ids stringlengths 6 10 | seqs stringlengths 16 1.02k | texts stringlengths 117 4.4k |
|---|---|---|
A0A2G9YJR9 | MDMRDKIKEALGDKVKGWQEHSAKRIYITLDKEDIYKSAELLFRKLGLRFIIASATDMPEYFEILYHFSNDPAGEIYSLRVLLRDKAHPEVDAITPIFPGAEWIEREIWEMLGISFKGHPNLKKLLLADDWPEGEYPLRNKK | Function: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain.
EC: 7.1.1.-
Catalytic Activity: a quinone + 5 H(+)(in) + NADH = a quinol + 4 H(+)(out) + NAD(+)
Sequence Length: 142
Sequence Mass (Da): 16635
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A0A843RE79 | MLADPDRPLLLLGCDGQVGREVRRLADARGLPIAALARGQLDITQRLEVMEAVGRGYGVVVNAAAYTAVDRAESEAAKAMAVNRDGAGHIAEACQASGAALIHLSTDYVFDGAKGVPYREDDSVHPLNVYGSSKQAGEAAVRAVCAGHVILRTSWVFGAAGANFVKTMLRLGSERAELSVVADQFGCPTPAAALAEAVLAVAERLDPGVYGTYHCAGAERTSWYDFAGAIFAGQQALTGRAGPELRPIATADYPTAARRPVDSTLDSSLFQATFGLGPIDWRGGLIELLRTLLAART | Cofactor: Binds 1 Mg(2+) ion per monomer.
Pathway: Carbohydrate biosynthesis; dTDP-L-rhamnose biosynthesis.
Function: Catalyzes the reduction of dTDP-6-deoxy-L-lyxo-4-hexulose to yield dTDP-L-rhamnose.
EC: 1.1.1.133
Catalytic Activity: dTDP-beta-L-rhamnose + NADP(+) = dTDP-4-dehydro-beta-L-rhamnose + H(+) + NADPH
Seque... |
A0A6B8RUZ2 | MSTKTINRPSMLRHWTYRYVIILCIGLLSIGLLSFLWVRHSTVQNRLQLMQLLAQELAEKVTSPEGSIKLPNNFGDLIDSRQRFYHIPDHVSVIIKNNSNQMIYSQSNQPNIADPQGDKPAQPEPPKAAQYTVSEPILYQDTTIGTITIGQTKKAITKINQESRLLALLLGGIGLLGWLVIYLILQKLTRPIRDIAEAAKKIEAGDYNIELQNTVKEKEIYELLVSFRGMAVRLEQLEDLRTELLAGVTHELKTPIASINGLIHAVRDKIVTGTEAEEFLDISIKETERLQQMVIALLDFNSFASGKINVEQIQFDLGKL... | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Membrane
Sequence Length: 465
Sequence Mass (Da): 52204
Location Topology: Multi-pass membrane protein
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A0A3P1BUW2 | MFSHLDSKDNPSMVDVGDKAVTRRVARARSIVVLNDEIMRQLQGQDIQTKKGPVFQTAIIAGTMAAKRTSDLIPLCHPLGLDSCKFTIVAEGNEVIIECTTALEAKTGVEMEALVGASVAALTVYDMCKAFSHDIVIKETRLLDKTGGKYDFHKTA | Pathway: Cofactor biosynthesis; molybdopterin biosynthesis.
EC: 4.6.1.17
Catalytic Activity: (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate = cyclic pyranopterin phosphate + diphosphate
Sequence Length: 156
Sequence Mass (Da): 16955
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A0A7C4VZV3 | MPQEHLLIVSNDAIGKRVDLFLSEAIPGMSRSHAASRIKDGHVWIEGVPVRKSGVRLRPGETVRVWIPDPVPIEARPEAIPLDVLYEDDHLLVINKEAGLVVHPAPGHADGTLVNAVLHHCDRLSSIGGCLRPGIVHRLDKDTSGVLIVTKSDAAQTGLTEQFKHRQVQKTYLALVVGKMPRPDGIIDLPIGRHPVDRKKMSVHATRSRNALTLWHEREVYTGFSLLEIEIKTGRTHQIRVHVAAMGHPIAGDDVYGGRLPQSAPSRWASLIRRPMLHAWKIGFTHPVTGRPITCCAPLAPDMEAVLRELREGASLSVAF... | Function: Responsible for synthesis of pseudouridine from uracil.
EC: 5.4.99.-
Catalytic Activity: a uridine in RNA = a pseudouridine in RNA
Sequence Length: 344
Sequence Mass (Da): 37894
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A0A7C4MMT8 | MTSIVFRCASLDETHRIGVLLGERFEAGTVLLLRGELGVGKTCLVRGVAEGIGVSPEQPVTSPSYALIHEYSGRLRLFHVDLYRIGYTDLEDIGFFDLPVEEGGAGRRGSACRRMGRTPPGRCLHRQSRSGIRYTGRREPDHRDFGKGRNERSMAPAVDFLAAAETDRPSAGHATRGRRKDRPMALIVQKYGGTSVANLERIQNVAKRVVKTYDQGNDVVVILSAMAGITDSLIEMAQEITRTPEKRELDVLLATGEQTTAALLAMTLNAMKYPAKSLLGYQAEVITDCTYGNARIMEIGARRIRELLAQRHIVVVAGFQ... | Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 1/4.
Catalytic Activity: ATP + L-aspartate = 4-phospho-L-aspartate + ADP
EC: 2.7.2.4
Subcellular Location: Cytoplasm
Sequence Length: 588
Sequence Mass (Da): 63857
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A0A1I3HR91 | MKKFLTIVMAFLLVSCNGQGKEAASKMAVEKIDKSNLEYVTIGGGCFWCVQTTFQMLKGVDSVVSGYSGGFKANPTYEEVSSGDTGHAETVRIGFDPKIISYQKLMDVFFFLHDPTQLNRQGNDVGTQYRSVVFYKDEAQKKETLAAEKVSEASGRWKGKYVTQVVPFEKFWPAETYHQDYYNQNPTQPYCSAVVGPEIARFKEHYGKLGWLKPNS | Function: Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine.
EC: 1.8.4.11
Catalytic Activity: [thioredoxin]-disulfide + H2O + L-methionine = [thioredoxin]-dithiol + L-methionin... |
A0A2S2NTT9 | MPETGYQVLSSEREEEVHFQFTPNVARNRWNHIEDLDTFFTRIYLYHQRHGFICLILQSALDLLQVIFLLVFSLFLFYCIDYPVLFRDKPADSNRVINGTDKVRLSDVFLPASKCTSKFTIFTYLYMIPLLMFALFRLMKVFNVAYHYADIKAFYNVALHIPDKELQNYTWREIIHKVIEAQKEQNMCIHKLDLTELDIYQRILRTKNYLIALVNKSVLPTNFNIPFLGDVIYFSNGMKYNLNLLLFWGPWSPFENN | Function: Phospholipid scramblase involved in autophagy. Cycles between the preautophagosomal structure/phagophore assembly site (PAS) and the cytoplasmic vesicle pool and supplies membrane for the growing autophagosome. Lipid scramblase activity plays a key role in preautophagosomal structure/phagophore assembly by di... |
A0A6B8RFP8 | MSNKNIEKRGRVHYNYYRFEVIVLVFKIINLLFAPIVKLLRMIRTKLLLKMIIVYSLLTVIPLTLVTGISYLNSQKIIEKKIADSANRTLIETVDKIEGILQVMEKVLDDLANDQVVKTLLKNDYDKITYPMTEARRHETESTLKETLNLQLSGDSIEEAFINSIYIFNNTEKYYTTETNGKVQYYDALKVLPYDKEGRPQWAFFMDNSQIICSIEIIDNVTGKLGFIAIMLNPDKVRQLYAGYPENTFYVTNDFNLILSASNLEEVGSLFTDYSKPETILNRRVSKDTGFIYISMVSTEDLNKEIKGLAYFSSTITLIT... | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Membrane
Sequence Length: 603
Sequence Mass (Da): 69517
Location Topology: Multi-pass membrane protein
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A0A6J4HWZ7 | MPGAGRSVASATTTTPDDPLADLGWGPDLDAALPIGLAPARVVRSDRGWVTALGRFGEVRLRFDPLHPLSPTPTTGDWVASAPGDDLVAAILPRRTALVRAGAHDEATPQVLAADVDLVGVCVPLSSPPRAGRIQRYVTLGWASGATPLLVLTKADGALGPQAASEVAAMAPGVEVVVVSARDGRGIDDLRARLRGGRTMVLVGPSGVGKSTLVNALVGRDAMATGAVRESDAKGRHTTSTRELVLVPGGGVLLDTPGLRALVPWDDGDGLARAFPDIAPLLGTCRFSDCQHRGQPGCALEAAVAAGQLASGRLEGWQRL... | Cofactor: Binds 1 zinc ion per subunit.
Function: One of several proteins that assist in the late maturation steps of the functional core of the 30S ribosomal subunit. Helps release RbfA from mature subunits. May play a role in the assembly of ribosomal proteins into the subunit. Circularly permuted GTPase that catalyz... |
A0A4P2VCH3 | MVDLIPESWYNVVPDLPEPLPPPMDPPGRDSSSIGLLNEIMPRAVLEHQFTVERWVRIPDEVRGAYANFGRPTPLLRAKKLEERIGTRPPRGFADAIRAARSRGVNPVIAELKLASPSGFRAGDVDVERYLRTVARGAAALSVITEPVAFGGSYDLLRMASSSVDLPVLMKDFVVTSGQVRSAHSLGADAVLLIVRLLRDAELELLYSEATSMGMDVLVEVHDEHDLERALRLRPRVIGVNSRDLLTLRMDGELQRRILGMIPGGIVRVAESGIRSADDLRRLRDSGADAFLVGTSLMENPGLLEELLDA | Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 4/5.
EC: 4.1.1.48
Catalytic Activity: 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate + H(+) = (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + CO2 + H2O
Sequence Length: 310
Sequence Mass (Da): 34010
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A0A914K1R3 | MAYSTAVSILYLILALTGFCGNLWVMTTVISQLVGCCMSPSFRARRRSPITGVQSSACLYLLLLSIVDLISLIPVPFVVTDVTLHKFIYPNWTCKMIYSFEAANKSLSPLVLTALSVDRYIAVCRPTMIWMRQTKFAIGIIVLCCALSLCFILPIAAVASVVEFPLVAKNKDVRKCMVDLPVILALILPQVSYVLPLIFICLVYVAILRRLYKHTHLSSVGRRTITDDGGPYMVEEEIPGSYDALYLSEMVMYLVHALPYTQSAFNWLFYAFLNHNLRHSSRCSLGNRSTVTNTADNGHTPSATGSAIPLWRNIQSVGTY... | Pathway: Glycan biosynthesis; glycogen biosynthesis.
