLAGLVFLHIVALHHVGSNNPDGIEIKEGPKGNRWSDKAPADGIPFHPYYTVKDLMGVVVFLAIFGYVMFFNPTMGGLFLEAPNFQPANPMQTPAHIAPVWYFTPFYAMLRAVPPMYGSQFPG... | Cofactor: Binds 2 heme b groups non-covalently.
Function: Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is a respiratory chain that generates an electrochemical potential coupled to ATP synthesis.
Location Topology: Multi-pass membrane protein
Sequence Mass (D... |
P29632 | FGSLLGICLVTQIITGLLLATHYTADTNLAFASVAHTCRNVQFGWLIRNLHANGASFFFICIYLHIGRGIYYGSYLNKETWNTGVILLLTLMATAFVGYVLPWGQMSFWGATVITNLFSAIPYIGQTLVEWAWGGFSVDNPTLTRFFALHFLLPFVIAGITLVHLTFLHETGSNNPLGIPSDCDKIPFHPYYSMKDILGFALLFIALVAMALFSPNLLGDPENFTPANPLSTPPHIKPEWYFLFAYAILRSIPNKLGGVLALAASVLVLFLIPLLHTSKQRSMTFRPLSQILFWTLVANLLVLTWVGS | Cofactor: Binds 2 heme b groups non-covalently.
Function: Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex) that is part of the mitochondrial respiratory chain. The b-c1 complex mediates electron transfer from ubiquinol to cytochrome c. Contributes to the generation of a... |
P69220 | TALFLAMHYTSDIATAFSSVAHICRDVNYGWLIRNMHANGASFFFICIYLHIGRGLYYGSYLYKETWNVGVVLLLLTMM | Cofactor: Binds 2 heme b groups non-covalently.
Function: Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex) that is part of the mitochondrial respiratory chain. The b-c1 complex mediates electron transfer from ubiquinol to cytochrome c. Contributes to the generation of a... |
O78790 | MTNIRKTHPLMKIVNNAFIDLPTPPNISSWWNFGSLLGICLILQILTGLFLAMHYTSDTTTAFSSVTHICRDVNYGWIIRYMHANGASMFFICLFMHVGRGLYYGSYTFLETWNIGVILLLTTMATAFMGYVLPWGQMSFWGATVITNLLSAIPYIGTNLVEWIWGGFSVDKATLTRFFAFHFILPFIIAALAMVHLLFLHETGSNNPTGIPSDTDKIPFHPYYTIKDILGIMLLILVLMLLVLFTPDLLGDPDNYIPANPLNTPPHIKPEWYFLFAYAILRSIPNKLGGVLALVLSILILVLVPFLHTSKQRSMMFRPI... | Cofactor: Binds 2 heme b groups non-covalently.
Function: Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex) that is part of the mitochondrial respiratory chain. The b-c1 complex mediates electron transfer from ubiquinol to cytochrome c. Contributes to the generation of a... |
P16359 | SALFLAMHYTPDTLTAFSSVAHICRDVNYGWLIRYMHANGSSLFFICLYLHIGRGIYYGSYSYTETWNIGIILLFLTMA | Cofactor: Binds 2 heme b groups non-covalently.
Function: Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex) that is part of the mitochondrial respiratory chain. The b-c1 complex mediates electron transfer from ubiquinol to cytochrome c. Contributes to the generation of a... |
P34862 | FGSLLGVCLITQILTGLFLAMHYTADIYFAFSSVAHICRDVNYGWLIRNIHTNGASLFFICIYMHIGRGIYHGSFMLKETWNIGVILFLMTMATAFMGYVFP | Cofactor: Binds 2 heme b groups non-covalently.
Function: Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex) that is part of the mitochondrial respiratory chain. The b-c1 complex mediates electron transfer from ubiquinol to cytochrome c. Contributes to the generation of a... |
P16362 | TALLLAAHYTADTSLAFASVTHMCRNVQFGWLIRNLHANGASFFFICIYLHIGRGLYYGSYLNKETWNIGVILLLTLMA | Cofactor: Binds 2 heme b groups non-covalently.
Function: Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex) that is part of the mitochondrial respiratory chain. The b-c1 complex mediates electron transfer from ubiquinol to cytochrome c. Contributes to the generation of a... |
Q9T9I2 | MATNIRKTHPLFKIINNSLIDLPTPTNISIWWNFGSLLGLCLIIQILTGLFLAMHYTADISSAFSSVAHICRDVNYGWLIRNIHANGASLFFICIYLHIARGLYYGSYIYKETWNIGVIILLLLMATAFVGYVLPWGQMSFWGATVITNLLSALPYIGDMLVQWIWGGFSIDNATLTRFFTFHFLLPFIIAALTMVHLLFLHETGSNNPTGLDSNMDKIPFHPYYSYKDLLGFFILLLLLTLLALFMPYSLGDVENFIPANPLVTPPHIKPEWYFLFAYAILRSIPNKLGGVLALAFSILILLLVPMLHTSKQRNLTFRP... | Cofactor: Binds 2 heme b groups non-covalently.
Function: Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex) that is part of the mitochondrial respiratory chain. The b-c1 complex mediates electron transfer from ubiquinol to cytochrome c. Contributes to the generation of a... |
O30881 | MKKLLAIALTVLATVFAFGTPAFAADAAAGAQVFAANCAACHAGGNNAVMPTKTLKADALKTYLAGYKDGSKSLEEAVAYQVTNGQGAMPAFGGRLSDADIANVAAYIADQAENNKW | Function: Functions as an electron carrier between membrane-bound cytochrome b6-f and photosystem I in oxygenic photosynthesis.
PTM: Binds 1 heme c group covalently per subunit.
Sequence Mass (Da): 11916
Sequence Length: 117
Subcellular Location: Cellular thylakoid lumen
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P00115 | MKTLLTILALTLVTLTTWLSTPAFAADIADGAKVFSANCAACHMGGGNVVMANKTLKKEALEQFGMNSADAIMYQVQNGKNAMPAFGGRLSEAQIENVAAYVLDQSSKNWAG | Function: Functions as an electron carrier between membrane-bound cytochrome b6-f and photosystem I in oxygenic photosynthesis.
PTM: Binds 1 heme c group covalently per subunit.
Sequence Mass (Da): 11801
Sequence Length: 112
Subcellular Location: Cellular thylakoid lumen
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P46445 | MFKLFNQASRIFFGIALPCLIFLGGIFSLGNTALAADLAHGKAIFAGNCAACHNGGLNAINPSKTLKMADLEANGKNSVAAIVAQITNGNGAMPGFKGRISDSDMEDVAAYVLDQAEKGW | Function: Functions as an electron carrier between membrane-bound cytochrome b6-f and photosystem I in oxygenic photosynthesis.
PTM: Binds 1 heme c group covalently per subunit.
Sequence Mass (Da): 12463
Sequence Length: 120
Subcellular Location: Cellular thylakoid lumen
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P57736 | SADLALGKQTFEANCAACHAGGNNSVIPDHTLRKAAMEQFLQGGFNLEAITYQVENGKGAMPAWSGTLDDDEIAAVAAYVYDQASGDKW | Function: Functions as an electron carrier between membrane-bound cytochrome b6-f and photosystem I in oxygenic photosynthesis.
PTM: Binds 1 heme c group covalently per subunit.
Sequence Mass (Da): 9408
Sequence Length: 89
Subcellular Location: Plastid
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P00114 | ADLANGAKVFSGNCAACHMGGGNVVMANKTLKKEALEQFGMNSEDAIIYQVQHGKNAMPAFAGRLTDEQIQDVAAYVLDQAAKGWAG | Function: Functions as an electron carrier between membrane-bound cytochrome b6-f and photosystem I in oxygenic photosynthesis.
PTM: Binds 1 heme c group covalently per subunit.
Sequence Mass (Da): 9129
Sequence Length: 87
Subcellular Location: Cellular thylakoid lumen
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G1CWH5 | MAFARLALIFFLAASVMFAVKETEAGIPCGESCVFIPCTVTALLGCSCKDKVCYKNHVIAAEANTVNDHHLLCQSHEDCFKKGTGNFCAPSLKHDVKYGWCFRAESEGFLLKDFLKTPVDILKMSNVIGN | Function: Probably participates in a plant defense mechanism.
PTM: Contains 3 disulfide bonds.
Sequence Mass (Da): 14256
Sequence Length: 130
Domain: The presence of a 'disulfide through disulfide knot' structurally defines this protein as a knottin.
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P14922 | MNPGGEQTIMEQPAQQQQQQQQQQQQQQQQAAVPQQPLDPLTQSTAETWLSIASLAETLGDGDRAAMAYDATLQFNPSSAKALTSLAHLYRSRDMFQRAAELYERALLVNPELSDVWATLGHCYLMLDDLQRAYNAYQQALYHLSNPNVPKLWHGIGILYDRYGSLDYAEEAFAKVLELDPHFEKANEIYFRLGIIYKHQGKWSQALECFRYILPQPPAPLQEWDIWFQLGSVLESMGEWQGAKEAYEHVLAQNQHHAKVLQQLGCLYGMSNVQFYDPQKALDYLLKSLEADPSDATTWYHLGRVHMIRTDYTAAYDAFQ... | Function: Acts as component of the CYC8-TUP1 corepressor complex which is involved in the repression of many genes in a wide variety of physiological processes including heme-regulated and catabolite repressed genes. May also be involved in the derepression of at least some target genes. The complex is recruited to tar... |
P94364 | MSELVLARIQFASTTLFHFLFVPMSIGLVFMVALMETLYLVKKNELYLKMAKFWGHLFLINFAVGVVTGILQEFQFGLNWSDYSRFVGDVFGAPLAIEALLAFFMESIFIGLWIFGWDRLPKKIHALCIWLVSFGTIMSSFWILTANSFMQEPVGFTIKNGRAEMNDFGALITNPQLWVEFPHVIFGALATGAFFIAGVSAFKLLKKKEVPFFKQSFKLAMIVGLCAGLGVGLSGHMQAEHLMESQPMKMAASEGLWEDSGDPAAWTAFATIDTKNEKSSNEIKVPYALSYLAYQKFSGSVKGMKTLQAEYEKIYGKGDY... | Cofactor: Binds 1 protoheme IX center (heme b558) per subunit.
