ids stringlengths 6 10 | seqs stringlengths 16 1.02k | texts stringlengths 117 4.4k |
|---|---|---|
A0A4Q7VND6 | MPLSPSPDPDAIDEIAGGRRRLTVGDGHRLWWTERGDPAAPALLVLHGGPGGRTREPTLAWWQGLPLRVLAFDQRGCGRSQPSGSLQHNTLAALVEDIEALRVELGVGRWALAGGSWGARLALAYAAQHPQRVNGLFLRSPFLGSRAETARYIEPWFDWLGMRGRAWVGEAAAQSLSRLYQAAPASFDADTGFTRGGDPAQTLPEWLDDTRLARAWAEFDDGQSLPGGVRRAGKLFTEPTSATGRDDGLASWRVHAWHALAHWGCADPGAGAWPEAEQLSRAWSGPVSIVAGAEDACCDPALARRLATLWPQALLQIVPG... | Catalytic Activity: Release of N-terminal proline from a peptide.
EC: 3.4.11.5
Subcellular Location: Cytoplasm
Sequence Length: 345
Sequence Mass (Da): 36859
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A0A3N9TY63 | MPSNWGWRCRSATASPLTPRPRILAATSPAWRRCKHWWRNAVSTEAAISREQILSHVQRTLVELFEVSPAEVTPEARLYEDLDIDSIDAVDLVVELKQFTGRRIDPEAFKSVRSIDDVVNAVDQLMRD | PTM: 4'-phosphopantetheine is transferred from CoA to a specific serine of apo-ACP by AcpS. This modification is essential for activity because fatty acids are bound in thioester linkage to the sulfhydryl of the prosthetic group.
Pathway: Lipid metabolism; fatty acid biosynthesis.
Function: Carrier of the growing fatty... |
A0A7K4LZK9 | QVQEYREALEGVLIKGKNGVRLLPELYSVPADKVDEECRNPHTVDRIPMGKLPLMWGQSLYILGCLMAEGFLAPGEIDPLNRRFATVPKPDVVVQVCILAETEGIKAILRKEGIHVETVADVYPIRVQPARILSHIYARLGKLHCGLPKQ | Pathway: Glycan biosynthesis; glycogen metabolism.
Function: Phosphorylase b kinase catalyzes the phosphorylation of serine in certain substrates, including troponin I.
Subcellular Location: Cell membrane
Sequence Length: 150
Sequence Mass (Da): 16731
Location Topology: Lipid-anchor
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A0A8S0RP17 | MAFVMSAIALAFIVNDYLGVALASYVGETGDNFSGLPHGLLIQAVCTLLPIFWSLCISDVKSKGKKKGNLDNQPIRPFYFTLTFPYMPGYTAVMQENYWVESQGSNYQFPSTYGNVPRRLSREHVQENYRHLNRTWQGSYDEVEVWDESDFIEHRRSNLSTNISHDDRVRNNFSQETILRHLKTRKFATSKEVKPTNEGPEICVVCQCEYGDNESIGRLRCGHEYHVDCITRWLCQKNVCPICKATAIPRREEVARV | 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.
EC: 2.3.2.27
Subcellular Location: Membrane
Sequence Length: 257
Sequence Mass (Da): 29558
Location Topology: Multi-... |
A0A8S0UQL5 | MEPQKYKIVKSTCSNADASNRKLDLLNSQSIYRVDNMYYKNLLNNTCLLESNQALIGDPKAAAIFKDYSMDPFLYSKDFAASMVKLGNTGVLNRKSGEQQQQPPPMVVAAQQASTAHSGHGSVGPVIGVLAVIIILGAISVMIGRLCSGRRIMGRGRYDFEEWAETKCASCFDGRALPPSLPPMVAEHSVSSSSSDATPAVVPQEETQIHEEDKVPEQHNNLRN | Cofactor: Binds 2 calcium ions per subunit.
EC: 1.11.1.7
Catalytic Activity: 2 a phenolic donor + H2O2 = 2 a phenolic radical donor + 2 H2O
Sequence Length: 224
Sequence Mass (Da): 24428
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A0A6A1WJE9 | MVGKYAGLSNSYLSVLKALVHASVACRQKLIVEWVAAGELEDITANPDVYKAVWDRLKGVMVFFFLGGFSDRGVQGKILAAKYAREKNVPFLGICLGVQIIVIEFVRSVLGLHDVGISFMQVDDYERRQTLVNLKMFKGEDLGRKTRNTISIKECEGASESKGKSKNQVERTKERIRITEITLEEDA | Pathway: Pyrimidine metabolism; CTP biosynthesis via de novo pathway; CTP from UDP: step 2/2.
EC: 6.3.4.2
Catalytic Activity: ATP + H2O + L-glutamine + UTP = ADP + CTP + 2 H(+) + L-glutamate + phosphate
Sequence Length: 187
Sequence Mass (Da): 20917
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A0A257MUV9 | MKARATFCLFNILRKDELLKKGGLAVDIEPRSGEQRSWPAPKQGVLAQALGRKTRTVVDATTGWGQDSLHIFRMGYELLCMERSPVIAELLIDAFKRLAEQDWMQKLNLQPPRLLIGNAIELLATLETQPDCIYLDPMFPPKRKKSALARKSMRVLHDLLGNDQDKEQLFAAALTAAGKRIVVKSPDYAEPLGGKPNESFQGKLLRYDVYIKNEKNGD | Function: Specifically methylates the guanosine in position 1516 of 16S rRNA.
Catalytic Activity: guanosine(1516) in 16S rRNA + S-adenosyl-L-methionine = H(+) + N(2)-methylguanosine(1516) in 16S rRNA + S-adenosyl-L-homocysteine
EC: 2.1.1.242
Subcellular Location: Cytoplasm
Sequence Length: 218
Sequence Mass (Da): 24534... |
R7Q0N4 | MWRFNHWAYVDIFVYFSHYCVTIPPVGYIHAAHKHGALVLGTLIFEWEKGAKELQNILVSFKTRARAASQLASIAKFYGFDGWLVNVEVELPGGSSAASDLAAFVGDLTRATRKIVGLVSEVIWYDSVTRDGSLRWQNELNQDNEQFFKAAGSIFTNYHWDRNAPVRSAVKAGTRRTDVFTGIDIHGRKTYGGGGFQAHLALRAIKQGGTSAALFAPAWTVEKCPPNVSDPRELEDRFWTGPSGRFGRESVAQYFKERPVLTQIPFSTSFDPGWGPRLMEKGVVKSPDRYFNMAQQHIQPSFMRTYVAAGDVSASELCLS... | Catalytic Activity: an N(4)-(oligosaccharide-(1->3)-[oligosaccharide-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc)-L-asparaginyl-[protein] + H2O = an oligosaccharide-(1->3)-[oligosaccharide-(1->6)]-beta-D-Man-(1->4)-D-GlcNAc + N(4)-(N-acetyl-beta-D-glucosaminyl)-L-asparaginyl-[protein]
EC: 3.2.1.96
Sub... |
A0A401RDY1 | IGTCPTKEDKEAFAIVSVPLSEVRDLDFANDASKVLYAMVQKLEDGSLTQNERRFVTKLLEDLVFFVAYVPSNGQDVLDVVITKPNRERQKLMREQNILKQIFGILRVPFIDKGEGPMLRLEDLGDQRYAPYRYILRLCYRVLRHSQQDYRKNQEYIAKMFGIMQSQIGYDVLAEDTITALLHNNRKLLEKHITAKEIETFVKLLRRNREPRWDSRLLCNLPLSLRFFCLAGFKTK | Function: Receptor for inositol 1,4,5-trisphosphate, a second messenger that mediates the release of intracellular calcium.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 236
Domain: The receptor contains a calcium channel in its C-terminal extremity. Its large N-terminal cytoplasmic region has t... |
A0A952HDU7 | MRIPIPALLLAFGASAGSLAQAQGCGSGGGATVCLTATGTASNVQLGWTVSGAVKSLEIYRDTDANPVGRNRIAVPAASATSYADATAADGTPYWYWVKFTTNAGSYNSGVATATRGSTCTPTAITPYISANGSWSQTSSATITAGNSAILGPQPITGGSWGWSGCGTSGSAREQLVTPGANCAATATYTNACGAKTVQAFAITVAGSAQPFAWKSSEPLIKPPADRADIFGVKDPSIVYHDGRYHVFMTTAGKNGWGIAYTSFANWAEAPTATQFMLDKSPIGPGYRAAPQVFYFAPQKLWYLIYQGGDPLYSTTPNIA... | Function: Involved in the degradation of xylan and is a key enzyme in the complete degradation of the plant cell wall. It has a specific arabinofuranose-debranching activity on xylan from gramineae. Acts synergistically with the xylanases and binds specifically to xylan. From small arabinoxylo-oligosides (ranging from ... |
A0A7S0BDP3 | MGCGITARKTTLKYNDLPESLKDLRLAIQESVPHGHSSLKHLSEDYGSWSSIPDGVQRLYNKHLATEYSRIGKRAPEAVIEQPEQQLGTLGLPDHFVEMSSDELENIWILVHTGSRKPGRKLGEYFTSVARKEMGVNAFSLPNVNLAYIEESSKSFRDYLAAHGWAKKFAKLNREMILRNVVNRLRQFVPSRVRNFKGQLEVIDCPHNFVSKETHMESELYVMRRGAISAKLDEVGIVAGTMTEKSYIVKGTGHDKSFESCSSGVGRTRSTS | Cofactor: Binds 2 manganese ions per subunit.
EC: 6.5.1.8
Catalytic Activity: a 3'-end 2',3'-cyclophospho-ribonucleotide-RNA + a 5'-end dephospho-ribonucleoside-RNA + GTP + H2O = a ribonucleotidyl-ribonucleotide-RNA + diphosphate + GMP + H(+)
Sequence Length: 272
Sequence Mass (Da): 30574
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A0A431K333 | MDWLQPLIILMGLSGQLLIAKKNPAGYACWIVGNISLMFVYVDLHQYGLMGLQAVNTVIQIYALNDWLKSFRHSKAVQPT | Function: Required for nicotinamide riboside transport across the inner membrane.
