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stringlengths 6
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stringlengths 16
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stringlengths 117
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A0A0H3YML1 | MFLILLIFXMISVXFFTLMERKXLGYIQCXSGPNKVGYLGILQPFXXGMKLFMKEQFFPMNSNYLIYMICPLFXXIXSLFMWMVFPFYVNTLEMNLGLLFFLCCSSLGVYGLVICGWSSNSIYSMLGCMRSVSQVISYEVTLSLILLSFFLLVDSYSLLSFYYIQVSLWFCVFSFPLFFSWIXCCMAETNRTPFDFSEGESELVSGFNVEXGGGGFXIXFIXEYXSIIFISLFTXVXXLGXDLNSLXFXFXXXXMCFLFVWVXXTLPRXXXXKXXYLAWXCYXPXSLNYXMXFXLVXLXXXYHFFXXXX | Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.
Catalytic Activity: a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) + NAD(+)
EC: 7.1.1.2
Subcellular Location: Membrane
Sequence Length: 309
Sequence Mass (Da): 35793
Location Topology: Multi-pass membrane protein
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A0A7C5VLE3 | KGIKDSLFDAIMIGLIFTITQTLVAFFIGPELVAVLGSSVSLISIVIINHFFRKPNGKLRGIFLSVVNYVILLVLVVLTRLVFNDVLNKYPFVITFDIGGHILKVDYLTTPGTLLLISSIIGAFIQGANFKTISMTLLETLDKIKWSSITIVSIVILAKVMGNTGMIISTAVLIATVSGKFYPIFSPLVGAIGTFITGSDTSSNILFGILQKETAKNLGFDTTWIASSNTSGATAGKMISPQSIAVASSAVGLQGLEKQIISTTLPICLVYSLILGMYVWIVSLLIV | Function: Uptake of L-lactate across the membrane. Can also transport D-lactate and glycolate.
Subcellular Location: Cell membrane
Sequence Length: 287
Sequence Mass (Da): 30713
Location Topology: Multi-pass membrane protein
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F0V8T3 | MVNVNPVDAVGESRTRPGVTVAFVEDIAREAGHTLRKFFSDRDKKVDTKESPADLVTEFDKAIEDHLKKRIREAFPTHQFLCEEQRFLLERKSTQSLTAAELGIQKRIDGTTNFVHTLPFTCVSIAFAVNKEVVVGVVYAPILNEMFSAEKGKGAFLNGERIYTSGRRDPSCAVVCCGFSVGTIRKIDMPGCDLAVKTAARDIERCVLNNLTYCSHNCRDIRHLGSTALELCYVAAGRMDAYQSLGPKEWDFAAGILIVQEAGGCVIDFDGKPLELHQRRAIAGSTEELARSFVGNLMAPGLSTAVDGPGVKTLCSAKKPVLEAAAEQLKWHGGEDVAVVVY | 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: 342
Sequence Mass (Da): 37341
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B4CVH8 | MICSELHPVAFWIAAGIAAGLAVTPLIFLILDKTGKLKPALRSDLWTRYKSWLVLAPLMVGPLLAGRLAAIIGVGVLSLACYREFARATGMFRYRAISAVVALGILLLTFAAADQWYGFFVALSSLTISLLVIIALFADQPKGYIQRVALGIFAFSLFGVCLGHYGYFANDKDGAGQAFLLAILLCVELNDVFAYCTGKMFGRRKLAPQTSPNKTIGGALGALILTSALFATLVHAIVHGSALDQPVHLVAMGMLLSLTGQWGDLVMSSIKRDLGVKDLGVTIPGHGGLLDRFDSLIFVGPAMFHYVNYFLGLGLDQPVRGITGH | 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: 325
Sequence Mass (Da): 34773
Location Topology: Multi-pass membrane protein
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A0A1C9P9G4 | TSLSVIIRTELGHPGALXGNDQIYNVVVTAHAFIMIFFMVMPIMIGGFGNWLVPLMXGAPDMAFPRMNNMSFWLLPPSLTLLLSSSLVEAGAGTGWTVYPPLSSTIAHAGSSVDLAIFSLHLAGISSILGAINFITTIINMRAPGMTFDRLPLFVWSVLITAVLLLLSLPVLAG | 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-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
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: Mitochondrion inner membrane
Sequence Length: 174
Sequence Mass (Da): 18549
Location Topology: Multi-pass membrane protein
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A0A1I8AHM4 | MEVFVYDKWNAKILPPYVQGEILTDVKVEMDESRTQAPPLLNEADLIALMDKYGIGTDATHAEHIETIKKRQYVGMNAENRFIPGYLGLALVDGYNLMGYEMSKPMMRAELEQNLKEICAGRKTKEEVLADQLGKYKRIFTVSEMKVDKLSEAFRNYLSIAGRNNRSINNIPGIDPPPQNGPPNPDGAMDATSARGGATRGRGRGRGRGRGARGGGDAPGRQANPPPAPANDATTKMCKCNQPAVKKKVTKEGPNKGKLFWTCPVGYNQPGNCKFFEWA | Function: Introduces a single-strand break via transesterification at a target site in duplex DNA. Releases the supercoiling and torsional tension of DNA introduced during the DNA replication and transcription by transiently cleaving and rejoining one strand of the DNA duplex. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(5'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3'-OH DNA strand.
EC: 5.6.2.1
Catalytic Activity: ATP-independent breakage of single-stranded DNA, followed by passage and rejoining.
Sequence Length: 279
Sequence Mass (Da): 30720
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A0A1I7ZQX4 | MDGMDIFASHTASIWERIGFEDALVEVCDSIMARRSIPTPLSYVPVVEENDLGTVMSFADRAENIRKYLVSVIVHRYGTDRSSAVFRKHVSPDFPNVRQIASESSLCFVNSDEFLDIAQPILHKTVFVGGLGIGPAKPLQEPYSSLLEKGSKGVVLMSLGTIVPTSSIPIPVRQGIFEAFGNFTDFHFIVKVDKEDTESAALVASIPNVDLVRWMPXXXXLDRPSLSRRTERQMDIMPT | Catalytic Activity: glucuronate acceptor + UDP-alpha-D-glucuronate = acceptor beta-D-glucuronoside + H(+) + UDP
EC: 2.4.1.17
Subcellular Location: Membrane
Sequence Length: 239
Sequence Mass (Da): 26518
Location Topology: Single-pass membrane protein
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A0A059WYP7 | MISIFVAMTKNRVIGEKDQLPWRLSSDLKRFKELTTGHPVIMGRQTYESLPIKFRPLPNRTNIVLTRNKDFDAPECIVAHSLAQGIEEAKLHNGSDEIFIMGGGQIYEQALPLTDRIYLTEVETTAQKGDTFFPKLHKNDWYIKKAGGFEQDEKNQYAATFYIYDRKETND | Pathway: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1.
Function: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis.
EC: 1.5.1.3
Catalytic Activity: (6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH
Sequence Length: 171
Sequence Mass (Da): 19718
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A0A257AEF0 | MHFNILKHDLVPYHSILSPKEAKKILEAYKINKDQLPKMLVTDPVARAIGARVGDIVKIIRKSPTAGESVAYRLVVGSPQE | Function: DNA-dependent RNA polymerase (RNAP) catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
Catalytic Activity: a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1)
EC: 2.7.7.6
Subcellular Location: Cytoplasm
Sequence Length: 81
Sequence Mass (Da): 9005
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A0A2P0QMR9 | MEYKASVNKLTQPLVTYLIDNADKLRVNVETMANGCTLVDAGIKVPGGLEAGRIIAEICLGGMGTV | 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: 3.5.4.27
Subcellular Location: Cytoplasm
Sequence Length: 66
Sequence Mass (Da): 6937
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A0A1I7Z2D2 | MFRTTLAMSFVDMWPPFLAPPTCTETGCMVISLAMRLWSVAVALLAVLLLSSSVQSKATGKDYTQYVCKGCEAAVKGFQFLFGKEATQDKVIQLLAFICKYFLDEKSAVCKAMGGQFRDQIIFVIGELIVQPTQLCGFISSECGDFHNPFHANWTIKLPKPPKCNLPQSSLIFPLPDIDYPKEPSSTLRVLQLSDLHFDMEYVPGSEADCDNNICCQSDSSEGRVNMGSYMQPINDKLQLITLNTGYCMNTNLSRQHDELVRXXXXEGVPVNSFAPHYAPKEAQPTWLYDAVSKAEQKWLDYEALKNLEFRGSYIVKINDNLKLITLNTGYCMNTNFWLYYNQTDPDNTMSWFVRKLHQAEEENKFVHVMAHVPPGNEECLEGWAYNYYSIVNHFRKTITAQFFGHTHVDSFTIFYDDMNHPNSRPSNMHYTAPSVTTYEGLNPAYRIYTIEGDYKDSRFRVLDYDNYFLNLTNLETESDTPRWEKLYSAKSEYDLPDLSADSWNRLIDRIIDDEEVFDRFVKNYVRRDDFPCNDKCRENLICSMKKAHHNELALCPEVADSFEAQVSKHLIYELGSKPALDPSFADQLTRTTFLQELLTGTMSPVTFDLL | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Converts sphingomyelin to ceramide.
EC: 3.1.4.12
Catalytic Activity: a sphingomyelin + H2O = an N-acylsphing-4-enine + H(+) + phosphocholine
Subcellular Location: Secreted
Sequence Length: 611
Sequence Mass (Da): 70065
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A0A151EVE6 | MIIKRGYILQNGIRKRDIRIEGNEITEIGKDLKGSDIIDASHHLIMPGFVNTHTHLAMTLLRGYADDVPLQEWLRDYVWPKEMKLTPKDCYYGNLLGIIEMIKSGTTCFNDMYFYEDQAVKAAKESGIRAVLSAGMADMGNLKRAEFQLKKSVEFAQTVRKEHLVKAAFGPHSPYACSFNFLSKIQEQAQKLKIPVHIHLHETAEEIRQFQKRHGKTPIEMLDSIGFLASNICAAHVVHTTEKELDILKTRNVKVLHCPSSNLKLANGIAPIAQMVKKGICVSLGTDGAASNNTLDLCAEMRLMALLQKIENPGAMNAETAVKIATDNGGYTLHWNIGKIEKGFLADVVFIDLKNVSMVPRHNLISNIVYSMNSSAVNTVIINGTVIMEDRKILTVDEGNVIEKARGHAYDLVNR | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the deamination of 5-methylthioadenosine and S-adenosyl-L-homocysteine into 5-methylthioinosine and S-inosyl-L-homocysteine, respectively. Is also able to deaminate adenosine.
EC: 3.5.4.28
Catalytic Activity: H(+) + H2O + S-adenosyl-L-homocysteine = NH4(+) + S-inosyl-L-homocysteine
Sequence Length: 415
Sequence Mass (Da): 46281
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A0A4R1FAS1 | MSNKIIKAGFALFTLSSLLFASSSFARPNTFSCAAGNTISKTFSSGAAWDLCWEVRDEEGVVLSDIHYKAANSTRRKVIGEMSLSQIQTEYDDDSADQFLVTDFGLGGNSLQTLNTSMCEGGQLHEYAGRNVLCEVSSANGYIYRYRDNIRRQGSKLEILSASNINSREFIIRSTFLENGTIETGVGITGQFTKTTTDSNAGWPVTSQNKLSTSFTDHFFWRLDFDIGSSNSNDVVEQIKSVPSSDRLTKTKQTQTISSELAASFTPADKKFWRIKDQSETNNANQPVSYEMVLLNYAQQSKGNSSSPWLKNDVYITAYNACERFAVNNTASSCGSNVSEFVNSQNTNAKDIVVWYRMAHHTLPRDEDFSPVAVQWSNFILLPRDWTSINRL | PTM: Topaquinone (TPQ) is generated by copper-dependent autoxidation of a specific tyrosyl residue.
Cofactor: Contains 1 topaquinone per subunit.
