ids
stringlengths 6
10
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stringlengths 16
1.02k
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stringlengths 117
4.4k
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A0A395JPN8 | MIRAFVYDPKTKTSQSGGEELIEMWKQSDRNIIWLDIEGKADEHDNALLAEFGIHPLAIQDALRPRHPPKIERFQQFLFILLRGLDADTNGINSGTIQLSCFISPRFLITRHAKPSASANWLFDQLEKDPSLIYDGPGALAIRLSNRLARRYVEILLELEPRLDEIEEEMFKSPDDTLLAELTGYKSRLRKLTRTANYHRDVAMALRSHDEPLLADSLVHEIVDLYEQIERTQTLANMYYQICNDLTDGYLGMSSHQLNRVMQLLTIITVIFVPLTFMAGIYGMNFEYIPELGFKGGYFVLLAIMAVVAVIQVFYFRRKRWL | Function: Mediates influx of magnesium ions.
Catalytic Activity: Mg(2+)(in) = Mg(2+)(out)
Subcellular Location: Membrane
Sequence Length: 322
Sequence Mass (Da): 37132
Location Topology: Multi-pass membrane protein
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A0A960MTY0 | YHATEVLRVSLDENLQMIGESVEFLAGHAKVIYDAEHFFDGYKDDPDHALATLAAAKEGGADWLVLCDTNGGTMPHEVAEITEVVMKAFGIPVGIHTHDDCGLGVANALASIRAGATQVQGTVNGYGERTGNCNLTSVIPNLQLKMGIEVVPDISQLRDLSMFVDDLANCAHNVRAPYVGATAFAHKGGMHVNAVQKVAHSFEHIRPGTVGNHQRILVSELSGQSNVLMKAEELGISLEKGGSEAKAILQRLKDLEQEGYEFEAAEASFELLIRQQLSTYQPFFDLHEYHCTFRHDGDRKYETCAATVRLSVNGNMEYTVAEGDGPVNALDAALRKALKPFYPSVEEMELEDYKVRIIDSHMGTAAKTRVLILSSDGHDRWGTVGVSYNIIQASWAALVDSIEYFLMRREAGKA | Pathway: Amino-acid biosynthesis; L-isoleucine biosynthesis; 2-oxobutanoate from pyruvate: step 1/3.
EC: 2.3.3.21
Catalytic Activity: acetyl-CoA + H2O + pyruvate = (3R)-citramalate + CoA + H(+)
Sequence Length: 414
Sequence Mass (Da): 45279
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A0A3D6DWU6 | MRSLAKELQCVRRGRPARGLRRHGSRQEVAVGACEQGICASGPDLRADPSRTGRGDPHRAPGSARRHDQPDRCSDQRRLRACQGLFQQSGRQREPGNDPARSAKSVRIPAQRAWQADQHSHHAATAFHLRRVARAWGPDVEADQGSIGDLRSDRPARRRLSLSIGKTWRRVDGVLLLDKPTGMTSNSALQAARRLFSAAKAGHTGTLDPLASGLLPLCFGEATKFAVDLLAADKTYEAELQFGARTATGDVDGLVVERCPVNFRLADLEAALPRFRGTVRQIPPMYSALKRDGKPLYELARQGLEVDREAREVTIHELTLLDFSAGRCRLRVTCSKGTYIRSLAEDLGKALASLAHLTALRRLAAGPLAVSDAVTLEQLAALADEDRRCWLLAPDRLLQSLPPVYLDDADALRFVHGNPVRSSGLPGKCRVYGGHRLLGLGERNEQGSLRPRRIVASA | Function: Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs.
EC: 5.4.99.25
Catalytic Activity: uridine(55) in tRNA = pseudouridine(55) in tRNA
Sequence Length: 458
Sequence Mass (Da): 50086
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A0A3D6E3F8 | MLLTLELLLILACLFYGARKGGVALGLLGGIGVVILLLVLEGPPSPRGREEGGILLCWGTFTWSGQKTTTQARLDACVEPSATVPPALGQTKGVLCGPGLSLERNLDASSSGL | Catalytic Activity: (S)-malate(in) + succinate(out) = (S)-malate(out) + succinate(in)
Subcellular Location: Cell inner membrane
Sequence Length: 113
Sequence Mass (Da): 11617
Location Topology: Multi-pass membrane protein
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A0A6A4V453 | MLKLIVAVDRNNGIGINNKLPWTNKEDLKEFKRITLGHGIIMGRKTLESIGKALPGRTNYVVTHKNELPYENVILIHDVNAFFESKRASKDVVFVIGGASLYEIALDYVDEMIISEVFGDYSCDTFFPKFNQDSFKLSTEVAYDGFIQKRYVRI | 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: 154
Sequence Mass (Da): 17587
|
D6SS21 | MSGFRNKKGNIYLIGPRASGKTTLAEDIAGRTGLKAVDADKALQEEQGQSIQEIVSGQGWEYFRDLESKFLQRTAGSGPMVVATGGGVVLGSANRELLKDFRHLTVYLQAEADLICSRLAEDPKPGQRPALSDLDFREEIRATLEKRQKLYMECADIVLAADQPLELLAEEVYRVYVDKKQEGQ | 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
Subcellular Location: Cytoplasm
Catalytic Activity: ATP + shikimate = 3-phosphoshikimate + ADP + H(+)
Sequence Length: 184
Sequence Mass (Da): 20376
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A0A7C1UJB1 | WTRLAGDGGGDGEKGGSGPRLKIHRARHLAELPSDVFPVPTEVGGTGAPGTLTVASRRVFVTAAEGFVELLEVQPEGRGRQRAADWVNGARVGTGDRLW | Function: Attaches a formyl group to the free amino group of methionyl-tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus.