Subcellular Location: Membrane
Sequence Length: 80
Sequence Mass (Da): 9021
Location Topology: Multi-pass membrane protein
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A0A5C6RWP3 | MEGRGTTHRGQRPDPLFHRPSAPPDGRRPRDKPDGGTGHLIVAQGHGLRGWMQRWREPHSASAAAPLPELALPTGDGPLIWLRIGGDVASLPDGGLPPTLIQLLMQLRRRGLQIAVSRAAGGPPDLATRGISAVPDAALSVGQADAHISAMRPAAILLIGADLPRPLIEAALARDIPIVLAETRLSASERGWGLASLGLGRRSVLSQLTLLLLPDAASRDAAIDMGVSESRIEVTGPITQTREPLKHLEAERESLAEAFTGRQLWLAINVTEPEEQALIDAHMTVLRYSHRAILIALPDDPRRADAMASRMSDAGLIVAQ... | Pathway: Bacterial outer membrane biogenesis; LPS core biosynthesis.
Function: Involved in lipopolysaccharide (LPS) biosynthesis. Catalyzes the transfer of 3-deoxy-D-manno-octulosonate (Kdo) residue(s) from CMP-Kdo to lipid IV(A), the tetraacyldisaccharide-1,4'-bisphosphate precursor of lipid A.
Catalytic Activity: CMP... |
A0A8S0S7U3 | MAPVIATTTTSLPPKKWSLDSWKSKPAWQLPEYPDKDSLESVLETIESFPPIVFAGEARSLEEKLGQAALGNAFLLQGGDCAESFREFNVDKVRDTFIVLLQMSLVLMFGGQVPVIKVSHFLF | Cofactor: Binds 1 divalent cation per subunit. The enzyme is active with manganese, cobalt or cadmium ions.
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 1/7.
Catalytic Activity: D-erythrose 4-phosphate + H2O + phosphoenolpyr... |
A0A8H7NPX2 | MDTMGLRKPGLSTEVTQTYASVPFIKEDDGHTYNHAPSYPTQSGRVASPFRWWTLEMLSCLGAVACMAAIVAILIVYDGKPQDSWPINNFSINSMIALLATFCRTFFMVGVGAAICQGRWHQFSSRHDDKSFTLDDFGLFEHASKNPFASLWLIWRFKGRNTACIGAALSVFALAFGPFSQQMITVKLDTVEQASSGATGAVSRVTLVNSVIGYSSSWNPISSTKLAIYNGFMAPEIDIPSTVCPTGNCTWPIVPTVGVCGACVDTTPDIKFNRSSGSYCSVTAGKLEVKGQCGVSDFGTVFKIGAGSGKVFSLEDVPLE... | Pathway: Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-gluconate from pectin: step 1/5.
EC: 3.1.1.11
Catalytic Activity: [(1->4)-alpha-D-galacturonosyl methyl ester](n) + n H2O = [(1->4)-alpha-D-galacturonosyl](n) + n H(+) + n methanol
Sequence Length: 835
Sequence Mass (Da): 90304
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A0A932RZR7 | MNTIYNFSAGPAVLPKEVLQEAASEMLDWHGSGMSVMEMSHRGPEFMSILAQAQADLRELLHVPANYKILFLQGGGLGENAIVPLNLVGRKPQPATVDFIHTGSWSGKSLKEAKKYANVNIAASSESTGFDGVPDPSSWKLSTNAAYVHLCTNETIDGVEYHFVPDVGQQTNGAPLVADMSSHILSRIIDVSKYGVIFGGAQKNIGPAGLTLVIVREDLLGTALPMNVPFFLKDESLNAAFLAAAKERGLLQLKGHKSVGGMRASIYNAMPIEGVQALVAFMRDFAGANG | 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.... |
A0A2T0XG54 | MQTTALEEKPISISNRGMILTGGVVFAVFIVLLAFTLAYFEHTQAENEWKKNIKNLSLSISAHANQSFFSSTVLLQSITDEINGNRFADEAGFKASMAERSFHENLQKKINSNPLIDVAIVTDKNGEVINFSRFYPPIKINLDGKLQYDWWKSHNDDSVFYGEPVFNNFGKWSFYMSQRINDTSGRFLGVVLIGMSIDNFSKFYKTIFSNIGRSASIILYRRNGLIVAAWPESEALTGRFKASETDNDASIRGFSDSSVFITSPDDSIRSSATKRRMIALSKVSDYPFYIEVSFGSDIYLDAYYRLLTPIFAIAFFANCL... | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Membrane
Sequence Length: 622
Sequence Mass (Da): 70615
Location Topology: Multi-pass membrane protein
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A0A967AEE8 | MKELIKRSITGLIYIFLIVASALLGKEALHIVFLFFGMICLYEVQRLLNYKTIISYILLFGLILLNQTSSYIQEYFIFLIPVFIIVGIVLIKNLFSNSKSLINVNKHLVINFYIIPAFVLLPNLPEISIISGKPSQSEPLILIGYFLLVWCNDSFAYVFGKNFGRKKLFERISPKKTIEGFLGGAIMCGIAGIVFYHFTHTLSVNAWIGMAVLVSVFGTIGDLVQSKFKRIAQVKDSGNIIPGHGGIYDRMDSTVFSITFVYGFLILLSYVS | Pathway: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-diacylglycerol from sn-glycerol 3-phosphate: step 3/3.
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phosphate + CTP + H(+) = a CDP-1,2-diacyl-sn-glycerol + diphosphate
EC: 2.7.7.41
Subcellular Location: Membrane
Sequence Length: 272
Sequence Mass (... |
A0A3N5MGR1 | GKVCTGIAYRISEDQAKSIIGYLRKRELVSGVYREAFLPVTLIGKVRQEVMALTYIVERAHPSYVARLSLAEQARLIRGAKGISGANLDYLANTMRHLSELDSRERSLERLLVVTGPHVARAPGGPLESPRVAALLRACRARPVIAPRMRPAERRRFLYRTRLSSQTYPTFGGLEEEAVNGG | Function: Catalyzes the cleavage of glutathione into 5-oxo-L-proline and a Cys-Gly dipeptide. Acts specifically on glutathione, but not on other gamma-glutamyl peptides.
EC: 4.3.2.7
Catalytic Activity: glutathione = 5-oxo-L-proline + L-cysteinylglycine
Sequence Length: 182
Sequence Mass (Da): 20214
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A0A397V6T8 | MYEKVKTRECLRKLYTHNNDALARYLGVKKSPVTIRFILGLPKDVYKDKLEEESKIHGDIVILNITENMNNGKTFEYFKWFAKHREDNYLLKLDDDSFLHLIHYYRDLQDLPRKRAYYGNAIFNKGSETNTFFGGAGYTLTRDLIMDITGSDWVSSDTVGTEDWLVGNWVCHVAREMKYFVHYVGFTSWVSIRQNPIHDFDENLDLHFLSETIMIHRIKEIEKLNAIMDMYSEYEEGLPIVRVIRNSTAKGLVTKR | EC: 2.4.1.-
Subcellular Location: Golgi apparatus membrane
Sequence Length: 256
Sequence Mass (Da): 30139
Location Topology: Single-pass type II membrane protein
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A0A1E2UV11 | MDSQPIAANQVARSSSPYVWQTLPDQAPAPENNPMTSEKVVLGKRLFFDKNLSWDRTLSCSSCHDVIGGSGDDGLPTSRGINNQLGGRNAPTVWNAAFQSVLFWDGRAASLEEQAKGPLFNPIEMGMPSWEEVVQRVLDDPAYVPLFADAFGADTAIDIERIAEAIASYERTLITPDAPYDRFVRGDLDALSAQQLRGMASFQTLGCVNCHTGPNFSGASLFDSRAPLRIFPIYPTPFEQQYELTRDTGAAMAGSGRGSWRVPSLRNVALTGPWLHNGSVSELKEVVRIMSSVQLGHTGRYLVWSDDHKVMTKLDRPALS... | PTM: Binds 2 heme groups per subunit.
Cofactor: Binds 2 heme groups.
Subcellular Location: Periplasm
Sequence Length: 357
Sequence Mass (Da): 39045
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A0A6J1WMZ3 | MLKVDSQKKKLFTHFITRNWFLSINCNLPVAIFKMNAPLARISNKLGRTAMTNFVRCHSHGGVPGENLPFDIYNRYKLTALFTVFVGSGLAAPYLITRHQLLKK | Pathway: Energy metabolism; oxidative phosphorylation.
Subcellular Location: Membrane
Sequence Length: 104
Sequence Mass (Da): 11852
Location Topology: Single-pass membrane protein
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A0A838JM34 | MSIAAQNQVTMKKLLLMVVLMSGFAFALVPMYRKICEVVGINDTRDVNFAAANSQVDLGRNVTVELMTAVNQNAPLRFEPVERQIKIHPGEIITIHYRIMNTTDHVLVGQAVPSYGPAAAAKYLTKLQCFCFAQQTFQPREVREMAVVFVVGRELPKDLNTITLAYTFFDITARKSG | Function: Exerts its effect at some terminal stage of cytochrome c oxidase synthesis, probably by being involved in the insertion of the copper B into subunit I.