Function: Transfers the glycosyl residue from UDP-Glc to the non-reducing end of alpha-1,4-glucan.
EC: 2.4.1.11
Catalytic Activity: [(1->4)-alpha-D-glucosyl](n) + UDP-alpha-D-glucose = [(1->4)-alpha-D-glucosyl](n+1) + H(+) + UDP
Sequence Length: 788
Sequence Mass (Da... |
A0A914F570 | MNMYKTDYDGTEFHIPNRYVALDYQGTVGNGIIISASDSKTQQPVATKKFTRPFADSVLARRTYREFVILNLINHRNVVKLLNTYTPQNNVNVFCDVYHVMEGNLRAIELQNHLHKPLSYLMYQILCGINHLHKSGIIHRNLTPDSLGFTSDAVVKIRDFGMACPENCSRLTAYVSQRYYRAPEIILGIGYKANADVWALGCIFVELLTRKILFPGKTCIDQWIQIISFVGTPNSAFPQRLENSVKEYIKSLQYFPTQSWEKVLPDSLFTPEKSDVPELEKAVLFRDLISRMLIIDPIQRISIQEALDHPYVKMWYDSSQ... | Function: Responds to activation by environmental stress and pro-inflammatory cytokines by phosphorylating a number of transcription factors, and thus regulates transcriptional activity.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
EC: 2.7.11.24
Subcellular Location: Cytoplasm
... |
R7MMP6 | MKIGIFGGSFNPIHKGHMHLAESVMEDIKLDKIIFVPSKISPHKSSDEYISENDRLEMVRLSIMNNRNFEVSDYELTQERVSYSVYTVRHFKEKYPDDELYLLVGTDMLLCFEKWYKFEEIMKLAAIVAVARENGEIDALNKKSKELSRYGKVIICKAEPFSVSSTEIRKKIVNNENWYCYLEKNVVQYIRLGGFYTIAPKTNS | Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; deamido-NAD(+) from nicotinate D-ribonucleotide: step 1/1.
Function: Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
EC: 2.7.7.18
Catalytic Activity: ATP + H(+) + nicotinate beta-D-ribonucleotide... |
A0A1F5E7W8 | MNQKKLFKTIKEKNCLCLDIGIGVDIENIERFKKIDRSKDRLFLKKIFTKIELEYCYSKKNSAPYLAARFAAKEAVVKSLTSLNQQSMPYNQIEVYNNEKGLPFVRLLNKKLSRLKIKISLSHCKDKALAFAIII | Function: Transfers the 4'-phosphopantetheine moiety from coenzyme A to a Ser of acyl-carrier-protein.
Catalytic Activity: apo-[ACP] + CoA = adenosine 3',5'-bisphosphate + H(+) + holo-[ACP]
EC: 2.7.8.7
Subcellular Location: Cytoplasm
Sequence Length: 135
Sequence Mass (Da): 15661
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A0A3L8B2G0 | MTVLHRFFNSIWYQPNALAWLFWPLACVFGCLVQHRRRQYLGGKKAAFHPAVPVIVVGNISVGGTGKTPVSIWLLEELKRRGLRPGLVSRGYGGKAPSYPYLVSETDEASVTGDEPLMIHLRTGVPVVVDPDRSSAVRYLLRECDVDVIISDDGLQHYPLARTVELAIVDGSRGFGNGKLMPMGPLREPVARLQTVDAIVVNGGLDHTLGQNLQIPADKCFDMTLQPDAWRPLHTRAGDDAQPWRGDECHLPVHALAGIGHPQRFFQTLDQLQIPHQPHPFPDHHDYTELDVEAFESGWVLTTEKDAVKLRKFAQLKGAY... | Pathway: Glycolipid biosynthesis; lipid IV(A) biosynthesis; lipid IV(A) from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and UDP-N-acetyl-alpha-D-glucosamine: step 6/6.
Function: Transfers the gamma-phosphate of ATP to the 4'-position of a tetraacyldisaccharide 1-phosphate intermediate (termed DS-1-P) to form te... |
W9GVY7 | MDKIRIRGGRPLRGTLTVGGAKNAALPLMTASLLTDETLTLAQLPHLADITTLANLLSQHGVAFGMDGSAPQDGAAGRVVDLTAKEITSTTAPYDLVRKMRASVLVLGALVARCGVAKVSLPGGCAIGARPVDLHIKGLVQMGAEIELEGGYILAAAPGGLRGAQIVFPTVSVGATENLLMAATLAKGETVLVNAAREPEVTDLARCLIAMGAEIEGLGTDTLRIQGKDRLHGAYHTIVPDRIETGTYAMAAAITGGDLELINGRLEHLQSVTKVLSGAGIAFSPTERGFRVSRANGALTGVDVMTEPFPGFPTDLQAQM... | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine.
Catalytic Activity: phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine
EC: 2.5.1.7
Subcellular Location: Cytoplas... |
A0A7V6H5F2 | MNFSISPEYMRAWEQHAFSKGVSSLYLMEKAARASLEAIKSIISYPLADKCILVVCGSGNNGGDGIALARMLADEGVETHVYILKEPHTYDAKYNLEKLKYTNAKILEKAEFVNYDLIVDAIFGTGLRGGVKGEAANIIHGINSSGVKVLSLDIPSGIDVNTGYAEGAFIRAKYTISFQKAKHGLFFSKEGAAGEIIVADIDLPSIYMPPITNLQDRAAIMHQEDFLSLIPKRNPYSYKGDFGRVLLYVGSFGMAGAASMAALACIKSGAGLVYVLCEDKVAEIMQNSVPNAMCVHEKPENISLFALGCGIEENASTWET... | Cofactor: Binds 1 potassium ion per subunit.
Function: Bifunctional enzyme that catalyzes the epimerization of the S- and R-forms of NAD(P)HX and the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. This allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that... |
U5SFA3 | MKIVIINGPNLNFLGTREPEIYGTQTLEEIESKIQKYAETQEVDCSFFQSNSEGELIDRIQQAHMDKADGIVLNPAAYTHYSYAIHDAVKSIMIPTVEVHLSAIHARESFRKESVIASACIGQISGFGPTGYLLAIHALKEVIK | Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7.
Function: Catalyzes a trans-dehydration via an enolate intermediate.
EC: 4.2.1.10
Catalytic Activity: 3-dehydroquinate = 3-dehydroshikimate + H2O
Sequence Length: 144
Sequenc... |
A0A2W4Y5M2 | MGDAIRCAIAAAGTEALSPALALEHVSDPAFGGQALFVGRVRNHSDGRPSTAVHYDLFEPLALAQFQRIAQDVIDRHGPGLRVSIVHAKGLLQIGDIAVVVAAGSAHRDTAFRACRELIEAVKHQAPIWKQEHYADGEAEWRAGASLRNDDHG | Pathway: Cofactor biosynthesis; molybdopterin biosynthesis.
EC: 2.8.1.12
Catalytic Activity: 2 [molybdopterin-synthase sulfur-carrier protein]-C-terminal Gly-NH-CH2-C(O)SH + cyclic pyranopterin phosphate + H2O = 2 [molybdopterin-synthase sulfur-carrier protein]-C-terminal Gly-Gly + 4 H(+) + molybdopterin
Sequence Lengt... |
A0A1B6M546 | FDHHCPWVGNCVGKRNYRYFYMFIVSLAFLCVFILGCSLTHLILLTKEDRLFFDAVKESPSSVIVVVVCFFSVWSVLGLAGFHTYLTTSNQTTNEDIKGAFASKRGQASFNPYSNGNVCSNCCHVLCAPSPPSLIDRRGLVTTEFLGEADTRQGAVIVNSRTYGSLPQVIQNGVTVGEGSPDANSPVTPPTTPPAPANLPAVCSVVAPSINGSDSSGEVPGIYESVVGECGVGVDSPKVDLSELDLYLDDVVVSVGLEPDTTSLVPLSASRLRLLQDTTMIESALDLDSLEESTSSVGAGSQAGLIKKKDTFGVHH | Catalytic Activity: hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein]
EC: 2.3.1.225
Subcellular Location: Membrane
Sequence Length: 316
Domain: The DHHC domain is required for palmitoyltransferase activity.
Sequence Mass (Da): 33585
Location Topology: Multi-pass membrane protein
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A0A2A4HRY2 | MARGDLLLTVLAPRLTADIHAQVAALVAQFGLQEVSMQQLADATASHGQGIDCTEQRLSMGSGSADLDALRHAALSLGETLDVDIVIQQDERDAVSPRLVCFDMDSTLIKAEVIDELARRHGVGDEVAEITEQAMRGELDFKQSFRARMSKLEGLDESVLAEIAAELPLMDGVERLMKNLKHLGFRTAILSGGFTYFAHYLQDRLGFDEVHANELIIEGGKVTGGVLEPIVDAERKADLLEHIAQREGFTLAQTVAVGDGANDLKMLAKAGLGVAFRAKPLVRAQARQALSTAGLDGVLYLMGYGAADLID | Pathway: Amino-acid biosynthesis; L-serine biosynthesis; L-serine from 3-phospho-D-glycerate: step 3/3.