EC: 1.4.3.-
Sequence Length: 392
Sequence Mass (Da): 43679
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A0A513Q872 | MANRRNRRNFQKRRPRGPRTPAETSTVTTTVSTNGQTKPTTKTTTVKTTKTAPRQQNNRQVRNFVRQELRKRVDGPKAAITQTATLTLGTLGTNGSGNLEIEGVAHLNPLLIKEKTAAAGAGPIQALASQYAMWRCLSLRVILVPTVGASAVSGTVARTSLNQPGAPAQTTWSGLGARKHVDATPGRRVEFRLGRRDLQGPRDGWWYTDTSNGVQNSAGPTIEIHSYGKTVSTFQATAWSGELWLVELRATWQFTNWNMNPKLLNLVDTTIPHGNIKLSSSAAGAPVVLTVEKAANAPLETQHAQNPHVTGSPSVSEVIWRAADVGVRVVASGLPPPLSWLIGGGWWFMKRAFNAPVGTGINASTVDAYYVYTTAVDAELNNPVKSSAPIAPVDVNGDIDIQQITLPDTAQVAQASGRAIDTPDFTNGTVSMLPTTSVFGPYSRGLLHQISLIGDRSSYTPALALPVDSSETYYAHLLHILAVPANRLTFLMGTQSARPPAGVDIRLCYKTKNPSPAVNDVAPAKLLAATPPLETSGAAKMQLYLF | PTM: Specific enzymatic cleavages in vivo yield mature protein(s). VP90 undergoes a cascade of proteolytic cleavages presumably mediated by host caspases and extracellular proteases.
Function: The capsid polyprotein VP90 self-assembles and undergoes a proteolytic cleavage by host caspases to yield the VP70 virions. This immature virion is composed of 180 VP70 subunits with 90 dimeric spikes and displays a T=3 icosahedral symmetry. The mature virion is obtained by further cleavages resulting in three structural proteins VP25, VP27 and VP34. This forms contains only 30 spikes located on the icosahedral 2-fold axes. Plays a role in the attachment to target host cell. This attachment induces virion internalization through clathrin-dependent endocytosis.
Subcellular Location: Virion
Sequence Length: 546
Sequence Mass (Da): 58529
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A0A060C2F5 | MPNVNFEVYAPSFLERFIESHAVMLQGNAGLKPKEGEITSRPWQWPINYRVNIS | Pathway: Protein modification; protein glycosylation.
Function: Transfers mannose from Dol-P-mannose to Ser or Thr residues on proteins.
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
Subcellular Location: Cell membrane
Sequence Length: 54
Sequence Mass (Da): 6263
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A0A7V3RKP2 | MEAFVELIENKIRESIEIKQKILSDKKILSDIEKAAKMIIHCYRINNGRVFFAGNGGSAADAQHLAAELVSKFYMEREALPAEALSTNTSILTAIGNDYSFDRVFSRQLEANAKKGDVFVGISTSGNAQNIIEALSICKMIGVKSIGLTGETGGNMTGLCDLLIKVPSIDTPRVQESHIMIGHIICEIVEKSLFGNKK | Cofactor: Binds 1 zinc ion per subunit.
Pathway: Carbohydrate biosynthesis; D-glycero-D-manno-heptose 7-phosphate biosynthesis; D-glycero-alpha-D-manno-heptose 7-phosphate and D-glycero-beta-D-manno-heptose 7-phosphate from sedoheptulose 7-phosphate: step 1/1.
Function: Catalyzes the isomerization of sedoheptulose 7-phosphate in D-glycero-D-manno-heptose 7-phosphate.
EC: 5.3.1.28
Subcellular Location: Cytoplasm
Catalytic Activity: 2 D-sedoheptulose 7-phosphate = D-glycero-alpha-D-manno-heptose 7-phosphate + D-glycero-beta-D-manno-heptose 7-phosphate
Sequence Length: 198
Sequence Mass (Da): 21592
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A0A059WZM1 | MRKQSFLRLSFGESTLRSAGVTDWLQVAKPDVVFETTSLNHETGQPAIDYLTAALKFGAHAITANKGAIVHGYDELNELAKASHRSFLFESTVLDSAPVFSLFRETLPAVKLRGFTGLFNSTANVILESMEAGRTFDEGVKTAQELGIAETDP | Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-homoserine from L-aspartate: step 3/3.
EC: 1.1.1.3
Catalytic Activity: L-homoserine + NAD(+) = H(+) + L-aspartate 4-semialdehyde + NADH
Sequence Length: 153
Sequence Mass (Da): 16652
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A0A1I7YLE5 | MLFQRISTRFCFRSALGLRTGYRTASSNTLANTLKKMKEQNQPINPLYVLSNTSPIVKLDCDEAFKSLTEKQKLYAHHISRASFLGSLATFAQVSRESLGIFVVLHRIFEANSPEMLQAKATQIGFTDEEYQAFLIYAVGFFANSGNYKGFGDTKFIPNLPKDKFRSLVAISEDDTTLGSRVPLMSLYNRIEHNLYSISNFVATLGFNDEHITTYHSGFVTKTDCDIADRYMKSRRMEAFNTRLQKTVEDGKPEYTIWVASEKQKETETTEFEGVTFRVKYGDHSDAMMLAVCELEKAKQYADNEIQRGMIGKYIDSFKYGNLQDHVEGSRLWIRDVGPAVESYIGFIENYRDPAGVRGEWEGFAAAVNEETSRVFQELVKQAEQLLKRLPWGEAYEKDKFLKPDFTALDVISFAGSGIPSGINIPNYDEIRQDEGFKNVTLSNVISAIPSNQRITFLTADDEALYHKYFKESFNVQVGLHELLGHGSGKLFFRDDEGKFNFDQSVVKDIVGGGPIQSWYEKGESWSSVFGEHSNAYEECRAEAVGYFLSCFDDILKIFGHEGQEAQDVKYVNWMNELRSGLCGLEFYNPEKDLWGQAHSRARYVLLKVCMAAGQDFVKVDECVGEDGEPDLLLTVDRSKIETVGKPAMADFLKSLQFYKSTADAKRGIAFFKDWDRVNERELRWHKIVLSRRSPRRLFLQSNTFITDQGVELKNYPLDPNGFIKSVVDRYDAEHIQAAQSIWDFNYVNSL | Cofactor: Binds 1 zinc ion per subunit.
EC: 3.4.14.4
Catalytic Activity: Release of an N-terminal dipeptide from a peptide comprising four or more residues, with broad specificity. Also acts on dipeptidyl 2-naphthylamides.
Sequence Length: 751
Sequence Mass (Da): 85617
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A0A660T952 | MNNFHTHTWRCKHASGTVQDYVDAAKKNDMKILGMSDHTPLPDNRWSHVRMDFSELDAYEEEFKKVETDDITILKGLECEWDPIYQGFYSDNLLGERNFDFLIGAVHYIKIDNEWSYLGEIRTAKDLSQYAKILIETMRTGLFSFIAHPDGFGAGYLEWDSNAEACAIDILTAAEELSIPLEINGYGLRKPKILNLKGSRNVYPLLDFWELASKFDITAICNSDAHRPEDVDASLKECRAIADRFNIKVIDDIRK | 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: 255
Sequence Mass (Da): 29267
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A0A0X9L4R5 | IKHYGGVENSDYPKVQEVVNQFIAGTLDKITAGAKKAASDATDRAVIGGVVKSNAGTSVDATSVNALVKGIKEIVDLVIKEGNGQADKITPVDYDKKKIDKLFGATTDAAQGAEDKHVAAAASASIGVV | Function: The Vlp and Vsp proteins are antigenically distinct proteins, only one vlp or vsp gene is transcriptionally active at any one time. Switching between these genes is a mechanism of host immune response evasion.
Subcellular Location: Cell outer membrane
Sequence Length: 129
Sequence Mass (Da): 13211
Location Topology: Lipid-anchor
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K2CYW1 | MQKYKKYFYWYILPLFFSLSPLILIYSLNLFAQPFNLYLLLLPSVAVSSYFGGLKGGILATTLTSLGMNYLFIVPNFTSLEIPQVLNLTFYILECIAVTVFITQGYHSELLQNYKTKAENLSKKLIKIQEDLTSAQSEIKLRDEFLSMASHELKTPLTSMLLQIQSALHNIKNVSLANFSVANLLKMLESVETQTERLSKMINDLLNVSLITTGKLELEKENFDLSKTVREVVNRFVEKLEKEGYTLSLEADKEILGNWDKLRIEQVITNLLTNAIKYGDKKPIEVRVINFNKSGKIHVKDQGIGIPAELQKKIFEKFERAVTSSQFQGSGLGLYITNQIVKAHNGKVHLKSREGKGSTFIVELPVAS | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Membrane
Sequence Length: 368
Sequence Mass (Da): 41687
Location Topology: Multi-pass membrane protein
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A0A1I7Z6Q3 | MRFCSISVLIRSFSHPLPASSMSPIPILSSFFSAIQSFPLPEMITDVQLGVMANVLGIGMFLLVVLFHYITANNARRGVSNTAGPN | Function: Subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). All subunits are required for a maximal enzyme activity.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 86
Sequence Mass (Da): 9298
Location Topology: Single-pass type III membrane protein
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A0A2T5Y4E1 | MLIVGQHGEGYPTIQEAVHAVRDFYESPVTIFVHKGIYHEKLNIPSWKHFIHIVGEDRDSTIITNDDYSGKRNVQNEFLTPFNTYTSYTVLVAGNDCVIENLTIQNTAGEKGQAVALHIDADRTHIRNCNILGWQDTFYLARAGSRNFIDQCFISGSTDFIFGAATAVFSKCTIESLKNSYITAPSNSQDHPYGFVFLNCDLRAKNEQVNQVYLGRPWRSNAKVLFYACNLGSHIVAEGWDPWNGDTMFPDKYKTAVFLEINCRGEGFKQLSKRVPWSKQILNNNYKQPSLSSIFTDWKPTENSN | 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: 305
Sequence Mass (Da): 34615
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A0A924IN21 | MRPLTGKRVLITRAHPGAETLANRLTALGAEVVLAPTIAIEPIADPAPLFAQVARLTAADWVVITSPTAARLWALCTGTVTVPARLAAIGEATAAELRSQGLPVAFTGARATGAALASSLLSLGPTGRFLLPRSDKAVADLPIKLRSAGADVIECDLYRTVSRPWTADEVRAVGAGVDAVTVMSPSALDGLLSQPGVTLWLSRARLVAMGPTTASAVTARLGRPDAVADPPSIEALIASLCAVLGHTGG | Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 3/4.
Function: Catalyzes cyclization of the linear tetrapyrrole, hydroxymethylbilane, to the macrocyclic uroporphyrinogen III.
EC: 4.2.1.75
Catalytic Activity: hydroxymethylbilane = H2O + uroporphyrinogen III
Sequence Length: 249
Sequence Mass (Da): 25386
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A0A7C4N204 | MNIQTIVTLFDWRSLIDIPILSFIVFLFYTTLRSSGSWRIGLGIIVALLFYLVARFIRLPGVEWIFNNVSNIALIALIVIFQPEIRKIFERAASAFKVKKLLKESSGFINEITKAAFVLAGRRWGAIIVIPGKDDVANKINGGIIINAEISVPLIMSIFDPHSPGHDGAILVENGKIVGFGYRLPLSSSEKLDYQFGTRHHASLGLSEMCDALIITVSEERGTVSIFHSGSYMQVDNEEKLESEIKSHLQNLSFLFPVSSKQRSRSIRLAEAFLSLVVGCCIWLAIAINASQVIHRTYTIPLQYNLPSKMVIIGEKPQTVRISVSGSASEIESIQPYELKAFIDLTNTSPGEHLVNLQQKNFNVPDGVHITDIEPPQIKLVLHTMEQRDIEIKPQLVGSLPPGYEITSIDVSPSKIPILYTTDLENPENIYLTTTPIYINTIQQSVKLSTKIVAPQGVYPLDSTNWPDVTVMIYIHQK | Function: Catalyzes the condensation of 2 ATP molecules into cyclic di-AMP (c-di-AMP), a second messenger used to regulate differing processes in different bacteria.