Subcellular Location: Cell inner membrane
Sequence Length: 177
Sequence Mass (Da): 19769
Location Topology: Single-pass type II membrane protein
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A0A4U1F4Q5 | TTQPPITGATHGARAAAAVAGRSPAELPGRGCRCDRPSRPRRARAVPGQDMRNEWWKSKNKVVGNPDDDQPGKCAKQPFLLLAIKSLTSHFDRRQVIWESWGKETNVGNQTVVRVFLLGQTPAGDNHPDLSVELKFESEKHQDILMWNYRDTLFNLSLKEVLLLRWVSTSCPNAEFKGDDDVFVNTRHILNHLNSLSKNKAKDLFIGDVIPSAAPRQDKKLKYYVPEVLYTGVYPPYAGGGGFLYSSHLALRLVQPPGSEASVTGQVLLYPIDAVYTGMCLQKLGLIPEKHKGFRTFDIEEKNRNNICSYVGLMLVHSRK... | EC: 2.4.1.-
Subcellular Location: Golgi apparatus membrane
Sequence Length: 338
Sequence Mass (Da): 37927
Location Topology: Single-pass type II membrane protein
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A0A2T0XEC5 | MVLELPFPPSLNTYWRRGKGRVYINERGLEYRKHVATYVRQHKLKAPEGFLTYAVWLYPPDKRRRDGDNFAFKAIWDSLTHAQCIEDDSLFKEWSGTWMPVVKSGLCRVFISEFVAPEKE | Function: Endonuclease that resolves Holliday junction intermediates made during homologous genetic recombination and DNA repair. Exhibits sequence and structure-selective cleavage of four-way DNA junctions, where it introduces symmetrical nicks in two strands of the same polarity at the 5' side of CC dinucleotides. Co... |
J7FAC1 | MINAFQEIPITQDASASAYQIMAYFLLDETMAMKTNLIINKFDWIVDIYEMFKEECLEYIHKNESDKHFCQTLSRVFTRKIVKNIFMPIIYGKTVNSTGKDLHILLGNDLLKPECFKLAKLCYAFWHDTYNHMYSFIDLIGLVGRVCASLERPVLFNTKFYDTHQDYKKVESCSVRVFDKINRKNRTVNLSVPSDVRDKRKSRAATFVNFIHQRDAKIAMSVAEIAGSYQIPLYTVHDNFISNTINSQKLPNIYCHVFREMEAPMTIINRFIYNNLIKPSLDLNDSQNKEYMEHLLNHRIDRQDLESILKKDIPMSEMKN... | Function: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
EC: 2.7.7.6
Catalytic Activity: a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1)
Sequence Length: 371
Sequence Mass (Da): 43603
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A0A849ICQ9 | MTNKIFRILLVLFSAISFHTAMADEAQLVNRIVAVVNDKPITQVELDDRVKAISQQIEKRGIPLPPPSVLEKQVLENMIMDKIQLEFAAEVGIKVDDEQLMKAMQKIASDNHMTLAQFKDAVEKEDGVPFDKFKEDIRGEIIKSRLRQREVDSKVVVTDAEVNNYLKNSEVQGKTQEYDLSHIFIQLPEQASPDQVKTQLAKAERALQAVRNGADFGQVAASFSDAPDALKGGAIGWKPAGQLPSAFVEMLQKLQPGEVSGIIRSPNGFHIIKLVDRREGKSASVVTQTHVRHILIKTGENVSEEDAKRKLETILAEIRK... | Function: Chaperone involved in the correct folding and assembly of outer membrane proteins. Recognizes specific patterns of aromatic residues and the orientation of their side chains, which are found more frequently in integral outer membrane proteins. May act in both early periplasmic and late outer membrane-associat... |
R7FQH7 | MEDIIIIGAGPVGIYAATLANLHGLKGIVLESLSTAGGQLTELYPQKDILDVPGFSRIAAKEYIEALLKQQESDSNHLQIVYGEQVKNIEKQEDKSIKVTTNKNTYLTKTILLTTGMGVFTPRKTGLEGEDDLTNIYYSVKDKSIFKDQEIVILGGGDSAVDWAIALSDIAKKVNIVHRRDEFRAQESSVNLMTSNGVNIYKPYGLVSFVKDGNKAKGIVIKHNVDGSEITLNFDSIIVNYGTVTSASNFAIEETNRAYNVDRTFRTSFENVFAVGNSCYYEGKVKNITCGLGEAVIAITEIDRIVHPGKNIPVHF | Cofactor: Binds 1 FAD per subunit.
EC: 1.18.1.2
Catalytic Activity: H(+) + NADP(+) + 2 reduced [2Fe-2S]-[ferredoxin] = NADPH + 2 oxidized [2Fe-2S]-[ferredoxin]
Sequence Length: 316
Sequence Mass (Da): 34689
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A0A1F1ZCQ0 | MTSIAYLGPAGTFTEQAARAFDLPDPQYVPVDSPAAALDAVRTGAADRAVVAIENSVDGAVTSTSDALVAPGVRILGETELAISFAIMTRKGFLLSDATTLSTHPVAHSQVSSWVAEHLPGVHFVPATSNAAAARMVADGEADVAAAPERAADLFDLEVHARGVADMDTARTRFVLVGPEDVPLPARTGRDRTSLVFQTPNQPGTLVAMLQEFASRGVDMSRIESRPTRTVANTYNFFVELVGHIEDAEVADAVAAVKQRATWSRFLGAWPRC | Pathway: Amino-acid biosynthesis; L-phenylalanine biosynthesis; phenylpyruvate from prephenate: step 1/1.
EC: 4.2.1.51
Catalytic Activity: H(+) + prephenate = 3-phenylpyruvate + CO2 + H2O
Sequence Length: 273
Sequence Mass (Da): 28913
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A0A4V5P8J2 | FYHLSLAPTPELGGCWPPTGIRPLNPPEVLPLNTSVLLASGPYGGNHKHVLQALFITIALGIYFTLLQASEYYEAPFTISDRVIPQTARNYWVHLPHYLFYAYQHITSRPTITSALKPLLDTGILNANISIPLNILTIMSRRHNIIAIPHGNPNDPKFTLHFSQHNTIILLVFAACEATLRLSLLVIVSNTYGTDYPYSAFHCSYSYPDSLKLYRSHCFNNHPRPHIIYTTLPSKLKSCTRANIVITALYYLYILITTQCSKYTHHINNITPSFTRENALIALHVLSLLLLSLNPTIILGPLYCKYSLKKTLDCESCNRR... | 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 proton gradient across the mitochondrial membra... |
A0A1F8MC45 | MKRIGILYHPLREKARDLSQKLEQFLSSRGVSSWRCSAWDEDKARPQLTGTELILSIGGDGTILHSTRIAAPLSIPILGINLGRLGFITEIDGDGVMSRLPGLLKGEGRIEERAMLEAQVADKTFHAMNDVVLRSVAVRLVNIKAEIDGAVLTTYRADGVIAATATGSTSYALAAGGPILHPQSKEIVLQPISCHLGLSHALVLPPQSIVDLKIARREKVILSIDGQVDLPLSNGQNVRVKLGPHTARFLRIHDQSYFYSSLWQKLGGRRNES | 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... |
A0A5D0RJV2 | MSGRNSLKIVVCGGGTGGHYYPLIAVISALKKKIELKVLYYTSKGRLDDRYAERDIENVKKMPLEVKGLKRPVYSPKNIMVIFDHLLTTDKVKRNMAEFSPNLVFSTGGYISFPVVKAASKIGLPVFLHEQNSIPGIANKRLARYAKKVFISFEKSRDYFKNIENGKVIYTGNPVRKVMKTRKEIFDSLGIDQNRKLIIICGGSQGSDFLNRIMIEIYDGIKDDKYFFYHITGNAEIKTKNYSFVRYRKFDPQLNEYIAVADGVVARGGATTIAELAHYGTPGVIIPWSEATENHQYYNGLMLQEMGLGYVILENAVTSG... | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Cell wall formation. Catalyzes the transfer of a GlcNAc subunit on undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide (lipid intermediate I) to form undecaprenyl-pyrophosphoryl-MurNAc-(pentapeptide)GlcNAc (lipid intermediate II).
Catalytic Activity: di-t... |
A0A2T0BGL2 | MESVKNKIAIIGMPGCGKTTLGKLLAKELQYNFCDMDSYIEKISDKTIPELFNEGEEVFREWESKACIDLVKKERIIISCGGGVVKKDENIEAFQKDCVILFIDRSVEDIIKDVNVSSRPLLKDGTFKLYEIYDERYNMYKKAAHVIIGNSGPVKEVIKKIKLLLQNKIKE | Cofactor: Binds 1 Mg(2+) ion per subunit.
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 5/7.
Function: Catalyzes the specific phosphorylation of the 3-hydroxyl group of shikimic acid using ATP as a cosubstrate.
EC: 2.7.1.71
S... |
A0A6J3BXD3 | MTFCYLAAFNWWLLLCPWSLSHDWQMGSVPLITSGWDPRNLLTCAAFGALLLLCYRFIADLEVQRHTPAVIGLLLLVIPFVPASNLLVTVGFVIAERVLYIPSVGSVIITAYGVQLMWYSKPWTKGFLVIGLALLAASGVARTYKRNADWRDRATLLRADLVTLPQNAKLHYNLGNFLRESEQQDSAIRHYKEALRLWPSYASAHNNIGTLVSGMDNAEHHFLQAIKYNRHHVNAHYNLGKLYKKSGQTIQAIKMLEKCIWLQPRFVQAHVELLALKPESEKKSILTKLVELEPNNWEHFVLYGDWLRMKGLQSPASKYY... | Pathway: Protein modification; protein glycosylation.
Function: Transfers mannosyl residues to the hydroxyl group of serine or threonine residues.
Catalytic Activity: a dolichyl beta-D-mannosyl phosphate + L-seryl-[protein] = 3-O-(alpha-D-mannosyl)-L-seryl-[protein] + a dolichyl phosphate + H(+)
EC: 2.4.1.109
Subcellul... |
A0A6J3CC73 | MPRLKVKNVSQNVCGQNSRMLHLCWVYYFSKLSEFADTVFFVLRKKKSQITWLHLYHHSLTPFEAWLLVKFIAGGHGTFSNIVNNLVHIIMYSYYMVAAMGPQYQKYLWWKKHLTTLQLVLLRQNIVMGLAILICTIGFVEFPKICLSAMMASSFVILVNGCCF | 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: 164
Sequence Mass (Da): 19036
Location Topology: Multi-pass membrane protein
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A0A8H7NAJ3 | MQPHDPETTILVEFKPKWLSQSPNAPKNAIRCRQCAKELYSYIVDPQVGKPVPTKAKPCPLMIGNDASNPAFTDSVCRRVPSTDKRRKRLNSTLDVLRNEPAFKTLRLAQEANDHVGPLKADKKDAQFALAMTLRDCTCFAQVLTTPTQQQDSFKPLKIRFGDFDMKMPEFKLIYWRTIEEQLIKGGFYTADMIYCRGQFYRPPTKCYLERGRPTRPMEELEVIHLQEPQQKNGVDSLPPTMKSMTHAIHTDVNLMEKCLEHYKVRKPEGSQKG | Function: Has kinase activity and phosphorylates inositol-1,3,4,5,6-pentakisphosphate (Ins(1,3,4,5,6)P5) to produce 1,2,3,4,5,6-hexakisphosphate (InsP6), also known as phytate.