EC: 3.1.3.3
Catalytic Activity: H2O + O-phospho-D-serine = D-serine + phosphate
Sequence Length: 311
Sequence Mass (Da): 33435
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A0A3S3Q8P6 | RSLIEAGARVNTRDSQGMTALHYATIANNRTAVQLLLNEGNASPQVRNNSGWVALHFAAHFGFDEIIVQLLKYGCALNPRTATDETPFDLALRQKHAKCVRLLESFENRALINCPLKHEWFHEYLIDRKSSEQLLQNQGLKDGLFLIRYSKQKQHVLVLVHNERVYHFLIQRKRQFYSINDGPYFKTLNELVSYYHRFADGLPATLQIPALRSLNSAELACQQQQMRWISAEDVQIGLLIGYGKYGRVHHGVWRKKAFLTIEIAVKVLHDSDNHDCRRANEEDVLLREMQALRTLRNPHIVKIYGFCKGSPLMILEEMMP... | Catalytic Activity: ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]
EC: 2.7.10.2
Subcellular Location: Cell membrane
Sequence Length: 513
Sequence Mass (Da): 59375
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I7GYI7 | MKSHLPLLIEILTEELPALPLLKELPHIIQKWQSIAKKHNVSSTPTLYYTPRRLVLYEEGFLAHTPDSLIESYGPPLSIAYIDGDKTKGLSKAGESFYKKNNLPLEQELETRIKDNKEVLYYAITQKGVETSSLLESMVVEWLHSLQFGKSMFWGDVEQGFIRPVRNILILLGEQSICVNAFNRHFGKQAQIFVHRDVSFEPFKITSIEQYFDTLQKNFVILSQDKRKELILSQIAELESAHKIQVEIDTDLLNEIVAITEYPQAAYGSFDSSFLALPSEVIITSMKENQRYFATYKDSVLHNGFVLVSNSTAKDLSPIV... | Catalytic Activity: ATP + glycine + tRNA(Gly) = AMP + diphosphate + glycyl-tRNA(Gly)
EC: 6.1.1.14
Subcellular Location: Cytoplasm
Sequence Length: 696
Sequence Mass (Da): 78927
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A0A7C4RQL4 | MSGIFRLHNPVKTYAWGSETAIPELIGIPAVPGRPVAEWWIGAHPLGPSEVERDGVRTPLDRWIAENPEERLGHRVCSRFGGNFPFLLKVLAAAHPLSIQVHPDREEAAAGFLRENEAGIPLDDPRRTFKDPNPKPECVCALTPFWVMCGFQPIEAIQSHFEPFAAFLGDDGLPQLHRSDPHLRLRDFLKRLLEMDPDRKNRLLQAVCEWLEGHSAPDVITEWVPRLMRAYPEDIGTLAPFFMNVRCLQPGEALYLPPKTLHAYLEGMAIEIMVNSDNVVRGGLTPKHIDIPTLLDIVRFSSQSLEVLKESPLGTFEQVY... | Cofactor: Binds 1 zinc ion per subunit.
EC: 5.3.1.8
Catalytic Activity: D-mannose 6-phosphate = D-fructose 6-phosphate
Sequence Length: 402
Sequence Mass (Da): 44833
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A0A971YAP6 | MILRHLLRHVTTLFARPETHIRTRYAHFKNLLRADGKALDLIADLESHLYGHDPADLERSIWMIDMLHQEVRTMVSCLHSMNPDAYPDLFPALERIAGKSSAEHLQSPLPDTPPYIIDLDQAADLPRQAGGKAANLSRVKQLGAPTPPGFVITASAFARVIRDNGLDEEIRHRFRQVRLSAPDEIIRITGEIQELILDAQIPADLAEQIVAATHALAPHGQLLAVRSSALAEDGEISFAGQYASELDVQPDAILSAYKRVLAGKYCPRALSYRVRHGLSDTDTAMAVLVLPMVQARWAGVVYTSDPACPAVGGEAMGVYV... | Pathway: Carbohydrate biosynthesis; gluconeogenesis.
Function: Catalyzes the phosphorylation of pyruvate to phosphoenolpyruvate.
EC: 2.7.9.2
Catalytic Activity: ATP + H2O + pyruvate = AMP + 2 H(+) + phosphate + phosphoenolpyruvate
Sequence Length: 623
Sequence Mass (Da): 67511
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R7MQ87 | MLKNEISYIAQGKSLSREMTENAFDKIMSGAVNDIQISAFLTALSIKGETIDEITAAATILRKYCLQLPHKSEVLDIVGTGGDKSDSFNISTTSAFVLSAAGIDVAKHGNRAASSKCGAADLIEALGAKLDISAEKSGEILDKTGVCFLFAQKYHSAMKYVGKVRKEIGIKTIFNLVGPLSNPAFPKYQLMGVYSEELLKPLAHSLANIGVKNLMTAYGRDGLDEISLCGETAVYEIIDGKESEYIITPEKLGFDRCSKNDLTGGSPQENAEITLSILNGEKGHKRNAVVLNCIYAYHLVHPEMELLDIKEIIENSIDSG... | Cofactor: Binds 2 magnesium ions per monomer.
Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 2/5.
Function: Catalyzes the transfer of the phosphoribosyl group of 5-phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'-phosphoribosyl)-anthranilate (PRA).
... |
A0A0M8K9D9 | MMNHSTPSRTTHLLRLLPPGVRDIFGDEAARLTLVHRAAEETFWRWGYAPVVLPTFEYYDVLARGFDEQASGKMHRFIDAQGNLLALRPDLTVPVARLVASRLVQEPPPVRLAYVAPVFRYVEPRAGQQREFREIWQAGVECVGVNNADADAEIIALHVATLQAMGVPRFQLNLGHMGFVHGVFDALDKQPPNLAAIRRAIDRKNRHILAEELDRAGVRGAARAALEALPTLWGQGDVLERAAALAPTPRARSAIERLQQIVARLEAYGVRDFVTIDLGEVRGMHYYTGITFETFAPHSGYPIAGGGRYDNLLALYGYDA... | Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/9.
Function: Required for the first step of histidine biosynthesis. May allow the feedback regulation of ATP phosphoribosyltransferase activity by histidine.
Subcellular Location: Cytoplasm
Sequen... |
A0A1B3XLN4 | MNHVLSVFIGGFFGSATRYVLQMIFNRLLPSGSIPFSILLINLVGSFGLGIAFPQKEAWDSSVQVFLTIGFLGAFTTFSTFSMETIELIRKYRYIDSLIYITVSILGCIGAFLSGYLIYV | Function: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Subcellular Location: Cell membrane
Sequence Length: 120
Sequence Mass (Da): 13315
Location Topology: Multi-pass membrane protein
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A0A0M8K9I7 | MIGWQKGDVLMKTIQLAIQGMTCDACARHVRDALSAVPGVAHVEVPGWESQQAIVQADEGVSPERLATAVEQAGYRAEVAAVASPAVASDEPDTTYDLLVIGGGSAGFAAAIKAAEAGARVALIERGLIGGTCVNVGCVPSKTLIRMVEAWHAADAARRFDGVQLAQGHLAWHRLIQQKDALVAELRQAKYVDVLAAYPTITLIRGRARFVDETTLAVDERLYRAEHVIIATGAHPWAPPIPGLAEAGYWTSTDALATKEQPRSLIVIGGSAVGLELAQVYARAGTFVTVLEALPRIVPQEEPEIGEALETYLEAEGMRI... | Cofactor: Binds 1 FAD per subunit.
Function: Resistance to Hg(2+) in bacteria appears to be governed by a specialized system which includes mercuric reductase. MerA protein is responsible for volatilizing mercury as Hg(0).
EC: 1.16.1.1
Catalytic Activity: (R)-N(6)-dihydrolipoyl-L-lysyl-[protein] + NAD(+) = (R)-N(6)-lip... |
A0A2D3RA35 | MKIRYLGIEYYSKTFEKMKKFTSLRNKNSEDELWLLEHYPIYTQGQNGNPKNILNVNKNIPIFQSDRGGQITYHGPGQLIGYILIDLKRKKMGIKKLIDSIHISLINLLTYYSIPASTKNKKPGVFVKNKKIASIGLRIKNNCTYHGFSLNVSMNLNPFKNINPCGFKKLEMTQISNYVTDISMNTVINIFVNNFTNQIKIYENNSSIKSYNHTKNMDL | Pathway: Protein modification; protein lipoylation via endogenous pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-protein]: step 1/2.
Function: Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate-dependent enzymes. Lipoyl-A... |
A0A2G9YIJ1 | MREMFRFGFILGIICIVAGGLLAGVNSLTKPRIFAQAQAEERLGLKEVLPDADRFEAVEEKEEIIYYKGHNKDGKFIGAAFKAVGKGYSSTIETLVGMLKDGTIVAIKVLSQNETPGLGARVAEPEFTAQFNNIRDLSKVQAITGATISSRAVIELVKKRAEEIRGLIKNEK | Function: Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane.
EC: 7.-.-.-
Subcellular Location: Cell membrane
Sequence Length: 172
Sequence Mass (Da): 18800
Location Topology: Single-pass membrane protein
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A0A914JM93 | MMRKRDGKSEQLETELEPEKPPKLTKISTEVGVKTFLLALKLRIVAHLFLYDYLNRSPEFTTPWNSFKRLQEAVFVVDEFKINAYQGDNFHLMPILLKLFGPLTHFPFVYHGAVIVLDIFAGFLLQNLAKKYLNQKEVEKKIENVEIYSDLACLIYLFNPMTIGASAVGSISTLLNFLVVLFLRCLIFQNIYMAASLMVVLVFIYPYYIVLMAPLLLAANSNKLITLSIIFATTGSLFAVNCLVENAIHWIPDTFYFFWSIKDLSPNVGLFWYLFVFVFDQYRQFFLWTFQLTSVFPVIPLALTVKKDAILLTFGCLAHV... | Pathway: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor biosynthesis.
Function: Component of the GPI transamidase complex. May be involved in the recognition of either the GPI attachment signal or the lipid portion of GPI.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 445
Sequence ... |
A0A443R453 | MEALKPFGDVPKKLTIEVKRSFVATRTFVRALFEGRDIVKKLMEILPTNDCGDEFMRMTYCAHCKGLTNLKPCLGYCLNVFKSCLFKQSQVNKEWSNYVDALLLLITRLETSFNIESVVDPIDIKISEAIMNFQENGVAVSQKLFDSCGKPRIGKRSATNSKASLNKYDFNYATFESRPVAALGTKFDRLLQDVKRKIKRTKDFWLKLPESMCSHSHLVGANIKHGSLNCWNGTDISQSDSLKSGHKSESRLGKHATNVVINQQLLSLRIISSKLNYAYNGLEVDNFDE | Function: Cell surface proteoglycan.
Subcellular Location: Cell membrane
Sequence Length: 289
Sequence Mass (Da): 32693
Location Topology: Lipid-anchor
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A0A914K3P8 | XTDQGWGCMLRCGQMLLSQALWILKLGRTWEWEKNSKNVDYRRLLRMFQDKRTSLYSIHQISQMGVSEGKALGEWFGPNTIAQVLKKLVIYDDWARIAIHVAMDNILISSDVKAMARAKPPCKDLNIGEKTKLENDSTKTEGEDSFWRPLLIIIPLRLGLTTINRCYLPAIEEYFKLPQCIGIIGGRPNHAVYFYGIAKDKLLYLDPHVCQESVSLETNQLEVINSEQQSGISSYQSNASMEMVDNPANSVRSNTKQQSGISSYQSNASMEMVDNPANSVRSNTSSPETTKEDDCDNNQVETEEVTDSSFHLGSPISETN... | Function: Cysteine protease that plays a key role in autophagy by mediating both proteolytic activation and delipidation of ATG8 family proteins.