EC: 2.7.7.85
Catalytic Activity: 2 ATP = 3',3'-c-di-AMP + 2 diphosphate
Sequence Length: 478
Sequence Mass (Da): 53311
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J8IW48 | MKIKKNNKGIKFLACLLVSLCIINYSSISFAETQTGNANDATKNASGIDTGIASLKYDSRDILAINGDRVESFVPKESINSNGKFVVVEREKKSLTTSPVDISIIDSVANRTYPGAVQLANKAFADNQPSLLVAKRKPLNISIDLPGMRKENTITVPNPTYGNVSGAVDDLVSTWNEKYSTTHTLPARMQYAESMVYSKSQIASALNVNAKYLDNGLNIDFNAIANGEKKVMVAAYKQIFYTVSAELPNNPSDLFDNSVTFSELTRKGVSNAAPPVMVSHVAYGRTIYVKLETTSKSKDV | Function: A cholesterol-dependent toxin that causes cytolysis by forming pores in cholesterol containing host membranes. After binding to target membranes, the protein undergoes a major conformation change, leading to its insertion in the host membrane and formation of an oligomeric pore complex. Cholesterol is required for binding to host membranes, membrane insertion and pore formation; cholesterol binding is mediated by a Thr-Leu pair in the C-terminus. Can be reversibly inactivated by oxidation.
Subcellular Location: Secreted
Sequence Length: 300
Sequence Mass (Da): 32637
Location Topology: Multi-pass membrane protein
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A0A0D9ZLV1 | MAECAWWGEVGMSEVSASSTAAVGRVGKHWLALRSGANLFMHSLELDELEKSVVKSWRKGANPLPPRCTVVVIRFRGESRVFGEGNGVVTPLHVPASGYPMMSMDEQTSLSFALFKDAAFNASIRRRGVRATRLRPSGGKPCFSTEGTANFYMHPIEGLTVLVDMDTTEVLHVSDRDAGIPIPTTANTDYRHGHSTPSPCSSADTQRELDSRSGGLPLPLLLLLLALPPAAAVELAPAPLVPSSPTHPPARTAMVGDPSPWRGQ | PTM: Topaquinone (TPQ) is generated by copper-dependent autoxidation of a specific tyrosyl residue.
Cofactor: Contains 1 topaquinone per subunit.
EC: 1.4.3.-
Sequence Length: 264
Sequence Mass (Da): 28289
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K2AWC6 | MQKIAVYTLHTDLKTAAKALAKKLQLPYTKEALYWILLTPEYLGLQKVSEKLAPLYIDFSSGKMAYRQQHASIREETLAKALGLKHGKERYIIDATAGLARDSFIIAALGFKVELIERSPIISALIEDAFKRARNHPHIAPIIERMHLVTGDAITLLANRSERPDIIYLDPMFPLRKKSALPKKDMQIFHDVIGPDEDTDELLKTALACAKDRVVVKRARLSSELGRIKPSFALSGTSSRFDIYLLRPHGHPALFNSICSAP | 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: 262
Sequence Mass (Da): 29367
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K2B6W9 | MAKILDGKIVRDKIARKLKSEISRLRSKCKLVILQVGDLSESNAYIRQKILFGQKIGCLVEHQKFDEKISQAELISQLSILNSQFDVTGIIVQLPIPIHLDKDAIIDAIDPKKDVDGLTSTNLKLLWENKSEGYLPATTKGILTLCDFYKIPTGAKKVVVVGRSFLVGKPTALAFLNHDATVTVCHKETRNLKAETRNADILVVAVGKPNLITKDHVKPGQVVIDVGINVVNGQHPRGEIKTKPGEHPGGEKGLSKPETEPSNRRIVGDVDFDNVSKIVQAITPVPGGIGPMTVASLFENLLEAYKRQT | Pathway: One-carbon metabolism; tetrahydrofolate interconversion.
Function: Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10-methenyltetrahydrofolate to 10-formyltetrahydrofolate.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + NADP(+) = 5,10-methenyltetrahydrofolate + NADPH
Sequence Length: 309
Sequence Mass (Da): 33814
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K2AGZ9 | MLTDVHDIAQAREAATVVDVIQIPAFLCRQTDLLLAAGDTGAVVNIKKGQFLAPWDMANVADKVASTGNDNILLTERGVSFGYNTLVADMRSLPIMARSGYPVIMDATHSVQQPG | Pathway: Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis.
Catalytic Activity: D-arabinose 5-phosphate + H2O + phosphoenolpyruvate = 3-deoxy-alpha-D-manno-2-octulosonate-8-phosphate + phosphate
EC: 2.5.1.55
Subcellular Location: Cytoplasm
Sequence Length: 115
Sequence Mass (Da): 12285
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K2EA30 | MTKNLFYKSSILASKLIGYTSKYLNLGAGTNFPGKIARLIAPDVLSYLVNQSRREIIVVTGTNGKTTTAGFVANILTKDNRKVAHNRKGANMLTGLTTSITQESKLNGQLDVDHCVLEIDEAFFFKAVDEFNPELLLVTNLFRDQLDRYGELDTTAKKIQSAIDKTIKKKPLKVALNADDPMVSALAQDDSIKKVYYGFSEVNFVNQDQTVKSPQEVAACSCGGKYNYSKIFYGHLGHYSCTCGKTRPELDVSTVAYIDVNSSTLTITVKNKESFSVNIKMPGLYNAYNALAAITLCLELNISPVTIIDGLENYSTIFGRAELTHLKGKPSLIQLIKNPIGATEVLRTVKDDKNSKLLIIINDNYADGRDVSWLWDANFELLNNHDKQIVTSGIRASDMALRLKYTGINHNQLKVIENIKQAIDYSLSNLKAGEKLYILPTYTALLELQHILRKY | 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 isoglutamine residue.
EC: 6.3.5.13
Catalytic Activity: ATP + beta-D-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-di-trans,octa-cis-undecaprenyl diphosphate + H2O + L-glutamine = ADP + beta-D-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-D-isoglutaminyl-L-Lys-D-Ala-D-Ala)-di-trans,octa-cis-undecaprenyl diphosphate + H(+) + L-glutamate + phosphate
Sequence Length: 455
Sequence Mass (Da): 50617
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K1XCA8 | MIKILIADDSPFIRKVLRQIYKDSEEFQIVGEASNGSDAIDLVKILRPDILILDLEMPVLNGFEALKVIMKEAPLPVIIFSSFNLKGAEQTIKALEFGAIDYLTKPFASYDKIDVITKDLSAKIKNIVKSFRQSVKNQNSKSDKKSNLIIGNCHNVNSRKIDLIVFGASTGGVQAASNILPQFSGKTCPIVWVQHMPQNFTATFAERLNDISELNVKEAIDNEPLKKGYCYIAPGGKHIEIRNNSGRFSLHTFIGDEICTNKPSINVMFYSVSEHFSNNAIGVVLTGMGNDGAKGILAMHKAGAFTIGQNKETSVIYGMPKAAKDKGAIDIELPLEKIADYINKLSFF | PTM: Phosphorylated by CheA. Phosphorylation of the N-terminal regulatory domain activates the methylesterase activity.
Function: Involved in chemotaxis. Part of a chemotaxis signal transduction system that modulates chemotaxis in response to various stimuli. Catalyzes the demethylation of specific methylglutamate residues introduced into the chemoreceptors (methyl-accepting chemotaxis proteins or MCP) by CheR. Also mediates the irreversible deamidation of specific glutamine residues to glutamic acid.
EC: 3.1.1.61
Catalytic Activity: H2O + L-glutaminyl-[protein] = L-glutamyl-[protein] + NH4(+)
Subcellular Location: Cytoplasm
Sequence Length: 348
Domain: Contains a C-terminal catalytic domain, and an N-terminal region which modulates catalytic activity.
Sequence Mass (Da): 38334
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K1XAZ4 | MKKLITLFFVLFLNFSVFSNPVAEVETSMGKFKIILYMDKAPKTALNFINLCKKNFYDGIVFHRIIKGFMNQTGDPTGTGMGGPGYSFEDEFHPDLKHSKPGIVSMANSGPNTNGSQFFITSAPTPHLDNRHSVFGEVIEGLDICDKINSVKTDSNDRPVNPVSIIKITLIGTEPPIVDEELLNYFKKVSEPCIKTSLEVSNLKSNNINLRAVHTRNNRYLAIWDITCEDNTKLAFWIKGAKTDAGFIFDELHTNFIKEK | 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: 260
Sequence Mass (Da): 29189
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A0A3L9LT91 | MCLPTCAQEIPRVNHKRDIKVSGAQERVSGLELFVRRLKCLGIIVIEKYAMNKLEIHGRSVQIFAWILGLSDIEYPIGRQRPVISFLYLMFLMGILTYNLKSVIGHIEINISGSTLSEELIRLLFIVGTGISYYILGSVWLFKKDESECLRQLNEVTECIASISSDTDFKDIKRNKMIQIISWITCVYYMAHFFIKYISDSESLSSFSNIFCINYESFLILYINLMFVNYIRIIQLNFAKMNKRLKELTAFTDCSSSISVYEIIKDISRIKQLHIRLTRVSRSFNDFYGIYTLLSITLRFGTMTFHLYNIYCTLYNVQSDSTTHVYTVIQHCLLMSVDLYVVFTVIDACRLTAMEANKTGYRIFELTNNGSSMEIDNEIERFSVQLLQNPLEFTAHGFFVLNRGIIFNIILMLISYLIVLVQLSTCEV | Function: Gustatory receptor which mediates acceptance or avoidance behavior, depending on its substrates.
Subcellular Location: Cell membrane
Sequence Length: 428
Sequence Mass (Da): 49546
Location Topology: Multi-pass membrane protein
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A0A3L9LY67 | MCIVRELKLFLQLTKLFGFTPYSLEKIELPIQKYAVAYSLFCAGFYGFVIYQRSIEVSLGDVDKLFVLMIIRTILANVALWNDILFGIFYRTKLVIAFQKIWRYDLETRTALDKRVVRYSWTVIFFIFFNDVCISFLTYFSETQKPGLVVVLYNMIYVPMSFSIFKFTLIVYAIQRRLQRLNKMVSAGMPTKNFVNFYLLYIFAIGILFFLTGMRSVIAEINIGCPRVSMKDVRWLHSCLISAIKDVNSLYQLPLFLWIVTLTFNITSRIYSIGQNSASLLLILRECNMILFCTVLLITVITICHVTACEANKTGCIMFSPQLKFVQNRTSTSGEVNEGISVGQYFLFHPIHFSAAAGIITIDLPLLLSIAGAMTTYLVILRVPNVG | Function: Gustatory receptor which mediates acceptance or avoidance behavior, depending on its substrates.
Subcellular Location: Cell membrane
Sequence Length: 387
Sequence Mass (Da): 44317
Location Topology: Multi-pass membrane protein
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A0A1M7L9L2 | MEAELVYKIKASLGEGPCWDTRNNILYWTDIAGNVIHQFDPVTKRNKTFSIGQMVGAVVVAEDGRLVLAAEHGFYYFDITTNELVEISDPEKGNLDNRFNDGKVDPAGRFWAGTMQKNDTQPRGALYCLFADHHIEEKLSGLRISNGIAWDLEKSRMYFIDTPTGNIYVFHYQKETGVITNQRVAFPFPEEYGSPDGMTIDSEGMLWIAGWGSGQVTRWDPSTGKVLLTIKLAAKNITSCTFGGKDLDTLYITTARIGMTDQELENLPLSGSLFSVKPGVKGVPAYYFANKP | Catalytic Activity: D-glucono-1,5-lactone + H2O = D-gluconate + H(+)
EC: 3.1.1.17
Subcellular Location: Cytoplasm
Sequence Length: 292
Sequence Mass (Da): 32501
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A0A3B9P3M1 | MDYLSFEKPIEELENQLTKALELANETGVDMAKTITDIQQKLDNAKKEIYNNLSAWERVQLSRHPQRPYTMAYINALTQGDFIEMHGDRGVKDDKAMVGGWGTIDGKSYMFIGQQKGVNTKMRQYRNFGMANPEG | Pathway: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1.