EC: 2.7.1.158
Catalytic Activity: 1D-myo-inositol 1,3,4,5,6-pentakisphosphate + ATP = 1D-myo-inositol hexakisphosphate + ADP + H(+)
Sequence Le... |
A0A0Q9SWG6 | MIKKNVAILSGKSAGKLSRLLGNHGSTLPGVVAIKIDPNIIRKLSHQIKHFIFITGTNGKTTTSNLLAHLLRSTGMKILNNFEGANMISGVAACLINHTTILGHLNYDYAVLEIDEASLPVILKQITPQMLIITNFFRDQLDRYGEIDMLIKDIEKAIHPIATKMILNADDPFVFRLSALNKDNIYYGLGKQAYTFGDYGMSESKYCPKCGEEMLYDHIHFNQLGFYSCSCGFKRPTPHYEIDRVQSTPLAFSLKNETYQMNMTGTYNVYNALAAITCAAELGIQDKNIKDSLHDFHMANGRMELFFYKEFPYIINLNKN... | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: The lipid II isoglutaminyl synthase complex catalyzes the formation of alpha-D-isoglutamine in the cell wall lipid II stem peptide. The MurT subunit catalyzes the ATP-dependent amidation of D-glutamate residue of lipid II, converting it to an isogluta... |
A0A0B7JWY6 | MYANVRCASGNSLESNHIRLHQPPSFIAIRGLSSLRNWRTWREISADHNWGPIYGTISTHAVNPAGQSILAKCWRFVVDQSKLGDHPRIVSYLGWQSEFPTGLLFVEASHGNLQVVLDQKQGINIDLRIKWLHQAIEAISYIHSRGVIHSDLRPDNFLIYGPEMDLRLCDFGGSTCKELNLSGNKLPDAGFFNPESKWEPSFAIDIFSLGSVLYTIITGHWPFRENESGGQFETLEEMEVYGDYVEEQFANHRFPDTEQIYKGEIILGCWTAQFPSIKDLNSTMTSSLKSRRARLPEF | Function: Component of the EKC/KEOPS complex that is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. The complex is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N... |
R7Q975 | MWWPFPFLAFADGKCPVDHKNMSNEQLDGMMAQYKRVGHDKFLAGLAESEKSQQPSAKPSPASPSPPENPDACPVDHKNMTPDQIAAYMSSRKKDTQSAPDATPPQPPDAPVYDVYGQELDRANLMPTTPNQLPSPGQKQPLSTDRVKSTIPKAGEDADQTWTYPSPQMFFNALKRKGKADGIQEADMDTVVHVHNNMNERTWMEVMQWETRFHCHECDNPKLKRFQGKPHELSPAARFRVWFRNYPMPFDRHDWVLDRCGKTEARYIIDYYYREGPDPIEIHVRPALDSVSAAFDRLRSRAETVRDAILGDSAKETSAT... | Function: Lyase that catalyzes the covalent linking of the heme group to the cytochrome C apoprotein to produce the mature functional cytochrome.
Catalytic Activity: holo-[cytochrome c] = apo-[cytochrome c] + heme b
EC: 4.4.1.17
Subcellular Location: Membrane
Sequence Length: 474
Sequence Mass (Da): 52488
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A0A7V2XK36 | AENAIVPMNLAGLRPSQAIDFVVTGSWSQKSAKEGQKYGNALVAASGADNGFTAIPDAASWQLRDDASYVHLCSNETIHGVEFQELPDLRALGCDAPLVIDFSSHVLSRTVDWSRVGLAFGGAQKNIGPAGVTLVVVREDLLGHALPVCPSAFDYKTVAENHSMYNTPPTYGIYMAGLTFQWIKTQKEASLTGVAAMEARNIAKAKLLYDFIDGSQLYVNKVDKACRSRMNVPFLLRDESRNDAFLAQAKARGLLQLKGHKSVGGMRASIYNAMPLAGVQALVDFMREFEKTQA | 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.... |
A0A396MKS3 | MPVNYCTEACDFIFRGKRKTSAWIRRTARTEGWDTGAVSVVFCSDERLLEVNNKYLNHNYFTDIITFDYSDPEKKKIAGDLMIGIGTVRDNAAAFGTTFENELQRVIIHGILHLCGYGDKTPEEAARMKSLENKYLDLFYNEIPGSAPRRADKKRKGEPEKQKK | Cofactor: Binds 1 zinc ion.
Function: Single strand-specific metallo-endoribonuclease involved in late-stage 70S ribosome quality control and in maturation of the 3' terminus of the 16S rRNA.
EC: 3.1.-.-
Subcellular Location: Cytoplasm
Sequence Length: 164
Sequence Mass (Da): 18777
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Q9DHD0 | MASFLVYLLFFIIFIVIAYYINYYPTNKLQIAVKNLNYEYQIYKQQDNEFPQKLSTLFFLDKQKFVGEEVNAYYNSSIGIVTLLTKSKKILFNINFSDDVSALLPILLLSK | Function: Component of the entry fusion complex (EFC), which consists of 11 proteins. During cell infection, this complex mediates entry of the virion core into the host cytoplasm by a two-step mechanism consisting of lipid mixing of the viral and cellular membranes and subsequent pore formation.
Subcellular Location: ... |
A0A447RLV0 | MNKKMAVPRSQAVGPNSTRTNTRHEQETDVLLIGGGIMSATLGTWLQELEPDWSITMVEQMSSVAEESSTGGIMRVPATRR | Pathway: Carbohydrate metabolism; tricarboxylic acid cycle; oxaloacetate from (S)-malate (quinone route): step 1/1.
EC: 1.1.5.4
Catalytic Activity: (S)-malate + a quinone = a quinol + oxaloacetate
Sequence Length: 81
Sequence Mass (Da): 8860
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A0A2Z6ME31 | MENQTRVRCPENEELASFMKNKWKEMASQPKGLSDNIEMALSKAHFNVCNSKNPIRTIKDFSTVKGVGKMMLKLMQGFFGTGSGGTEPDDLTKKGKKTKGTKRYVPQRNSVAYALLITLYRGTSNGNEFMRKQELIDAAEASGLSRAPIAPEKGKGKPGHFGSSPQDWYSGWSCMKILISKGLVVKSSCPAKYMLTQEGKEAACDCLKRSGMAESLDKSASVEIPIHMDKQNSLDMEVDARDLESEVTSPLNKQKKPLDVPLDSLERV | Function: Interacts with EME1 to form a DNA structure-specific endonuclease with substrate preference for branched DNA structures with a 5'-end at the branch nick. Typical substrates include 3'-flap structures, D-loops, replication forks and nicked Holliday junctions. May be required in mitosis for the processing of st... |
A0A4Q7V3W1 | MIGVAFPQPSGGWPWTTFLVNVSGCLLIGVLLTVLSELTVPHPLLRPLLGVGVLGGYTTFSTYAVDVVALVDAGRPVVALGYVVATPLAAVAACVLGVAVTRRAAGRTGGEPE | Function: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Subcellular Location: Cell membrane
Sequence Length: 113
Sequence Mass (Da): 11470
Location Topology: Multi-pass membrane protein
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A0A5C6EF42 | MKGAALSDSDASEPRDSQPLLFESHSHTPLCNHAIGEPTLYAAAAKNRGLRGLIVTCHNPMPDGFSSRVRMREDQLDEYIDLVDDTRQQWAGSVDVRLGLEADYFEGYEAYLEKQLSSADFHFVLGSVHPQIDEFRQKYWSADPIEIQRTYFRLLAKAAKTGLFDSLAHPDLIKNMFSDSWNEQAVIDDIRSALDDIADTGIAMELNTSGVNKMISEMNPFPGMLREMQTRGIPVTLGADAHQPERVADGYETALELLADCGYKHVNFFLDRKRHSVAIDDAMASLVHPTTIG | Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 8/9.
EC: 3.1.3.15
Catalytic Activity: H2O + L-histidinol phosphate = L-histidinol + phosphate
Sequence Length: 293
Sequence Mass (Da): 32706
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A0A919P6B9 | MRAPAHTHHRRVLRAHAPPRAERTHPPPRAERTRAPPRAERTRAPPRAERTHSPPRAERTHSPPRAERTHAPPRAAHAPTTYPTRTRRRPHHPVHPHRHIRRLGSAGSPSPSDRIVMNALKPWHIVVLLVVILLLFGARRLPDLAKSVGESLRIFKREVKDLQSDDEPRTAPTPPPTADPAPPIAQPTVNPAPTASPAPSLDPRVQQPPAGGSTTPSA | Function: Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes. TatA could form the protein-conducting channel of the Tat system.
Subcellular Location: Cell membrane
Sequence Length: 218
Sequen... |
A0A2X3FA23 | MRIPRIHHPERLIVGSQIALSDDAANHVGRVLRMTAGQHLQLFDGSNQVFDAVITEAGKKNVTAEVLSGEPDDRESPLHIHLGQVMSRGEKMEFTIQKSIELGVSLITPLFSERCGVKLDAERLQKKIQQWQKIAIAACEQSGRNVVPEIRPAMQLEAWCAEQDSGLKLNLHPRASASINTLPLPVERVPSADWPGRRAVG | Function: Specifically methylates the N3 position of the uracil ring of uridine 1498 (m3U1498) in 16S rRNA. Acts on the fully assembled 30S ribosomal subunit.
Catalytic Activity: S-adenosyl-L-methionine + uridine(1498) in 16S rRNA = H(+) + N(3)-methyluridine(1498) in 16S rRNA + S-adenosyl-L-homocysteine
EC: 2.1.1.193
S... |
A0A378C1X2 | MGVDLIEQPVSAHDNAALVRLSQQIETAILADEAVATAYDGYQLAQQGFTGAYALKIAKAGGPNSVLALARVAQAAGIGLYGGTMLEGTVGTVASLHAWSTLPLQWGTEMFGPLLLKDDIVSVPLTFADGQVALPQTPGLGVELDEDKLHFIPASRSGEQEKKMLFKVEMTVNIPPGFPANEAEEIKKREKAYSQQLQREGKWRHIWRVAGLYANVSIFDVQDAEELHQILMGLPLYPFMAIKVEALCRHPSSIRDDDR | Pathway: Aromatic compound metabolism; beta-ketoadipate pathway; 5-oxo-4,5-dihydro-2-furylacetate from catechol: step 3/3.