EC: 2.1.2.9
Catalytic Activity: (6S)-10-formyltetrahydrofolate + L-methionyl-tRNA(fMet) = (6S)-5,6,7,8-tetrahydrofolate + H(+) + N-formyl-L-methionyl-tRNA(fMet)
Sequence Length: 99
Sequence Mass (Da): 10416
|
A0A7L2CHL2 | PYRAEDETSARFVPRFNFSVDDLLRRVDFNIKGDDLIVFLHIQKTGGTTFGRHLVRNIQLEQPCECRAGQKKCTCHRPGKRETWLFSRFSTGW | Function: 6-O-sulfation enzyme which catalyzes the transfer of sulfate from 3'-phosphoadenosine 5'-phosphosulfate (PAPS) to position 6 of the N-sulfoglucosamine residue (GlcNS) of heparan sulfate.
Catalytic Activity: 3'-phosphoadenylyl sulfate + alpha-D-glucosaminyl-[heparan sulfate](n) = 6-sulfo-alpha-D-glucosaminyl-[heparan sulfate](n) + adenosine 3',5'-bisphosphate + H(+)
EC: 2.8.2.-
Subcellular Location: Membrane
Sequence Length: 93
Sequence Mass (Da): 10902
Location Topology: Single-pass type II membrane protein
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A0A3E2HAC2 | MAVGSSAAISGSKALSGWETACLIQFLKMADVEFGTEFPELNLLTLEEATIDGEAVERVVVDENVIATTSHGSSMWTQTACISTTLPDGTPKSYFLKVAAGDLGLGMVEGEYESIAAIHAVKPEFCPKPQAWGTFKSNPDLHFLLTDFVEMEQEIPEKDAFTTMLADFHLTSRAMSPNGKFGFHCTTYNGNLAQDNTWTDTWEEYYKNNIVRMLQLEEEARGSSEELKELSEQLLEKVIPRLLRPLETGPNTLKPCLIHGDLWYGNTAIELDTGKPITFDASAFWGHNEYEVRTMRPAGVQFGRKYLNAYHDKFRQSEPTEDAEDRLALYALRSRIHDSALYPMNAGFRNLLIEQMRLLVEKYPNGYESQTPKLTIVDREVQTECVETECKKXPKTQYKEQVTMDTLRTTLQPITHNLPPPIRDLGISILGEECYKTLLLDIDPTATECIKLAISKGLGIGIIAASSIVKVPQILKLLKSRSAEGISFLSYLLETSSYLISLAYNYRQEFPFSTYGETALIAVQNVIIAVMVLNFTGKATTSAVFVAGLAVSAVTLFSRDILDMQTLSYLQAGAGALGVASKLPQIVAIWQEGTTGQLSAFAVFNYLAGSLSRIFTTLQEVDDKLILYGFIAGFALNAVLAAQMVYYWNAPAKSTTTAPATTTTKKSTKDKKRAKTPAKKADGAQKAAPATPATPTPKGKSPTTRRRG | Catalytic Activity: ATP + N(6)-D-ribulosyl-L-lysyl-[protein] = ADP + H(+) + N(6)-(3-O-phospho-D-ribulosyl)-L-lysyl-[protein]
EC: 2.7.1.172
Subcellular Location: Membrane
Sequence Length: 708
Sequence Mass (Da): 77924
Location Topology: Multi-pass membrane protein
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A0A219AQ60 | MRPPEADLLNKAIERGVKGLAKVVGYHEEVTSISKLREGLVFSTPHKFRGVPRSANTSFSQSQPPLSHSFSQFPGLSIASSGHRKRKSTDWSSNASKRSRSNSQLAKADHVENGATYSVQEPQGTSLVHQDHDQTPYANRIFRVLAISPAGRSISQFKAVIELLEGLRDAIKVHQSLYTDGKILHRDISENNIIITNPGNADGFKGMLIDLDLAKEEGKGPSGARHRTGTMEFMAIEVLLGISHTYRHDLEAFFYVLIWLCARRGWSLSKASGRRPKKSMLSRWYTGGYEDIAQSKRGDMDKNGLEVILREFPEVFDGVKPLCRAIRDVLFPHKYGLFTGTPQDPNILYDPIIKAFDDAIAEIGLGEVKT | 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 N6 group of A37. BUD32 has ATPase activity in the context of the EKC/KEOPS complex and likely plays a supporting role to the catalytic subunit KAE1. The EKC/KEOPS complex also promotes both telomere uncapping and telomere elongation. The complex is required for efficient recruitment of transcriptional coactivators.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
EC: 2.7.11.1
Subcellular Location: Chromosome
Sequence Length: 370
Sequence Mass (Da): 41159
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A0A2E8TZL1 | MYNNLRVNLIQPRFKLFAGAIVVSIAAVEGGPPAHASCMAAIKVCAAKAGVFAIQSFHPAASATRIGADILVTNRHVVANQPVARVVAPNGVRLNATVVPSSYPGDLIMLRVQDLPPGPVLVPSPTQSATTSLQTIGFDVGRQAIRIYTPGQITAVPPANAPLARLHHNAPSQPGNSGGALVNSDGHLLAIVAAGGEGRHDGIPATEIKTLKSLSGPAHRAAHDQISLAYRQCTAATDAAGRGRKPLTPDQSAFLDERCRASKNRQLFDLAAQAFGRRGHFDKSIELFTMALDQDPNAVNTRLSLVVTLHLAGRYADEIPHLRVLINTLPADVQVLRFAIQAGTWGGATDLADRGMALLKQHHPKLAPLAERFRNTPPPPPQGR | EC: 3.4.21.-