Catalytic Activity: [protein]-C-terminal L-amino acid-glycyl-phosphatidylethanolamide + H2O = [protein]-C-terminal L-amino acid-glycine + a 1,2-diacyl-sn-glycero-3-phosphoeth... |
A0A919Z3S8 | MKKIVVSGKTVDDAIEQGLGQWEVAEDRVKVTVLEQPSRGLFGWIGAKDAKVELELIPDPLEEALLFLKDVFRTMNVQMDVDVQSGKDLTTFNLSGEELGILIGRRGQTLDALQYLVNIVANRYSNTHVKIVLDAEDFRNRRRKTLEDLAMRLASRVMRSKKEVILEPMSSLERKIIHSRLQDHPSVKTYSKGEEPNRRVVIALK | Function: A probable RNA chaperone. Forms a complex with KhpA which binds to cellular RNA and controls its expression. Plays a role in peptidoglycan (PG) homeostasis and cell length regulation.
Subcellular Location: Cytoplasm
Sequence Length: 205
Domain: Has an N-terminal Jag-N domain and 2 RNA-binding domains (KH and ... |
A0A919Z4M8 | MKARKIYPTLMWNYFMIILITSLVVIISFIYIGYSIYQSIKASTLPLVNAEDLVQSDYQNLSIGELVELGAWVEIVNAEYELVYVIGEKQDSYERYTTAELLLLLSYSPERDVYTSAVSFVADDGEPYSMLLKIPKEAVSGSIDLMRNSDQTFGEVAVHLLLSFLAIPVLLLLIVFIYTFWTAKRISRPLQTIAKGLSRMVRGDYGTRIQLKAVPKSEIGQIRDAFNVLSDRLEASERETKRLEESKQRMLIDLSHDLKTPMTTIQGYAKTLSDPIEIDDEKKKRYLKIIYNKSVRMTALIDSMFDLLKLDAPDFHLSLQ... | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Membrane
Sequence Length: 469
Sequence Mass (Da): 53403
Location Topology: Multi-pass membrane protein
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U4E199 | MGKVYSFSAGPAMLPSEVLLRAQSELLDWQQTGMSVMEFSHQSDEFAIIREETEARLRALMSIPDDYHVLFSHGGGSGQFSAVPLNLIDQRESASKQRADFLVYGHWASGAYEEAKKFCLPRKLDVTCIREGRHAISPEQDWQIDPSAQFVFVCPNETVNGMEYHALPETIVPIVADMSSSILSRPIDVSRYGVIYAGTQKNIGPSGLAITIIRKDLIRADRHNIPKILDYRRQIEQLSMANTPPTFTWYLCGEVLKWVEQQGGVSALFARNQAKASALYRCIDESDLYINDIHPDYRSIMNVTFRIACPETEQRFLDRA... | Cofactor: Binds 1 pyridoxal phosphate per subunit.
Pathway: Amino-acid biosynthesis; L-serine biosynthesis; L-serine from 3-phospho-D-glycerate: step 2/3.
Function: Catalyzes the reversible conversion of 3-phosphohydroxypyruvate to phosphoserine and of 3-hydroxy-2-oxo-4-phosphonooxybutanoate to phosphohydroxythreonine.... |
A0A0Q0XAB2 | MTGAIGGSILASPFRLGFDVQRLLGFPSCLPSYVYFLDYRKPIRAPKRGDYAVFSYPATNLGVGAREGQRAVKIVAALPGELVEIAGTELYMRGVPWAYDRLWLAKSISGKTVGDFDAKYKVPEGTWFAYGTEKESLDSRYFGPVEQSRIVGYAKPLF | Catalytic Activity: Cleavage of hydrophobic, N-terminal signal or leader sequences from secreted and periplasmic proteins.
EC: 3.4.21.89
Subcellular Location: Membrane
Sequence Length: 158
Sequence Mass (Da): 17475
Location Topology: Single-pass type II membrane protein
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A0A068TTI4 | MVCLVYLLFMPFLECPGYYLKVLPLEFKDHHCVWLNNCVGHVNYKTFFCLRCLRRCFMHILPGMSIYLFQFSKRFLFFYSMLPSGHFRAPAGAIDSCADHLYYHEGVRAMWLAEKEGYLYSHPYDLGAYENMISVLGPNIFCWVCPTSEQIGSGLRFRAGVDKLLGISFFRPM | Catalytic Activity: hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein]
EC: 2.3.1.225
Subcellular Location: Membrane
Sequence Length: 173
Domain: The DHHC domain is required for palmitoyltransferase activity.
Sequence Mass (Da): 20176
Location Topology: Multi-pass membrane protein
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A0A101FL83 | MTGGELLRLLARHPSLELAATVSRSQAGKPIWHQHPVLRPDYPDMTFSNPEDALKEEVDLAFLALPHGTSCPIIEEYRKKGVPVVDLSADVRLRDEGAYKRWYGRAHPSPELLKEAVYGLPELHREELKGATLASGVGCNATCAILGLFPLTREGQIEHLHLEVRVGSSEGGASPTQGSHHPYRSRAMRVIDPFRHRHLAEILQELKLPEESVAMTTTAVEMVRGVQMMAYVTLKDRVSEAELWKLYRKAFRNEPFLHLCPAQPAHLRFPDPRYVLGSNRALIGFALHDDGRRLLVASAIDNLMKGASGTALQAANVMLG... | Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 3/4.
Function: Catalyzes the NADPH-dependent reduction of N-acetyl-5-glutamyl phosphate to yield N-acetyl-L-glutamate 5-semialdehyde.
Catalytic Activity: N-acetyl-L-glutamate 5-semialdehyde + NADP(+) + phosphate = ... |
A0A0K6I3U7 | MRWVTILLVSLLVLLQWPLWFGERGWFAVQRLENQLSQQNQANALAQQSNDRLAAEVHDLKEGLGGVQDQARREMGMVKPDEIFVQIVPPKGAAPAMPSTAAASSPTGTSASAHQ | Function: Essential cell division protein. May link together the upstream cell division proteins, which are predominantly cytoplasmic, with the downstream cell division proteins, which are predominantly periplasmic.
Subcellular Location: Cell inner membrane
Sequence Length: 115
Sequence Mass (Da): 12560
Location Topolo... |
A0A2D3R8C1 | MKILISNDDGIYSPGIKFLKKEMSLIAETIVIAPDRNCSGYSNALTLTKPLKINKLKNNYYSVTGTPVDCVHLGLTGLINKKFDIVISGINDQPNLGDDILYSGTIAAAMEGRYLKLPAISLSISKNKNDNIYYYNVAAIIARQLVTNLYKNIFPPKTILNINVPNIPLNKIKGIKISRLGTRHYPKSLIKDYDPRGNKIYWIGLPGLKSDTGPGTDFYAIKNNYISITPINTNLTNYRIFNELKIWINSIHIEYDIIKN | Cofactor: Binds 1 divalent metal cation per subunit.
Function: Nucleotidase that shows phosphatase activity on nucleoside 5'-monophosphates.
EC: 3.1.3.5
Catalytic Activity: a ribonucleoside 5'-phosphate + H2O = a ribonucleoside + phosphate
Subcellular Location: Cytoplasm
Sequence Length: 260
Sequence Mass (Da): 29184
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A0A2D3R8C9 | MNLHEYQSKQLFVSFGLKVPIGKVVFNVDEALLFISKYNHILEWVIKAQIHSGERGKNGGVKFTSNNKMDIVNTINSLLHKKLSIGKESHSIFPVEKILLEEKIGEINKEFYLGITVDNFKQKIILMVSDFGGMDIEESIKKDSGKIFKFCIDPFLRIMPFQLRSIAFKLGLKDELLKNFVFLIEKVSEMFFKYDLSLLEINPLVLTNNNEYICLDGKIRVDDNALYRQSYLKGMRDIKQEDYKESWASKWNLNYISLNGNIGCMVNGAGLAMATMDMIKFYGGVPANFLDVGGSVTRDQVVEACKIIFSDKRIKGVLIN... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Pathway: Carbohydrate metabolism; tricarboxylic acid cycle; succinate from succinyl-CoA (ligase route): step 1/1.
Function: Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of either ATP or GTP and thus r... |
A0A2D3R8C0 | MATWIKMQELYKKILETIGEDVKRDGLKKTPERAAKTFRYLTNGYKKDLNKITNNSIFQSDIKDLILIKKIKIYSICEHHLLPFLGYCHIGYIPNGKILGISKIVEIIECYSRRLQIQERLTTEIANYISYILQAKGVGVMIEAKHLCIEMREFKKQNPYITTLSMTDEIKNKPYKRNEFLTLIK | Pathway: Cofactor biosynthesis; 7,8-dihydroneopterin triphosphate biosynthesis; 7,8-dihydroneopterin triphosphate from GTP: step 1/1.
EC: 3.5.4.16
Catalytic Activity: GTP + H2O = 7,8-dihydroneopterin 3'-triphosphate + formate + H(+)
Sequence Length: 185
Sequence Mass (Da): 21709
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A0A2A5V8L3 | MKFFENFKFTNLLSKKKIDENLLDKFEELLIESDVGPVMAAQLKDEFKKEKIGKEIKDEKEIFNFLGNQISKILQPYEKSLKKIQKNSPTVVVVAGVNGVGKTTTIGKLGRLYKDEGKKIVFGAADTFRAAAIEQLEVWSKKINVDFIKSDLGSDSASVAYKTVKFAEEKKLDLALIDTAGRLQNKKNLMDEYKKIFKVLQKINSDYPHETILVLDATTGQNAINQVSEFKKASNITSLIITKLDSEARAGIILSICKKFNLPIIAVGVGEKESDLRPFNAKEFTKLMLEN | Function: Involved in targeting and insertion of nascent membrane proteins into the cytoplasmic membrane. Acts as a receptor for the complex formed by the signal recognition particle (SRP) and the ribosome-nascent chain (RNC). Interaction with SRP-RNC leads to the transfer of the RNC complex to the Sec translocase for ... |
A0A2M7UTD0 | MLQTVTTEQMREIDRLMTEEFGVSLLQTSTIAGLHVAKVTRDYMSGVARDKKVVICAGKGHNGSVGLVVARNLVNWGAKVSVYITSPKEELGPESQQHWYALEKAGVLPLIVTDEVAIETRDADCIVDALLGYGMEGNPRGTVAHIIDHINRSAKKIISIDLPSGLDSTTGVIYAPCVVAKATVALGLPKAGLAKPESKQVMGELFVADIGIPQTLYQKMNIEVGPVFTQDEVLEVKIKVVKVRT | Cofactor: Binds 1 potassium ion per subunit.