Catalytic Activity: 2 a ubiquinol + 4 H(+)(in) + O2(in) = 2 a ubiquinone + 4 H(+)(out) + 2 H2O(in)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 52293
Sequence Length: 468
Subcellular Location: Cell membrane
EC: 7.1.1.7
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P0ABK0 | MLDIVELSRLQFALTAMYHFLFVPLTLGMAFLLAIMETVYVLSGKQIYKDMTKFWGKLFGINFALGVATGLTMEFQFGTNWSYYSHYVGDIFGAPLAIEGLMAFFLESTFVGLFFFGWDRLGKVQHMCVTWLVALGSNLSALWILVANGWMQNPIASDFNFETMRMEMVSFSELVLNPVAQVKFVHTVASGYVTGAMFILGISAWYMLKGRDFAFAKRSFAIAASFGMAAVLSVIVLGDESGYEMGDVQKTKLAAIEAEWETQPAPAAFTLFGIPDQEEETNKFAIQIPYALGIIATRSVDTPVIGLKELMVQHEERIRN... | Cofactor: Binds 1 protoheme IX center (heme b558) per subunit.
Function: A terminal oxidase that produces a proton motive force by the vectorial transfer of protons across the inner membrane. It is the component of the aerobic respiratory chain of E.coli that predominates when cells are grown at low aeration. Generates... |
P94365 | MASLHDLWFILVAVLFVGFFFLEGFDFGVGMATRFLGHNELERRVLINTIGPFWDANEVWLLTGAGAIFAAFPNWYATMLSGYYIPFVIVLLALMGRGVAFEFRGKVDHLKWVKVWDWVVFFGSLIPPFVLGVLFTTLFRGMPIDADMNIHAHVSDYINVYSILGGVTVTLLCFQHGLMFITLRTIGDLQNRARKMAQKIMGVVFVAVLAFAALSAYQTDMFTRRGEITIPLAVLIVICFMLAAVFIRKKKDGWTFGMTGAGLALTVGMIFISLFPRVMVSSLHSAYDLTVANASSGDYSLKVMSIAALTLLPFVIGSQI... | Cofactor: Binds 1 protoheme IX center (heme b595) per heterodimer, in conjunction with CydA.
Catalytic Activity: 2 a ubiquinol + 4 H(+)(in) + O2(in) = 2 a ubiquinone + 4 H(+)(out) + 2 H2O(in)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 37861
Sequence Length: 338
Subcellular Location: Cell membran... |
P0ABK4 | MIDYEVLRFIWWLLVGVLLIGFAVTDGFDMGVGMLTRFLGRNDTERRIMINSIAPHWDGNQVWLITAGGALFAAWPMVYAAAFSGFYVAMILVLASLFFRPVGFDYRSKIEETRWRNMWDWGIFIGSFVPPLVIGVAFGNLLQGVPFNVDEYLRLYYTGNFFQLLNPFGLLAGVVSVGMIITQGATYLQMRTVGELHLRTRATAQVAALVTLVCFALAGVWVMYGIDGYVVKSTMDHYAASNPLNKEVVREAGAWLVNFNNTPILWAIPALGVVLPLLTILTARMDKAAWAFVFSSLTLACIILTAGIAMFPFVMPSSTM... | Cofactor: Binds 1 protoheme IX center (heme b595) per heterodimer, in conjunction with CydA.
Function: A terminal oxidase that produces a proton motive force by the vectorial transfer of protons across the inner membrane. It is the component of the aerobic respiratory chain of E.coli that predominates when cells are gr... |
P94366 | MGKDLFRYKGMKRILTLITCLTLIQTAAIIMQAEWLSEAVTGLFNGKGITSLLPVIGFFLIAFIARHGMTVARQKIVYQYAARTGADLRKSFLDQLFRLGPRFAKKEGTGQMVTLAMEGISQFRRYLELFLPKMVSMAIVPAAVVIYVFFQDRTSAIILVAAMPILIIFMILLGLVAQRKADRQWKSYQRLSNHFVDSLRGLETLRFLGLSKSHSKNIFYVSERYRKATMSTLRVAFLSSFALDFFTMLSVATVAVFLGLRLIDGDILLGPALTALILAPEYFLPVREVGNDYHATLNGQEAGKTIQEILSQPGFKEETP... | Function: Part of the ABC transporter complex CydDC that exports the reduced low-molecular-weight thiols cysteine and glutathione from the cell. Export of these thiol-containing redox-active molecules may be crucial for redox homeostasis, permitting correct assembly of various respiratory complexes and formation of cor... |
P23886 | MRALLPYLALYKRHKWMLSLGIVLAIVTLLASIGLLTLSGWFLSASAVAGVAGLYSFNYMLPAAGVRGAAITRTAGRYFERLVSHDATFRVLQHLRIYTFSKLLPLSPAGLARYRQGELLNRVVADVDTLDHLYLRVISPLVGAFVVIMVVTIGLSFLDFTLAFTLGGIMLLTLFLMPPLFYRAGKSTGQNLTHLRGQYRQQLTAWLQGQAELTIFGASDRYRTQLENTEIQWLEAQRRQSELTALSQAIMLLIGALAVILMLWMASGGVGGNAQPGALIALFVFCALAAFEALAPVTGAFQHLGQVIASAVRISDLTDQ... | Function: Part of the ABC transporter complex CydDC that exports the reduced low-molecular-weight thiols cysteine and glutathione to the periplasm . Export of these thiol-containing redox-active molecules may be crucial for redox homeostasis in the periplasm, permitting correct assembly of various respiratory complexes... |
P45081 | MRTLLPFIRLFKFAKFPLILGLVLMILGLGSSMGLLTVSGWFLAATAIAGLGTLFNFFYPSASVRGLAIGRTVMRYFEKIVTHDATFRILSKLRVQVFEKIIPLSPAVLNRYRNSDLLNRLVSDVDTLDSLYLRLLAPFFTAVFVIIAMMIGLSFINIPLALGLGLFLLILLMIIPTVFYRLGQQFGERLIQARATYRTQFLEFIQAQAELLLFNAEDKLKEKMLVTEKTWQEDQAKEAKLSGFSTALVLFLNGLLISGMLWFASNADFGTDEYHTAYIALFTFAALAAFEIIMPLGAAFLHIGQVIAAAERVTEIIEQK... | Function: Part of the ABC transporter complex CydDC that exports the reduced low-molecular-weight thiols cysteine and glutathione to the periplasm. Export of these thiol-containing redox-active molecules may be crucial for redox homeostasis in the periplasm, permitting correct assembly of various respiratory complexes ... |
P94367 | MKKEEWILPYIKQNARLFVLVIFLGAVTIFSAAFLMFTSGFLISKAATRPENILLIYVPIVAVRTFGIARSVSRYVERLVGHHIILKIVSDMRVRLYNMLEPGALMLRSRFRTGDMLGILSEDIEHLQDAFLKTIFPAISALLLYAVSVIALGFFSWPFAILLALYLFVLVVLFPVVSLLVTRAKNAKLKSGRNVLYSRLTDAVMGVSDWMFSGRRHAFIDAYEKEERDWFELERKKQRFTRWRDFAAQCLVAGLILLMLFWTAGQQADGELAKTMIAAFVLVVFPLTEAFLPLSDALGEVPGYQDSIRRMNNVAPQPEA... | Function: Part of the ABC transporter complex CydDC that exports the reduced low-molecular-weight thiols cysteine and glutathione from the cell. Export of these thiol-containing redox-active molecules may be crucial for redox homeostasis, permitting correct assembly of various respiratory complexes and formation of cor... |
P29018 | MNKSRQKELTRWLKQQSVISQRWLNISRLLGFVSGILIIAQAWFMARILQHMIMENIPREALLLPFTLLVLTFVLRAWVVWLRERVGYHAGQHIRFAIRRQVLDRLQQAGPAWIQGKPAGSWATLVLEQIDDMHDYYARYLPQMALAVSVPLLIVVAIFPSNWAAALILLGTAPLIPLFMALVGMGAADANRRNFLALARLSGHFLDRLRGMETLRIFGRGEAEIESIRSASEDFRQRTMEVLRLAFLSSGILEFFTSLSIALVAVYFGFSYLGELDFGHYDTGVTLAAGFLALILAPEFFQPLRDLGTFYHAKAQAVGA... | Function: Part of the ABC transporter complex CydDC that exports the reduced low-molecular-weight thiols cysteine and glutathione to the periplasm . Export of these thiol-containing redox-active molecules may be crucial for redox homeostasis in the periplasm, permitting correct assembly of various respiratory complexes... |
P45082 | MNKLRQKYLQKWLRAQQEPIKKLMRANIVLATLSSFILVAQTYFLATLLDKLIMQNVPRDELIPYFLGLIIGFGMRAIILWAREKIGFQSGQLLRNHIRQKILDKIHLVGPATINQKPAGSWASIMLEQVENLHNFYARFLPQQSLSAIVPVVIFIAVFPLNWAAGLILMITAPLVPLFMIIVGIAAADNSQKNMDTLSRLSAQFLDRLRGLETLRLFNRTSEQTEHIENATEDFRETTMDVLKLAFLSSAVLEFFTSISIALMAVYFGFSYLGQIEFGTYNAPLTLFTGFFCLILAPEFYQPLRDLGTYYHDRAAGIGA... | Function: Part of the ABC transporter complex CydDC that exports the reduced low-molecular-weight thiols cysteine and glutathione to the periplasm. Export of these thiol-containing redox-active molecules may be crucial for redox homeostasis in the periplasm, permitting correct assembly of various respiratory complexes ... |
Q58431 | MVSIMNKNELITEILKNEVVKALGCTEVGLIGYTVAKAKPEDLYSIKEIKLILDKGTFKNAFSVGVPNTNKFGILPAVVGGLLGREENKLEVFKDIKYDEKLEEFIENKLKIEVIDSDVYCKVIIKANKVYEAETKGSHSGKSLSDDLKNAYKSLTLKDFIDYIEDIPEEVIKIIKETIETNKNLSTPEVPEDFISLDLKDEILNHMLKKTVSAVYNRMIGINKPAMAIAGSGNMGLTATLPIIAYDEIKGHDEEKLTKSITLSALTTIYSAYHSSYISAMCGCVNRGGIGAVSGLSYYIFGFDRIEESIKSFTANLPGI... | Cofactor: Binds 1 [4Fe-4S] cluster per subunit.