Subcellular Location: Membrane
Sequence Length: 384
Sequence Mass (Da): 40637
Location Topology: Peripheral membrane protein
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A0A0B8NQU5 | MLKSLMKITDKICNTLGHLSSVLFLLLLANVVYDVVMRYVFNDVSIAMQELEWHLFAAVFLFGVPFAVKTHGHVRVDIFYERFSPKVQSIIDILGVLFWLMPFSLLVAWYGIDFAYQAYDIGETSGDPGGLPYRWIIKATISVFSIYCNQWYRFDPPLA | Function: Part of the tripartite ATP-independent periplasmic (TRAP) transport system.
Subcellular Location: Cell inner membrane
Sequence Length: 159
Sequence Mass (Da): 18301
Location Topology: Multi-pass membrane protein
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A0A345DD66 | MKTLIDFFPVVLFFLSYKLTNDMFLATGVAMASTAVQMLLMKWKKIPIQIIHWVSLVLIVLLGSMSIYFHETIFLKWKFSVLEWSMGLAILVGQYVFNKNMLKLLLGHELVLADGVWKQLGLMWAGFFIFLGTLNIYIAYSFSDDVWFNFKLYGSLALTLLFTVLQGVWLAKHLPQDEA | Function: Plays a role in cell envelope biogenesis, maintenance of cell envelope integrity and membrane homeostasis.
Subcellular Location: Cell inner membrane
Sequence Length: 179
Sequence Mass (Da): 20615
Location Topology: Multi-pass membrane protein
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A0A2W6BXR3 | MTRRVLLVAHTGKASAVMHARRSAEHLMAAGFVVDVGSAEAAELAIDSVQAVTAAVLGTEIVLAFGGDGTVLRAAELARPAGVPLLGVNFGRMGFLTTAEVEDIAEVLDRVVRREYHAAQRLTLDVRVQRQNKMPTQPSSQWALNEVSLEHTTHSRMLEVLLRVDDQPVSRWGCDGVICATPTGSTAYAFSAGGPVIWPDTQTLLVVPNAAHALFSRPLVVSPDSTISLAVAGDALLVCDGRRSLSVYAGDVVHVKRGELPLLLAGLSRADFARRVVAKFQLPVTGWRRDAPLDPVEPTTSGSDYKNVTTTKTSGGG | 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 Location: Cytoplasm
Sequence Length: 317
Sequence Mass (Da): 33691
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A0A2W6E190 | FEVRDVHTSHYGRMCPIETPEGPNIGLIGHLATYGRINEYGFIETPYRRVIDGRVSDEIVYLAADEEEEHVIAQANAALDDQGGFSEDRILVRRGPQGAGVRVGATTTAYGATSEIDYVPSSEVDLMDVSPKQIVSVCTSLIPFIEHDDANRALMGANMQKQAVPLLVPEAPYIGTGVEARAARDAGAVILAEGDGTVVEVGGEHITVEYRPGQHDREGRPLGRRVHPLAKFRRSNQNTCINHKSLVNEGQGVSAGDILADGPSTHNGELALGKNLLVAFMPWEGYNFEDAIILSERLVRDDVLTSIHIEEHEVDARDTKLGAEEITRDIPNLSEEILKDLDDRGIIRVGAEVGPGDVLVGKVTPKGETELTPEERLLRAIFGEKAREVRDTSLKVPHGEEGKVIDVRVFSREDSHELPPGVNQLVRIYVAQKRKISEGDKLAGRHGNKGVISKILPVEDMPFMDDGTPVDIILNPLGVPSRMNVGQVLESHLGYAARWGWEGDGASSNDGASSNGSGASDGNRSGVSPKTQPRTDPAVWVSTPVFDGAHWDEEADAGRHPTIQHLFEILRPESASGTRLIGRDGKATLHNGRTGETYDNPISVGYVYILKLAHLVDDKIHARSTGPYSMITQQPLGGKAQFGGQRFGEMEVWALEAYGAAYALQELLTIKSDDVLGRVKVYEAIVKGENIPEPGIPESFKVLIKEMQSLCLNVEVLSTTGEEIEMRELDEDVFRTAEELGIDISRPERGSDEEDARRAAERSF | 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: 764
Sequence Mass (Da): 83368
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A0A6I9WIE4 | MEKEDTNIFIGDQWGKVDVRFSFCAVATLSLLNRLDAIDVEKAVQFVLKCMNFDGGFGSKPGSESHAGLIYCSVGLLSITGHLHLIDANRLGWXLCERQLPSGGLNGRPEKLPDVCYSWWVLSTLTILGRLHWIDKKGMIDYILICQDVETGGFSDRPGDMVDPFHILFGLTALSLLDENFSLKPINPTYCMPEYIIERLGLKSSRLEA | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the transfer of a geranylgeranyl moiety from geranylgeranyl diphosphate to both cysteines of proteins with the C-terminal sequence -XXCC, -XCXC and -CCXX.