Function: Catalyzes the epimerization of the S- and R-forms of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. This is a prerequisite for the S-specific NAD(P)H-hydrate dehydratase to allow the repair of both epimers of NAD(P)HX... |
A0A7D4T1X7 | MSPNNSNVTLQADAKALCFNLQGELLLRQFADGAADVKEESVESLLQQGRITSEQLRQIGVVWVPTSQLVIAQVVLPGSRQSELRAALPYALEEQLSDAVENYHFVILHKQPAQEGTQLQVAVIAKVLMNQWYQALKRLELDNCLLSADCFALPEPETDVSVAMVLPGAPVVIYRDGRYSGFAIPETLSEQLASSSEEVRNLTPQQAQWQKIAFSPSAWQQLQSTNLAVGEFALKESQNLWRQWLWPNLAAGLLFVVLLGSNWLEKEQALQDAQVYRSQSEQLFKAMFPDVKRVVSIKTQTMTRLRAPSQDVTSARLMPL... | Function: Inner membrane component of the type II secretion system required for the energy-dependent secretion of extracellular factors such as proteases and toxins from the periplasm.
Subcellular Location: Cell inner membrane
Sequence Length: 399
Sequence Mass (Da): 44522
Location Topology: Single-pass membrane protei... |
A0A914IXN9 | MVIITTFIALVTACLITFDLNPGILERTETIERVITEYYKDSDEIILVELSELVLEKQYAIALSEAIFISVIYNNILFVSSFLVFFHYLNHVHLLDPKLSYFDCLLASSLFIELLPILKDCMALLIARWRTTLA | Function: TRAP proteins are part of a complex whose function is to bind calcium to the ER membrane and thereby regulate the retention of ER resident proteins.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 134
Sequence Mass (Da): 15408
Location Topology: Multi-pass membrane protein
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A0A914J145 | MLNSILFFIISSIYGLIKILSRLFGVDYIFAVIEAAFEPIQELKQKKNVNVAPSHIAVAVLEKKLLSWFLFRVXXXXHLFDLVQHSANSGVKRITFYDPFDILKENQEKFIGRLKIYLKSRNSNVFPIVNFETPTISNLDGYNFINLTILGSDDGRGSLTRVCKKLCHEKTEILISDIDNKLEEENIFEPDLLVKIGTINSLGGYSPWSLRITEIVSLSRFQNDSNFTMKEFEQILDDFSSRDRRIGK | Pathway: Protein modification; protein glycosylation.
EC: 2.5.1.87
Catalytic Activity: (2E,6E)-farnesyl diphosphate + n isopentenyl diphosphate = di-trans,poly-cis-polyprenyl diphosphate + n diphosphate
Sequence Length: 248
Sequence Mass (Da): 28494
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A0A6A6G066 | MEGGSFFVPSYLRRSRYVERLEGAWRRSQLRERGGGVAGTFGGGREGLSRTGSHSNLNAGVSATKQSRGVVQDVIERLPPLTGDEGLRALPSRWSETDKCYGLEIMGSTSGMEVKYQGTVRTPDDAAAVRSDVPVPREVGVYYFEVTVLSRGKEGLIGIGFSSGKPSLNRLPGWELESWGYHGDDGFSFACSASGKPYGPKFSSLDVVGCGINFRTGTAFFTKNGIFLGEAFHGIKPLDRLYPSVGIKKPGEHLRANFGQSPFVFDIDSLIERERLNVLNEISRVDTSNSVLRPGLDETDTIHELISQYLAHEGFIESAN... | Function: Components of the endosome-vacuole trafficking pathway that regulates nutrient transport. May be involved in processes which determine whether plasma membrane proteins are degraded or routed to the plasma membrane.
Subcellular Location: Endosome membrane
Sequence Length: 599
Sequence Mass (Da): 65423
Location... |
A0A3L8AZ88 | MKTDITGDDLIRCFLAVPLAAQSSALLDSAVTRLKPFYAEGSVRWVAASNRHMTLAFLGDQSPETVLCLQAPLQSALAAVPAFVLESVAVSGFPDAKSRIVALELECTAALKGLLSSVHAVLARQGLAVEKRPYRPHVTLGRLDGRLDGRLGRGGSRRPLFQPVAINMPVSSLVLYRSRLLPSGSEYEPVWEVALI | Function: Hydrolyzes RNA 2',3'-cyclic phosphodiester to an RNA 2'-phosphomonoester.
EC: 3.1.4.58
Catalytic Activity: a 3'-end 2',3'-cyclophospho-ribonucleotide-RNA + H2O = a 3'-end 2'-phospho-ribonucleotide-RNA + H(+)
Sequence Length: 196
Sequence Mass (Da): 21090
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A0A4P2VDP2 | MYRIGVLRLLGYREWTEGLGDDREWIIQVVQSGIYGLVSAEGAAIGAHAMPLRYDYMILLDSGAYPDGLRKISSAASSVAPTPVSISAACAPTPMDAQRIASADPGIYEGCASDPIAAVHMDMDDISSRTQRESAYATFEEVLGIVHAATKEASSLGGLVQYLGGDNLMAFLPRDSLDEFLKFVRGLEGVKAGVGVHRIPREAIALAARDLRSIRASRSRG | Function: Catalyzes the formation of 2-amino-5-formylamino-6-ribofuranosylamino-4(3H)-pyrimidinone ribonucleotide monophosphate and inorganic phosphate from GTP. Also has an independent pyrophosphate phosphohydrolase activity.
EC: 3.5.4.29
Catalytic Activity: GTP + 3 H2O = 2-amino-5-formylamino-6-(5-phospho-D-ribosylam... |
A0A3N4WZJ3 | MNFQQLRQQHPDLPFSEQLRLYSDEEWQKIIHHRFVNELGEGTLANQVLSNYLIQDYTFVDSLTRLVCTAIADAPTMEIRHVLANFLTAITSDENTYFIRSFEALGVSESLYLSPKLNDVSLEFQQALSDGSTKGYAYAITTLFVAEWSYHTWAIRLRGKRPRHFYHKEWIALHDNIEFNAFVDWVRKQVDQFASQSEQEQNALAEQFKRLCRLEYQFFDAAYQ | Pathway: Cofactor biosynthesis; thiamine diphosphate biosynthesis.
Function: Catalyzes an amino-pyrimidine hydrolysis reaction at the C5' of the pyrimidine moiety of thiamine compounds, a reaction that is part of a thiamine salvage pathway. Thus, catalyzes the conversion of 4-amino-5-aminomethyl-2-methylpyrimidine to 4... |
A0A2K3MFR2 | MELPCRYRNLGCLDIFAYHTKLKHEQNCRFRPYNCPYAGSECSMMCDIPTLMTHLKEDHKVDIHDGFTFNHRYVKSNPHEVENATWMLTVFNCFGKHFCLHFEAFLLGTSPVYMAFLRFLGDEKEAKKFRYSLEVGANSRKLIWQGIPRSIRESHRKVRDSQDGLIIQRNLALYFSGGDKQQLKLRVTGRIWKEE | Pathway: Protein modification; protein ubiquitination.
EC: 2.3.2.27
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
Sequence Length: 195
Sequence Mass (Da): 23001
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A0A914F2J3 | MEPSNEESEPMIKKLNNDDAIDRLNYRYTSLFLAFLILFFGFKYYVNAPPIKCWLPDEIEESSKKYVENYCYFENTYFVSGAENEEFPLELLEGERYEQSYYRWIPTLLFFQLGLFLLPKYFWNILSWKTGLSVTRIINRSSYCSAKCGETSEASYAARHIRCVIVFNSRLHSCCGVNSLSFKYFLFKLLNFFNTYIQLLMLIRFLPSSTFGGFGLVRDLMNGNNWKLTGQFPRVTLCDFMFRNETTTLPIHATVKCLLTNNHFNEWLYIILWFWIFALNFLNFINLFYWLFTSAKNEWKIYFIQRQLDFAGKNCSEVEV... | Function: Structural component of the gap junctions.
Subcellular Location: Cell membrane
Sequence Length: 381
Sequence Mass (Da): 44926
Location Topology: Multi-pass membrane protein
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A0A068V0M0 | MTDKKGDTTASSTTSNSKNTPKKANLLDHHSIKHLLDESVTEIVTGKGFIEDVRMSNIRLLMGSVIIIIALFAQFYNKKFPENRNFLIGCIVLYPFRVFNVVVIDRNFILVIVLHFLCHLNLSFYDRDRKLVEKK | Function: Component of the signal peptidase complex (SPC) which catalyzes the cleavage of N-terminal signal sequences from nascent proteins as they are translocated into the lumen of the endoplasmic reticulum. Enhances the enzymatic activity of SPC and facilitates the interactions between different components of the tr... |
G0SFJ9 | MAAPPPSTDATSSSPKPCAKCKSSPSTLESRSKPVCQDCFQKFISNKLIRHITLLGKQIPPYPTRRYALGLSFGVSSSVLLSLLAENVEHNIRQGRKLPFELVVVHVAQSLPGEKAEETEKAVEEILQSYREKYPRFEFIISHITLPSPNGEETSSINFATLSPASREDLLRILTRQALIRAAKEKECRVLLVGHSTTAIAEMTLAEAAKGRGRGVSWLVRDGEAYEEGDEEEEGESQPDGDGTKRTVTKKKLLIHHPLRETLRHELSTYARLFSVHVGDRSFIPIDPSKSQTKQPAVVSHRSLSIEDVMTRYFADVELQ... | Pathway: tRNA modification; 5-methoxycarbonylmethyl-2-thiouridine-tRNA biosynthesis.
Function: Plays a central role in 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of tRNA(Lys), tRNA(Glu) and tRNA(Gln). May act by forming a heterodimer with NCS6 that ligates sulfur from thiocarboxylated URM1 onto the uridine of... |
A0A1B6M721 | MRVSISIVFILLFATTFAHDLDYYFEVVLNITKDAGEIINEKIWQVKNVEIKFSAVDFVTETDREIEEKFKREISAKFPDHKFIGEEETGDGVKMELTDSPTWIIDPIDGTMNFVHGYPYVCISVALLVNKETQMGIIYNPVLNQLFTARKGQGAFYNQKPIRVSTIKELSEAVVSTEVGLSRDEEKLRVVAENIKNFVPLAQGIRSVGTRAMNLALVALGGTEPSSSHA | Pathway: Polyol metabolism; myo-inositol biosynthesis; myo-inositol from D-glucose 6-phosphate: step 2/2.