Function: Catalyzes the cleavage of L-cysteine to form 2-aminoprop-2-enoate and sulfide. The former then spontaneously hydrolyzes to pyruvate and NH(3). May be responsible for the production of sulfide required for the biosynthesis of iron-sulfur centers in this archaea. ... |
Q21S14 | MNRLEVTEKIISTKVTKGIKWEAVAKKVGLSKEWVTAACLGQMTLNAEQAKIVGKMFGLTVEEQKWLQVAPYKGSLPTLVPTDPLIYRWYEIVNVYGSTIKELIHEEFGDGIMSAIDFSMDIVRQPDPKGDRVNVVLSGKFLPYKQY | Function: Catalyzes the reaction of cyanate with bicarbonate to produce ammonia and carbon dioxide.
Catalytic Activity: cyanate + 3 H(+) + hydrogencarbonate = 2 CO2 + NH4(+)
Sequence Mass (Da): 16595
Sequence Length: 147
EC: 4.2.1.104
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O66587 | MRSDIGRLSKYLIERKKNLGLTWEDVSRKLGKSPVYCAMLFYGYAQADDEEVKAVAELLNLEEKELAELKDAPYREPQQPVPPTDPFVYRLYEVVILYGPALKDVAHEMFGDGIMSAIDMSVELEKVEQEGAERMVLTFNGKWLKYRKF | Function: Catalyzes the reaction of cyanate with bicarbonate to produce ammonia and carbon dioxide.
Catalytic Activity: cyanate + 3 H(+) + hydrogencarbonate = 2 CO2 + NH4(+)
Sequence Mass (Da): 17201
Sequence Length: 149
EC: 4.2.1.104
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O22683 | MEAAKKQSVTNQLLAVKSASGKTFSQLAAETGLTNVYVAQLLRRQAQLKPDTVPKLKEALPALTDELIGDMMSPPWRSYDPNLIQEPTIYRLNEAVMHFGESIKEIINEDFGDGIMSAIDFYCSVDKIKGVDGNNRVVVTLDGKYLSHSEQRTENMVSRLNLKGGTSE | Function: Catalyzes the reaction of cyanate with bicarbonate to produce ammonia and carbon dioxide.
Catalytic Activity: cyanate + 3 H(+) + hydrogencarbonate = 2 CO2 + NH4(+)
Sequence Mass (Da): 18592
Sequence Length: 168
EC: 4.2.1.104
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B8NQ08 | MSLATLDTSQHPNLPSASATLFKAKAAKKFSFEQIAQHIGRNEVATAAIFYGQAKASPEDITNLASLLEIPQEVLEDQLSGFPDRGKSVEMPPKEPLIYRLYEIVQNYGYAYKAVLNEKFGDGIMSAISFSTKVEKETDADGNNWAVITLRGKWLPFSRF | Function: Catalyzes the reaction of cyanate with bicarbonate to produce ammonia and carbon dioxide.
Catalytic Activity: cyanate + 3 H(+) + hydrogencarbonate = 2 CO2 + NH4(+)
Sequence Mass (Da): 17749
Sequence Length: 160
EC: 4.2.1.104
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Q89AA3 | MQFIKYKSYILKFLLVSCIFCINGCDCTILCPNGLIAQEQRFVLFVSFFTMLLIIIPVIFMTIFFVLRYRESNFSKTYDPKWSHSNIIELLIWGIPIIIIVFLSIFSWKSVHDLDPKKPIVSNVQPIKINVISLDWKWLFIYPDQKIATINKLIIPINTPIIFNLTSGSVMNSFFIPSLGSQIYVMPGMKTNLNLIANKLGQFKGFSSNYSGKGFSNMKFDVLVTSDHIFFYEWVKKIQKSKYKLNSMYQFNQLAIPSDNNAIKYFSNLKENLFNVVIANVLKISL | Function: Cytochrome bo(3) ubiquinol terminal oxidase is the component of the aerobic respiratory chain of E.coli that predominates when cells are grown at high aeration. Has proton pump activity across the membrane in addition to electron transfer, pumping 2 protons/electron (By similarity).
Location Topology: Multi-p... |
P0ABJ2 | MRLRKYNKSLGWLSLFAGTVLLSGCNSALLDPKGQIGLEQRSLILTAFGLMLIVVIPAILMAVGFAWKYRASNKDAKYSPNWSHSNKVEAVVWTVPILIIIFLAVLTWKTTHALEPSKPLAHDEKPITIEVVSMDWKWFFIYPEQGIATVNEIAFPANTPVYFKVTSNSVMNSFFIPRLGSQIYAMAGMQTRLHLIANEPGTYDGISASYSGPGFSGMKFKAIATPDRAAFDQWVAKAKQSPNTMSDMAAFEKLAAPSEYNQVEYFSNVKPDLFADVINKFMAHGKSMDMTQPEGEHSAHEGMEGMDMSHAESAH | Function: Cytochrome bo(3) ubiquinol terminal oxidase is the component of the aerobic respiratory chain of E.coli that predominates when cells are grown at high aeration. Has proton pump activity across the membrane in addition to electron transfer, pumping 2 protons/electron (By similarity).
Location Topology: Multi-p... |
Q9I427 | MTKANPFAALKWLSLAPALLLGGCDMTLFNPKGQVGMDERTLIITATLLMLIVVIPVIVMTLAFAWKYRASNTQAEYKPDWHHSNRIEAVVWLVPCVIIAILGWITWESTHKLDPYRPLDSEVKPVTIQAVSLDWKWLFIYPEQGIATVNEIAFPKDTPVNFQITSDSVMNSFFIPQLGSQIYSMAGMMTKLHLIANEEGVFDGISANYSGGGFSGMRFKAIATSEQGFQDWVAKVKAAPASLSIGTYPELVKPSENVPPTYFSSVSPELFGHILTKYEHHGDAKGAAHGEHAGAEHEAAMTGHDMQDMDMQAMQGMKDM... | Function: Cytochrome bo(3) ubiquinol terminal oxidase is the component of the aerobic respiratory chain of E.coli that predominates when cells are grown at high aeration. Has proton pump activity across the membrane in addition to electron transfer, pumping 2 protons/electron (By similarity).
Location Topology: Multi-p... |
Q9WWR1 | MSKKRYPRLFGILPFLGMLLLSGCNWTLLDPKGQVGIEQKNLILIATGLMLLVVIPVIIMTVVFAWKYRASNKAATYTPDWSHSTKIEAAVWIIPILIIIALGYFTYHSTHKLDPYRPLDSDVKPVQIDVVALDWKWLFIYPEQGIATVNKIVFPANTPVNFRVTSDAVMNSFFIPGLGGQIYAMAGMTTKLHLIANENGEFDGISANYSGAGFTGMKFKATATSQEDFDKWVAEVKQSPKKLDKAEYEALAKPSENNPVALYSEASPDQFQLIVDKYEGMNRGRPSHEEAGSKDLATTKGVESSMQPAAGAEE | Function: Cytochrome bo(3) ubiquinol terminal oxidase is the component of the aerobic respiratory chain of E.coli that predominates when cells are grown at high aeration. Has proton pump activity across the membrane in addition to electron transfer, pumping 2 protons/electron (By similarity).
Location Topology: Multi-p... |
P57543 | MFGKLTFDAIPYHEPIIMITYIAIILIALCIASTITYYKKWKYLWYEWFTTVDHKKISIMYGILAFVMLFRGFVDAILMRTQQVVASAGFKGFLPPHHYDQIFTAHGVIMIFFVAMPLVIGLMNLVIPLQIGARDVAFPFLNNLSFWLNVSSAVLLTLSLGIGEFAQTGWLAYPPLSGIKYSSGVGVDYWIWSLQISGVGTTLTGINFLVTILKMRAPGMSFFKMPVFTWTSLCTNILIVISFPVLTVTLVLLTLDRYFNFHFFTNDLGGNAMMYVNLIWIWGHPEVYILVLPVFGVFSEVVATFSKKRLFGYVSLVWAT... | Cofactor: Binds 1 copper B ion per subunit.