EC: 2.5.1.60
Catalytic Activity: geranylgeranyl diphosphate + L-cysteinyl-[protein] = diphosphate + S-geranylgeranyl-L-cysteinyl-[protein]
Sequence Length: 209
Sequence Mass (Da): 23325
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A0A832QTL8 | MNLFDFFLAISPIFFVLIGILVFNRSGSFVSVVGWLFAVLVATYYFKTPLNVVLGATLTGVVKAFGISLAVIFTMFLIFLMKETGALKQIIEYVKGIARNKEEQTLFIGMGFGSLSTALGMVTPAMFPPIFLLLGFTPIAAIGVSVLCYAPMTSFSLFTIPLTLPVKVALAFGIKPEGITDINNFIWDYTLKVTILLPVISVMFAFLMLKVVSGKEAAKKHWIAALIAGLVLSGSALVISIFRILPVEIIGIVSGLITMLAVYIVYRKNSNKEIVTKSVFNKKVFKSCMPFILLIITSLIVNIPFIKMKLENILGQTEVVRIIADKTEDLNIFGNVWFWIMVVSIFSIFMLKPTTTQLNNIFKLWMKRIWGPFLAYSLFFAVAFIMAWSAMEVMDGRLVQSRYFGQYNMDIIIGSTLADIFGSAYPFTAPFLGLFGAFVGGSETASNVLFAKIQWEATHATVGSNIFMWIYAAHAVGGGIASAITPSKITNAAATIGVGGKEEAQFIKAVLVPALIMCAITGAMLMAIIYL | Function: Uptake of L-lactate across the membrane. Can also transport D-lactate and glycolate.
Subcellular Location: Cell membrane
Sequence Length: 531
Sequence Mass (Da): 58113
Location Topology: Multi-pass membrane protein
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A0A3L8T0W6 | MLIASPAPRSLQSVNKIATSMGLLADSQECFRQMLSMSCYMNNTAFVFWKQKRPVSTTGLQLLMHFQSGVSGEDTKEDAGMLKTSENVERFFYFEDEQAGETGLTSEPQIAAQLCPTCSKWYPHPQLPPQVVLSFLWTLRPLGVTLYSRASITLAGTCGILLHESGKKLQQETINQKHNIRFQASILKALAGKQEPGFQSKCAGLTSGINTQQFDQLPAKSVYSCGQGNGYRIKTGQGEEGQLVQRQELGIYEVSAKDKWISPVSLGKLQPEFIARILSLMETIKTYISQPVKAAQGQASVSQTPVRTFSPVHPLPSALCGQDFTLQPLGMPRKAAWRRNAPVGFSNPEMAVSSSRHWQGRADPFGVVAASSRSRLPEQKTSESPLSWFRGVYLPPALHPLNKTFVKGGEWQDIDSTQEKRRAFLQGFCRNHNSRKKLQTHLVHLVSRIYVEDRHKVLYCEVPKAGCSNWKRVLMVLSGLAASANNISHDDVHYGKHLRKLDSYDLKGIYARLNMYTKFVFVRDPMERLVSAFRDKFEHPNSYYHPVFGKAIIKKYRHNADEEALKTGSGVKFKEFIQYLLDSHRPVGMDIHWEQVSKLCYPCLINYDFIGKFETLEEDANYFLQLVGAPANLKFPKFKDRHSSDERTKEEKSHLQSPWCQSVIKEALHISPGGRTSHSKGKSQVDPTVGPRQCAAPDYRNSPNGSALTQQNLAHNLFAALLYLKISLCNTEAQAGWFSIASHTPRTSQAAVGAPGITVPVKRVAEKNPFHWCVGSAVLREPDVVVREEAEHFELGSLETAEGLGIE | EC: 2.8.2.-
Subcellular Location: Golgi apparatus membrane
Sequence Length: 807
Sequence Mass (Da): 90231
Location Topology: Single-pass type II membrane protein
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A0A1Y1SHD6 | MIEERVVAVDDDWIIFDPGLIVEPTPASFDPAAWGRAVVGSAEGRSSAWFIEHEEQAWVLRHYWRGGLPGKLFKDKYFYPGRERARPFREWRVLVQAHADGVNVPRPVAARLHRHSLLNYSGDILMQRIVGAHSLADKLADGSMTPALWDAMAMAIARCHQAGYWHADLNARNLLCRDGQWWLIDFDRARKRTAGTWGYENIRRLKRSLDKLSAAGELRYSRQQWRDFVEAWHVGLCGPG | Pathway: Bacterial outer membrane biogenesis; LPS core biosynthesis.