EC: 5.3.3.4
Catalytic Activity: (S)-muconolactone = (4,5-dihydro-5-oxofuran-2-yl)-acetate
Sequence Length: 259
Sequence Mass (Da): 28208
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A0A3E0JQN7 | MGRFPYSPVLTLHRTRTQIFISFLVVMGVVLLVSGQYLYRNVSQLILSNAEAQVGETADQISARLDAVLSEVDTLTLQLAMDPRVQGMLLKIYRNQAVSVDDRLSLRPITENLMAFSWAIEGVEIYADRSPLYPLDLPRLHNRVDEDTIRIADERGGPLVWRGPIRRNPDQLLAIRQVPLEDEKLKGGGYIVAWVRSSILDFIRTEFSSPTGMLVRVYDENGTILAESHSAAETAGDQAAGATGWDLAAGNEEAYLKIDRRSSVTNWSISILVPKHNLTGGLELFRRALVWSLLVGTAVSLLLMGVVSGMITRPIRRLRR... | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Membrane
Sequence Length: 589
Sequence Mass (Da): 66200
Location Topology: Multi-pass membrane protein
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R5M334 | MREKVSRYMEKNGMLKAGQRVVVGLSGGADSVCLLSLLSDMRSSLSIRLRAVHVHHGLRGQEADRDADFSRELCRKLDIPFILKMENAHQEAQNRRISEEEAGRLLRYEAFEQEAARWEDKEREQEGAALPVRIAVAHHGDDSAETILYHLFRGSGLRGLAGIAPVRGRVIRPLLCVSRQEILEYLREEGLSYVTDSTNLLNDYTRNRLRNQILPMAVQEINRGAVEHILRAGEIIGEADQFFRERAGKFLKKEGIWKESCLEKSRMLAVPVSALGSLAHIEQGYVIREAFSELGWPLRNIDASHIESILSLLDGRTGAG... | Function: Ligates lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine.
Catalytic Activity: ATP + cytidine(34)... |
L0DXG2 | MPLPPETLKEHQRRIRLLILDVDGVLTDGSLFLGDAGEEYKAFNSRDGHGIRMAQQGGLELAILTGRSSEVVLHRMRDLGVEHILQGRREKGDAVTELLAQSGYQPEHAAFVGDDVVDLPAMRRVSLGIAVADAHPLVLENAHWVTAAPGGRGAVREICEQLLAARGSLEKILDAYLRH | Function: Catalyzes the hydrolysis of 3-deoxy-D-manno-octulosonate 8-phosphate (KDO 8-P) to 3-deoxy-D-manno-octulosonate (KDO) and inorganic phosphate.
EC: 3.1.3.45
Catalytic Activity: 3-deoxy-alpha-D-manno-2-octulosonate-8-phosphate + H2O = 3-deoxy-alpha-D-manno-oct-2-ulosonate + phosphate
Sequence Length: 179
Sequenc... |
G9MS03 | GISNIILLSTFIYATAPASGGHLNPMISFSAILTGLCSVPRGILYMCGQTLGGALAGGILLGVWGPERATSLKGGGCWYDPSQANPGQIYLNEVFASFVLLFLSFGVGLDPRQAALFGPRMGPLLVGASLGLVSFSTSGIIPGYAGA | Catalytic Activity: H2O(in) = H2O(out)
Subcellular Location: Membrane
Sequence Length: 147
Sequence Mass (Da): 14967
Location Topology: Multi-pass membrane protein
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A0A1J5B8N6 | MLYKLIIIGSGPAGYTAGIYAGRAGLNPLLFAGEKSGGQLINTMVVENWPGAKDGVTGPKLMRDLREQAEKFGTKIIDKKVIKVDFSNRPFEIFTPEVKDAHTSGVYAAGAIIVATGAESIKLNIPGEERLLGRGVATCAVCDALFYRDKKAAVVGGGDAAVEDALALTKFAKEVVLVVRREELRASKIMQQRVENNPKIKILWKSQVTEIMGEDKVEAIKINNAETVKTDGVFLAIGHKPASGIFKGQLDLDEKGYIKVWQTMTSVQGVFAAGDCVDYRYRQAITAAGMGCQAAIDAEKWLENQSQ | Cofactor: Binds 1 FAD per subunit.
EC: 1.8.1.9
Catalytic Activity: [thioredoxin]-dithiol + NADP(+) = [thioredoxin]-disulfide + H(+) + NADPH
Sequence Length: 307
Sequence Mass (Da): 33183
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A0A1H2GZU6 | MNELFKNVQQVWTGIPANRRMPILIAAAVMIIALTTVIVYSANKPKMDVLFGGMQITEAAKVVDFLKQKKVPYELADQGRTVRVPSTEVDGLRLGLAESGIPRADDTAGGSGFELFDKPSFGMPDFMQKANYNRAIQGELARTIRHMDDVEQARVMIVTPEQRLFQKDQKEAKASVFLLLKSGRSLGPNQIKAIQFLVANSVEGLQPNHVSIVDSTGKSLVENDEGNSLGALSNTQLAAKKAYEDYLRQKVQVMLDQTLGMNQSSVQISADLNFDAVQQTSEQFDPKSQVISQETISNESTHSKTSGTDATVGSKTNTEQ... | Function: The M ring may be actively involved in energy transduction.
Subcellular Location: Bacterial flagellum basal body
Sequence Length: 533
Sequence Mass (Da): 58549
Location Topology: Multi-pass membrane protein
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D6Z1H2 | MKVGHPCPTTATSHCSLRDDSGWLLVTAATAMELEPLRQSLNGGNYSGRGAEIDFLNCGVGPTATAASLAAWLACRPGRYAGVIMTGVAGAYMLESAGAAVQSARVLDICVAEREVLGDFGLACDHGADPFDNPQLAAEREFSLHHQLLQTACDTLRQRRIPFHRGTFVTVNAASTTRRRGMALAHRHLALCENMEGAAAALVCQRLGLPLLEIRCISNLVEDRDLSRWQLPEAVARNAEILSLLLPELLAAVAASS | Pathway: Quinol/quinone metabolism; menaquinone biosynthesis.
Function: Catalyzes the hydrolysis of futalosine (FL) to dehypoxanthine futalosine (DHFL) and hypoxanthine, a step in the biosynthesis of menaquinone (MK, vitamin K2).
EC: 3.2.2.26
Catalytic Activity: futalosine + H2O = dehypoxanthine futalosine + hypoxanthi... |
A0A293LJQ7 | MTTDITRGQPEVIGLDRPELKKRHNLTDTIDLIKQTEYVPLPKGEFLKGDIINAQTTTTTTTTTTAASKPVPKEVPEKEFNAQIVWRNVAIFAALHSMALYGFYVALAHAMWSTWLVAFIWGQCAGLGVTAGAHRLWSHRAYKARFPLRVVLMIFNCMACQNDLYE | Subcellular Location: Membrane
Sequence Length: 166
Domain: The histidine box domains are involved in binding the catalytic metal ions.
Sequence Mass (Da): 18684
Location Topology: Multi-pass membrane protein
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H6AZR4 | LYLLFGAWAGMVGTALSILIRAELGQPGALLGDDQIYNVVVTAHAFVMIFFMVMPMMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAMTQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPIF | 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... |
A0A3Q1N9C3 | MPALHIEDLPEKEKLKMEVEQLRKEVKLQRQQVSKCSEEIKNYIEERSREETVLDTNPFRSTLVISFTT | Function: Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein-effector interaction.
Subcellular Location: Cell membrane
Sequ... |
E1B928 | MAAAAAAGPEGRLVSQEAAAAAPERGGGSCVLCCGDLEATALGRCDHPVCYRCSTKMRVLCEQRYCAVCREELRQVVFGKTLPAFATIPLHQLQHEKKYDIYFMDGRVFALYRQLLQHECPRCPERPPFSLFGDLEQHMRKQHELFCCKLCLRHLQIFTHERKWYSRKDLARHRMQGDPDDTSHRGHPLCKFCDERYLDNDELLKHLRRDHYFCHFCDADGAQDYYSDYAYLREHFREKHFLCEEGRCSTEQFTHAFRTEIDLKAHRTACHSRSRAEARQNRQIDLQFSYAPRHSRRSEGVIGGEDYEELDRYNRQGRTG... | 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: 946
Sequence Mass (Da): 102727
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A0A2X3C6V8 | MKNNNTAPARTAPSTSTAAAKPTVTAPSGPRAISRVQPSYPARAQALRIEGTVRVKFDVSPDGRIDNLQILSAQPANMFEREVKSAMRRWRYEQGRPGTGVTMTIKFRLNGVEIN | Function: Interacts with outer membrane receptor proteins that carry out high-affinity binding and energy dependent uptake into the periplasmic space of specific substrates. It could act to transduce energy from the cytoplasmic membrane to specific energy-requiring processes in the outer membrane, resulting in the rele... |
E0NTZ3 | MTYTELWHRLTPLYDSNEAKAIVRIVLEERFGLSVTDIYTGKVTQLSAHAVAELRKIMMRLEQAEPVQYVLGKACFYGRSFTVSQGVLIPRPETEDLCTWVIETVLSSFSCPEPCLLDIGTGSGCIAATLALNIPHAHVSAWDISPEALVVARANVKALKASVDVAEVDALNLPSDSDRWEIIVSNPPYICRKEKADMEDNVVCYEPAEALFVPDDDPLLFYRAIARYAFSALRVGGMLFFEINPLYVQSLETLLCETGFKDTELKLDRFGRQRFIKVMR | Function: Methylates the class 1 translation termination release factors RF1/PrfA and RF2/PrfB on the glutamine residue of the universally conserved GGQ motif.
EC: 2.1.1.297
Catalytic Activity: L-glutaminyl-[peptide chain release factor] + S-adenosyl-L-methionine = H(+) + N(5)-methyl-L-glutaminyl-[peptide chain release... |
D6Z0C1 | MNAYLNLAVVGPGALGCLLAARLHLAGACRVRLVDHDAGRAATLNRQGIILEGPAAPSASPLPIPVTADYADTAGCSAVIFCVKSLTLPQALADAVPFADPATPFITFTNGISHLEQLCRLRGRCLPVPGICTAGATLLAPGRVRPGGPGTLTMGHVDSASSHWAHNLADPLHQISQTFRQAGFDTRISTNIQRELWHKLLVNVGINALTVVHDCPNGRLLEIPAARQQMALAVNEAAAVAEASGIALGMDPLAMVEEVCRRTATNISSMLQDIRQHRATEIMAINGEIVRRAHQLGMTAPANEELTKAIKQRHPKQ | Pathway: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantoate from 3-methyl-2-oxobutanoate: step 2/2.
Function: Catalyzes the NADPH-dependent reduction of ketopantoate into pantoic acid.
EC: 1.1.1.169
Catalytic Activity: (R)-pantoate + NADP(+) = 2-dehydropantoate + H(+) + NADPH
Sequence Length: 317
Sequen... |
A0A4S2H9G8 | MSTRASDTSLEGQRPLSPHLQIWRWHATMATSIFHRASGVGNYIGAIALTLFLIVLSGGPESYASIAFLFEGALGWVTRIVMFLLTLSYSYHWLNGLRHLVWDAGAGFDPKVANRVSWLVMIATPIPAIVIWVLALGVAQ | Cofactor: The heme is bound between the two transmembrane subunits.