EC: 3.1.3.25
Catalytic Activity: a myo-inositol phosphate + H2O = myo-inositol + phosphate
Sequence Length: 230
Sequence Mass (Da): 25765
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A0A2K3MDQ6 | MVHHAKLISQQPHIIKINGIHRGLCGSTLLLALILKKLGFRAIPVIIYMSQAKKLESLNAFKSGECNILLCSDGASRGLDIPAVDTVINYEIPLDPNDYMYRVGTAHADVTISFDRETYRQSATSVFCTT | Function: RNA helicase.
EC: 3.6.4.13
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Length: 130
Domain: The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.
Sequence Mass (Da): 14349
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A0A178ZAK5 | MDLKEEFYEAAAAAARLNWATTPDTSCNMFETNIRYLGGLLAAYDLSQEPTLLRKAVELGDMLYAGFDTPNHMPPFWFDFEKAKAGQLAAENHQSSAAVGSFALEFTRLSQITGNPKYYDAIARVTRTFIEHQASTQLPGMWPRLVNARDQTFHDTTFTLGALADSLYEYLPKMHYLLGGLEPAYEKAYRDSMATAIDHLLFRPMLPNNTDILVAGSATVAGGNSSLKPEGQHLSCFAGGMFILGGKLLSLSEHVDIGAKLTRGCIYAYNAFPTGIMPEIFKMRACPSLEACEWDGEQVSELLPEGFESVSDRSYKLRPE... | Pathway: Protein modification; protein glycosylation.
EC: 3.2.1.-
Catalytic Activity: 3 H2O + N(4)-(alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc)-L-asparaginyl-[protein] (N-gl... |
A0A3S3S055 | MFRASLQQALRKPLLLRSNIINGQSSRKQSTDSGNTAKVVLTVGGVSAVTVGGTVLYAKYDDNFRSKLESSIPYSDRVLNSILGPKNESKPIETKQAIKTSTSPQVTDESLLKKKLERNMNTVNKNTSKEPSTSSPTPSDKASPSTSATTKTESSQARKEIETTKKNVELTASLRKEIEKLEKQLKETLTAQQAAISSINEYTQKLSDALELEESSDANIWREVVASNEKREKEVENAVKKFSDTRLQVEKIKSGIENAKREKDTAGSSALGVAEESLIRVLYQLDNSEKEMSKAQAKHEVMEKYRDLFNKSREELENEI... | Function: Component of the MICOS complex, a large protein complex of the mitochondrial inner membrane that plays crucial roles in the maintenance of crista junctions, inner membrane architecture, and formation of contact sites to the outer membrane.
Subcellular Location: Mitochondrion inner membrane
Sequence Length: 69... |
A0A843RNY8 | MCESDRTGERFAQFHMLKTIDRLNDAFGWLAAAAFVAVGAMITYEVVMRYVFLAPTVWAEELSRFLQIWATYIAAAYVLRHRQLIAITLLVNKLGPQGRRVADAFALIWILLFCAVAVFYGLEIMLDSIRQGRASATMLGVPKWMTEAAIPFGFTLLGLQALAELIRLPQNPPPLGGDRGEF | Function: Part of the tripartite ATP-independent periplasmic (TRAP) transport system.
Subcellular Location: Cell inner membrane
Sequence Length: 182
Sequence Mass (Da): 20325
Location Topology: Multi-pass membrane protein
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R6EIQ7 | MKILVTGYNGQLGFDVIKELNSRSIECKGVDRDDFDITDREETVGYICGYAPDAVIHCAAYTAVDRAEDDXGGGQSKGRRKKMPQGEC | Pathway: Carbohydrate biosynthesis; dTDP-L-rhamnose biosynthesis.
Function: Catalyzes the reduction of dTDP-6-deoxy-L-lyxo-4-hexulose to yield dTDP-L-rhamnose.
EC: 1.1.1.133
Catalytic Activity: dTDP-beta-L-rhamnose + NADP(+) = dTDP-4-dehydro-beta-L-rhamnose + H(+) + NADPH
Sequence Length: 88
Sequence Mass (Da): 9660
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T1YZC2 | LSANMAHSGSSVDLVIFSLHLAGVSSILGAINFMTTTINMRSYEMNMMRIPLFVWGVFITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGG | Pathway: Energy metabolism; oxidative phosphorylation.
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytoc... |
A0A2V3JHT4 | MIELAGISFSYPERPVLMDINLCIGRGEYLGITGDNGSGKTTLVKLLNGLLLPQEGQVTVDGASTSDRESLLAIRRSVGIVFQNPDAQAVGETVEEDIVFGLENIRVPGREIDRRIDSYLGMLGIPELRDRNASLLSGGQKQLVNIAAVMAMEPACIVFDEALSMLDASNRRNVLMRISELTRRGTSIIQITHNPEDLGSCHRVIAISDGRISGTVGFSSEIAMPSDSNVSVDGRAATAECANETNEGKKGKSAVVNWMHNTATDVDDINRRYNPIDFTACMRSIRPQRIKGKRCGEFIDHRTGPVSGVSREGDGIEIRH... | Function: Probably part of an ABC transporter complex. Responsible for energy coupling to the transport system.
Subcellular Location: Cell membrane
Sequence Length: 544
Sequence Mass (Da): 58681
Location Topology: Peripheral membrane protein
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A0A344VAX2 | TLYFIFGAWAGMVGTSLSIMIRAELGHPGALIGDDQIYNVIVTXHAFIMIFFMVMPIMMGGFGNWLVPLMLGAPDMAFPRMNNMSFWMLPPSLTLLLASSMVENGAGTGWTVYPPLSSSIAHSGASVDLAIFSLHLAGISSILGAVNFITTIINMRSSGITFDRMPLFVWSVGITALLLLLSLPVLAGAITMLLTDRN | Pathway: Energy metabolism; oxidative phosphorylation.
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytoc... |
I0ICG3 | MSKAGEAVVLRCPAKLNLFLHVGPPAEAGGRHPVLSAMAAIDLVDDLEAERRDGAGLSLARTWAASAAAPTPLDWPAERDLAWRAAEAFAAEAGTRPDVRLTLSKRIPCGGGLGGGSADAAGVLAAMDRLWPGAVEEAALTGLAAGLGSDVPFALAAIRGRPLALVGGFGEAVQPLPRPPGAGLHAALVFPAFGCPTGSVFAAFDAAPPAGRSDPGKARAAAEAGWRALAALGNALAEPACAVRPALRRVLEALAGAGLDARITGSGSTVFVLAEDAAQAADAARRAGAATGLPAVAVSGWPR | Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 3/6.
Function: Catalyzes the phosphorylation of the position 2 hydroxy group of 4-diphosphocytidyl-2C-methyl-D-erythritol.
EC: 2.7.1.148
Catalytic Activity: 4-CDP-2-C... |
G3GLN7 | DMALPRMNNMSFWLLPPSFMLLIVSSLVESGVGTGWTVYPPLSGTSAHSGSAVDLAIFSLHLAGASSILGAINFISTITNMRSAGMSMDQAPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPSGGGDPIL | Pathway: Energy metabolism; oxidative phosphorylation.
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytoc... |
R6DN01 | MNTKVKSLRMITVTAIMSALSAVLMFVEFSIPIMPSFIKLDISDLPALITSYAFGPVCGVAVCLVKNLIHLLATQTAGVGELSNFIHGVVFVFVAGMFYKYHHNRKFAFIGAMAGDFAMAAMSFFINYFFVYPIYFKLMAPEAAILGAYQEILPSVDSLWKAILFFNVPFTFAKGLISVAITFAIYPKISPILKGKK | Function: Probably a riboflavin-binding protein that interacts with the energy-coupling factor (ECF) ABC-transporter complex.
Subcellular Location: Cell membrane
Sequence Length: 197
Sequence Mass (Da): 21723
Location Topology: Multi-pass membrane protein
|
A0A2K3LSQ8 | MSNWPEQPVNVIIKWLKKQNPSFVVADFGCGEALISKSVKNTVFSLDLVSNDPDVIACDMANALITAYILRNXYNESGLKHGITAYGGNMADIIGGAWYGNNDTKFVMLMPYCIGGTMSEI | Function: Probable methyltransferase required to silence rDNA.
EC: 2.1.1.-
Subcellular Location: Nucleus
Sequence Length: 121
Sequence Mass (Da): 13210
|
I1T0F7 | CRGPLGSIRNLAMEKVANSVLFPCKYASSGCEVTLPHTDKADHEDLCEFRPYSCPCPGASCKWQGSLDAVMPHLLHQHKSITTLQGEDIVFLATDINLPGAVDWVMMQTCFGFHFLYCV | Pathway: Protein modification; protein ubiquitination.
Function: E3 ubiquitin-protein ligase that mediates ubiquitination and subsequent proteasomal degradation of target proteins. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ub... |
A0A3P6TQR9 | MLRLRKLQITLVLAELLILSSNGQISEPFDSHPLTGQSSVYEASPSVPTTNQQGLSNTTTIQNESTTWLGAAVQLPSRNINIRGLNSPTLRSDSPEPYSGPGIIRLYSMRFCPYAERAIIYLARKRLPTEITNINPENVPKWFLKKSPLGRVPALEMNGVTIYESSVIAEYLDEVFPETAILPHHPLLKAKQKILVERMSPLISVMFKTLLPNNSTVQRNVDKSLHNALRNAETLLTDDFYGGKTLGFADIMMWPFLERLQLVTVNPYTEFRYFPGINYSKMGAYMARMQRQPEVL | Function: Exhibits glutathione-dependent thiol transferase activity. Has high dehydroascorbate reductase activity and may contribute to the recycling of ascorbic acid. Participates in the biotransformation of inorganic arsenic and reduces monomethylarsonic acid (MMA).
EC: 1.20.4.2
Catalytic Activity: 2 glutathione + H(... |
A0A7I7Q978 | MAAAFLAATAMLLGFPLVPRALAACPAVEVVFARGTNEPPGVGKVGGAFISSLRQQTQRNVGAYGVNYPANDDFLAATDGANDASAHIQHMADNCPSTKLVLGGYSQGAAVIDIVTAAPLPALGFRDPLPSDAADHVAAVALFGNPSGRAGNLMTALSPDFGGKILNLCNPGDPICSDGSSWQAHLSYVPGLTNKAAHFVAAKI | Function: Catalyzes the hydrolysis of complex carboxylic polyesters found in the cell wall of plants. Degrades cutin, a macromolecule that forms the structure of the plant cuticle.
EC: 3.1.1.-
Subcellular Location: Secreted
Sequence Length: 204
Sequence Mass (Da): 20711
|
A0A267TE94 | MIKPIYVYDQQILEQPCPDVPHNSPILTNLILDLWDTMRNAQGCGLSAPQIGVSYSVFIIDSKSVFQSIGKAFRHKYYEPDDTGITETFINAKLVQTSSEIWTAKEGCLSLPSLVRDVSRPWKIKISYLNQNLEKQECEFTGLTARMILHELDHINGVLLLAHLLPFSQKMLYFKLKSIKNGKVKVTYPTMKKQKLVA | Cofactor: Binds 1 Fe(2+) ion.