EC: 2.1.3.15
Catalytic Activity: acetyl-CoA + N(6)-carboxybiotinyl-L-lysyl-[protein] = malonyl-CoA + N(6)-biotinyl-L-lysyl-[protein]
Sequence Length: 135
Sequence Mass (Da): 15425
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F7XKQ0 | MMDIEEIDAIDAVIIGGVGFTNFSGSTDIAENIHLREIETPYGTAAAYLFHLDNKYVALIPRHYGKKHIPPHKINYRANIWAVKELGCKRIISTNSVGSMKDHKPGSFVIVNDFIDFTRNRACTFYEEETVHLDMTYPYCDELIKAIEKSCQDLDIEYTEGIYVCTEGPRFETRAEVSMLKQFGDVVGMTGVPEVILAKELNLCYASICTVTNYASGIGEHKLTVDEVLEYLDKSKHELYNILIQTLSHLPEERHCNCKMSMDGAHI | Pathway: Purine metabolism; purine nucleoside salvage.
Function: Catalyzes the reversible phosphorylation of S-methyl-5'-thioinosine (MTI) to hypoxanthine and 5-methylthioribose-1-phosphate. Involved in the breakdown of S-methyl-5'-thioadenosine (MTA), a major by-product of polyamine biosynthesis. Catabolism of (MTA) occurs via deamination to MTI and phosphorolysis to hypoxanthine.
EC: 2.4.2.44
Catalytic Activity: phosphate + S-methyl-5'-thioinosine = hypoxanthine + S-methyl-5-thio-alpha-D-ribose 1-phosphate
Sequence Length: 267
Sequence Mass (Da): 30196
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A0A256LP02 | LDGYPRNLEQAEYLSEITDLDAVIHLDVDEEVLVDRLTGRRVCDDCGANFHVDFQPPEEAGVCDECGGELIQREDDTEETARERLQVFYDNTEPVIEHFRDEGDLVEVDGEAAPDEVFARIREVLDE | Catalytic Activity: AMP + ATP = 2 ADP
EC: 2.7.4.3
Subcellular Location: Cytoplasm
Sequence Length: 127
Sequence Mass (Da): 14470
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A0A924ILP6 | METAAAHTTTYAVLLQNLAFYTLASFSVLSAAGMLLVRNLIHSAYLLVLTFLSVAGTFFLLNAEFLGVAQILIYASAVAIMMIFGLMLTNKPAAPMPNHGILFRYIAMAIGIGIFSYACRLALIAPWVTSTPVLVDTPVVIGRAFFNEFLLPFEVAAVLLLMALVGALSVARKEA | Function: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.
Catalytic Activity: a quinone + 5 H(+)(in) + NADH = a quinol + 4 H(+)(out) + NAD(+)
EC: 7.1.1.-
Subcellular Location: Cell membrane
Sequence Length: 175
Sequence Mass (Da): 18776
Location Topology: Multi-pass membrane protein
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A0A7G9G8C2 | MKENGEEYNKIITIPNMMSFFRLALLPVFACIYLNAKTVRGYQAAALVLFISALTDMLDGRIARKFHMISRLGKALDPIADKLTHIVVVFCLCSRYRQVWILLIILAVKESFMGIMGIIYLRKGRMLDGAHFFGKVCTTVLFAVLLVLVFLPQLSVLWVNVLAAAACAACLVTWALYIPVFWKMKDK | Pathway: Phospholipid metabolism; phosphatidylglycerol biosynthesis; phosphatidylglycerol from CDP-diacylglycerol: step 1/2.
Function: This protein catalyzes the committed step to the synthesis of the acidic phospholipids.
Catalytic Activity: a CDP-1,2-diacyl-sn-glycerol + sn-glycerol 3-phosphate = 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycero-3'-phosphate) + CMP + H(+)
EC: 2.7.8.5
Subcellular Location: Membrane
Sequence Length: 187
Sequence Mass (Da): 21126
Location Topology: Multi-pass membrane protein
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A0A2M8UFK8 | MLPVLLLTVVIDLIGFGLILPLLPFYATSFGASPVTIAMLAAVFSIAQFLSATPLGGLSDRMGRRPVFLACMALTVIGYIWLAFADSLLTIFLARTVAGIGSGKISIARAIIADSTPPEQRARGMGLIGGAFGIGMILGPLIGGLLVGPDPQHPNYTLPALAAATSSGIALLLAIFTVRETRPNASHTLAGLALWRNPFAPLRQLNRVVVALIAINFSINFVFSQIEVLFPLFSAARLDWHAYEVGIAFTFIGTIVLSMQGFLIGPLTRLFGERKLLTMGMINLAAGTAMAHWIVSTPTMAFSIVLTATGVAMIGPTINSLASRSTEATQQGIALGTMESLAALGRTFGPLWGGWLFDRIGINVPYWIGGAILIVTLTLGWRSIHPKEQP | Function: Resistance to tetracycline by an active tetracycline efflux. This is an energy-dependent process that decreases the accumulation of the antibiotic in whole cells. This protein functions as a metal-tetracycline/H(+) antiporter.
Subcellular Location: Membrane
Sequence Length: 390
Sequence Mass (Da): 41337
Location Topology: Multi-pass membrane protein
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A0A2N2F4S3 | MSSNIVCPSAPKRILLKITGKLFTGPDGKTADATAVRALIPQLAVLAKSHCVGIVIGGGNFFRGSQQGTALGITPSVGHQVGMLATLMNGLMLQDLLAQQGLTSTLLSALPCPTVGHCICPQAINQALTRGDIILFGGGTGAPYVTTDTNAVIRGLQMDADQVWKCTDVDGVYSVDPKKNPLAERFATISYEKALALHVGVIDQTALIIAQQNDLPIRLFSIQEPEALLRAAQEPQFGTLISNQE | Pathway: Pyrimidine metabolism; CTP biosynthesis via de novo pathway; UDP from UMP (UMPK route): step 1/1.
EC: 2.7.4.22
Catalytic Activity: ATP + UMP = ADP + UDP
Sequence Length: 245
Sequence Mass (Da): 25815
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A0A1I7YUD0 | MVPLSEGFSSAQSTNIPSPCLLLGAFRQQRPKAMANISAADVEWLCPSLKLPADVVKLDLQDLLKYPECAGMPTFLAGGSLSELDEGIYAMHTRILMTFIFACLSIVGIVGNVLVITVVFKVPGMITPTNCYLVSLALSDCLFFIAATPTELSTLHLPSDYIFGSIGCSLFSYLPYLAINTSSLSIAAFTIERFIGICYPIQARYICTVKRAKMIIAGIWSFCIMYNSPWLYLATVKEDEEGSMCGFKLERDNWTYKTIFFGDFFAFYVFPMFLYMIIYGKIAFTLKKNDIRHQVTKKSHSNN | Function: Receptor for thyrotropin-releasing hormone (TRH). Upon ligand binding, this G-protein-coupled receptor triggers activation of the phosphatidylinositol (IP3)-calcium-protein kinase C (PKC) pathway.
Subcellular Location: Cell membrane
Sequence Length: 303
Sequence Mass (Da): 33824
Location Topology: Multi-pass membrane protein
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A0A1I7YYE3 | MTVTYSLDVSSSTFLGIHKLLFRWKGSIWKSTYPELLLWLFLYTILSMTYRYVLDQEQQTTFEDLAAFFYTYGDYIPITFMLGFYVSAVFARWGEIFNNLGWIDSPALLIATYMRGADDTARMMRRNVLRYLVLTQALVYRDVSTTVRKRFPTLNHLVTAGIMTENELKEFDKIVSPHIKYWQPMQWAFTLIRKARDARIIDNDIIYADLLEKLRQYRVQVLNLTLYDWVPVPLVYTQVVNLAVRSYFIIALMGRQYLITDRNIPNARSIDLKVPIMTILQFLFYVGWIKVAEVLLNPLGEDDDDFETNYIIDRNLQVGYSIVDDGYNRCPELEKDIFWESVVPELLYTVESAQRPYNPIIGSCSDLNTADDAFMLRPRKKRLFSTASSTIGAGPDRRTSIFGTDENCDVVPVLNHPFPRSGSVDQNFNGRHFSFHERSSRFGDFLKRKFTRQCSRRSRQDSESSVDLPPDKFNGMYSVSARLPSKNDNNRNWYQNGISRNSSMCSSVFMDSHTNPFNQTVVSNFGHSLHASIPGAMENADTSQLNTILEQTQAGEDNERAANSGTWTVNELLPVIQEEEQEKVRKIANSNNSPTASISGVSSEGTSMRKKSVASNDIRKEALVKSISRRNDSRKSSACPVDNSTSTETQIRPITVKDLKRAVDNDAFQYSSDDEDESDDQLRSAIEERRKQTERKRRKASSSTPQLRRNSSSAPGKMRWSLGDRDTASD | Function: Forms chloride channels.
Subcellular Location: Cell membrane
Sequence Length: 730
Sequence Mass (Da): 83638
Location Topology: Multi-pass membrane protein
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A0A059WSW0 | MIMSEIIESKIIRPEIVRPEIIGIAAVAANGVIGARNDIPWRIPADWQRFKALTMGNVLIMGRKTYDSIGRPLPGRTTFVITRDRMWRCNGVRAVPSVEEAIDQAILLDSQKIFVAGGGEIYRAAWNRLNGLEITEVDQYPQGDVRFPDISPDDWIETRRERHEGYSFVSYSRRSRRESTL | Pathway: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1.
Function: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis.
EC: 1.5.1.3
Catalytic Activity: (6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH
Sequence Length: 181
Sequence Mass (Da): 20661
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A0A059X004 | MKKLNVAIVVAMDKNRLIGKSGDLPWNIPEDRKRFKDLTMGHAVIMGRKTFESILKYIHKPLPGRTNIIVTRDQSYTADGCIVCHTLEDALKKATKIEEQNPNPEVHIGGGAELYKQVLPFVDKLYLSIVEGDYQGDAYFPDYSMFKKVVRNEQKTSNGYLYTILDLER | Pathway: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1.
Function: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis.
EC: 1.5.1.3
Catalytic Activity: (6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH
Sequence Length: 169
Sequence Mass (Da): 19294
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K8Z927 | MRSCGVIVEYNPFHQGHAYHLQKAKEKSGADCCIAVMSGNFVQRGEPAILDKWTRTKLALEAGADLVIELPWFGAVQPADYFGSMAVQLLSALQVDAFCFGTEKENEFSYMDFVKKEKAHQKELDQRIQQLNCEHPEWSYPKKMAEAYREIFPEEYKDMDQSNHLLGLAYARANLQLERPLELLTIERKGSQHREKELTSFASGTAIRKAVQQKDWTELKNYVPIATYQALKEGPCHRWEDYWAQLQGIGLSLSSSQWKQLYEVHDGLEERLQKSFYEANSFSEWKESLSCAHLTQAKIQRLATYILTQTTKEEVTYAWNHPYIKILGFSLQGRQWLKEKEISLPIVVNIRQQEERLLRLEQRYDMIYLSPYQTPKDYFSLYKPISKEEL | Function: Catalyzes the formation of N(4)-acetylcytidine (ac(4)C) at the wobble position of elongator tRNA(Met), using acetate and ATP as substrates. First activates an acetate ion to form acetyladenylate (Ac-AMP) and then transfers the acetyl group to tRNA to form ac(4)C34.
Catalytic Activity: acetate + ATP + cytidine(34) in elongator tRNA(Met) = AMP + diphosphate + N(4)-acetylcytidine(34) in elongator tRNA(Met)
EC: 6.3.4.-
Subcellular Location: Cytoplasm
Sequence Length: 390
Sequence Mass (Da): 45504
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K2BTJ6 | MLAGKQFNIPVVGTMAHSWIMAFDDELTAFQEYARLMPDNVILLVDTYDTMTGVDHAITIGKKLKGIRLDSGDLLSLSKMAREKLNQAGLYDTQIFASGDLTEDRLIDLKSCDAPINGWGVGTHLSTAYEQPALDMVYKLGAIEKNARWQYKMKCTDNHIKTSDPGILQVKRFYDGKKWLRDLIYHVDLGIAQSELNLAEKSQDLLIPIFKNGTLIYSRPSLSDSRNFCREQVKAFNASKAVSYSVQRDQQLIILKKQCMDSAQ | Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; nicotinate D-ribonucleotide from nicotinate: step 1/1.