Function: Membrane-anchoring subunit of succinate dehydrogenase (SDH).
Subcellular Location: Membrane
Sequence Length: 140
Sequence Mass (Da): 15379
Location Topology: Multi-pass membrane protein
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A0A897MWE2 | MSGTHPLVRVETLLLIAVGGFAGSNLRYFIELIVPSTLGATFLVNVLGSFALAVILYEASTIGALSDRSKFVFGTGFLSSFTTFSTFVFDVISVDPVVGLAYVLASYASGFAAVLLGRVFVTRAIVPRVEVA | Function: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Subcellular Location: Cell membrane
Sequence Length: 132
Sequence Mass (Da): 13917
Location Topology: Multi-pass membrane protein
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A0A354DKN7 | MTKKVEIKDHNTLFQSEKYQQQVENKREFENPCTLQEVEEVKEYTKTEEYKDKNFAREGLTINPAKACQPLGAVLAGLGFEGTLPFVHGSQGCVAYFRSHFSRHFKEPVPASSSSMTEDSAVFGGMRNLVEGLGNSASLYKPKMIAMSTTCMAEVIGDDLQAFIETARQEGNISEDFPVPFANTPSFVGSHITGYDSMMKSILSYLFEKEPGEIDKTEKINLIPGFETYTGNIVELKKILSLMGVEYTVLGDHSDNLDSPANGEYELYY | Cofactor: Binds 1 [8Fe-7S] cluster per heterodimer.
Function: This molybdenum-iron protein is part of the nitrogenase complex that catalyzes the key enzymatic reactions in nitrogen fixation.
EC: 1.18.6.1
Catalytic Activity: 16 ATP + 16 H2O + N2 + 8 reduced [2Fe-2S]-[ferredoxin] = 16 ADP + 6 H(+) + H2 + 2 NH4(+) + 8 oxi... |
A0A4Y8WRZ6 | MKKGIKITLWTMVALLLVSGAAIFYLGYRFAYKSGFNIGGELPARLYVYPGMDWGMVCDSISERTEAPLLWDLKWQLKHRAKGQPIVGAYTIEPNMTVRALYNRLVYGMQTPINFYFNSSRLPEQIYARMDKLLLADSLSIARAMNDSALVHSLGIPDTTLVYYLHPNTYEIYWDITPEKLVKRMAEESKAFWSSDRRSKAEAIGLTPYEVINLAAIVQEESSKVDEYPMIAGLYLNRLRMGMRLQADPTVKFALKDFGLRRIRQEHLRVDSPYNTYQVVGLPKGPIRIPSAEAIDGVLNAEEHHYIYMCAKADFSGYHA... | Function: Functions as a peptidoglycan terminase that cleaves nascent peptidoglycan strands endolytically to terminate their elongation.
EC: 4.2.2.-
Subcellular Location: Cell membrane
Sequence Length: 345
Sequence Mass (Da): 39481
Location Topology: Single-pass membrane protein
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A0A919LPW9 | MIVGGDRGTAGAIRMCGEAALRSGAGLVRVLTHPENVAPIVTVRPELMVDELTPQTLKAALEWADVVAIGRPGQREWGRSALRTVESFNKPMVWDADALNLLAFNPDKRHNRVLTPHPGEAARLLNVSVAEIESDRLLSAQRLVKRYGGVVVLKGAGTVVASESGAMGIIDAGNAGMASGGMGDVLTGIIAALLGQHLTPYDAACAGCVAHGDAADRLAAREGTRGMLATDLFPRSGVLLTRM | Function: Catalyzes the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. Together with NAD(P)HX epimerase, which catalyzes the epimerization of the S- and R-forms, the enzyme allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or ... |
A0A136MEN3 | MISVNNLRRGLLVEVEGTVYAVVEYQHHKPGKGHAIVRVKLKNAQTGAVIDRTFNGKEKIPLANAQRKKMQFLYNDDQWHFMDQVSYEQVALSADEVDDSANYLTEGLEVEILFNEGRPLAIDLPSAVVLKVTYSEPGLKGDTATGATKKATVETGYVIDVPLFINEGDMLKIDTRTGDYLERAR | Pathway: Protein biosynthesis; polypeptide chain elongation.
Function: Involved in peptide bond synthesis. Stimulates efficient translation and peptide-bond synthesis on native or reconstituted 70S ribosomes in vitro. Probably functions indirectly by altering the affinity of the ribosome for aminoacyl-tRNA, thus increa... |
I6PQL6 | LLIRTELIQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASAGVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILASINFITTIINMKPPAISQYQTPLFVWSILITAVLLLLSLPVLAAGIT | 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... |
F5S5G2 | MSKHILLAITGSIAAYKSCELVRLLKKQEHEVTVAMSEAACTFVTPQTFQALSGNPILTAQGGAGNGMAHINATRAADIMLIAPASANTIAKIAHGIADNIITEMVAARNCPLVLAPAMNVEMWQNPANLRNIKQLQADGVHIMQPAHGEQACGEVGVGRMLEAAEIADLLPDFWSPKPLLHKKIVITVGATYEAIDPVRGITNISSGQMGVALARACRRAGANVVLIHGKMQAALPVGMAHTQEAISAKAMYDAVLEHLPNADAFIAVAAVADYRVSNQSAQKIKKDQSGKPPVIKLAENTDILQQVAKSENAPFCVGF... | Cofactor: Binds 1 FMN per subunit.
Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 2/5.
Function: Catalyzes two sequential steps in the biosynthesis of coenzyme A. In the first step cysteine is conjugated to 4'-phosphopantothenate to form 4-phosphopantothenoylcysteine. In the se... |
A0A076H7F5 | MRNLLRLPALAAVLITLGVSGCASDQSSSKPAPTAETANATEGRATWYGPGLYGNKTASGEVLKEGTMTAAHSSLPLGTEVKVTRLDTDESVTVVINDRKPYKEGTVIDLAHGAADALDIDDDGTANVSIEVMD | Function: Lytic transglycosylase with a strong preference for naked glycan strands that lack stem peptides.
EC: 4.2.2.-
Subcellular Location: Cell membrane
Sequence Length: 134
Sequence Mass (Da): 13902
Location Topology: Lipid-anchor
|
A0A3D8GP81 | MLGLSPIYLSLAAAAMSSGFVYAGIKCSSYFSHWRWFEKISFFPGVLLIILGIWKLYSIGVIIMVLTIGLTGGIASGKSTVANMCKEMGIPVIDADIEARLAVEPSEPAYRKIVEAFGPGILLPNGELDRQALGALIFHDVAKRNLLNGIVHPEVRKRMAEKREAAEKSGAEVIILDIPLLFESKLTHLADRTLVVQVDWETQLSRLMARNSFSKEEAEARIRSQMPLSEKAALADAVIDNNKGIEETKRQLLEILARWRAEHVI | Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 5/5.
Function: Catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A.
Catalytic Activity: 3'-dephospho-CoA + ATP = ADP + CoA + H(+)
EC: 2.7.1.24
Subcellular Location: Cytoplasm
Sequence Le... |
A0A0D6QCT8 | MTELPIRTLHLLAGAGPGYLPAQASSVAAGVDRVFLFLFWGSAFFLALIILLTIVFVLRYRRRATRLHPEPSPAHSTRLELVWTVIPLVLVLALFAMSTRTWIQMTSADPGADPVRVQVTGRKWSWWFDHPSGKGANELHVVAGRPVELILSATDVIHSLYVPEFRLKQDAVPGRFTRLTFTPTVPGSYPILCAEYCGTDHSRMLSTVVVHADQASFDAWSKEGLPADATLAELGEQVFAEKGCAACHSVDGTRSVGPSVRGLWKRHEKLADGTTALVDEEYLRESLVKPGAKVVAGYPNIMPPMPLEERELKAVAAYLE... | Cofactor: Binds a copper A center.
Function: Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B).
EC: 7.1.1.9
Catalytic Activity: 4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(... |
A0A377WL38 | MLGISGGQDSTLTGKLCQIAINELRAETGDSSLQFIAVRLPYGVQADEQDCQDAIAFIQPDRVLTVNIKAAVLASEQALREAGIELSDFVRGNEKPVSE | Pathway: Cofactor biosynthesis; NAD(+) biosynthesis.
EC: 6.3.1.5
Catalytic Activity: ATP + deamido-NAD(+) + NH4(+) = AMP + diphosphate + H(+) + NAD(+)
Sequence Length: 99
Sequence Mass (Da): 10606
|
A0A372BZX0 | MARARSERLVIHAAGSQWSWAQVDRGSRVTDSGGCDPAEPDWPLDRPAIVLLDASRCLGLKLDLPPLRGHKLQQAMRWAAEEHLAGSAEDEHVVAGPRDDAGQLCCVSIANAVMADLAARLEYVEAERMLPDALCLPWQPGRVSLAENDGRILVRWGDWSFTSFDAELAGDMVDSVAPADTEWDWYGGERPDWVDLRGAADRGDGQPLPAILVRQADSVDLNLLAGSWAPRSAATTRSRWRWTAILAAVAVVLIIGHAALERYQLGQRSAELETAIEQQFQQAFPDVGRIVRPKAQAERELARLRFGQAAGLLDLMHRVA... | 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: 391
Sequence Mass (Da): 42629
Location Topology: Single-pass membrane protei... |
A0A4Y8WPJ0 | MPNPFPTIDPKHLIAYGKVRRTHGNQGEVILALVSPAFEVLEPQFLFLLIDEIPVPYRLASIRGGGEQFIIGFEGIDTLTDAETLVGLEAQIHQDELPEEHSNISLTFRNYQLQHVGGELIGRIVDIDSSTTNILILIERPNHSEVTIPLVEQWIASIDDHHRIITMDFPLELLDL | Function: An accessory protein needed during the final step in the assembly of 30S ribosomal subunit, possibly for assembly of the head region. Essential for efficient processing of 16S rRNA. May be needed both before and after RbfA during the maturation of 16S rRNA. It has affinity for free ribosomal 30S subunits but ... |
F1MIF7 | ISVEVVNNVTEFIFLGLSQDPGMQLMLFALFLLFYMVILGGNLLILLMVFSDPRLHTPMYFFLSNLSFVDIAYSSATAPKMIADFVSEKKIISYWGCVTQMFTFHFFGCTEIFVLTVMAFDRYAAICQPLRYANIMSTTACTLLASLSWLGGLAHSFVQTLLTFQLPFCSSQIIDHYFCDVHPVLKLACADTTLVNMLVIANSGLISLGCFLILLASYTVILVSLRKQSAEGRRKALSTCGSHFTVVTSFFVPCIFIYLRPSTTFPLDKAVSVFYTTITPMLNPLIYTLRNKDVKNAMNRVWNHKVSLKEKRKA | Function: Putative odorant or sperm cell receptor.