Function: Cytochrome bo(3) ubiquinol oxidase is the terminal enzyme in the aerobic respiratory chain. Catalyzes the four-electron reduction of O2 to water, using a ubiquinol as a membrane soluble electron donor for molecular oxygen reduction. Has proton pump activity across t... |
Q8K994 | MFGKLTLKAIPVDEPIIMVTYISIILIALFISFSITYFKKWKYLWYEWFTTVDHKKISIMYGILAFIMLFRGFVDAILMRTQQVIASSGNTGFLPPHHYDQIFTAHGVIMIFFVAMPLVIGLMNLVVPLQIGARDVAFPFLNNLSFWLNVSGAILLTLSLGIGEFAQTGWLAYPPLSEVKYSPGVGVDYWIWSLQISGVGTTLTGINFLITILKMRAPGMCFFKMPVFTWAALCTNILIVISFPVLTTTLLLLTLDRCFDFHFFTNNFGGNPMMYVNLIWIWGHPEVYILVLPVFGVFSEVVATFSKKRLFGYVSLVWAT... | Cofactor: Binds 1 copper B ion per subunit.
Function: Cytochrome bo(3) ubiquinol oxidase is the terminal enzyme in the aerobic respiratory chain. Catalyzes the four-electron reduction of O2 to water, using a ubiquinol as a membrane soluble electron donor for molecular oxygen reduction. Has proton pump activity across t... |
P52017 | MSVTLHTTSGDIKIELYVDDAPKACENFLALCASDYYNGCIFHRNIKDFMVQTGDPTHSGKGGESIWGGPFEDEFVSALKHDSRGCVSMANNGPDSNRSQFFITYAKQAHLDMKYTLFGKVIDGFDTLEEIETIKVDNKYRPLVQQKIQNVTIHANPMAAD | Function: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Mass (Da): 17960
Sequence Length: 161
EC: 5.2.1.8
|
P0C1I9 | MINPRVFFDIDVDGNRIGRIVIELFADQVPKTAENFRALCTGEKGIGKVSNMPLHYKGSIFHRIIKGFMCQGGDFTHRTGKGGESIYGANFPDESFSRKHDTHGLLSMANRGPNTQTSQFFITTRPTPHLDGKHVVFGRVVSGYNVVEMMENEPVDDQDRPLHNVMIANCGELVLKLPPGALLKKASAVSDESEDEIKNRKRSRSSDDDSSSDEDSEEEERKRTKKKRSRKHSKKDKKKKKRESSNRKRSPEANRHVSRERRDISREKRDNSRERRLSRKEDDRRSPSDKRKEDRRSLSPEKRSSERRVARPVRPRLNYN... | Function: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity).
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Mass (Da): 39077
Sequence Length: 338
EC: 5.2.1.8
|
P0C1J0 | MPEDSNTNDNNKRPLEDNNAVDGESDDDIGPMLPPPPGEDAPRKKKRTLAHEKLYLDQLPCADMYEKSYMHRDVLSQVAVTKKDFIITTSVDGHLKFWKKTASGIEFVKHYKSHLSSIVDISISANHELLATISDDTTLKVYDITNFDMINMIKLRYKPKSVCWIHQSGQAQALVAVSEADNSNIHIYDGHADGKPLHTLSKMHSKPVHIIEFNSRFNCVVSVDAIGMIEYWSPEAPFALPDNLDFELKSQTDLYEFRKKKSVPTCLTFSPDGLSFATMSFPDRQVRLFKFLRGKMFREYDESLQAVSEMQQAGTTIHHL... | Function: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity).
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Mass (Da): 71282
Sequence Length: 630
EC: 5.2.1.8
|
G4MVZ7 | MMTPTELITHYRIVQHSFAPLRLSWWETNRVIAVQIWRDSSFFTRILIAFIGLCLLSIFSRLTRPRSLRRLGIPGAVQPRFSTWSLDFKKVLEDSAKKYPNSPFCLNAFGTEYAVLPSKCYDEVKRLPEHQASAFAFFREAFHGAWTGAGVQTPELGRTIAVELTRGIPSLVHWRQMDCAEAFKMCIGEPSEWREIQLFEAIQRIVISVNSSSFVGRELGTNQNWLRLIYNMPLQLGIPTVILGWTPFLLQPLLKPFLFAPLRMTQRKIKSMLRPVLENDVQEYEASSDKKNLLSPKEQGKVQLTGWLLSRYKGKLDFEV... | Function: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of a tyrosine-derived cytochalasan acting as a fungal signal recognized by resistant rice plants and leads to avirulence in Pi33 resistant rice cultivars . The first step in the pathway is catalyzed by the hybrid PKS-NRPS A... |
Q27450 | MSKKDRRRVFLDVTIDGNLAGRIVMELYNDIAPRTCNNFLMLCTGMAGTGKISGKPLHYKGSTFHRVIKNFMIQGGDFTKGDGTGGESIYGGMFDDEEFVMKHDEPFVVSMANKGPNTNGSQFFITTTPAPHLNNIHVVFGKVVSGQEVVTKIEYLKTNSKNRPLADVVILNCGELVRRKKRQHSSRSNESVSSSTSTEKSHKKTKKTKMKEKKRKESDEVEQLEIGTVVPEAELQLSSVKAEDLPDEPDHQNKYLMRRSKTPENSRKGKKEKQRQSPHRFSRRDIGHRLNRMRRTRTGHKIKGRGALRFRTPEGSSDHD... | Function: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Mass (Da): 97818
Sequence Length: 843
EC: 5.2.1.8
|
P52009 | MKFLLRASSLAGQSLRFASQRPKVFFDVSIGEEPAGRVTMELFNDVVPKTAENFRALCTGEKGVGEQGVALHFKGSKFHRIIPEFMIQGGDFTRHNGTGGESIYGNKFKDENFDLKHTGPGCLSMANAGPNTNGSQFFICTVDTPWLDGGHVVFGQVTDGMSVVKKIEKMGSRSGAPAKTVTIADCGELKSE | Function: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Mass (Da): 20711
Sequence Length: 192
EC: 5.2.1.8
|
A0A4D6Q415 | MLTFFFLWISTLLLSSFIVYLLYRRRSAQCPPLPPGPNGWPILGNLPQLGAKPHQTLDALSKQYGPLFRLRLGSVNVVVASSSAVAAQFLRTHDVNFSNRPPNSGAEHVAYNYQDLVFAPYGPRWRMLRKLCSVHLFSLKALDDLRPVRQGEVACLVRNLRRHADTGVLVNLGKALNVCATNALARAMLGRRVFADEDAQLAEADEFKEMVVELMRLAGVFNVGDFVPGLGWLDLQGVVGKMKRLHRRYDAFLDRVIEENQANAKSGDLLSVLIRLKEADAEGEIKLNNTDIKALLLNLFTAGTDTSSSTVEWVLAELIR... | Function: Flavonoid 3'-hydroxylase that catalyzes the 3'-hydroxylation of flavanones, dihydroflavonols and flavonols . Converts narigenin to eriodictyol, dihydrokaempferol to dihydroquercetin and kaempferol to quercetin .
Catalytic Activity: a 3'-unsubstituted flavone + O2 + reduced [NADPH--hemoprotein reductase] = a 3... |
Q8W171 | MPNPKVFFDMTIGGQSAGRIVMELYADVTPRTAENFRALCTGEKGVGRSGKPLHYKGSSFHRVIPSFMCQGGDFTAGNGTGGESIYGAKFADENFVKKHTGPGILSMANAGPGTNGSQFFICTEKTEWLDGKHVVFGQVIEGLNVVKDIEKVGSGSGRTSKPVVIANCGQPS | Function: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity).
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Mass (Da): 18179
Sequence Length: 172
Subcellular Loca... |
A0A0D1DMJ7 | MRQRADVEVGPLKSGLLFSYMQNFCALQTRLRRPSRTTELDTMDFKPFLTLQHFRPQGFAGDVLAPGASYNQTWNTMASKFNGRGGNRVETGKVLEAASESLKETVPLLQLVVRARHHPLLVFLVGLFLGTIYLLYRYWDCAVGCERRPDLKGPKGLPLIGNLMWALKNRDPLSYQVYAQQKYGYGNTHTLPGLGRLIDISRPDWIEHVQKIKFSNYVKGEQFHDQMRDVLGDGIFTSDGERWKMQRKVASRIFTVSSFKAIITQTIREDCALVEQLIETYARQGTVFNLQELYFKFTLSSFVKIAFSQDIKSLSEPDRP... | Function: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of the glycolipid biosurfactant ustilagic acid (UA) . UA is a secreted cellobiose glycolipid that is toxic for many microorganisms and confers biocontrol activity to U.maydis . UA consists of 15,16-dihydroxypalmitic or 2,15... |
E9RHV4 | NTHTLPGLGRLIDVSRPDWIEHVQKTNFSNYVKGEQFHDQMRDVLGDGIFTSDGERWKMQRKVASRIFTVSSFKAIITQTIREDCALVEKLIETYAKEGTVFNLQELYFKFTLSSFVKIAFSQDIMSLSEPDRPDTFGDAFNYAQKVLDMRFVQPWWKIAERFNETGRKMRAARKIVEEFTNNIVEARREESDAMGEKSKPESGRKDLLDLFMGYRSSDGQRLSNQQLKDTILNLMIAGRDTTAEALSWMSWHMLTKPEVYSRIRREIDTSLDEDGEQAGLEIDYDVFEQHTAKLSTFQETLRLHPSIPKNIRRALKDDV... | Function: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of the glycolipid biosurfactant ustilagic acid (UA) . UA is a secreted cellobiose glycolipid that is toxic for many microorganisms and confers biocontrol activity to U.maydis . UA consists of 15,16-dihydroxypalmitic or 2,15... |
Q9ZVJ4 | MNSGGGIVAAAAPSSGGGNVEWHVRPPNPKNPVVFFDVSIGGIPAGRIKMELFADIAPKTAENFRQFCTGELRKAGKPLGYKECQFHRVIKDFMVQSGDFLKNDGSGCMSIYGHKFEDENFTAKHTGPGLLSMANSGPNTNGCQFFITCAKCDWLDNKHVVFGRVLGDGLLVMRKIENVAIGPNNRPKLAVVITECGEM | Function: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity).