Function: Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions.
EC: 3.5.1.88
Catalytic ... |
A0A2K3JU32 | MNMKGALKSKYDVDKNTAIFPASVAFNAGDVKLRASAADFNFTNGVKLTGLSLAVEKPGSFSIDYDVGKKVI | Function: High-conductance voltage-dependent solute channel with a slight selectivity for cations transporting triosephosphates, dicarboxylic acids, ATP, inorganic phosphate (Pi), sugars, and positively or negatively charged amino acids.
Subcellular Location: Membrane
Sequence Length: 72
Sequence Mass (Da): 7644
Locati... |
G0S9I9 | MSACNSTDQHPALSLPPRCCFVTVGATAGFRDLLDEVSTPGFLRALAEQGYGRLDVQCGPDLAHFRARVAALADKDRQGIEVSAFDLVDDITPFLVACRGEEGVRLAGCVISHAGTVLEVQRVGAPLVVVANPTLMDNHQLELAEDLARRKLAVHGRIGHLDEALAKIAQLVNEGMLDRLPPYAPPTLPVLPENRVTFFDWMVLTCYPDELRKQRHLATLNQAAVRIAAPKHKGEEEDIARMQVE | Function: Involved in protein N-glycosylation. Essential for the second step of the dolichol-linked oligosaccharide pathway.
Catalytic Activity: N-acetyl-alpha-D-glucosaminyl-diphosphodolichol + UDP-N-acetyl-alpha-D-glucosamine = H(+) + N,N'-diacetylchitobiosyl diphosphodolichol + UDP
EC: 2.4.1.141
Subcellular Location... |
A7L485 | QFWRWFGANLASGGAAGATSLCLVYPLDFARTRLAADTGKGAAEREFSGLGNCLVKIFKSDGLTGLYRGFGVSVQGIIIYRAAYFGFYDTVRGMLPPKQNLFISWAIAQCVTTVSGIVSYPFDTVRRRMMMQSGRAKGDMMYKGTLDCWAKIYKSEGGGAFFKGALSNVFRGTGGALVLVFYDELKVLIG | Function: Catalyzes the exchange of ADP and ATP across the membrane.
Subcellular Location: Membrane
Sequence Length: 190
Sequence Mass (Da): 20661
Location Topology: Multi-pass membrane protein
|
A0A914G1P4 | XFTYPHEHPNSSKADILATSKTGSGKTLAFLVPILQKAIERRGIQPNKDERLPQTLIFVNSTELAMTLFHVVKELLRGLRLKVVVMAASLNFIEETNFDIGICTNGRFQNHFGHTLTLGDKAVALDLSELEYIVIDEVDKMVSDSKFLSVLEKLKAEPKKPRIFGFSATIDADTTRIVRYSSVFQIKCGQHNVVPPNIKQFYWEVYHNSVSRVFRAGNGKAVVREPVKYSGPVHPFDTLFNALTEAPLLKGKRIMVFVKRTRIADLIAIRLRDYGIPAVSIHKRREDIQDSIDMYNKGLVDVAIVTQYFTRGIDTEVDV | Function: RNA helicase.
EC: 3.6.4.13
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Length: 319
Domain: The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.
Sequence Mass (Da): 36031
|
A0A7G8QBA5 | MNKTFTHKKRANPANAFLKMKWLKHRHTISSGQKFLTGYHLLEQSKWPVYVSLAACSIAMGLVMVMHQKLVVVGFMLVGLGLGALAKSVQSWFEEFNMEKWKRQHSSMTVRGVKVGMALFIMSEAAFFASFFWAFSHACWGSCSMNMVWPPMGFRCISPWKWPMYNCALLIGSGLTVTYAHKAAKWQERSPYVHEERVHKALNITCLLGGFFMLIQGYEYWSMPFSMNDSVYGSCFFMMTGFHGLHVIAGSVWLCCCSQAASNKAYMMRRPHLGVQLGVWYWHFVDVVWLMVWGVVYVNGSVWY | Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, comple... |
I0IEB7 | MSVERVDLGDGAEARDPAVRAVGEAAVPAGGVPRVRVLLLVNAGKEPVLEALRSFEPWLEERAEVVGRFETGDTAGREDELPDADVAMVLGGDGTFLSQARVLVDRGVPMLGINFGKVGFLAEWDIDYVKRHWASIACGGCRVTQRILMDVDVYGPEVPLYDTGAHEPLSTHLAMNDAVINAGPPYRVCEFDLAIEPAEVRQPAVTIAGDGIVVSTPSGSTAYNLSAGGPIVSPGVEAMMITALSPYTLAFRPIVFGADADVWITLTRGNDGTALVIDGQAAAVLEEGSHVHVRRHHPMLTLIQNPELTYWSMLSHKMRW... | 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(+)
EC: 2.7.1.23
Subcellular Loc... |
Q59KM6 | MMSRKASRNPKLYVSALIATSAIALTYKLYSTYLAPTPTPTNKDKKQRELDGSSTDIELKPKFRISKRYSNKSIAITLSSTFLSSNLPLNEILINSENMIFIIPPNLNEDDLPIIETKDTDTDNANTNTNTSFYKDQSNFKLLKCSNFQGYLQILKNLKPDLLLLCSDDLGINFKKLQSDLLNNLKLDFINIDQNIDALIQLESIFD | Function: Involved in peroxisome biogenesis.
Subcellular Location: Membrane
Sequence Length: 207
Sequence Mass (Da): 23452
Location Topology: Single-pass membrane protein
|
A0A7S3R0P0 | AKDTAAAAAASGKSTGGEAMRREGRQLPTGASLVQMLVEQKWVEWDSTHTRFRENPQPPSTPPYRQTAAVLLKDKVQGRTSIEIQLHAGNTDTCSYLGRHPEVAAHHRLLWVKSFEGTERVAEQLIMNGLVLGGRQFNILYFKFDKKASTLVFFATKDSRGSSTNPAQTHALPPMSVEAAVAKLGAVQHLWQQPGKMMERMGLFSSSTLPFPLPAAYIYYVDDIAASGVDGSVQGISEIMTDGAGLISTDLAHLVPYSQEGMKLGSCQSHISNGHSSVLQVRLYDPRGPCPIISKGTLTPCAALPPRTVLVTRSMVKAPS... | Function: Probably involved in the RNA silencing pathway and required for the generation of small interfering RNAs (siRNAs).
EC: 2.7.7.48
Catalytic Activity: a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1)
Sequence Length: 835
Sequence Mass (Da): 88961
|
A0A2K3P5E3 | MGSGRIENSFSDLSISSTGTGFGSGSGFGLNTDADSFSVKPKGRPTASATAPSKGLGMKLGKSQKTNQFLESLKAEGEVILEDVQPKLGQSRTAAPPLTDPVTLSVEEKLNVTLKRDGGVSNFDVQGQLSLQILNQEDAHIQVQVQTGDNHAISFKTHPNMNKELFANEYILGLKDPNRPFPTGQASDAAGVGLLKWRMQSTDESIVPLTINCWPSSSGNETYVSIEYEASSMFDLRNVVISVPLPALREAPSVSQIDGEWRYDSRNSILEWSVLLIDNSNRSGSMEFVVPQADSSAFFPISVRFMATDTFSDLKVTSII... | Function: The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membra... |
A0A365U8Z3 | MPRGGVFPPPLRRARDHPDRGTADRELPSGSARPGRDGSRRARRTDPPLPRIRHRGRVARDCPPCPAPVGGPARCLRRGAPQQQRRGAGMTPLTDSAGRPLPEIETPDAERLRIYGDMMFLALRSARHARMPVADLRSYLEVPILTGQFRIFRFDGIPRGMFTWALLDTNAQEKLVTGRPLAPQDWNSGTALWIIDMIGPYRGVTRGMVRWIMQRGNFAKRDFHFRRVGAGNETRRIVHVDFDAPRLSRVFTEAGFLERLHGGHGG | Function: Involved in fatty acylation of protoxin at internal lysine residues, thereby converting it to the active toxin.
EC: 2.3.1.-
Subcellular Location: Cytoplasm
Sequence Length: 266
Sequence Mass (Da): 29902
|
A0A2K3KVX3 | MERLSLQSDLERNNSTSEGDSLLNVTGDGDSSELADGKGRKTISEWISKISYVDAWKVYLQQEVVLPGVALALLFFTVL | Function: May be involved in iron transport and iron homeostasis.
Subcellular Location: Membrane
Sequence Length: 79
Sequence Mass (Da): 8706
Location Topology: Multi-pass membrane protein
|
A0A1D8PKA6 | MSSILLAVIFLVNLVLSSVIPQTDLKLSVEEQSHLEGDPSVTHKVVFTIKHGDELLGDLTLALFGETCPITVENFYQLAIRGEDGQGYKNSKFHRIINNFVIQGGDYDGRGGKSIYGDSFNDENFILKHNKLGRLSMANAGPNTNGGQFFILNGKPTPHLDGHHVVFGQLVDGFDTLQKISTVETKDSSPLKPVVISDVKTAIDKSKVNQKEETGTSSSSETEGITAVSTSVYSYLFIILLLGVVFAAYKMMPRRDQITTIKD | Function: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
EC: 5.2.1.8
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Length: 263
Sequence Mass (Da): 28783
|
A0A173G4T6 | MQNVFIYYNMVIYVSLLCLFLCFFVFFILILNSNIQSSWLLSSENHTIEIVWTLLPVILVTILCILNLDNINKDLVEKINYVVKIVGQQWRWSYENSLGLEYTSNFSMDRGVSSVDTPLYLPYGGSIQLLLSSVDVIHAFSLPDLGLKIDCIPGRINQLMYHSDCVGVFSGYCSELCGVGHSYMPIVCEIY | Catalytic Activity: 4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-[cytochrome c] + 4 H(+)(out) + 2 H2O
EC: 7.1.1.9
Subcellular Location: Membrane
Sequence Length: 191
Sequence Mass (Da): 21749
Location Topology: Multi-pass membrane protein
|
A0A7S3QKS5 | MFTTSSTVVGLRAFANNCGVPLAAQLDVQPSEDIPKVIRSPSPPRCRNCRAFWSQYCMVNLQRQMWHCACCGVGNISKSALANPDPTSYPELYNDTVEYRVLHQDGLQRPGARKHIVVAVDATMDAALLHNLQKAVLQTLESELEPDTLVSAIAFDGSVAVLDLASGRHQVPSLVLSGSTPLDQAGRDALAQQPGLVFSAEHRHCADRLAAALSSIRPFETDKPMRSRSRCLAVAVEAGLELLGKSVAGSQTLEPHAEGPHTLKHTGSQPQLAPGSRLLVFMGGPITKGPGTWPLDVVDGLEKPSKAQQKQMKEDEVHMI... | Function: Component of the coat protein complex II (COPII) which promotes the formation of transport vesicles from the endoplasmic reticulum (ER). The coat has two main functions, the physical deformation of the endoplasmic reticulum membrane into vesicles and the selection of cargo molecules.