Function: Catalyzes the ATP-dependent phosphorylation of the 3-deoxy-D-manno-octulosonic acid (Kdo) residue in Kdo-lipid IV(A) at the 4-OH position.
Catalytic Activity: an alpha-Kdo-(2->6)-lipid IVA + ATP = a 4-O-phospho-alpha-Kdo-(2->6)-lipid IVA + ADP + H(+)
EC: 2.7.1.166
Subcellular Location: Cell inner membrane
Sequence Length: 240
Sequence Mass (Da): 27517
Location Topology: Peripheral membrane protein
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A0A1T2KTU2 | MRIIIGILIVILIVLQYRLWVGEGSLAEVHGLKREIESQKAELKQLKLRNQALQAEVADLKQGLEAIEERARSELGMIREGEVFYQVIEPQEGKSQ | Function: Essential cell division protein. May link together the upstream cell division proteins, which are predominantly cytoplasmic, with the downstream cell division proteins, which are predominantly periplasmic.
Subcellular Location: Cell inner membrane
Sequence Length: 96
Sequence Mass (Da): 10939
Location Topology: Single-pass type II membrane protein
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A0A2S9JFV2 | MVCLVRLRRIILSSPLICAAASCANAGEIGDAVKSLAGAATIRERISLKDLGLTQPVVLGSTDARREIYLPVPANVSLAEPSLVINGHYLRADGGRTTYTLALDGNVVAARSPADDAGDANIRIGVDGAPRPSGFVRLGLAWSSVTGRFLCDDERSIGNVLQISPDSYFDYGYDPSGVKDIAGAWSALPRKVLLLIAADTLENASYDAAWRLGVALERAGKAVEIVALPKPGSEVDVTGLDIPAPLAAVPAFAALAKGGKITLSSDAEVGALLLLNAPQVRAHIAVADPALAAGLKAALDAVAGELAKADPAAAGVLDALSTRNDTLLQPAGPKAVEIRTMAGRPVIAVAPDAAAAASNLFDSLWRRTALASRLVLNTVGKPEIGADSVALGAIDQAAGNLDVVARGDWTTTFDMGAGLFAGKVPSTMDIEVAAAPGATATSPVASVFINDYLLGAKRLAADGKPERISVAVPSYTLLPRNTVRVQFQRQPASDNCREVPQAFPAAVLPGSRIWLKSAPAAQDFSGMVSQLSGDSVVMVPQAWQAIATRTLPAVIHVADAAGVSPARADFSASATNASLTPQKPFLAFDVAVAGAAEAVKVAGDRVSIADKKGNIFYDVSGLDRIAVLQAVTDMKQPGISYRTIGQGPQFDAPFRFARGDIAVLGQEGILASTSSSGVPLYLNEDGSQGASNEPFTWSKLLDPDFWAHNLSWLITVIIIAAFLLLLLLAQRARKRAGSDQA | Pathway: Glycan metabolism; bacterial cellulose biosynthesis.
Function: Binds the cellulose synthase activator, bis-(3'-5') cyclic diguanylic acid (c-di-GMP).
Subcellular Location: Cell inner membrane
Sequence Length: 741
Sequence Mass (Da): 76797
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A0A960I6P0 | MDNDRDRDDDLDEGVRLIGLQDDDDDVALPHWTEPATSQVPTVGEDDDLTAWASLSSTPRWRDDSRDYDDEVRLVDPAQVPLDDDIESAAPRRRQSSVFGDDYDDVDIEDELDDVGLTAPPRPATARRSRTGAAHQAPQRSAPRRPGAPRGVGADRNMGQAVLTGVGLAALAIVCFVIGEEITLILVAGVLTLAASEYFVNLRRVGYQPATLLGLAAVASLPIAAYWRGDVAIPVIIVLTMVFGVVWFLLGLGEERPVPNLGVTLLVVVHLGVFGSTAGLMLDAPHGIGMLLSAILLAVAYDVGGYLIGSSKGRSPLSEASPNKTVEGLLGGCLAVILVALAVIGIAGIEPFGGDAGGIFEALMLGIVAAIAAPIGDLGESLVKRDLGIKDMGSILPGHGGFLDRFDALLFVLPATYYMARLVL | 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: 424
Sequence Mass (Da): 44672
Location Topology: Multi-pass membrane protein
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A0A6I9VRW8 | MKTQKWEELNVQLSDSILKTLKQLRFFDMTPVQAACIPLLLNGKDVAAEAVTGSGKTLAFLIPLLEILQKRTEKWKLMEVGAIVISPTRELATQINEILKEFLNKIPSLKQALLVGGVTLKEDTEKLKKGANIIVATPGISCIR | Function: RNA helicase.