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Mass (Da): 21492
Sequence Length: 199
EC: 5.2.1.8
|
Q8LDR3 | MGITRNLILGLACLAFVSIAKALPHEPELGSARVVFQTSYGDIEFGFYPTVAPKTVDHIFKLVRLGGYNTNHFFRVDKGFVAQVADVASGRSAPMNEEQRKEAEKKIVGEFSDVKHVRGTLSMGRYDDPNSAQSSFSMLLGNAPHLDRQYAVFGKVTKGDETLSKLEEVPTRREGIFVMPTERITILSTYYYDTKMESCEEERSVLKRRLQASFVEVERQRMKCFP | Function: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity).
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Mass (Da): 25515
Sequence Length: 226
Subcellular Loca... |
Q8AAQ1 | MEEKNHIYPIFDRMMTREDKEELLGQHSVMIWFTGLSGSGKSTIAIALERELHKRGLLCRILDGDNIRSGINNNLGFSETDRVENIRRIAEVSKLFLDSGIITIAAFISPNNDIREMAANIIGKDDFLEVFVSTPLEECEKRDVKGLYAKARKGEIQNFTGISAPFEVPEHPALALDTSKLSLEESVNRLLEMVLPKIEKK | Function: Catalyzes the synthesis of activated sulfate.
Catalytic Activity: adenosine 5'-phosphosulfate + ATP = 3'-phosphoadenylyl sulfate + ADP + H(+)
Sequence Mass (Da): 22674
Sequence Length: 201
Pathway: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from sulfate: step 2/3.
EC: 2.7.1.25
|
P57497 | MNNNFQNNIFWQKHSITRLKREKKNGHKSIVLWFTGLSGSGKSTIANFLEEILFKNGINSYLLDGDNIRSGLCSDLSFSLADRNENIRRIGEVVKMMLHAGLIILVSVISPYRNQREMVRQMLGKKNFLEVFIDTPIEICESRDPKKLYKQARTGQISDFTGIQCTYETPNTPDVLLKGTDSLKNNSKKLIKILYNHNIISFINID | Function: Catalyzes the synthesis of activated sulfate.
Catalytic Activity: adenosine 5'-phosphosulfate + ATP = 3'-phosphoadenylyl sulfate + ADP + H(+)
Sequence Mass (Da): 23613
Sequence Length: 206
Pathway: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from sulfate: step 2/3.
EC: 2.7.1.25
|
Q0BI00 | MKQKKVFVVWLTGVSGAGKSTLANLLKQQLDARGLRTYLLDGDTLRNGLNQDLGFSDADRRENIRRTAEVARLMMDAGFIVIAALISPFRDARSRARARFAPGTFIEVFVDVALEVAEARDPKGLYVLARQGAIPQFTGIGSAYENPLSPEVHVRTAETSPSECIATIMQKLPLDTDVGAP | Function: Catalyzes the synthesis of activated sulfate.
Catalytic Activity: adenosine 5'-phosphosulfate + ATP = 3'-phosphoadenylyl sulfate + ADP + H(+)
Sequence Mass (Da): 19732
Sequence Length: 181
Pathway: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from sulfate: step 2/3.
EC: 2.7.1.25
|
Q97MT8 | MNNKKSTNVVWQETKIKRQNREKMLKQKGAVLWFTGLSGSGKSTVASALEKKLYEMGYLTYLLDGDNLRYGLNSDLGFKSEDRTENIRRVSEVAKLFADAGIITITTFISPFIEDRNNARKLLGKDFVEVYIDCPIEVCEKRDPKGIYKKARNGEIKNFTGIDSPYEKPEKPEITVETYKDTEEKCVDNIIEYLKQHKIL | Function: Catalyzes the synthesis of activated sulfate.
Catalytic Activity: adenosine 5'-phosphosulfate + ATP = 3'-phosphoadenylyl sulfate + ADP + H(+)
Sequence Mass (Da): 23001
Sequence Length: 200
Pathway: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from sulfate: step 2/3.
EC: 2.7.1.25
|
A9H259 | MSDATDPGWFPLALRLRGARVVVVGGGGIALNKVRLLLAHAARIDILAPRLEDTLAAWQAEGRITHIAGEATPDRVRALLPGSRLVYAATDDRAVNRAVAAQADALNIPVCAVDDPEPSSFITPAQIHRGPVRIAISTGGAAPVLARRLRERIEAVMPAGLDALARFLQAERAHVVAACPDIGRRRRVWEDFLDGPGGEAAQRGEHAAARQVLDHLLAGAQTGGEVWLVGAGPGDPDLLTLRALHLMQNADSVLYDQLLPPALMDRVRRDAERVFVGKQRDRHTMPQDDINAELIRRARAGERVLRLKGGDPFIFGRGGE... | Function: Multifunctional enzyme that catalyzes the SAM-dependent methylations of uroporphyrinogen III at position C-2 and C-7 to form precorrin-2 via precorrin-1. Then it catalyzes the NAD-dependent ring dehydrogenation of precorrin-2 to yield sirohydrochlorin. Finally, it catalyzes the ferrochelation of sirohydrochlo... |
Q31GG8 | MDYLPIFMKIEQQHCLIVGGGTVAARKADLFIKSGAIVTVVAPKLGNEMTFHLAQGKIIWHMNTFSTALVSELPRPSLVISATDDQNVNLAVYKTYHAQDIPVNVADQTEYCDFILPAIVDRSPMTIAISTGGRSPVLARVMKARLETMIPHGFSVLTDLVGRYRQTVKNVISDIDGRKTFWETLLSGLFIDKAVHGNTGEAEALLEAELETIKNNGQSLPQGEVYIIGAGPGDPDLMTFKGLRLLQQADVILYDRLVAPEILEMGRREAERIYVGKKEKWHKMDQKDINQMLVDLARQGKRVARLKGGDPYIFGRGAEE... | Function: Multifunctional enzyme that catalyzes the SAM-dependent methylations of uroporphyrinogen III at position C-2 and C-7 to form precorrin-2 via precorrin-1. Then it catalyzes the NAD-dependent ring dehydrogenation of precorrin-2 to yield sirohydrochlorin. Finally, it catalyzes the ferrochelation of sirohydrochlo... |
Q65T49 | MNYFPVFADLNNRPVLVVGGGTIAARKVNLLLKANAEVRITAQKLNAELTALVEQDRIIWIAKEFHGEQIRNVFLVVAATDDEQLNEQVFQVAESRQKLVNVVDDQARCSFIFPSIIDRSPIQVAVSSGGAAPVLARLLREKLEALLPQHLGVMADISGKWRHKVKQQLKTITERRRFWESLFNGRFSRLLKNRQIEAAKKELELQLTKDYQGGSVSLVGAGPGDAGLLTLKGLQEIQQADVVLYDALVSAEILDLVRRDAELIFVGKRAQGRQVAQQETNQLLADLALQGKRVVRLKGGDPFVFGRGGEELEVLAQQGI... | Function: Multifunctional enzyme that catalyzes the SAM-dependent methylations of uroporphyrinogen III at position C-2 and C-7 to form precorrin-2 via precorrin-1. Then it catalyzes the NAD-dependent ring dehydrogenation of precorrin-2 to yield sirohydrochlorin. Finally, it catalyzes the ferrochelation of sirohydrochlo... |
Q3BPY3 | MTALPAASITSSAFDDLDALNAQLEGLHADQRVAWALQHGPQNAALSSSFGAQSAVTLHLLSQQRPDIPVILIDTGYLFPETYRFADALTERLKLNLKVYRPLVSRAWMEARHGRLWEQGMVGIDQYNNLRKVEPMRRALDELEVGTWFTGLRRSQSGGRAQTPIVQKRGERYKISPIADWTDRDVWQYLQAHDLPYHPLWEQGYVSIGDFHTTRRWEPGMREEDTRFFGLKRECGIHEDI | Function: Catalyzes the formation of sulfite from phosphoadenosine 5'-phosphosulfate (PAPS) using thioredoxin as an electron donor.
Catalytic Activity: [thioredoxin]-disulfide + adenosine 3',5'-bisphosphate + 2 H(+) + sulfite = 3'-phosphoadenylyl sulfate + [thioredoxin]-dithiol
Sequence Mass (Da): 27674
Sequence Length... |
Q9PD82 | MTVLPALPPLDDLETLNVHLETLSAENRVCWALERGPDHPALSSSFGAQSAVMLHLLTRFAPDIPVILVDTGYLFPETYRFADTLTERLKLNLKVYQPLRSGAWTEARHGRLWEQGIDGINQYNTLHKVEPMRRALEELQVGTWFTGLRRGQSSTRTQTSIVQQRDERYKISPIADWTDRDIWEYMKHHDLPYHPLWEQGYVSIGDIHTTRPLEPGMREEDTRFFGFKRECGIHENI | Function: Catalyzes the formation of sulfite from phosphoadenosine 5'-phosphosulfate (PAPS) using thioredoxin as an electron donor.