Subcellular Location: Cyt... |
A0A4P2VHD3 | MLEDLREELARESRYIAMQGLVAGREGNISARRGDLIAIKATGVRMLDASPADFSVMDLTGRVLEGPRPSSEYRMHLMIYTASDAAGAIVHAHPPYTLSLASAGTWPSPSTEEARLYYDRVCDVRRLPPGSEELARAVSEAASSGCRAILLRDHGIVFVARDLKEAVDGAVAEERSSQVQFMSTILDLLQKIYLSCGNP | Pathway: Cofactor biosynthesis; coenzyme F420 biosynthesis.
EC: 4.1.2.17
Catalytic Activity: L-fuculose 1-phosphate = (S)-lactaldehyde + dihydroxyacetone phosphate
Sequence Length: 199
Sequence Mass (Da): 21681
|
A0A7S3VSU8 | MLLYHEPQVAGLCGVHCINTVLQGPIFTAMDLASIAQELDAMERALLGGSSEAGEHGNVDASGMFSVQVLSKALEVWGLTTTPLTSPDVPEVAQAPEKETAFICNLQEHWFTIRKMPDGSFYNFNSLYPAPEALSPFYLAAYLASLREQGYTIFVVRSVSGDWDSAQVRNAATQGGKEGGRWFTPEEAKALTAEAASARERGKVTNALETALSRAEASGGTMALRSKRKAPDSMQTGNADEDADLEAAIAASLGEGGGSEGLQGLPEAQLQQQQWQQQQQWQQWQSEDRVQGGEDAGPSGVAGVEAGNDNEDFELAAAIA... | Catalytic Activity: Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).
EC: 3.4.19.12
Subcellular Location: Nucleus
Sequence Length: 449
Sequence Mass (Da): 47745
|
R5APE9 | MNDYIEIRLDLTPCSETATDVMAAMLADAGCESFVADSDGLTAYAPAATFDRDAIDAAINDFPLPGITVSRRDSRIEGRDWNAEWERHYFKPIVIGDNEAVVHSSFHTDIPRCRYDITIDPKMAFGTGHHATTSLIATRLLSLDLENRKMVDMGTGTGILAILAAMRGASPVTAIEIDPPAYANAVDNVALNGQPQIDVRLGDAALLEGISGVDLFVANINRNVITGDIAAYRSTLAPGATMLLSGFYVDDIPIVAKAAEATGLTPLGHTERDRWACLELTLKPRRCEE | Function: Methylates ribosomal protein L11.
Catalytic Activity: L-lysyl-[protein] + 3 S-adenosyl-L-methionine = 3 H(+) + N(6),N(6),N(6)-trimethyl-L-lysyl-[protein] + 3 S-adenosyl-L-homocysteine
EC: 2.1.1.-
Subcellular Location: Cytoplasm
Sequence Length: 289
Sequence Mass (Da): 31192
|
A0A7S3VTW9 | EEQEAGAVTREEQALRNLMNEDSSIAVAAKVGQVHLVIGDLSGSGSSRSSSGQPLGTQGGTGASATGTVEGLMEGELSPSYRMRVLWEAATALRALAPGGCLVLRLGDCLTNFTASVLYVLHRSFAKLCIIKPFTSCAASGERMVVGLGRLHGDGHAGADVLLAVLEQQLLLLRQQHQQQRDGSSSSSSSSSSPVMEVGVFVPPQLLTEAPFFKYLLQRNVELAKHEGRCLVAAVERSKKRGPNNPAPAPAGAPETESADVDSRSGLGGGGLGS | Function: S-adenosyl-L-methionine-dependent methyltransferase that mediates RNA cap1 2'-O-ribose methylation to the 5'-cap structure of RNAs. Methylates the ribose of the first nucleotide of a m(7)GpppG-capped mRNA to produce m(7)GpppNmp (cap1).
Catalytic Activity: a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucl... |
A0A443R962 | MDAMQLAPEHLHLVSVRIGDFLPQEENEAEGIVQSSQVARPYFMLPEMITMLNKSFYHSVCYSSVVERAQYWMWLFAVSKIVELGDTLFIVLRKQNLIFLHWSHHIISLVYTWFSCAQNISLGRWFVTMNYCVHSLMYGYYAFRALQYKVPRSVAIFITTLQIIQMVLGFYVSYYAFSAKLNAVYCEIPMKTATIGITMYIAFFYMFAQFFVQTYFPNLKGAKLWLPLATWTRNKTNSHYKQ | Catalytic Activity: a very-long-chain acyl-CoA + H(+) + malonyl-CoA = a very-long-chain 3-oxoacyl-CoA + CO2 + CoA
EC: 2.3.1.199
Subcellular Location: Membrane
Sequence Length: 242
Sequence Mass (Da): 28440
Location Topology: Multi-pass membrane protein
|
A0A023U6Z5 | TLYFIFGIWAGMVGTSLSLLIRAELGNPGSLIGEVQIYNTIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLISSSIVENGAGTGWTVYPPLSSNIAHGGSSVDLAIFSLHLAGISSILGAINFITTIINMRLNNLSFDQMPLFIWAVGITAFLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF | Pathway: Energy metabolism; oxidative phosphorylation.
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytoc... |
W9H8Z0 | MATWLLICCGMVFAMAVIGAVTRLTESGLSMVEWKPLIGILPPLTETEWNRVFDLYRETPEYRYVNAGMGLEEFKHIFFWEWFHRFWGQMIGFVFLLPFLWFWATKRIPKGLMPTLVGLFLLGGLQGGIGWFMVVSGLVDRPSVSHYRLALHLGVAFLIFALMLWVALGLLDPKPEGSRSAAAPALRRHAGLALGLVAVTAAWGAFVAGLDAGMIYNTWPLMGGQIIPSDMWFLNPAPLNFVENHAGVQFTHRWLAMVTGLVVLGLWWRAGKADIGPRGHRLGQAVGVMVVVQIALGIATLLTVVAIPLAAVHQAGALTL... | Pathway: Porphyrin-containing compound metabolism; heme A biosynthesis; heme A from heme O: step 1/1.
Function: Catalyzes the conversion of heme O to heme A by two successive hydroxylations of the methyl group at C8. The first hydroxylation forms heme I, the second hydroxylation results in an unstable dihydroxymethyl g... |
G0S1Z1 | MRRSSSSGGTPFISLLEPHPLTGWDRTLPADEQPDLDSLPRTFVDAMRVRQEVFVQEQNVPLANEFDADDPRSCHWVIYASVNKTVEPARTDPVTGKIIQPRRSETQSVPIGTIRLVPFPHPPHPLDGGVYVDGELVNSGEPVARVHSIHPAAGGERTTSQYSSNSTSPTLPNSQIVPPAPPSLIKPAFTPDRPTTYHDGVEPYLKLGRLAVIPAFRGRGIAQQLIKTAVAWARSHPEYFNPSATEQGFEQLGMEEGSRMRGGGVVPRWQGLICVHAQVEAIKVWERCGFVLDEGMGKWMEEGIPHVGMFLRVSLDKRED... | Pathway: Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; N-acetyl-alpha-D-glucosamine 1-phosphate from alpha-D-glucosamine 6-phosphate (route I): step 1/2.
EC: 2.3.1.4
Catalytic Activity: acetyl-CoA + D-glucosamine 6-phosphate = CoA + H(+) + N-acetyl-D-glucosamine 6-phosphate
Sequence Leng... |
A0A2K3KCI3 | IRDSNRAMLLAAAVQHHCKVVDLGIAKDDEECQGRILDKAFASGINILITSGGVSMGDKDFIRPLLENCRNSKIFKISSNALVSVIKPGKPFTFAEIGSQSTESKILAFGLPGNPXSSSVCFHLFVVPAIRQLAGWTNPHHLRVQAWLQ | Pathway: Cofactor biosynthesis; molybdopterin biosynthesis.
Function: Catalyzes two steps in the biosynthesis of the molybdenum cofactor. In the first step, molybdopterin is adenylated. Subsequently, molybdate is inserted into adenylated molybdopterin and AMP is released.
Catalytic Activity: ATP + H(+) + molybdopterin ... |
A0A1M2YUU4 | MAIAYAFSVVGAILILLIGYVIAGLAERSVFAGLGRIRGVDQTLRIFLSKVLRYAILILVGVTVLAQFGVQTASIIATLGAAGLAIGLALQGTLQNIASGIMLLVLRPFRVGEYITVGGISGTVLEIGLFATQLRTWDGLYVMAPNNQLWNTAVTNYSRNPRRLDECAIRITYDDDIGLALRTFVELAKADTRILKEPAPVPYVKELGDTGIMVVLRYWTTSSDNWATKNDLLKTVRETFEQRGISIPFTQRQIQVVGKPAAGAADASASTAGSPPDAGSEKGKRKPPAASRSK | Function: Mechanosensitive channel that participates in the regulation of osmotic pressure changes within the cell, opening in response to stretch forces in the membrane lipid bilayer, without the need for other proteins. Contributes to normal resistance to hypoosmotic shock. Forms an ion channel of 1.0 nanosiemens con... |
U2T284 | MSTPAAVPAESTAPEETSDTPTGFALWAVLRRDPARPDDLDGTDVPKAVAELEGVIADITLQGVTTRGLYDVSGLRADADLMIWLHGPDAEGLQWALRQLRRTQLLKALLPTWNAMGVHRDAEFNKAHVPGFLRGKEPKAWLCVYPFVRSYEWYLLPDEERGRMLSEHGRKGAAFRSVLANTVASFALGDYEWILPLESDELVDLVDLMRDLRQTDARLHVREEVPFFTGRRVEPAEVVEVLQ | Cofactor: Fe-coproporphyrin III acts as both substrate and redox cofactor.
Pathway: Porphyrin-containing compound metabolism; protoheme biosynthesis.
Function: Involved in coproporphyrin-dependent heme b biosynthesis. Catalyzes the decarboxylation of Fe-coproporphyrin III (coproheme) to heme b (protoheme IX), the last ... |
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