EC: 3.6.4.13
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Length: 144
Domain: The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.
Sequence Mass (Da): 15911
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A0A1T2KSX8 | MLSQADHCVKCGLCLPHCPTYRLTSDEGDSPRGRIALMQALAEGTIQSPRAGFHLQRCLGCRSCETACPSGVKYGAMLDATRELLLQESGNEAGLNWLATNAYKPWGRHILRAYQKSGLRHLARTVGGTRFRRLDQLLPPVESDASSREVYPAAGKTRGRVGLFTGCVSRLTDKTAIEGAITTLTLLGIEVIVPRTQACCGAVQLHSGNTTKNSQLTENNRQAFSRWELDAILTLASGCGGHLLEQQQGGSLDTAPIKEFSQFIMQLPWVEELNFQPTAQRIMLHTPCSLKNVQRCPDEPFRMLNLIPGIQIEPLPDTGCCGGAGTYMLNQPEMADRLRSPMIELIAKTKPDFVATSNTGCALHLRAGLVEAGITIPVVHPTEIIARQLPIEAGN | Cofactor: Binds 2 [4Fe-4S] clusters.
Function: Component of a complex that catalyzes the oxidation of glycolate to glyoxylate.
EC: 1.1.99.14
Catalytic Activity: (R)-lactate + A = AH2 + pyruvate
Sequence Length: 395
Sequence Mass (Da): 42964
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A0A2E6X9D9 | MTLSGSAFSKLNRSLQLSEEERDRLFKKMIIEAPDPVHIWVFGFGSLMWKPGFVPIERHPALLRGFERRFNIWSTKGRGTEKHPGLTLCLEPAIYGRCKGIVYKISPKTRIRDLKYLWDREMTSGVYNPKWITVELDDGSELRTLTWVVNKFHSRYAGPRSAAEMAKIMAHSKGKYGTCRDYLVNTIKEMAKIGECDPKLNEVLELIENNSSLS | 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: 214
Sequence Mass (Da): 24584
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A0A832JS67 | MDLWLEVLLLSVGVSVDAFAVCLAAGLCLRGGAALKGLRLPLSFGFFQFLMPLLGFRLVSASLGFLSSLDHWVGFALLFWVGLRMIRRGLEGEVEEVPFWEEMGLRKVLVFSVATSLDAFAVGMAFPSLRVPPLPTSISMGVLTASISTAGLMLGCGTSRALGNRAEVLGGAILLGLGLKVLLEHL | Function: Probably functions as a manganese efflux pump.
Subcellular Location: Cell membrane
Sequence Length: 186
Sequence Mass (Da): 19765
Location Topology: Multi-pass membrane protein
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A0A7X7XQ10 | MHKVSIRSKLTPDQVFTIPNILSFFRLLLIPLIVFLYVGKELYGWTLVVLIISLVTDIIDGLVARKLNMVTDFGKFIDPVADKLTQLAVLFCLVTRFPLMWIPISIMLLKEILQFALRFVVFRYTGEVHSAEWHGKVATFLIYVMMSLHVIWYGITDVVSTLTITITSLSMLLSCVLYTISSAVIIINIKRRKKDKEQLNN | 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: 201
Sequence Mass (Da): 23038
Location Topology: Multi-pass membrane protein
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A0A389M7R0 | MRKYGLVGKKLSYSYSKIIHTFLIEYYNLSAVYDLIEVDFIDSKLLAQYDGLNITIPYKADVIPFLQKNLSPIAAVNTILKNGDELIGYNTDIIGFSYLVEKLAITDIKKIVILGSGASSKMVAHFFADAEIIVISRNHPQYNYEYLQTITADLLINTTPVGMDAYDSPIPSELLTHYRGIIDINYNPLNSKLGMDAKKQNIPYINGLYMLIIQAVRAFEIWFELSVDPSVVEEIYYHICFLTHPKIALIGMPMSGKTTAITAFFGCDLDDQIIKRSGEKIADMLDRGTFRRAESRTLQALVNEGHKLIALGGGAILNFENLEIIKDYLIIFLNTPLEVLQKRIQTDTRPLLKKKGDLEKLYEKRIPLYKQYANITIETNELEAKLNEYFNN | 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
Subcellular Location: Cytoplasm
Catalytic Activity: ATP + shikimate = 3-phosphoshikimate + ADP + H(+)
Sequence Length: 392
Sequence Mass (Da): 44552
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A0A7L2CEA2 | RWRLQPEDFQRNYLPMQIGQKVYLLYEIRWSSGSIWRNWCSNHSKKHAEVNFLENHFSDRPQAPCSITWFLSTSPCGKCSGRILEFLRLHPNVTLQIYAAKLFRHHDIRNRQGLRSLIMNGVPIRIMTPPDYSYCWRNFVAY | Catalytic Activity: a cytidine in mRNA + H(+) + H2O = a uridine in mRNA + NH4(+)