EC: 6.3.4.21
Catalytic Activity: 5-phospho-alpha-D-ribose 1-diphosphate + ATP + H2O + nicotinate = ADP + diphosphate + nicotinate beta-D-ribonucleotide + phosphate
Sequence Length: 264
Sequence Mass (Da): 29763
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A0A1I7YGV5 | MVCLVDLDLSVDIIVTFSWPPSSPMAFIRRRRSHVLAALCFIVLFCFLFMSTHFRGANEGEGGYGVNIRREDLSEDERTEYDKGFKNNAFNQYVSDRISLRRSLSSPPRQCRYEKYPKNLPKTSIIICFHNEAWSTLLRSVHSVLDRSPLHLVSEILLVDDFSDAAHLKKPLDEYMAQFEKVRIIRLGRREGLIRARLVGASRATGTVLTFLDSHIECMEGWLEPLLARIKQSSKNVASPVIDTINSINLEYGFASTSLYGGFDWNLNFKWYKAPDRVLDARERKIDPLPTPTIAGGLFSIDKRFFYTLGAYDPDFETWGAENLELSFKTWMCGGRLEIIPCSHVGHIFRKKSPYKWPRGTGIIGYNNLRLAAVWMDDYKRYYYKWRNVTEDTDYGDVSDRVALRKRLNCKSFQWYMENVFPEQFVPGEAIGSGEIRSKANRSLCLDAKMEKYSPLTASPCNGKEWYLSQRGEIRLFDFCLQYGEGLPIPRLASLLRMSVEMTSCNLQQDSQEWKYDSYTGQISHALTGWCLTMTEDSGTMAMNDCDDTDPHQKWEFQNFYGFRARNYTLSQL | Pathway: Protein modification; protein glycosylation.
EC: 2.4.1.-
Subcellular Location: Golgi apparatus membrane
Sequence Length: 573
Sequence Mass (Da): 66156
Location Topology: Single-pass type II membrane protein
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A0A1I7Y928 | MLREEVMLYNDVIETTIPDTYNYTAFKVHAGYNLHVRHCSDVRFVLRADDDIITLPDRFVHFIDTGYFGNEDKAIYGIILKGGKPFREPESKWYIPKEYYSPDDYPPYINGPAYLMTQNSTKAILDKTNETTFFWIEDVLFTGXXXXIYGIILKGGKPFRDPNSKWYIPKEYYSPDDYPPYINGPAYLMTQNSTKAILDKTNETTFFWIEDVLFTGXXXXPSKNCGLDDIVVENNLLSEQLSVDYVFWKSHDKKDERVFVLNQSNKLLISAQISKNWRETVHSRRRTDPAQFEPTHVGTDPARAGSN | EC: 2.4.1.-
Subcellular Location: Golgi apparatus membrane
Sequence Length: 307
Sequence Mass (Da): 35588
Location Topology: Single-pass type II membrane protein
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A0A0D9ZXR0 | MEEQFILRVPPSVAERIERLMNESAAASSSSNPEDASLDLSFSEDGRNGTFMIGNESFPASLLDLPTVVESYKTYDDSVLIKTADIGQMIMVREEEDPAPEGVEYKHGLTPPMRDARRRRFRREPDLNAELVHRVEKDLISIMHGNASAILRAGEGGDRKKAGPAPATKPNVKQPAANGEEAEAERSDSDESVDPQVYVLDRCLPGFGYPSQIDIYIYIYIYIXGHDPGAYALWHWHLIDVFVYFSHYLVTLPPPCWVNAAHLHGVKVLGTFITEWEKGAEICEEMLATEASAQMYAERLTELAAYLGFDGWLINIEVKLDIQFIDNLKEFINHLTKTMHAAVPGSLVIWYDAITIKGALDWQNKLNEYNKPFFDLCDGLFSNYTWKAKYPQESAVVAGERKYDVYMGIDVYGRNTFGGGQWNTNVALDLLKKDDVSAAIFAPGWVYETKQPPNFRTAQNRWWGLVQESWGVLQSYPKQLPFYSDFDQGHGYQVSIEGVKVYGAPWDNISCQSFQPMPKYAGDRGLQTVINFEDEPYSGGNCVTVKGSLQQNEIFSEQLFNGGLSMEGESVKADERSGLGLSLDLSSGNNESSSILIADDTAAFTRKKQHRKYGSYVKADKAEPHTPVHQNWVVYKATIQPSAGFTLTGINIVCTMKTTSGTDPETDGDGISEAGANRSLHYHASLGHVSIRNTEETEFPPARSWVTEGEYISWSNGSDESKLASLKISWELENKQQAPFMKYNVYVEKLTADSNAKAPRIFLGVASVQVFYVSDLEVPSEVTALKFFIQPCGRDGSCQGLHECPKFHLVPVDSAM | 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
Subcellular Location: Cytoplasm
Sequence Length: 816
Sequence Mass (Da): 91010
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S4GJB6 | VRIDSGDLCVMARRVRAQLDALGAKNTKITVTNDLDEYALASLQNAPVDSYGIGTMLVTGSGAPTCAMVYKLTEREGADGVMQPVAKKSKNKATVPGRKLAYRSYDFSVDVNGGVASNGVADCEHVISGSESALATFKPQDSWEDLLVDYVQNGEFNTEFMGHDAIMRAQDYCAKALSRLPISAQSLMRGDPAIPTEINVLG | Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; nicotinate D-ribonucleotide from nicotinate: step 1/1.
EC: 6.3.4.21
Catalytic Activity: 5-phospho-alpha-D-ribose 1-diphosphate + ATP + H2O + nicotinate = ADP + diphosphate + nicotinate beta-D-ribonucleotide + phosphate
Sequence Length: 202
Sequence Mass (Da): 21611
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A0A385PPC2 | YARGCQLLLLGVFTIFYVMFTWWRDVILEASFEGQHTLAVQDGLRLGMILFIVSEIMFFFAFFWAFFTSSLAPVFNIGGVCPPMGLDLINPWVFPLLTPILSLSSGGTFTWGHHRIARGWSDPCITAFHLPLILATCQPSFTALACVEAPFSTSESLYGSAVVKATGFPRVQALGGTDFLFVREERP | 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, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Subcellular Location: Membrane
Sequence Length: 187
Sequence Mass (Da): 20757
Location Topology: Multi-pass membrane protein
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F0V8I8 | MTVISACIMSRQKPLLARQFVEISKVRIEGLMNAFLKLVEHAGADHTYVESDCARYVYQPLDNVYLVLITTKHSNILEDLQTLRVFATIVQDACSGEGLSGGVNVEQVVLENAFSIIFMVDELISFGLREAISLAQIKTFTDMDSHEEKLQRIIQEGKEKEEKERRRQIAQRLDKERAAKAKPPSSGDAPFLASASLFAPTGAPPPSVPSLAAAADYIQMYGGSPEHVSALTSGVLGVGGSGGPDANAGYSSSSGFAGLGASKGMQLGPQRTTPLASLGLDARAPAERQPAVGTTLGAPGTGLVEATRLGAADGADEASALAAVGGSAGGAPVIVNPLVEPVHALVEEKVKGTLQAEGGVDELDIQGTFFVTVYDPSKAGLAAFRVSPEDKRFKTKVHPNMNRASYTQNVLELRCPTRAYTPNAPAAILKWRLQTKDESLCPLSISCWPSVAANGVTLTIEVEATEPSRTLHDVHFSFTCPSNVPHQILRVDGGETQHDGVSLHWRLPQMSVSELSTATLEFFAATSVSTVLPFSVEMHSKETICEFDVSEKRADAFVTLSRVFAFALVTLSLDRVFFERRWFAACSACQAAAATMRRPFYLFAQVLECFHMEKTEPIAYALTRRTDYMLTVRA | 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.
Subcellular Location: Cytoplasm
Sequence Length: 634
Sequence Mass (Da): 68348
Location Topology: Peripheral membrane protein
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B1PJY3 | TLALFNPNMLGDPENFTPANPLATPPHIKPEWYFLFAYAILRSIPNKLGGVLALAASVLVLFLIPLLHVSKQRSMTFRPLSQILFWTLVTDLLILTWVGSQPAEHPFIIIGQLASLAYFTIILILFPIASALENKMLNP | 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 membrane that is then used for ATP synthesis.
Subcellular Location: Membrane
Sequence Length: 139
Sequence Mass (Da): 15464
Location Topology: Multi-pass membrane protein
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A0A7C5MN51 | MKRILVINGPNLNMLGVREVDIYGKRDLDWINQKMSELAATLGITLDFFQSNCEGEIITKIQEGMNYDGIIINPGGFSHTSVAILDAIRSIDKPVIEVHLTNIFAREDFRNTVITGRGAKGIITGLGYISYLSALYSFYLLFKEEE | 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: 146
Sequence Mass (Da): 16364
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A0A1I8AKX9 | MSNKFEAVLLLQVSMMLLDIGFNTAEIVLSQHSSILLMLYILQDTNILMTLIVMLISFSSTFVFQAGLISLLLRRFTPTIIVSLLYLALTVAFHIVSLRLDVNKPAGNLWDVGITVLSVLQKLRSFLLLLLQTNVSFALRSPIPSRQCMAAIEDSAFRHDRASRTTIKTLCALSVSVNRNGFQIGETSHSEDVLEDVDVANCPSKNLVLAHLSVHGKRGDHHAKLNNKGCWTQVQLRTLIVPGRKHGSPGCGAFFPGRSVRRQRPTTCQTAW | Function: Required for ciliogenesis.
Subcellular Location: Membrane
Sequence Length: 272
Sequence Mass (Da): 30150
Location Topology: Multi-pass membrane protein
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A0A3L9LU15 | MILLTDIKPLFYINLLFGNPPHVIFNNSFAITKLGSICSLLWSSVFLCYGYKKTLYIVNDANEIRSLILKVFRLFLVLLCIFNNVVVGYYSHKKLCCVTDNLRSYDLATKIGHTGNRRIRYTMWTLVTVRIICCIIVGYTYHLYHEHDFLILFRMIEVACFFLQIDKFMGIVLLLYSRFRHLNELLLTNDVRVNVHVRSDRGLRLQDAWWLHNCLMDAAEILNSTYSMQLLFWITTITVNITSRIYIISEAWSDEYISKFQDKFFTVYDIITLVTLTTICHVTADQANKSGPTIFSSSLAPSRKFGFATENIEVGMYFKLRQLEFSTNGGSIRVNLPLLLSISAGITTFLVILSS | Function: Gustatory receptor which mediates acceptance or avoidance behavior, depending on its substrates.
Subcellular Location: Cell membrane
Sequence Length: 355
Sequence Mass (Da): 40975
Location Topology: Multi-pass membrane protein
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A0A9E7EVZ2 | MALDPRANNFDLMYQQVKAPEEGVAIEKPIYIHLTGLPEPRELIQPSKLLVLVRRTAPNVSFHCVSFGDNGFELLVLREWSLLDFSIYLDISSKVKFAWRIQRDMAEGGHSLESIKAGIEARKPDSDAYIDPQKQHAGAAIEVLPTQLIAGDSEGSWHTRTLASSSFMAQRLANSSEVVCQESVSEMDGEFDRSDELIYVERHPSNQSTNRW | Pathway: Carbohydrate biosynthesis; Calvin cycle.
EC: 2.7.1.19
Catalytic Activity: ATP + D-ribulose 5-phosphate = ADP + D-ribulose 1,5-bisphosphate + H(+)
Sequence Length: 212
Sequence Mass (Da): 23847
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A0A841QXX2 | MSAATEVVGIVAEYNPLHQGHVAQIKAVRKAFGDAPIVIALTGAFVQRGEPAVADPWTRARWALHAGADLVVELPAIFALRSAEHFAAGGVRLLHAVGVTTLVCGAENPDLAALKKLADGPNPTALQTALAQGLSYPAAMEAAFAATDPDIAPLLRTPNNILAAGYLRAIERYAPSLCLAPLLRERSDSAEGIAGISGSAVRARLQEGLVPRDMLPAYTYDDLSEALRAGVFPQPERYELLALQALRLLTPATLAQLGEFSEGLEDRWYAARNAATLAELWNDVKTKRYPQTRLSRLLVQVLLGMRRQDLNDAAKTGPAWVYPLAFTPRGAALLRNVTLPILDRYGKMRKTLPPQAVDWLVYDERATDLAALCCANPEYRAGGARFYRRPVTPTKELQ | Function: Catalyzes the formation of N(4)-acetylcytidine (ac(4)C) at the wobble position of elongator tRNA(Met), using acetate and ATP as substrates. First activates an acetate ion to form acetyladenylate (Ac-AMP) and then transfers the acetyl group to tRNA to form ac(4)C34.