Subcellular Location: Cell membrane
Sequence Length: 314
Sequence Mass (Da): 35312
Location Topology: Multi-pass membrane protein
|
A0A3Q1MPJ5 | MGKRISGRGGASEDAGVFGIRPPRWPSWGGDYETQSRWVFVYEKGYQTSGSLISSVSVKLKGLAVTQLPSLGPQVWDVADYVFPVQGDSSFVVMTNFIATPRQAQGHCAENPEGGTCTNNSGCTPGKAERKAQGIRTGKCVAFNDTVQTCEIFGWCPVEVDDNIPCPALLREAENFTLFIKNSISFPRFKVTRRNLVEEVDARYMKTCLFHKTLHPLCPVFKLGYVVQESGQNFSTLAEKGGVVGITIDWHCDLDWHVRHCKPIYEFHGLYEEKKLSQGFNFRFARHFVENGTNYRHLFKVFGIRFDILVDGKAGKFDII... | Function: Receptor for ATP that acts as a ligand-gated ion channel.
Subcellular Location: Membrane
Sequence Length: 390
Sequence Mass (Da): 43440
Location Topology: Multi-pass membrane protein
|
A0A2Z6LPU9 | MENQTRVRCPENEELASFMKNKWKEMASQPKGLSDNIEMALSKAHFNVCNSKNPIRTIKDFSTVKGVGKMMLKLMQGFFGTGSGGTEPDDLTKKGKKTKGTKRYVPQRNSVAYALLITLYRGTSNGNEFMRKQELIDAAEASGLSRAPIAPEKGKGKPGHFGSSPQDWYSGWSCMKILISKGLVVKSSCPAKYMLTQEGKEAACDCLKRSGMAESLDKSASVEIPIHMDKQNSLDMEVDARDLESEVTSPLNKQKKPLDVPLDSLERFTKMGYSKEQIITAFEDVSRSHPNKDVSSLWPAVLCQLREEQVYGSQPESRIM... | Function: Interacts with EME1 to form a DNA structure-specific endonuclease with substrate preference for branched DNA structures with a 5'-end at the branch nick. Typical substrates include 3'-flap structures, D-loops, replication forks and nicked Holliday junctions. May be required in mitosis for the processing of st... |
K5XEX2 | MSKSFKDRPRNALCLFDVDGTLTLARQGASKEMIDTLRQLRKNVAVGFVSGSDLAKIIEQLETNGFNVINDLDYAFAENGLSAYKLGQLLPSESFINFVGEEKYKVLVNFILRYLADMDIPIKRGTFIEFRRGMINVSPIGRNATIKERIEFEKLDKEKRYREKFVQVLREKFSDYGLTFSIGGQISFDVFPNGWDKRYALRRVEDEGFDEIHFFGDKTFEGGNDYEIFADPRTIGHSVNNPEDTIRILKEQFL | Pathway: Nucleotide-sugar biosynthesis; GDP-alpha-D-mannose biosynthesis; alpha-D-mannose 1-phosphate from D-fructose 6-phosphate: step 2/2.
Function: Involved in the synthesis of the GDP-mannose and dolichol-phosphate-mannose required for a number of critical mannosyl transfer reactions.
Catalytic Activity: alpha-D-ma... |
A9V986 | MKRRYNEVNNLPTNEDVDATTAALELEHEKHTKVKFVNRIYFGVYAMDTWYFSPYPDEYGKSPALFVCEWCLKYMLQPTSLRDHDCQHRQPPGREIYRKGNVSVYEVDGAEHKLYCQNLCLLAKVFLDHKTLYFDVSTFLFYILTEVDADGAHFVGYFSKEKVSVDNNNLACICTLPPYQKKGYGRFLIEFSYALSQAEGKIGSPEKPLSDLGKLGYRSYWSWLLLNALRGKKGTISMPALSKATGIAPDDVFNTLQALNLTKYWKGEHVVCITPKLIDDLLATGKFKGPKVPVDVRCLRWSSPL | Catalytic Activity: acetyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-acetyl-L-lysyl-[protein]
EC: 2.3.1.48
Subcellular Location: Nucleus
Sequence Length: 305
Sequence Mass (Da): 34857
|
L0EB51 | MIIGLTGGIACGKSTVAAMLSERGAFVVDADRIAREVVMPGEPALAEVAAVFGQAVIRDDGTLDRRKLGEIVFADPDKRRQLEAILHPAIRERMWTLIRQAKADEPGRMVVADIPLLYETGQEGLYNGVLVVYVPREMQIKRLLARNPELDEAQARERIDAQMDIERKKELADWVIDNSGSLESTKRQVEALWRRLSDMRKP | Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 5/5.
Function: Catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A.
Catalytic Activity: 3'-dephospho-CoA + ATP = ADP + CoA + H(+)
EC: 2.7.1.24
Subcellular Location: Cytoplasm
Sequence Le... |
A0A7Y3W4Q9 | MSATIFAKASGSGRSGVAVYRISGPEAGRVLSTLTGSTGKPRAARRVTVRDGDGAQVDDGLALWFPGPASFTGEDVAELQLHGSIAVERRLTEVLTGLGIEPAGPGAFSMRAFANGKMDLTQAEGLSDLLEAETELQLKQALAGHSGQLRALADEWRGLLISALAQLEAAVDFPDEEDVPAQIAERALPLVRDVRTALSDQLATAARARRVAEGVTIAILGPPNAGKSSLFNRLVADERAIVSPEEGTTRDVVSERVELHGHLVSFLDTAGVREDPSSSVEATGIGLAVRAAEQADLRLLCYPSGAGDLPGWLQSYRRDG... | Cofactor: Binds 1 potassium ion per subunit.
Function: Exhibits a very high intrinsic GTPase hydrolysis rate. Involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34.
EC: 3.6.-.-
Subcellular Location: Cytoplasm
Sequence Length: 430
S... |
A0A2X3CRM3 | MDKLQAIRGIAFDLDGTLVDSAPGLTSAVDNALYALELPVAGEERVITWIGNGADVLMERALTWARQERATLRAAMGKPSVDDHDIPQDEQLRILRKLFDRYYAEAAEEGSFLFPAVADTLGALHAKGLPLALVTNKPTPFVAPLLDALDIAKYFTVVIGGDDVQNKKRIRNRCCWWRKSSLWLQPSCCLSAIRAMIFRRPKRQAAALLV | Pathway: Organic acid metabolism; glycolate biosynthesis; glycolate from 2-phosphoglycolate: step 1/1.
EC: 3.1.3.18
Catalytic Activity: 2-phosphoglycolate + H2O = glycolate + phosphate
Sequence Length: 210
Sequence Mass (Da): 23261
|
A0A4Q5PYJ2 | MIDSSEVQKPELIRRYIVVGSRRFSNYWWASVILLGGFGFLLTGISSYLSFNLLPFINEKNILFFPQGLVMCFYGILGLIFSCYLWLTIFWGVGGGFNEFNKRQGIVRIFRWGFPGKNRRIDLSYDIKDIEAIRVEIKEGLNPRRILYIRVKGNTTVSNPVKDNENLLPASNDKKLSINPVDSSLMKGKKNVVGITKNLSLQNKRDIPLTRIGQPTTLEDIEKQAAELAKFLQVSLEMI | Function: Seems to be required for the assembly of the photosystem I complex.
Subcellular Location: Cellular thylakoid membrane
Sequence Length: 239
Sequence Mass (Da): 27286
Location Topology: Multi-pass membrane protein
|
A0A6I2GTR7 | MSDIWTVRRVLTWTTGHFEKRHIDSPRLTAEVLLAHVLKVGRVRLYVDLDRPLSKEELALFKALIERRMAGEPTQYLTGVREFYNRPFKVDPRVLIPRPETELLVEAALHALPKDAPARALDLCTGSGCIAISLAAERPQAEVVAVDLSPDACALARENAEALGVGARVSVLHGDLYAPLPPAPRFRLVVSNPPYVGTGEIAGLSAEVRREPRMALDGGADGLALVRRVVTGARKWLEPGGLLALEIGETQGAALLALLTEAGFESPRVERDLERRERMAFGTQPAAAEPQPS | Function: Methylates the class 1 translation termination release factors RF1/PrfA and RF2/PrfB on the glutamine residue of the universally conserved GGQ motif.
EC: 2.1.1.297
Catalytic Activity: L-glutaminyl-[peptide chain release factor] + S-adenosyl-L-methionine = H(+) + N(5)-methyl-L-glutaminyl-[peptide chain release... |
A0A076HA27 | MSDATGIVVALQANYLEVELDSAPEGVPPRLLCTRRTRLSHRGEVVHVGDRVVVEAIDSVQGRAVVARVDARSSLLSRPPVANASTVVVALAVEQPGFDPDQASRFLLTAERTGLAVELLLTKADLVSRDHLEALQVRLQGWGYAPIAVSSRTDEGLDRVRQRLSASPLTVVCGPSGVGKSSLLNRLMPHLALRVGAVSGRLQRGRHTTRHVELFPLAEGCRVADTPGFNRPDLPDEPREFALLFPELRHQLDPWPCRFRDCLHRAEPGCGIRRDWERYDLYTTGLEELSKLSRSSRAG | 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... |
A0A8J3YI91 | MDGDSVERSGGYPPRRRGRPRRPAAAPPPPIPSAEWDIGQAPSANGNGRSHGNGRRHGRSPEEEYLDEEPARGRYDRGRRDPRGGRPAPVDREPWSGRSREQTNGYGQRPVDPGLTNGRGAGRVPPDATNGRGIGRTSGAPVSGIPRGAEPGATNGYGQRPVDPGSTNGRGIGRTPGAPVSGIPRGADPGSTNGRGLGRDAINGRGIGRDATDGRGIGRTPGAPVSGIPRGAGRDATNGRGIGRVPDEPVSGIPRGIDPGSTDGRGIGRVPGETTTGRRGRGSADPWSTRSGREPADGWPRSPESTNGYGRARLPLPIDP... | 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: 667
Sequence Mass (Da): 71450
Location Topology: Single-pass type II membrane protein
|
A0A921ZI88 | MLACERNSCRLALTDHSQSVGIMEIELKEAGTMLSTGIHLWSVEVLNQTKHHRCKALRTVGKQWRSWVIQVKKAKAIYHTMNMFNMDVTKKCLIGQCWVPSLDVKRVQDILEYCTQVVDTNVPSFMYKTVSKAVPPTFYRTNKFTNGFQVLIRAYGESAYRELNPGLYAVVTFPFLFAVMFGDVGHSIIILSMALWMVRKEKQFMSKKSDNEIWNIIFGGRYVLLLLGVFSFFTGFVYNDYFGRGLVLSHSYWYNTYTEVDLANTEILELSPADATRKPYLFGFDPLWELSKNKVMIDNSIKMKLSIIIGVVHMIFGLVL... | Function: Essential component of the vacuolar proton pump (V-ATPase), a multimeric enzyme that catalyzes the translocation of protons across the membranes. Required for assembly and activity of the V-ATPase.