EC: 3.5.4.36
Subcellular Location: Nucleus
Sequence Length: 142
Sequence Mass (Da): 17017
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A0A2C5XVD7 | MSSPDVFITSSPRARRQALTANMSSSPGLPSVQEILSQKPQRPPIRSTPLEKNAPACKSRPWRALHGEEAAKRNDSGIHEAVEDIDTSFSVIEVPADSLKAGAKAQRLKKAGQKSAETPQPPATPTRSPVDDQPWRKYKSPNRSSEPLANELKPASSGNDAPDCSRYFIKPSEANKTAKKVEDEPLNLEAAMTRRTDWTPPTQRVRIILDSDDTPDVDPMRHSQDFNEKATSFETVLAPFKCDDAVQMQTGSETTDDSGFPKKRKLLELVQTNAGTASKPCKKRKAPKKTRTITEIATAAYRPVTQPDDVASQGKAPDGAQAADTGNGKTKPRKRPPKASKKKEAPPKPILLSPEAAMRRVAHQDFLFGTSSQLAREQSPSSKPRPTTSHSANVDLVDLRTPINSDAIEPAEQRQTLWDAAARDEDGDLFDVELGLLTDAPPELAEAAPEADPFGYVRSDNPVTVSLPSLSDTDEGRGGEPSASLPVMITAESMHNIPKYVPGAERPSAAEKEKQKTQAVKGPEGRAGPRYELFTDAQLAKQVAQYGFKPVKKREAMVALLNRCRPDAVLDPSGTRSASTMAVVKKRGQGRTKAANAGGKEAQEPAAKEKRSRGRGFDISDEELLKMVPTRKRSPARISDAVKEPTKGRRRQSRSRAGSVSHDEAISPTIEKPGRGRSRRASKVRDSAEPPVEKKRRRSRSRVGSVSDDELEMWFMTPTRGERSRDRTIREQPPPSAQPPLSPRKGKSAASKPAAKRSTRKTAPATPKRRSRSRRKTPEMGDSQSESGSDTSASSSMGFGPSVDETELTLAMSSPTDQQRELFAQINKAVTTAPRTREPTQPSWHEKILMYDPIVLEDLTAWLNSGQLTRVGLDEEVSPVEVKAWCESRSICCVWRMSIHGKERKRY | PTM: Phosphorylated in response to DNA damage.
Function: Regulatory subunit of the SLX1-SLX4 structure-specific endonuclease that resolves DNA secondary structures generated during DNA repair and recombination. Has endonuclease activity towards branched DNA substrates, introducing single-strand cuts in duplex DNA close to junctions with ss-DNA.
Subcellular Location: Nucleus
Sequence Length: 907
Sequence Mass (Da): 99432
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C7Z6D9 | MASIQRPNRRIVGVSTKLYFSAARTREYVDQLLQLLSVDSSLLNDIDVFIIPDHVTLVSVINQVKDHKIWCGAQDTFWEDSGAYTGEVSSSVLAEVGTRLVEVGHAERRRIFGETDEITAKKAAAAARNGMIPLVCIGEQTRGETHTTAVTQCQTQIEAVLSAVPEDAEVVFAYEPVWAIGAAEPAAADYVVGVTSAIRKLESIQKRSGSTRILYGGSAGPGLFEKLKDGVDGLFLGRFAHDPDRFVKTIQEVARG | Pathway: Carbohydrate biosynthesis; gluconeogenesis.
EC: 5.3.1.1
Catalytic Activity: D-glyceraldehyde 3-phosphate = dihydroxyacetone phosphate
Sequence Length: 256
Sequence Mass (Da): 27793
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A0A0C5DFC0 | VMVTSHAFIMIFFLVMPMMIGGFGNWLIPMMIGAPDMAFPRMNNLSFWLLPPSLILLLISSTVEMGCGTGWTLYPPLSSNMAHNGAAVDMTIFSLHLAGISSILGAINFISTIFNMRTNNYSMKFMPLFVWSILITTILLLLALPVLAGAITMLLTDRNFNTTFFDPLGGG | 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: 171
Sequence Mass (Da): 18747
Location Topology: Multi-pass membrane protein
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A0A7Y3TB71 | MNYRHAYHAGNHTEVFKHSILVFLLEHLTQKMQPFFVLDTHAGIGMYDLESNQALLTGEKADGIEKIYDIGIPSCQRYLDIIVSVNAGPLKYYPGSPEISRQMLRPTDRLIACELHPDDYFALQSRYRSDRRVTIQNRSGYEAINALVPPVERRGLVFIDPPFEQKDEVQQMISALNKGMRKWATGIFCLWYPIKGSKIGDAIADAVVSAQHPKSLRIEFLPFRKDGENLAGSGIIICNTPWKLDEWARSLCQDISSKLGDRNGTWSVKWLTAEGGAQ | Function: Specifically methylates the adenine in position 2030 of 23S rRNA.