Catalytic Activity: acetate + ATP + cytidine(34) in elongator tRNA(Met) = AMP + diphosphate + N(4)-acetylcytidine(34) in elongator tRNA(Met)
EC: 6.3.4.-
Subcellular Location: Cytoplasm
Sequence Length: 398
Sequence Mass (Da): 43101
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A0A345UJB8 | MHWLLKFFGILIAIIFISGSLFLLIFTRGSFFPHTDAIEPEEGRQPVAELTTVTLGGFEQHLLLRGHDDTKPVLLWLHGGPGTPQMPFAHAFGRELEEHFIVVHWDQRGAGKSNTADFDEASLTFEQQTADALELVHWLRERFGQDRIFLLGHSWGTRVGIALAAEHPELFYAWIGVSQVVDHGRATVMARDWLERRISLEERWTLGEIKIPAMQHDDYRRLAKIVERRGGGTDLPVSELIRIALRAPEYSMRDNLQLLTGMNRGGKPMHAQGIIKPYNLTEQIASLDIPAWFLNGRNDFNTPAALVREFYEQLEAPLKRYIIFPQAHTPFFASPELFVTTLIEMQAEVLAYHAEEGEP | Catalytic Activity: Release of N-terminal proline from a peptide.
EC: 3.4.11.5
Subcellular Location: Cytoplasm
Sequence Length: 359
Sequence Mass (Da): 40882
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A0A3D0PXH2 | MSVLDELVSGAVEDARAREKVVPLDEVKRRAAQAAAPIDASQWLKRPDGIPVIAEIKRASPSKGHLSDIPDPAALAREYEQGGASAISVLTEGRRFLGSLGDFDKVRAAVHIPVLRKDFIV | 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: 121
Sequence Mass (Da): 13022
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A0A1L5KW81 | MDDLFAKRKQHIQHYLYDAPCTYSLSVELDITHLLSELKSRGLKLYPALIYGLSRIVNRHEEFRMYLNADQQLCVYHEVHPLYTIFHPESETFSCLWSRNPEDFPAFYQGYLNDLKQYGHCTDFSAKPDAPENVFNISCLPWISFTGFQLNIQGGYTYLLPIFTFGKYHSENGRTLMPLAIQVHHAACDGFHVARLIQELQKWADEFKAPSHI | Function: This enzyme is an effector of chloramphenicol resistance in bacteria.
EC: 2.3.1.28
Catalytic Activity: acetyl-CoA + chloramphenicol = chloramphenicol 3-acetate + CoA
Sequence Length: 213
Sequence Mass (Da): 24840
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A0A6S4QNL8 | MSVEGTEKVSKLLNKALKMELTAVKQYLYNAALLRDWGFDNLAKIEVKEAYEELEHVNKFSDRILFLNKNPKFDGPERIKKVNSVEDIIKCNLSMELDAVKTYKTFIKACLDSKDYGSYKIFLDVLIDEESHVEHLMKQKNLIKTVGIEGFLHAQE | Function: Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex.
EC: 1.16.3.1
Catalytic Activity: 4 Fe(2+) + 4 H(+) + O2 = 4 Fe(3+) + 2 H2O
Sequence Length: 156
Sequence Mass (Da): 18032
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A0A1I5MU33 | MYKNKMSPVNHVLIGLDCLLGRVESAVLGMAILALAAFACANVFGRFVFSESIYFVEELNEFLMVLITFFGLGYVTRNGRHIRMTAIYDQLPAVTKKALMIVIALVTAGIMFALAYFAIEYVAKTASRGRLTPALKVPLYLAYVPVVLGFVITGVQYLLTAWRNLDFTDPDVYVSYRTRDEYEAVELADSSVMDDAGRDKHSPQPCNDARDAVLKEVK | Function: Part of the tripartite ATP-independent periplasmic (TRAP) transport system.
Subcellular Location: Cell inner membrane
Sequence Length: 218
Sequence Mass (Da): 24268
Location Topology: Multi-pass membrane protein
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A0A345UK64 | MISGLQANGAGSGHSNDLKKQICRHLEKFVTTQRLTRMRQVLDKRTRYVTVVLEDIYQPHNAAAVLRSCECFGVQDVYAVEGRNTFDISSKISRKAHQWLTLHTFKQAEAGDESCFKALKNKGYKIATLTPEAETRLDQLPLNLPLAFVFGTEKEGVSALARNESDFQVQVPMAGFSESFNVSVTVAITLYETMKRLRMPEIESGFPLSLTSAEKEAIWYVWLKNTVKKSQLLEQEFLQNIKRASNPGK | Function: Catalyzes the 2'-O methylation of guanosine at position 18 in tRNA.
EC: 2.1.1.34
Catalytic Activity: guanosine(18) in tRNA + S-adenosyl-L-methionine = 2'-O-methylguanosine(18) in tRNA + H(+) + S-adenosyl-L-homocysteine
Sequence Length: 249
Sequence Mass (Da): 28092
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A0A3G9FT71 | MKTNLKKLSMILLAIILATGFVFISCEDVGLAVEGDGARATTITNSSTGTHDGYDYELWKDNGNVSMTLENGGNFSCQWSNIGNMLCRKGKKFGASQTYSQIGNITIKYDAQFTPGGNSYLCVYGWSKDPLVEYYIIESYGTYKPTGTSKGSVSIDGGTYELYETTRNNQPSIEGTKTFKQFWSVRTSKRTSGTISVTEHFKAWDSKGMKLGKIYEAALTVEGYQSSGNAKITSHTLTVGGSSSGTSTGSTNTSSNNTSSGGTVSSTTTSSGATKVEAENMTKGGKYTGSTSSPFNGVKLYANDDKVSFSQNFANNSHTFKVRGASSNDKEAQVQLKIGGTSYGTFKFKGTSATEQSITANHNQGGKTATVELVCVNDNDTWDVMIDWIEISASSGGTTSTPATSTPAASTPAASTPAASTPAASSGATKVEAESMTKAGKYTGSCSSPFNGVKLYANDDKVSFSQKFGNNKHAFKVRGASSNDKEAQVQLKIGGTVAGTFKFKGTSATEQTIEFQHNKSGQTVTIELVCVNDNDTWDVLVDWIEMTAK | Pathway: Glycan degradation; xylan degradation.
EC: 3.2.1.8
Catalytic Activity: Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.
Sequence Length: 549
Sequence Mass (Da): 58264
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A0A1Z1N0S2 | GLVGTSLSLLIRAELGNPGSLIGDDQIYNTIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLAAPDMAFPRMNNMSFWLLPPSLTLLISSSIVESGAGTGWTVYPPLSSNIAHGGSSVDLAIFSLHLAGISSILGAINFITTIINMKSNGLTFDRMPLFVWSVSITAVLLLLSLRVLAGAITMLLTDRNLNTSFFDPSGGGDPILFQHLF | 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-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
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: Mitochondrion inner membrane
Sequence Length: 209
Sequence Mass (Da): 22360
Location Topology: Multi-pass membrane protein
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A0A6S4QM32 | MKGPVILIFEDALFEGVRESVQPATSHSNGKKRLRLGEIESAACSLMMRLRPRATTGLVKLVEFGCQFLLIVKNKKRLKAFETELTLHTEQLMGESTSESTGESTSEIALSVKKLLAREGIVFRAILTVEELAAQSFFSKKPLLRSSIQATRFNDPIRFEADILLPETTFLTVFGEESVHWHLHTHNTNNNKNNNNNNNNNANNHTNNNANSNANNNANNNVNSTITANHLDSNSTSIGLGMLEIVQPIEPDIAKTVNDDNDDNNNNNGHWKATSRYILSEKAVTVDTGIDKNNRNVNNSDVNNSNVKDRIQPAEIMKSSEKDEHLRHGLYETAYIEKWQAVSCHNWEQLAQNIMTRSRIVTVRRTTKETDIALALNLDGTGKSNIRTGLHFFNHMLENFAKHAQFDLNVAVEGDLHVDEHHTIEDTAIVLGTALKKALGGKQGITRYAFSLPMDESSATCLLDLSGRAYTVWQDQLKRERVGDFPIELVRHFFETLATAGAFNLHLTLAGANDHHQIESGFKALAKCFREASHRIGTVVPSTKGGL | Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 6/9.
Catalytic Activity: D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + H2O
EC: 4.2.1.19
Subcellular Location: Cytoplasm
Sequence Length: 547
Sequence Mass (Da): 60910
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A0A059X9M2 | MVGRREWSVWMITLVLAMAENGVIGNKGAIPWRIADDMKRFKALTVGKIVVMGRKTWDSLPRKPLVDRTNIVVTRRTGWSADGAVTASSLDDALNKAANATDVMVIGGGEIYHAALPRADRIELTEVHGAFDGDAHFAFDRASWREDARETHTTPDGLAYSYVTLTRR | Pathway: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1.
Function: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis.
EC: 1.5.1.3
Catalytic Activity: (6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH
Sequence Length: 168
Sequence Mass (Da): 18583
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A0A1V6DZC7 | MLFHNQVAEMATGEGKTLSAVLAAYLSVLSGRKVHIITANDYLAQRDSIWMKPLFEKLGCSVGLLQTGQPMPERQAAYRCDVLYATASALIFDYLSDNGLIASPEQRLQQGLDFAIVDEADSVLIDEARTPFAISGRKDSDLSLYTTLHKPVREVHKLQADYVGQLEQSVAEMLASGSAEHPELGRKCFLIQQADPNNERLQEWLMESSVRRKLEEFVEKAEGSPLLLAELHNQGFYSINPRDHSIQLSDSCQEQFAKLLGHSLVIPDLPAQIARLEKSAHSDEEKQRRREALSTEMEAIASQLNVINQLIKAYALYRRDVEYIVRDSEIVLVDTNTGRLLPGRHFADGLHQAIELKEQLRMSPESQTLAETTIQNFIRQYKYLGGMTGTARIDADEFLGTYKLDVIPIPPHKKCIRRYHPDLHFMGHAAKMNRIVADIQQVHAQGRPILVGTSSVQESEQVSARLTALGLAHTVLNAKNHSREAAIIAQAGQRGAITIATSMAGRGTDIKLAPESVALGGLHIIGTTRYYLRRLDEQLLGRSARQGDPGSIQFYVSLEDDLIKESKLSVARYMQFFQAADPGAHNLLVNKVVAEAQEKFSGYYHGARRQLVAFDNVVATQRLQIFAMRNDIIDGHMTVEQLLEEQLREVQAAGQSCLDWFTHTFPISFEQTPENTPAALIEIYRSAIGQAAAQLGFEKQAFDQLVLLGNLDASWRDYITALGVLKEGAQLQSYAQTDPVVAFSNQSAKMFIQFLEQYRTNVCKRVFPTLALIRRQSHRRN | Function: Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. Has a central role in coupling the hydrolysis of ATP to the transfer of proteins into and across the cell membrane, serving as an ATP-driven molecular motor driving the stepwise translocation of polypeptide chains across the membrane.
Catalytic Activity: ATP + H2O + cellular proteinSide 1 = ADP + phosphate + cellular proteinSide 2.
EC: 7.4.2.8
Subcellular Location: Cell membrane
Sequence Length: 781
Sequence Mass (Da): 87366
Location Topology: Peripheral membrane protein
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A0A7C3TQ55 | MKQHTFHVIHGPNLNLLGAREPEIYGTLTLEE | Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7.
EC: 4.2.1.10
Catalytic Activity: 3-dehydroquinate = 3-dehydroshikimate + H2O
Sequence Length: 32
Sequence Mass (Da): 3659
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A0A127SGS2 | MKLYPAMLYYLATIVNHHPEFRTAINQAGELGIYDEMIPSYTIFHEDTETFSDLWTEYVPNIEEFSRAYENDIQLYGSNHGMIGKPDVPENVFTVSMIPWSTFESFNLNLQKGYSYLIPIFTLGKYYEEDGRIVLPLAVQVHHAVCDGFHICRFVNELQELINS | Function: This enzyme is an effector of chloramphenicol resistance in bacteria.