Catalytic Activity: [thioredoxin]-disulfide + adenosine 3',5'-bisphosphate + 2 H(+) + sulfite = 3'-phosphoadenylyl sulfate + [thioredoxin]-dithiol
Sequence Mass (Da): 27509
Sequence Length... |
Q8EB00 | MSEQKLALNEYLKTDSDYLRGTIKEGLDSSVTGSFSDGDQQLIKFHGFYQQDDRDLRNERKEQKLEPLYSFMLRARVPGGVCTPKQWLGVDEIASTLTSSNSIRLTTRQTFQYHGIPKRNLKTIIQGLDREALDSIAACGDVNRNVMCNPNPVESKLHAQAYEVAKKLSDHLLPHTRAYAEIWLDEEKLLTTEDETVEPVYGKTYLPRKFKMAVAVPPDNDVDVYTNDLGFIAVAENGELVGFNLTAGGGMGSTHGEVETFPRLADDFGFIKTEDVMKFAEAVMTVQRDWGNRTNRKRSRLKYTIVDHGYEKFKAEVEVR... | Cofactor: Binds 1 siroheme per subunit.
Function: Component of the sulfite reductase complex that catalyzes the 6-electron reduction of sulfite to sulfide. This is one of several activities required for the biosynthesis of L-cysteine from sulfate.
Catalytic Activity: 3 H2O + hydrogen sulfide + 3 NADP(+) = 4 H(+) + 3 NA... |
P04862 | MASATLTAWIKMPSFLKKILKLRGRRQEDESRSRMLSDSSMLSCRVNQLTSEGTEAGSTTPSTLPKDQALLIEPKVRAKEKSQHRRPKIIDQVRRVESLGEQASQRQKHMLETLINKIYTGPLGEELVQTLYLRIWAMEETPESLKILQMREDIRDQVLKMKTERWLRTLIRGEKTKLKDFQKRYEEVHPYLMKEKVEQVIMEEAWSLAAHIVQE | Function: The different isoforms prevent the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN-alpha/beta) and IFN-gamma signaling pathways. They inhibit IFN-alpha/beta induced tyrosine phosphorylation of STAT1 and STAT2. Blocking the IFN-alpha/beta pathway requires binding to STAT1 i... |
Q54Q40 | MAAELPFYIASSVEELVKKHVEGVEVDKNYSIFHYLSTCNNLVKQADIYKSEGDIERTYIYSLRFCILIFEKLQKHPDFNKESFTKSRNEIKRKAELKLKELEGLKETLKKGYERIQHKKEEERKRIEREKEKERIFKQEKLKLEREQQLLREEEEQRKREDLELESEIQRLKEVEDFENRKLQAQKNIKRATSARTFELLRQEALLEERKRLQGIETEKKRILAEKQEALEKEFQQQLFEQQEKERLEKERLEKEEQLRLASLPPPPPDYSSFDSDQLLNLIENNNKKLENNNQTDDKLDNEFLLDPSFLPPPPPIITQ... | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: May be a zinc metalloprotease that specifically cleaves ubiquitin chains.
Sequence Mass (Da): 83674
Sequence Length: 715
Domain: The JAMM motif is essential for the protease activity.
EC: 3.4.19.-
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Q58408 | MIAKYIIKHGLELAYDIKADAFMIFTETGKSYELLKSFLKKDEHSGIIKILDKISHKNVKIIVATPNQVTYKKISSENEENIYPIFIKHREDNRCMIISSGIVHALKMKILKENNKIVAVVGEPKTPGKLDTIMVVNVKEHVKTITLYELFETLDEKQKRTLKEIIKLAMEIGREGREGEYVGTIFVMGDTLNVMSMSKPLILNPFAGHNASIFDENVKGTIKELSSIDGAFIITDEGKVVSAGRFLEIKGDVNIPKGLGARHLAAASISKNTNAIAVTVSQSGGIVRVFKDGKIVFETDPRANILFFD | Function: Diadenylate cyclase that catalyzes the condensation of 2 ATP molecules into cyclic di-AMP (c-di-AMP) . c-di-AMP is a second messenger for intracellular signal transduction involved in the control of important regulatory processes such as osmoregulation (By similarity).
Catalytic Activity: 2 ATP = 3',3'-c-di-A... |
P39045 | MKQSSPEPLRPRRTGGRGGARRAAALVTIPLLPMTLLGASPALADASGARLTELREDIDAILEDPALEGAVSGVVVVDTATGEELYSRDGGEQLLPASNMKLFTAAAALEVLGADHSFGTEVAAESAPGRRGEVQDLYLVGRGDPTLSAEDLDAMAAEVAASGVRTVRGDLYADDTWFDSERLVDDWWPEDEPYAYSAQISALTVAHGERFDTGVTEVSVTPAAEGEPADVDLGAAEGYAELDNRAVTGAAGSANTLVIDRPVGTNTIAVTGSLPADAAPVTALRTVDEPAALAGHLFEEALESNGVTVKGDVGLGGVPA... | Function: Removes C-terminal D-alanyl residues from sugar-peptide cell wall precursors.
Catalytic Activity: Preferential cleavage: (Ac)2-L-Lys-D-Ala-|-D-Ala. Also transpeptidation of peptidyl-alanyl moieties that are N-acyl substituents of D-alanine.
Sequence Mass (Da): 54974
Sequence Length: 538
Pathway: Cell wall bio... |
P15555 | MVSGTVGRGTALGAVLLALLAVPAQAGTAAAADLPAPDDTGLQAVLHTALSQGAPGAMVRVDDNGTIHQLSEGVADRATGRAITTTDRFRVGSVTKSFSAVVLLQLVDEGKLDLDASVNTYLPGLLPDDRITVRQVMSHRSGLYDYTNDMFAQTVPGFESVRNKVFSYQDLITLSLKHGVTNAPGAAYSYSNTNFVVAGMLIEKLTGHSVATEYQNRIFTPLNLTDTFYVHPDTVIPGTHANGYLTPDEAGGALVDSTEQTVSWAQSAGAVISSTQDLDTFFSALMSGQLMSAAQLAQMQQWTTVNSTQGYGLGLRRRDL... | Function: Catalyzes distinct carboxypeptidation and transpeptidation reactions during the last stages of wall peptidoglycan synthesis. Mistaking a beta-lactam antibiotic molecule for a normal substrate (i.e. a D-alanyl-D-alanine-terminated peptide), it becomes immobilized in the form of a long-lived, serine-ester-linke... |
Q39080 | MVKSTSKDAQDLFRSLRSAYSATPTNLKIIDLYVVFAVFTALIQVVYMALVGSFPFNSFLSGVLSCIGTAVLAVCLRIQVNKENKEFKDLAPERAFADFVLCNLVLHLVIINFLG | Function: Subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in ... |
Q8I7Z2 | MGSSAFEVLTFFLKDYKANTPQKLKIIDAYLLYILLTGINQFLYCCLVGTFPFNSFLSGFISCVASFVLGVCLRLQVNPQNSSNFCGIPPERAFADFIFAHVVLHLVVMNFIG | Function: Subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in ... |
Q5E9C2 | MSASVLSVISRFLEEYLSATPQRLKLLDAYLLYILLTGALQFGYCLLVGTFPFNSFLSGFISCVGSFILAVCLRIQINPQNKADFQGISPERAFADFLFASTILHLVVMNFVG | Function: Subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in ... |
P52872 | MAAQVVPVLSKLFDDYQKTTSSKLKIIDAYMTYILFTGIFQFIYCLLVGTFPFNSFLSGFISTVTSFVLASCLRMQVNQENRSEFTAVSTERAFADFIFANLILHLVVVNFLG | Function: Subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in ... |
E2R4X3 | MSASVASVISRFLEEYLSSTPQRLKLLDAYLLYILLTGALQFGYCLLVGTFPFNSFLSGFISCVGSFILAGNGSLRNRSNNVFTLVRCFSSLVTLFYSRSPPREVPRGACIALFCERGN | Function: Subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in ... |
Q9VLM5 | MVELSSVISKFYNDYVQNTPKKLKLVDIYLGYILLTGIIQFVYCCLVGTFPFNSFLSGFISTVSCFVLAVCLRLQANPQNKSVFAGISPERGFADFIFAHVILHLVVMNFIG | Function: Subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in ... |
P61803 | MSASVVSVISRFLEEYLSSTPQRLKLLDAYLLYILLTGALQFGYCLLVGTFPFNSFLSGFISCVGSFILAVCLRIQINPQNKADFQGISPERAFADFLFASTILHLVVMNFVG | Function: Subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in ... |
O81214 | AVATALIQVAYMGLVGSFPFNSFLSGVLSCIGTAVLAVCLRIQVNKDNKEFKDLPPERAFADFVLCNLVLHLVIMNFLG | Function: Subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in ... |
O24060 | MGKASHSSTAQDAVALFDSLRSAYSATPTTLKIIDLYIGFAVSTALIQVVYMAIVGSFPFNSFLSGVLSCIGTAVLAVCLRIQVNKENKEFKDLAPERAFADFVLCNLVLHMVIMNFLG | Function: Subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in ... |
Q01IX6 | MVEIPAIDLRLAGGGGGAEETARLRDACARLGCFRVSGHGVPPGLQAEMKAAVRALFDLPDDAKRRNADIIPGSGYVPPGTANPLYEAFGLCDAAAPADVDAFCARLDAPPHVRETVKAYAERMHSLIVDVAGKVAASLGLHGASFQDWPCQFRMNRYNYTQDSVGSPGVQVHTDSGFLTVLQEDECVGGLEVLDPAAGEFVPVDPLPGSFVVNVGDVGQAWSNGRLHNVKHRVQCVAAVPRVSIAMFLLAPKDDTVSAPGELVDGEHPRRYREFKYDDYRRLRLSTGERAGEALARLAA | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: 2-oxoglutarate-dependent dioxygenase essential for auxin catabolism and maintenance of auxin homeostasis in reproductive organs. Catalyzes the irreversible oxidation of indole-3-acetic acid (IAA) to the biologically inactive 2-oxoindole-3-acetic acid (OxIAA) (By simil... |
O67216 | MFQGSIVALITPFKEGEVDYEALGNLIEFHVDNGTDAILVCGTTGESPTLTFEEHEKVIEFAVKRAAGRIKVIAGTGGNATHEAVHLTAHAKEVGADGALVVVPYYNKPTQRGLYEHFKTVAQEVDIPIIIYNIPSRTCVEISVDTMFKLASECENIVASKESTPNMDRISEIVKRLGESFSVLSGDDSLTLPMMALGAKGVISVANNVMPREVKELIRAALEGDFRRAREIHYYLHDLFKVLFIETNPIPVKTACWMLGMCEKEFRLPLTEMSPENENKLREVLKKYNLPLKN | Function: Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).