Subcellular Location: Membrane
Sequence Length: 619
Sequence Mass (Da): 71958
Location Topology: Multi-pass memb... |
A0A0G1KNQ2 | MKYVVANWKQNFNLVDTENWCSEFLHKITTYDLRNTHIIVCPPLPFLTKAREFLSPAGIFVGAQDISEWNSGAHTGYVGGRQLVGLCSYAIVGHSERGEPRESVERKVEVSLNSGIQPIVCFKSPSDFAAYKSSIYALEDPANISKGGVYSPKPISNVTELVKEARAFFGSGAPIIYGGSVTSETAGELAGVSGLDGVLVGNASLNPIEFAGIVEKFIL | Pathway: Carbohydrate biosynthesis; gluconeogenesis.
Catalytic Activity: D-glyceraldehyde 3-phosphate = dihydroxyacetone phosphate
EC: 5.3.1.1
Subcellular Location: Cytoplasm
Sequence Length: 219
Sequence Mass (Da): 23592
|
E0NS51 | MKNILHSDGKLACLIVLSILVIDQIIKIEVKTHMTLHQSIEVTQWFYISFIENNGMAYGMTFINKFMLSLFRLLAIGVIAIYLYKQVKVKARTRYIVFLSMVLAGAMGNMIDSMFYGLIFNASSPYYVSYFVPWGNGYAPFLMGKVVDMFYFPLIVSTWPDWVPFWGGQEFIFFSPVFNFADACISVGFVLLMIYCRQDLSTISFRLKKKKD | Pathway: Protein modification; lipoprotein biosynthesis (signal peptide cleavage).
Function: This protein specifically catalyzes the removal of signal peptides from prolipoproteins.
Catalytic Activity: Release of signal peptides from bacterial membrane prolipoproteins. Hydrolyzes -Xaa-Yaa-Zaa-|-(S,diacylglyceryl)Cys-, ... |
A9VBD8 | MQLGVLTVTTSRTAATDASGGVLAEAFDGVFERVERGVVDDDVEAIQAAMLSWIREWDPDCILTTGGTGLDARDVTPEAVRGLLDREAPGIATMLTVQSLAKTPMAALSRFVAGVKRQTLIICLPGSPKACRECAEMLHPVLRHAIDTIRGRKRAVQKVHHTMQADTATTGNQDHTVSAPTPPAHTGCNCGRDAPVTSVQTSDYPVFYAAPPVPSETASERGSGAAARHRKSPYPMLPWSMARQRGLEALTPLRPVQRDVAAVALHEVLASPVTSTVNVPAYPASIKDGYAVRAADVDVESSASPVQLTVQGVSTAGAGW... | 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 ... |
A0A2S8FAJ0 | MAADEILLHIKDSYYFEVPKWLWKHDHQSHSDFPDVWVKLDPGFQSWQAHEVYHRLAEDGAVGLPSEADFIHDYEHWLHEPGNHGKPITRYLTHKVDESLTSGGEALVWAERGVEVAEEYTVADYKALPADHQHVKWAPTKIEGYNQALSGKILIPQVFGGELRNLYQKEAGFAISKFMVIEFFVAVIITAVFIAYARRVSQGQLPKGWFWNLIDVFITFLRKDVAKANIHHGADHFVPIIWTLFFFILGCNLFGLIPWMGSPTGSISVTVTLAVAVLFIGMAAGARTFGVVGVWLNLVPGMELPTVIAIIIKPMMFIIE... | Function: Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane.
Subcellular Location: Cell membrane
Sequence Length: 411
Sequence Mass (Da): 45675
Location Topology: Multi-pass membrane protein
|
A0A0D6QMM9 | MADERFLAKLWATIESRRADAAPAESYTKKLLAAPARIRRKIIEEAYEVNEAHQALLDGKDTKDHLAHEAADLLYHLYVLLASADVTPTEVYGVLERRHLQPPAPKTGNP | Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 2/9.
EC: 3.6.1.31
Catalytic Activity: 1-(5-phospho-beta-D-ribosyl)-ATP + H2O = 1-(5-phospho-beta-D-ribosyl)-5'-AMP + diphosphate + H(+)
Sequence Length: 110
Sequence Mass (Da): 12314
|
A9UZL6 | MSKSVASEAAACMSVEDVVAAVNGNVKHGLSAIEAGQRLREHGANEFATSEPDPLWQKYLEQFKEPLILLLIGSAVVSLIMQQYDDAFSIFLAIMIVVTVAFVQEYKSEQALEALTKLVPQKCWLIRDNTKQGALAADVVVGDLVTFGVGDRIPADCRLIEAVNLEIDESNLTGENKTRSKRCHHPSTPLPSQSILHLLLIRLRTLAILRDNMAFMGTLVRQGHGKGIVTATAGATEFGIIFQMLDDVEERKTPLQEQMGVLGQQLSFLSFGIIGVIMIIGVLQGKPLVKMFTIAVSLAVAAIPEGLPIVVTVTLALGVM... | Function: Catalyzes the hydrolysis of ATP coupled with the transport of calcium.
Catalytic Activity: ATP + Ca(2+)(in) + H2O = ADP + Ca(2+)(out) + H(+) + phosphate
EC: 7.2.2.10
Subcellular Location: Membrane
Sequence Length: 894
Sequence Mass (Da): 97155
Location Topology: Multi-pass membrane protein
|
A0A2S8F027 | MAAFGKDRDDGGSFAGVNFSAPSKTPHPIPRPSGARGSEYNAEEKILELNQRAHALVQPIIETPREIGAELVQLECGAKVLDLGVATGRGGLEAGRQMAEICLAGLGEVSFSLGDAPGTRTFVNVCTDRPELACIASQYAGWQIKTENFFGMGSGPMRVKAAKEPVIRELNLTDDYPVAVGVLETSRLPGDEVCQKIAADCHVDPKNLVLLAARTASIAGHVQVVARSVETSLHKLHELEFDLSKIASGFGAAPLPPIAADDVAGIGRTNDAILYGGTVTLWVNETSERLKEFGEKLPSSTSTMYGQPFEKILRDAKFDF... | Pathway: One-carbon metabolism; formaldehyde degradation; formate from formaldehyde (H(4)MPT route): step 3/5.
Function: Catalyzes the hydrolysis of methenyl-H(4)MPT(+) to 5-formyl-H(4)MPT.
Catalytic Activity: 5,10-methenyl-5,6,7,8-tetrahydromethanopterin + H2O = H(+) + N(5)-formyl-5,6,7,8-tetrahydromethanopterin
EC: 3... |
A0A8C4BDX4 | MNSGLPASAAPLGGVGIPNVPKVKFCRYYAKDKTCFYGDECQFLHEDPSMASLSLHGGSSPVPLSMAAGGVAPAGYGLGGAPLDGQLLTIPGMEGGTLTDANLTNSYFSSSFIGVNGFGSPAESKYSMMQRMTTSSSSPSLLNDGVSTRPFKKKNPIVFSSEFIPKAAPRMASMSQAPVQSFPSPLFAHPGMSGSTAAALAPGMSLSAGSSPLHSPKITPHTSPAPRRRSHTPNPNPANYMAPTSASDPGGAHIIQKETVGGTTYFYTDNTPAPMAGMVFPTYHIYPPTAPHVAYMQPKANAPSFFMTDELRQELINRHL... | Function: Regulatory subunit of the poly(A)-nuclease (PAN) deadenylation complex, one of two cytoplasmic mRNA deadenylases involved in general and miRNA-mediated mRNA turnover. PAN specifically shortens poly(A) tails of RNA and the activity is stimulated by poly(A)-binding protein (PABP). PAN deadenylation is followed ... |
A0A8C4CA38 | MNNILGKGKVNFVSGLGKGAGKGGGGGGTVREAGGGLGKRGAVQEESYFRKKTQENLKDLKEKKTENISGISNKIIYYYDEIM | Function: Endogenous F(1)F(o)-ATPase inhibitor limiting ATP depletion when the mitochondrial membrane potential falls below a threshold and the F(1)F(o)-ATP synthase starts hydrolyzing ATP to pump protons out of the mitochondrial matrix. Required to avoid the consumption of cellular ATP when the F(1)F(o)-ATP synthase e... |
A0A1G0GUH1 | MNPIAITMGEPAGIGPDVILQLWAKKPDLFSAEKIIIIGNKTVLSERARALGIACDCDQLPIHDVPLSEPCIPGQLNPNNARFVIDMLTIATENALQKKCAGIVTAPIHKGILNDAGFSFAGHTDFFAKYTQCHTVMMLMTESLKVALLTDHVSLRKVPDCVTEENIARCLTIMINDFQNRFGILKPRILVCGLNPHAGEQGYLGTEEKNTMIPVLEKFRQQGHLITGPIGADVAFTDHYRNSADVILAMYHDQGLPMIKYTGFHEAINVTLGLPFVRTSVDHGTALDIAGKALADTTSLHRALLFAAKMRAHEITPAA | Cofactor: Binds 1 divalent metal cation per subunit. Can use ions such as Zn(2+), Mg(2+) or Co(2+).
Pathway: Cofactor biosynthesis; pyridoxine 5'-phosphate biosynthesis; pyridoxine 5'-phosphate from D-erythrose 4-phosphate: step 4/5.
Function: Catalyzes the NAD(P)-dependent oxidation of 4-(phosphooxy)-L-threonine (HTP)... |
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