EC: 2.3.1.28
Catalytic Activity: acetyl-CoA + chloramphenicol = chloramphenicol 3-acetate + CoA
Sequence Length: 164
Sequence Mass (Da): 19043
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A0A660TG68 | ENIIFRIAVKPTSSISKEQKTVDIQGIEKKIKTEGRHDPCICPRIVPVVEAMTALVVIDMYKRQAALMA | Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 7/7.
EC: 4.2.3.5
Catalytic Activity: 5-O-(1-carboxyvinyl)-3-phosphoshikimate = chorismate + phosphate
Sequence Length: 69
Sequence Mass (Da): 7723
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A0A660T305 | MDAFYASVEQEDFPEYRGKPVIIGASPGHRGVVAACSYEARKFGVHSAMPISQAYTRCKAGIYLPVRMKRYLEVSRKIMGVFNDFTPEVTQISVDEAFLNMTGTEKLFGTPEEAAYKIKTRIKATTGLNISIGIAHNRFLAKLASEYKKPNGLYIVSKGEELRFIDSINLGDLWGLGKKTLARLENNNIFTAKDLRAKDKTQLKAVLGNSSGDFLYKIVRGIDPGMYTGEIKNRSVSNEVTFGEDTKDPEVLKLTLMELSYKIIFRTLENEEKGRTVQLKLRYSDFTTITARETQTSPIISAEELYNIANKLLKKKWRKAEAIRLIGLGLGSLENINTPGQIDLFENNYEQSKKIEQVAMAIRKKGQKITKASLLNRNSRGDM | Cofactor: Binds 2 magnesium ions per subunit.
Function: Poorly processive, error-prone DNA polymerase involved in untargeted mutagenesis. Copies undamaged DNA at stalled replication forks, which arise in vivo from mismatched or misaligned primer ends. These misaligned primers can be extended by PolIV. Exhibits no 3'-5' exonuclease (proofreading) activity. May be involved in translesional synthesis, in conjunction with the beta clamp from PolIII.
EC: 2.7.7.7
Catalytic Activity: a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)
Subcellular Location: Cytoplasm
Sequence Length: 383
Sequence Mass (Da): 43050
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A0A4D6I7P6 | NCYLSVYALTRNPLVEYHIVESFGTYNPHRGATKKGTVEADHRTYDIFETTRTNAHSIDGTQTFPQYWSVR | Pathway: Glycan degradation; xylan degradation.
EC: 3.2.1.8
Catalytic Activity: Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.
Sequence Length: 71
Sequence Mass (Da): 8226
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C7S5J0 | GWGQMSFWGATVITNLLSATPYIGPQLVEWIWGGFSVDNATLTRFFTFHFLLPFAIAAAAVLHLMFLHETGSNNPTGLNSNSDKIPFHPFFSYKDLLGALLTTIFLLLLALFMPNLLGDPENFTPANPLVTPPHIKPEWYFLFAYAILRSIPNKLGGVLALLFSIMVLMLIPALHTAKQRSLMFRPISQTIFWTTAANIMILTWIGGQPVEDPYITIGQLSSILYFSLLLLLTPTLAILENKLLKL | Cofactor: Binds 2 heme groups non-covalently.
Function: Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex) that is part of the mitochondrial respiratory chain. The b-c1 complex mediates electron transfer from ubiquinol to cytochrome c. Contributes to the generation of a proton gradient across the mitochondrial membrane that is then used for ATP synthesis.
Subcellular Location: Membrane
Sequence Length: 246
Sequence Mass (Da): 27437
Location Topology: Multi-pass membrane protein
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A0A847YCJ0 | MRCKPLCTVRRFEVRLRVRVCAVVGIGIVGGMLPVPGGMTAAAAEETAETEGIRTAPALTLPFPGFERGDFRWKIGPPVVERPRDDAETTYFSIKDPSVVFFGERWHLFCTVRARPRTHQVEYLSLRDWRDRKPQRTFLDIVDGYYCAPQVFYFRPHRKWYLLYQTVMPDRKPQLQPAFSTNDRVDAPSAWSPPQPLFETSPDNVERWIDFWIICDEERAYLFFTSLDGRFWRASTLLEDFPGGWSRPVIALQADIFEAAHVYRLRQAEAYLAIIEAQGGGRRYYKAFLSDSLDGHWRPLAAERDHPFLGPSNVEFEGEPWCQSFSHGELLRSGYDQRMEVDAQAGLTMLFQGVGDAEMAGKAYGEIPWRLGLAVQRR | Catalytic Activity: Hydrolysis of terminal non-reducing alpha-L-arabinofuranoside residues in alpha-L-arabinosides.
EC: 3.2.1.55
Subcellular Location: Secreted
Sequence Length: 378
Sequence Mass (Da): 43440
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A0A847YB26 | MMSNILDRIVATKREEIERAKVRVPEAELLRRIENAPPPRDFLGAIRRSESIALIAEVKKASPSKGLIREDFQPVAIAQTYERHGAACISVLTDEPHFQGHLEVLASVREAVSIPLLRKDFILDPYQVLEARAHGADAVLLIAECLDDAMLAALYEAVIHWQMTPLVELYEASNLPRVIALGAPLIGVNNRNLRTFEVDLEHTIRLRAEIPADRSVVGESGIQTHADLRRLAACGVQAVLVGESLMREPDIGAAVDRLLGREPIRPEASPDTSPKASSEASAEA | 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: 284
Sequence Mass (Da): 31129
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A0A947VRX5 | MLSFSVTFFITVANLAVLYLVLRKLLWKPLRAFMDDRAERIRRDVDEAASVKRSAEEMRQRYDDLITNADEEAEWVLRDAEDRAAVRSREIVAEAEREAEAALRRAAERSALEVARARDQLAEEIAGIAVAAASVAARKGLDGEAERLAALEFIRELGGTGERSDA | Function: Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0).
Subcellular Location: Cell membrane
Sequence Length: 166
Sequence Mass (Da): 18520
Location Topology: Single-pass membrane protein
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A0A059WZU7 | MLIIIAAIAANWVIGKDNDLPWYYPEDLEHFKNITTGHPIIMGWNTYVSILSRVHKRTGKAKPLPKRMHFVLTSKKAAVIKIELQKLFPGFDQESFSDQVIFCSSFGEAVQRAEVLDKEVYVIGGEKVFETAIRDANAMEITEIDAEYDGDAFFPKFDKSLWNREVRKRDGFSFVRYTRKKLDA | Pathway: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1.
Function: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis.
EC: 1.5.1.3
Catalytic Activity: (6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH
Sequence Length: 184
Sequence Mass (Da): 21197
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A0A1I8A9P5 | MSRDDGVVHEEIIVRKYHGASPWAHLFHTLIYVTTLVLPLIIAFLTQGFWRKVELYREQPIVDFDGKSIMLIRGSRENEYVVWSSFHALNEAVESHLSVPLIEKQKFDWDDDGRVDKISIYAEFANVQFPVHSVVWVILLQYRLDQHFLVEVGALVIL | Function: Transmembrane component of the tectonic-like complex, a complex localized at the transition zone of primary cilia and acting as a barrier that prevents diffusion of transmembrane proteins between the cilia and plasma membranes. Required for ciliogenesis and sonic hedgehog/SHH signaling.
Subcellular Location: Cell projection
Sequence Length: 158
Sequence Mass (Da): 18419
Location Topology: Multi-pass membrane protein
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A0A0D9YH33 | MVFSCADSRVCPTLTFGLQPGEAFTVRNIASMVPAYDKRGQCSIGSAIEYAVVVLKVECIIVIGHSCCGGIKELLSLKEDRPNTFHFVDDWVKIGLAAKKVERENMLLPFDDQCTVLEKEAVNVSLRNLQSYPFVKERLQKGTLKLLGARYDFVYGSFEMWDL | Function: Reversible hydration of carbon dioxide.
EC: 4.2.1.1
Catalytic Activity: H(+) + hydrogencarbonate = CO2 + H2O
Sequence Length: 163
Sequence Mass (Da): 18291
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A0A1I8A3H5 | MNYLLQDLSSSFMKGIFRRFQDLTRRSCVDLRQNLSSWCRVKKTSKQKNRPPDLPKEENPNLDQYSNTSLVNQGSLDWCIASSSCLRPTGASLPSPSPSPPSRDLLPAILWVIPGKWTTPTDVPTSCRRRSGNVXXXXFSVHKEKIHIKKPRNRKTAHRTFLTKKIRISTXXXXKQIRISTNTVIHHSSIREVSIGASLRLLVSVQLELHCLPVIYFQDLSGKRFCGEHAIHDPEDQDRIPCPNDPKHTVAKSELEDHLANRCNARISGDPWIVENINIVSQSTEASEEEFRPSEEELSEVIGLVEKGYESIESTVQTRILEAPLVEKHLEEVQDTINATHIKHLQQISSIIGNLLADSLLMDDEEHGIFELGAGKAQLAYWMAKTAPKTQLAYWMAKTAPKSQFLLIDKMGSRNKWDNRAIRENESLKMSRLRCSIEHLDLSKVNNLKGVKRIVSVCKHFCGNATDGGIRCLVNAVKNGFDMSGFALAPCCHHKSTFEDYTGHDFLRSLGIETSXXXXSGFALAPCCHHKSMFEDYTGHDFLRSLGIETSRHFSALRHIATWATCGIKRSEQPKDQLANDPEELSPEKKEELGIKAKTILETGRARYLATIGYTVALYRYVDSSTSPENLLIVGKKIV | Function: tRNA methylase which 2'-O-methylates cytidine(4) in tRNA(Pro) and tRNA(Gly)(GCC), and adenosine(4) in tRNA(His).
EC: 2.1.1.225
Catalytic Activity: adenosine(4) in tRNA(His) + S-adenosyl-L-methionine = 2'-O-methyladenosine(4) in tRNA(His) + H(+) + S-adenosyl-L-homocysteine
Sequence Length: 639
Sequence Mass (Da): 71940
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A0A060CPC5 | VEPLLDSIEGANDRYLVANDFPAYLDAQAEVDDAFRDQERWDRMTICSTIRSGKFSSDRTIAEYASKIWEIEPVFIPEHESDDDDEDRVVAGLVDE | Function: Allosteric enzyme that catalyzes the rate-limiting step in glycogen catabolism, the phosphorolytic cleavage of glycogen to produce glucose-1-phosphate, and plays a central role in maintaining cellular and organismal glucose homeostasis.
EC: 2.4.1.1
Catalytic Activity: [(1->4)-alpha-D-glucosyl](n) + phosphate = [(1->4)-alpha-D-glucosyl](n-1) + alpha-D-glucose 1-phosphate
Sequence Length: 96
Sequence Mass (Da): 10985
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A0A1I7Y9L7 | MFVFRILHTVPYSNKPIVKDVVASLHSYFTFNMLLGLAILVSYKQFAGRPIECMLPMGFSGAWEQYAENYCYAQDTYFVPFGEAVANVGKDRRQNRQISYYQWISFFLLFEAFCFKLPTFIWKYFATQSGMRVGEILRLASNDANTDPDVKKSNIDALRVHLEGALRFHSRLKEKNLIPHKVIRCLNIKYSRFYVSFIYMISKVAFFVNIVVQLELLNRYLLPDELKNAFGINVVHKFITSNETWKENGLFPRVREMGQRQTHTVQCVLLINLFIEKIFIFLWAWYMSLAAFTVANIFSWLFVLFNFTSTHHFLMNHLEMAENLFDKQATENQKHAEKFINCYLGGDGVFLLRMIAQHADVVFTTELVHELWKSFCSIEAERKRRKQIREEMSRPFRFDIPRDVQKAADDFRDSIASSRRPSRAQLAGFVSPPKKLSIASLERKSYDDMLIEMMDRRASDSEDDESPRTQSRQSKQSKRSRVSFRNKFGV | Function: Structural component of the gap junctions.