Catalytic Activity: L-aspartate 4-semialdehyde + pyruvate = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + H2O
Sequence Mass (Da): 32670
Sequence Length: 294
Pathway: Ami... |
O29352 | MFEGVIPAMVTPFKEDFSVDYEGIAKNLDYLEKHVNALVPAGTTGEAATLSYEEHIDVVRYVAETSKLPVIGGAGSNSTREAIWLAKEVEKAGAEAAMLVTPYYNKPNAEGLYQHYKAVASEVSIPIIVYNVPSRTGINTTPELVRRLAEIDNIFGIKEASGNLKQISEIIRTTPDDFVLLSGDDFLTLPILCLGGKGVISVAANVAPHLMKEMYEAFVEGNIERAREMHHRLTPLFDVLFIDTNPIPVKKALQLMGLAAGKPRLPLVELSEEKTQKVKEVLKSLELIS | Function: Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).
Catalytic Activity: L-aspartate 4-semialdehyde + pyruvate = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + H2O
Sequence Mass (Da): 31692
Sequence Length: 289
Pathway: Ami... |
B6YQ20 | MRQIVLRGMGVALITPFKCDGTVDYPALSYLVDYQLQNGIDYLIVLGTTAETPTLSYEEQKEIVRLVVSIVRERIPIVVGVGGNNTQAVIHKLNTEDFGKIDAILSVVPYYNKPTQDGIYQHFKYIAQATSLPIILYNVPSRTGVNMTAETSLLLANDFENIVAIKEASGNIDQIGVIIENKPSGFQVLSGDDELSLSLIGIGAVGVISVIGNVFPKEFGKMIRLALNGDSDNARIIHGQFAELFELLFIEGNPAGVKGMLNVMGFIENKLRLPLVPVLEATYERIKKALLMFRTQ | Function: Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).
Catalytic Activity: L-aspartate 4-semialdehyde + pyruvate = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + H2O
Sequence Mass (Da): 32488
Sequence Length: 296
Pathway: Ami... |
Q04796 | MNFGNVSTAMITPFDNKGNVDFQKLSTLIDYLLKNGTDSLVVAGTTGESPTLSTEEKIALFEYTVKEVNGRVPVIAGTGSNNTKDSIKLTKKAEEAGVDAVMLVTPYYNKPSQEGMYQHFKAIAAETSLPVMLYNVPGRTVASLAPETTIRLAADIPNVVAIKEASGDLEAITKIIAETPEDFYVYSGDDALTLPILSVGGRGVVSVASHIAGTDMQQMIKNYTNGQTANAALIHQKLLPIMKELFKAPNPAPVKTALQLRGLDVGSVRLPLVPLTEDERLSLSSTISEL | Function: Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).
Catalytic Activity: L-aspartate 4-semialdehyde + pyruvate = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + H2O
Sequence Mass (Da): 31042
Sequence Length: 290
Pathway: Ami... |
Q6MRM9 | MKNFKGTFTALVTPFKNGKIDFASLDKLLKQQLAGGVDGFVVNGTTGESPVLTSSEKAELFKHIRNVCGDKVVLIMGTGSNNTAQTIEDSRKAEEMGADAILVVVPYYNKPPQRGLYEHFKAVASSVKIPTILYNVPGRTITSLETGTIRDLAKVKGVVGIKEATGKIDLASEIIKACGSEFVMLSGDDGTYVEFLGVGGHGVISVASHVIPAQMVQWKKWVSEGALDKARADIAKYNDLINLLFVEANPIPVKKALQLMGILESAELRLPLVELGAENTAKLQAEMKKVGVL | Function: Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).
Catalytic Activity: L-aspartate 4-semialdehyde + pyruvate = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + H2O
Sequence Mass (Da): 31444
Sequence Length: 293
Pathway: Ami... |
B8DWI2 | MSDGIMHLLDPAPFGRVLPAMITPMKPNGDVDFDMAQTVAKQLVADGADGLVVNGTTGESPTTHMDEKVELVKAVKEVVDVPVISGAGSNDTAHTVRMVEQTQEAGADAVLVVCPYYSRPSQQGIFCHYQAVNESADKPIIVYDVPGRTGVRIALDTYVHLAELDHVKAVKDATGDIAGAVRKRMETGLTWYSGDDALYLPFLSIGAVGIISVVAHAAAKPMRELAEAFDRGDIAKAQGLANRIAPVIEAMNGTGFQAVMAKAALKVRGIMECTTMRLPNIGPNDEQIEVVRDGLRASGLIPE | Function: Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).
Catalytic Activity: L-aspartate 4-semialdehyde + pyruvate = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + H2O
Sequence Mass (Da): 32204
Sequence Length: 303
Pathway: Ami... |
Q9RH76 | MAAKTKFRGSFTALVTPFKNGSLDEAAFRSLVNWQISEGTNGLVPVGTTGESPTLSHDEHKKVVEWCIEEAKGRVPVVAGAGSNSTKEAIELAQHAEKAGADAVLVVTPYYNKPTQEGMYQHFKAINDAIGIPIIIYNIPPRSVIDMSVDTMKRLWELKNIAGVKDATASMVRVSQQRAAMGEDFNQLSGEDATILGYMAHGGHGCISVTSNVAPRLCSEFHTAWQKGDHATALKLHDKLMPLHNNLFIESNPAPIKYAMSLLGKLDETLRLPMVPVTEPTRVAVRSAMVHAGLIN | Function: Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).
Catalytic Activity: L-aspartate 4-semialdehyde + pyruvate = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + H2O
Sequence Mass (Da): 32098
Sequence Length: 296
Pathway: Ami... |
C0R176 | MSLFEGAGVALITPFTEDNQINYEKLEELIEFQIANKTDAIIAAGTTAESATLTPEERMQVIKFCIERTKKRTIVIAGTGTNNTASAVEFSKKSYEYGADMVMAVTPYYNKGNESGLIDYYTQIANSVKCPVIMYSVPSRTGVKLSLNVIKTLSEISNIQGIKEASGDISYVADIVNVAPKLDLYSGNDDMVTPMMALGAKGVISVTSNIIPKENHDMVMNFLNGNVNEAIKTQIKYIDFVRAMFIETNPAPIKEAMNIMGFNVGECRSPLGPLSEKNREHVKNIINKYGLKK | Function: Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).
Catalytic Activity: L-aspartate 4-semialdehyde + pyruvate = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + H2O
Sequence Mass (Da): 32192
Sequence Length: 293
Pathway: Ami... |
Q12ZG2 | MFEGVLPALITPFTKDDTIDRTGLIKNIEFAENGKVTGVVVCGTTGESATLSTAEHMEVIDIAVECANVPVVAGTGSNNTAEAVELTKHAEEAGASGALVISPYYNKPNKAGLISHFRTIAEAVEIPIVLYNVPSRTGQDISLEVITELAKIDNIVGIKEASGNLDKASQIIENTMDEDFKVTSGDDGLTLPIMSIGGCGVISVVANIVPDRMSRLVNAFNEGDTATAQQLHYEIAPLIRALFTETNPVPIKRAMNLVGLNAGHLRPPLAPISAENNKLLANCLKELGCLQ | Function: Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).
Catalytic Activity: L-aspartate 4-semialdehyde + pyruvate = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + H2O
Sequence Mass (Da): 30788
Sequence Length: 291
Pathway: Ami... |
Q2FNR0 | MFEGVFPALITPFQRNHGKNLDLDGLRSNIAHLVAAGVHGVVPCGSTGESATLSFAEHEQVVEVTMDEAGGKVPVLAGTGSNNTSEALRFTRAAKDVGADGVLVISPYYNKPNRSGLIKHYTAIADLDIPVVVYNVPGRTGQNITPDIIAELAKHPNIVGVKEASGDLGQISTIIELTRDEDFAVISGDDNLTLPILSLGGKGVISVAANIYPRPLIEMYEAAQKGDYETAREIHFKYSPLFRAMFYESNPIPVKKAAEILGMAAGPLRLPLDEASEQTTERLKEVLSRYD | Function: Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).
Catalytic Activity: L-aspartate 4-semialdehyde + pyruvate = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + H2O
Sequence Mass (Da): 31284
Sequence Length: 291
Pathway: Ami... |
Q57695 | MFKGVYPAIITPFKNKEVDFDGLEENINFLIENGVSGIVAVGTTGESPTLSHEEHKKVIEKVVDVVNGRVQVIAGAGSNCTEEAIELSVFAEDVGADAVLSITPYYNKPTQEGLRKHFGKVAESINLPIVLYNVPSRTAVNLEPKTVKLLAEEYSNISAVKEANPNLSQVSELIHDAKITVLSGNDELTLPIIALGGKGVISVVANIVPKEFVEMVNYALEGDFEKAREIHYKLFPLMKAMFIETNPIPVKTALNMMGRPAGELRLPLCEMSEEHKKILENVLKDLGLI | Function: Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).
Catalytic Activity: L-aspartate 4-semialdehyde + pyruvate = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + H2O
Sequence Mass (Da): 31580
Sequence Length: 289
Pathway: Ami... |
Q6LZP8 | MQGVYPAIITPLKENKVDYDGLRNNIDFLIENGVSGVIPVGTTGESPTLTPLEHEKVVEKVVEFVDGRVEVIAGTGSNSTSEALEFSQYAEDVGVDGVLLITPYYNKPTQEGLKRHFGEIANSINVPIVLYNVPSRTALNIEPETIKYLFNEYSNISAVKEANPNLSQVSEVLDSCDIDILSGNDELTLPIISLGGKGVVSVIANIAPKEFVQMVDFANAGKFDKAKEIHYKLFPLMKLMFVETNPIPIKTAMNMLGMPSGELRLPLCEMAESNKLKLQNALNNLGLLK | Function: Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).
Catalytic Activity: L-aspartate 4-semialdehyde + pyruvate = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + H2O
Sequence Mass (Da): 31584
Sequence Length: 289
Pathway: Ami... |
Q2NHW2 | MNLEGTHVAMITPFNNDNTINEEKYREFIDFLIEGGVDGILAAGTTGESATLTLEEHQKVIDIMVDQANGRVTTIAGAGSNATSEALDLVNYSKDAGADVALVITPYYNKPQQSGLYNHFKLLNDQCDMPIIAYNVPSRTGVDLSVDNIINLAKLDNIVAIKEANPDLNKLAHVFSRLNSENLLDDFTVLSGNDSLTLPMISQGSKGVISVVANIMPNKTSTMVNNALNGNYDEARTLSNELFNLMDVLFIEASPAPTKRALNLMGMDVGGLRMPINEICDENEVILKEILKENNLI | Function: Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).
Catalytic Activity: L-aspartate 4-semialdehyde + pyruvate = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + H2O
Sequence Mass (Da): 32319
Sequence Length: 297
Pathway: Ami... |
A9FHA5 | MSQLPLSGTFTALVTPFTPDGEAVDFDALDALVEAQIAGGVSGLVPCGTTGESPTLSEAETTAVIRRVVEAARGRVPVIAGTGSFSTKKTIEASRAALAAGAAGVMIVMPYYSKPSQDGLREHTLAVARAVPAPIVLYNIPGRTVVDLSAETTERICAAAPNVVAIKDASGNVFRCQELVRRLGDRLTILSGDDALTLAMMALGAQGVISVTSNVLPRETSAVTRRFLAGDLAGARAAHLALLELHGLLFVEPNPAPAKAALAALGRMSAAVRLPLVPAGEATRQQIAEAMRRLEARREAS | Function: Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).
Catalytic Activity: L-aspartate 4-semialdehyde + pyruvate = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + H2O
Sequence Mass (Da): 31168
Sequence Length: 301
Pathway: Ami... |
Q6GH13 | MTHLFEGVGVALTTPFTNNKVNLEALKAHVNFLLENNAQAIIVNGTTAESPTLTTDEKELILKTVIDLVDKRVPVIAGTGTNDTEKSIQASIQAKALGADAIMLITPYYNKTNQRGLVKHFEAIADAVKLPVVLYNVPSRTNMTIEPETVEILSQHPYIVALKDATNDFEYLEEVKKRIDTNSFALYSGNDDNVVEYYQRGGQGVISVIANVIPKEFQALYDAQQSGLDIQDQFKPIGTLLSALSVDINPIPIKALTSYLGFGNYELRLPLVSLEDTDTKVLREAYDTFKAGENE | Function: Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).
Catalytic Activity: L-aspartate 4-semialdehyde + pyruvate = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + H2O
Sequence Mass (Da): 32481
Sequence Length: 295
Pathway: Ami... |
Q8YDC8 | MGLVVVGAGGRMGQTLIRTIQSIEGAKLVGAIERSGSPFLGKDAGEVTGIGTLGVAITDDPLPVFAKAHGVLDFTSPAASVEFAGLAAQARIVHVIGTTGCSAEDDEKIRAAARHATIVKSGNMSLGVNLLSVLVQKAAEALGPEDFDIEILEMHHRHKVDAPSGTALLLGEAAARGRDIALADNSVRVRDGYTGPRETGTIGFATLRGGSVIGDHSVILADTGERVVLSHHAEDRSIFARGAIKAALWAHGKKPGLYSMLDVLGLNT | Function: Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate.
Catalytic Activity: (S)-2,3,4,5-tetrahydrodipicolinate + H2O + NAD(+) = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADH
Sequence Mass (Da): 27693
Sequence Length: 268
Pathway: Amino-acid biosynthesis;... |
P57246 | MNKKTRIAITGPIGRMGRMLIKEIQNNKHSHLTVAVVQKKHQLIGQDIGRIIGIGEIGVLISDELNIKKNDFDVLIDFTRPAGTLEYLKYCNKFKKNIVIGTTGFSKEEIDIIKSYSQKIAIIIASNFSIGINLLFQLIKKTTQIIGKDSDINILEYHHRNKIDAPSGTALEIGEVISKVMNWNLNQDSIYYQKGITGIRDAKKIGFSIVRAGNIVGKHTVMFSSYDEEIKITHTASNRMSFARGAIQSALWIHKKNTGLFDMTDVLSL | Function: Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate.
Catalytic Activity: (S)-2,3,4,5-tetrahydrodipicolinate + H2O + NAD(+) = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADH
Sequence Mass (Da): 30146
Sequence Length: 269
Pathway: Amino-acid biosynthesis;... |
P59474 | MKKTTLNIAISGALGKMGINLIHEIYHTKNVFLTAAIVKNNSPYVQKNVGKITKIGEINIPITNSLEENINKFDILIDFTNPKTTLKNLEICAVAKKNIIIGTTGFTQEEQKKIKLLSKKIGIVQSSNYSIGINLMISLLEKTTQIIGKNTDIEIIEAHHNKKIDAPSGTSLEIGKKICKTMNWDFSKQAIYERHSSMKSRANNEIGFSSIRAGNIVGEHKVLFANSGEHIEITHKAISRSIFSKGAIQAAIWLFSKNYKNGLFNMNHILNI | Function: Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate.
Catalytic Activity: (S)-2,3,4,5-tetrahydrodipicolinate + H2O + NAD(+) = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADH
Sequence Mass (Da): 30261
Sequence Length: 272
Pathway: Amino-acid biosynthesis;... |
Q057Y0 | MKNKTKIIISGALGRMGKILIKETKKNKLIKLVYALINNNIDIKNHNQFYKVKEKKKFITLNNLKKKKKILKFDTIIDFSSPKYSIKIIKYCLKNNKKIVLGTTGFNTEQIKIINNASKKIPIIYSPNFSIGINIIYKILKNISKILGKNSDIEIIESHHRNKIDAPSGTALQLGKIISKSMKWNFKKSAIFSRYGNIGIRKKKRIGFSTIREGNTIGEHTVLFSNKYEKISIFHKAIHRSVFAKGALKAAIWISRKKNGLYNMSDMLKKIKI | Function: Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate.
Catalytic Activity: (S)-2,3,4,5-tetrahydrodipicolinate + H2O + NAD(+) = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADH
Sequence Mass (Da): 31312
Sequence Length: 273
Pathway: Amino-acid biosynthesis;... |
Q5ZZ80 | MRTRIIVNGANGKMGILACETLENHEQFEIVAKLSRQDNLGQSILDTKAQIVVDLTRADCVYENSLTIINHGARPVIGTSGLVETQIDELTKLCEIKQIGGIIAPNFSLGAILMMILATKASEYFSEVEIIEGHHQQKLDAPSGTALKTAEMIAAARKKPKNKLPLKELTPGARGGSHHDINIHSLRLPGLLARQEVLFGNIGETLSITHNSIDRRCFMPGIVLACQKVLNLNNLVYGLEHLL | Function: Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate.
Catalytic Activity: (S)-2,3,4,5-tetrahydrodipicolinate + H2O + NAD(+) = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADH
Sequence Mass (Da): 26543
Sequence Length: 243
Pathway: Amino-acid biosynthesis;... |
Q72U21 | MSQPSKTQIALIGASGRMGRAIVSVLSTSVKSTLSSSVVSQSSVFLGMDSGLHSGIKQNGVNFSSDLEAAVRSADCVIDFSTHQNLDFTLKACIQYQKPVVIGITGLTELQKDALQVASKEIGIVYSPNMSIGVNLLFKLTEIAAKVMGEISDIEIQDIHHRHKKDAPSGTAEKLKSILLETLGRTSKNVVHGRHGILKERDSKEIGIHTFRAGEVIGDHTVYFFTPEERIEITHKAQDRKTFAVGSVHAAEFLVGRKPGLYDMFAVLGL | Function: Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate.
Catalytic Activity: (S)-2,3,4,5-tetrahydrodipicolinate + H2O + NAD(+) = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADH
Sequence Mass (Da): 29259
Sequence Length: 270
Pathway: Amino-acid biosynthesis;... |
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