Subcellular Location: Cell membrane
Sequence Length: 490
Sequence Mass (Da): 57454
Location Topology: Multi-pass membrane protein
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E2BEX1 | MYTHYLLSSLKIDTKSWKKHITQLQMLQFFILAYHISQLLWTDCGYPQWPALVLLPQHVFMLVLFAEFYYNAYIKKEPASAAATTKTETDSVSTEISHAKLEER | 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: 104
Sequence Mass (Da): 12173
Location Topology: Multi-pass membrane protein
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A0A1B1YVW1 | MMIFNTRFGRLFFFSTEPQTCSYLPDREAVMLFADPNKVIDTETYARLIDYGFRRSGDNVYRPHCRGCQACVPVRIPVADFAPDRAQRRAWQRNQDLAISTARTEFGTEHLDLYHRYQVARHDGRAVVRDAREQLEFLRSRFINTSSLEYRLDGRLVMVSVIDAMPQGLSAVYTFYEPDDAQLAKRSLGTFGVLRLIEECRTRGLPWLYLGYWIADSDKMAYKSRYQPLHAYQQGRWERLAPTGQEPETDP | Function: Functions in the N-end rule pathway of protein degradation where it conjugates Leu from its aminoacyl-tRNA to the N-termini of proteins containing an N-terminal aspartate or glutamate.
Catalytic Activity: L-leucyl-tRNA(Leu) + N-terminal L-aspartyl-[protein] = H(+) + N-terminal L-leucyl-L-aspartyl-[protein] + tRNA(Leu)
EC: 2.3.2.29
Subcellular Location: Cytoplasm
Sequence Length: 251
Sequence Mass (Da): 29270
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A0A0K0L8U4 | EMYLIEGLAGGRVATYTKLHHAAIDGVSGAEILTILLDPKPEGRKVAGPEEQWAGEQVPDPKSLFVRSAARLAISPARALRVGYEVARSLPGLKPLKSLPALVGIGGGDDDVVSRPTLIAPRLRLNGAISAHRRWAFGDVDLERVKAIKNAAHTTVNDVVISISAGAVRRWLVEHDDVPERSLQALIPISIRTDEEQGEIGNKVSGMIAPIGTHIEDPLDRLQFVHHTMLVAKETHQATPATLLQDFAQFAPPAIAARAAQVVFRNGRAGRFTPFNLT | Pathway: Glycerolipid metabolism; triacylglycerol biosynthesis.
EC: 2.3.1.20
Catalytic Activity: a 1,2-diacyl-sn-glycerol + an acyl-CoA = a triacyl-sn-glycerol + CoA
Sequence Length: 278
Sequence Mass (Da): 29968
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E2BKG6 | MNHQNPVTGLFPASPNNDHAWIRDNIYCILAVWGLSMAYKKIADADEDRAKTYELEQSCVKLMRGLLMAMMQQKEKVEKFKSSQNPHDALHAKYSSVNCQTVVGDTEWGHLQIDAISLYLLILAQMTASGLQIIFNLDEVAFIQNLVFYIESAYCTPDYGIWERGDKTNHGLPELNASSIGMAKAAMEAMNELDLFGARGGPTSVIHVLGDEAQKCQAVLQSMLPRESNSKELDSGLLSIISFPAFAVDEPNLIHLTRDAIVKKLQGRYGCKRLYYEPWELRMFENIECEWPLFFCYLILDYCFQGNKEGVAIYMKYLEDVMIKAEDGMKLVPELYSVASEDVSAEYAEPGSQSRIALGRCPFMWAQSLYILGKLLQEGFLAVGELDPLNRRLCSEKKPDVVVQVVILAEDTEIREKMAQHDIHVQTIAEVAPIEVQPAKVLSNLYTYLGRNKKLGLSGRKSRDVGILSTSKLYSLQDKIFAFTPQLTDMTRFYIASDYELMIDIFKGEINFLKSSWQNMLGRPLVVMPLKSIHLALDFVQAIIVKQSGLPNTEFPVCEIFVRFESYGCPLWND | 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: 574
Sequence Mass (Da): 64915
Location Topology: Lipid-anchor
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A0A3D3XQV2 | MVQFTGYNWYAFGITHKHAAAQERQNFALSETQLEAYFREIFPQNECAGFIINTCNRTSFFLFGKHPENIEKKFVQESGHIDISEIGDRYIGKQAITYLFEVMAGLDSQILGDFEIVGQMKTAFDKSKTYGTALGIIEKVVNQAIYSSRRIKNETGLSGGTSSTSYAAVQFLKSTLPNFSCAKILVFGMGQIGKRTLDNLVAEKGNKNIFVANRSFSKSQKQAALHCVQALRWDEALNQIGQFDAIVSAVSAPQPVFTAEILANANTKCIVDLSIPFSVGENVQKELDIELANVDQLSIAISEQMEQRKKWVPRAYEIIREELDKFKEWELAVDAVPIIKELQRQLHEEWSSKHTDIEKIERISAKIEARLFERIRKNPKELKELQKQLNGRS | Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 1/2.
Function: Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA).
EC: 1.2.1.70
Catalytic Activity: (S)-4-amino-5-oxopentanoate + NADP(+) + tRNA(Glu) = H(+) + L-glutamyl-tRNA(Glu) + NADPH
Sequence Length: 393
Domain: Possesses an unusual extended V-shaped dimeric structure with each monomer consisting of three distinct domains arranged along a curved 'spinal' alpha-helix. The N-terminal catalytic domain specifically recognizes the glutamate moiety of the substrate. The second domain is the NADPH-binding domain, and the third C-terminal domain is responsible for dimerization.
Sequence Mass (Da): 44516
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A0A291C3N6 | IDFLMFSLHLAGVSSILSSINFICTVQTAVFYTVNHEMISVIVWTYMFTSVLLLLSLPVLAAGITMLLFDRNFGSAFFDPMGGGDPILFQHMFXFXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXFASFAIVCLGCVVWAHHMFTVGMDIKSTVFFSSVT | 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-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
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: Mitochondrion inner membrane
Sequence Length: 167
Sequence Mass (Da): 18544
Location Topology: Multi-pass membrane protein
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A0A1M5DEI7 | MTSGPAEQVHDAVRDLVAAWLPTQRWFPGKGRQADIEVRRLTELLHSPQVTIWTARADYGDGEVETYQLPLVSRGEPVDNLEHVLLGTVETEAGNRWVYDALHDKDTTRAWLAGLVDQPAGDVRFTRYVAAEDVPVDEASLVMSGEQSNTSLVYGDAAIMKVFRRLQPGVNPDIEIGGELSRVGAHNVATLLGSVEADVDGAPTSLAMVQEFLTSATDGWVLATASVRDLMAEADLHADEAGGDFAGEAERLGGAVAQTHADLVTAFGTREATADEMVARSQAMQQRLDHALGVVGELADVADGLRAIFAAVAELEGGVTLQRIHGDLHLGQALRTVYRWVLIDFEGEPMAAIDSRREFDSPLRDVAGMLRSFEYAGHHRIADAGNDPQLAYRANEWSARNRDAFCAGYADVAGGDPRRHATLLRALEAEKAVYEAVYESRNRPTWLPIPLASLGRLAQDGDTA | Pathway: Glycan biosynthesis; glycogen biosynthesis.
EC: 2.7.1.175
Catalytic Activity: ATP + D-maltose = ADP + alpha-maltose 1-phosphate + H(+)
Sequence Length: 464
Sequence Mass (Da): 50268
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A0A5C9D0F2 | VAEIQRLLKVGFEAARGRRRKLCVVDKANVLESSRLWRETAKRIAPDYPEVELDFMYVDNCAMQLIRAPGRFDVIATSNIFGDILSDEASVLTGSIGMLPSASLGSVLNSSGLPRGLYEPIHGSAPDIAGKNLANPLGTILSAAMLLRHSFGLVEEAAAVEAAVFSALGAGYRTADLASASTPVEMRVGTKEMGVLVLASLLRPVPKTA | Pathway: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 3/4.
EC: 1.1.1.85
Catalytic Activity: (2R,3S)-3-isopropylmalate + NAD(+) = 4-methyl-2-oxopentanoate + CO2 + NADH
Sequence Length: 209
Sequence Mass (Da): 22166
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H9CTS0 | FVASHPWEVIVGTVTLTICMMSMNMFTGNDKICGWNYECPKFEEDVLSSDIIILTITRCIAILYIYFQFQNLRQLGSKYILGIAGLFTIFSSFVFSTVVIHFLDKELTGLNEALPFFLLLIDLSRASALAKFALSSNSQDEVRENIARGMALLGPTFTLDALVECLVIGVGTMSGVRQLEIMCCFGCMSVLANYFVFMTFFPACVSLVLELSRESREGRPIWQLSHFARVLEEEENKPNPVTQRVKMIMSLGLVLVHAHSRWIADP | Function: Catalyzes the conversion of (3S)-hydroxy-3-methylglutaryl-CoA (HMG-CoA) to mevalonic acid, the rate-limiting step in the synthesis of cholesterol and other isoprenoids, thus plays a critical role in cellular cholesterol homeostasis.
Catalytic Activity: (R)-mevalonate + CoA + 2 NADP(+) = (3S)-hydroxy-3-methylglutaryl-CoA + 2 H(+) + 2 NADPH
Subcellular Location: Peroxisome membrane
Sequence Length: 266
Sequence Mass (Da): 29907
Location Topology: Multi-pass membrane protein
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A0A256IMF6 | GYGIESDLARCEDEGRRPDARPEYVSQKAMDRGRNQMGSLGSGNHFLEVQRVTDVFREGVAEEYGLREDGIVVLIHCGSRGLGHQTCNDYLRRIEKEHGDLLADLPDKELAAAPAGSELAEEYYGAMGACINFAWVNRQLITHQARETFGEVFDADPIEDLGMELLYDVAHNIAKKETHEVGVDADGRPAVGDEAVDRTERELYVHRKGATRAFPAGHDDVPEVYRDAGQPVIIPGSMGAGSYVLRGGDESMSVSFGSTAHGAGRLMSRTQAKQEFWGGDVQDDLEAGQQIYVKAQSGATIAEEAPGVYKDIDEVIRVSDDLGIGDKVARTFPVCNIKG | 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: 339
Sequence Mass (Da): 36916
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A0A1I8APH9 | MMRHPHAWMGLLLWSLFTPAHAAWTVNMAPGATEVSNAVFDLHMTIFWICVVIGIVVFGAMFWSMMVHRRSTGQQPAHFHEHTWVEIMWTVVPFLILVAMATDRKSGSAG | 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: 110
Sequence Mass (Da): 12449
Location Topology: Multi-pass membrane protein
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S5XAS3 | TLYFIFGIWAGMVGTSLSLLIRAELGNPGSLIGDDQIYNTIVTAHAFIMIFFMMMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLISSSIVENGAGTGWTVYPPLSSNIAHGGSSVDLAIFSLHLAGISSILGAINFITTIINMRINGLSFDQMPLFVWAVGLTALLLLLSL | 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-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
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: Mitochondrion inner membrane
Sequence Length: 183
Sequence Mass (Da): 19698
Location Topology: Multi-pass membrane protein
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A0A1I6IJ21 | MGARVVVVGSINVDSVVRVVEHPAPGETVLGLGVELLPGGKGANLAAGAAASGADVLLIGRVGDDDLGRRYVERLAEHGVDTSAVSADAKQPTGQAFITVAESGENSIVVIAGANGDLAPDAAARAIPDDAAVVVTQLELGPEVAEAVLRRGRTLGATTVLNASPVSPAASALLELADVVIVNEHEWAALGSPADACVTLGAAGARWGDADAAPDPVEVVDTTGAGDAFAGALVAQFAAGASRADALRAAVAAGARATTYAGAQPWGFAAATG | Cofactor: Requires a divalent cation, most likely magnesium in vivo, as an electrophilic catalyst to aid phosphoryl group transfer. It is the chelate of the metal and the nucleotide that is the actual substrate.
Pathway: Carbohydrate metabolism; D-ribose degradation; D-ribose 5-phosphate from beta-D-ribopyranose: step 2/2.
Function: Catalyzes the phosphorylation of ribose at O-5 in a reaction requiring ATP and magnesium. The resulting D-ribose-5-phosphate can then be used either for sythesis of nucleotides, histidine, and tryptophan, or as a component of the pentose phosphate pathway.
EC: 2.7.1.15
Subcellular Location: Cytoplasm
Catalytic Activity: ATP + D-ribose = ADP + D-ribose 5-phosphate + H(+)
Sequence Length: 273
Sequence Mass (Da): 26735
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Subsets and Splits