EC: 2.1.1.266
Catalytic Activity: adenosine(2030) in 23S rRNA + S-adenosyl-L-methionine = H(+) + N(6)-methyladenosine(2030) in 23S rRNA + S-adenosyl-L-homocysteine
Sequence Length: 278
Sequence Mass (Da): 31455
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A0A0B8NWM4 | MQARQAFVFAHAEQLGLFNQAKAADTAIAKGFDQFKNDAGEFIFCINSEENAKDDVNAYEHAFALLAYAWHYKVSGSAASLEQMENTYNWINTVLKDEQNLGLFYSRTEREFKSQNPHMHLFEALMSCYEVTQDSKWLARAEEIYQLFNNYFLEDDKMREFFDMEMGTSHPACQHIDPGHHYEWIWLLNHYAHLSGKSLGHQMKALESFVKPNGQNANGLVRDEMHQDWSEYRNTSRLWCQTEYLKAQIALFEQTQDESYIPEIEGAVNRIFDVYFAPAFPGGWVDQVDEHGAHVSKTAPASTFYHIYVAFTELLRLSNSMKKETIPSFNFVTGKIDGENVIAKSTILSSLEGIFSDTEAFAKLDPNKVIYNVEMVAAEEKNGELHFGVSHIEPGTVGNEFHITRGHIHKVEEQAEYYFGIAGNGLLLLQDEAGEVTYQDVYPGSVNYITGHVAHRLVNIGDEKLSVMAVWPAIAGHNYAFNNGEGFNARVFKTETGYEIK | Pathway: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 2/4.
EC: 5.3.1.9
Catalytic Activity: alpha-D-glucose 6-phosphate = beta-D-fructose 6-phosphate
Sequence Length: 501
Sequence Mass (Da): 56986
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A0A7S0Z4G2 | HLDAWRSANVEGGVSQWTRAMRLVTALGDHGAELLDHAYNVDPTSPNANEKPIRILSLDGGGMRGIATLVMLERILKATQNWCVGDCFDLIVGTSTGGIIAVGTGLLRMTTEELNELYTNMGDEIFPKKDSYITQVYKAFQRGQEEARNFEIMLNKALDGEAEKPLYTIASHPRWYSSRFPPPRVALVSRLVSRSPTTTFLMRSYHHEGQAKGHLGRLPGEHRASLVQSIRATTAAPWYLEELKVDKEIGGTGGCACEAKTDSEQRQGEASASGANGKDSPGTGASGAVEDDVVKYDVQKTPTHVQSELRLIDGAIASNNPTAVAVFEARRLFSQSRPLCVVSLGTGASVPHARGARNPGWLDNTIHATCDVDQVDATIRHLLGSKDSYYRFQPIADIFGCELNDTSPETAAGLRRGAAAYMDSMEHQVNKLASVLRREYVPAANSASSSVRGGDSS | Function: Lipolytic acyl hydrolase (LAH).
EC: 3.1.1.-
Sequence Length: 457
Domain: The nitrogen atoms of the two glycine residues in the GGXR motif define the oxyanion hole, and stabilize the oxyanion that forms during the nucleophilic attack by the catalytic serine during substrate cleavage.
Sequence Mass (Da): 49458
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A0A0Q9XF07 | MKILKDLEGVARPTQLCALLPFFNGNQSDNFSINSAGKIYGRVMALILLVSSVFFCHDVLFASENYKLMVHSQGETEDINRTIETLFCIVSYTIIVVSSVLNTSKHFRTLRDLSLLDGYLEAHGYTSSYSCRYLGSLLIFVSASVVVVAFYYIHFLSNIDVKRQCILMCIYGLQMLYSCVFAIYLRTVLMCLALRIEFLNARLEQFTQKDREQYLKDDWCELSNLIEILCKFRYITENMNSVTGVALLFFFGFSFYTVTNQSYLAFSTLTTPDQLRKEHDTIGLSCAWVIAETAIMAVICSSFDCLASEVSI | Function: Gustatory receptor which mediates acceptance or avoidance behavior, depending on its substrates.
Subcellular Location: Cell membrane
Sequence Length: 312
Sequence Mass (Da): 35485
Location Topology: Multi-pass membrane protein
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A0A7Y7IR50 | MEPIPVAGLRVCCLVRTAPPPAGTTGHWRLEKVHARHLPEFGPKHPEFYFNESAGISWPIPPLQPDIPVHGRTRRAGFGDGRASRTLVVGANGQLGRALRARYLGDPDVDFLTRTELDLAAPEPFLGVDFSRYATVINAAAYTSVDAAETPAGRAAAWAVNATAVGALARACTEHRMNLVQLSSDHVFDGTVEIHDEDEPVSPLGVYGQSQAAGDIAAATTPRHYILRTSRLTGDGSNFVTSMASLARRGARPTVVNDEYGRLTFAEDLAAAIAHLLGTGARYGVYNMSNSGPVQSWAEVAADVFGLLGLPRDSVTGVPAADYYADRPGSAPRPAHSALNLAKLKASGFTPPPARERLEGFLGGWTAHHSGSRPK | Pathway: Carbohydrate biosynthesis; dTDP-L-rhamnose biosynthesis.
Function: Catalyzes the reduction of dTDP-6-deoxy-L-lyxo-4-hexulose to yield dTDP-L-rhamnose.
EC: 1.1.1.133
Catalytic Activity: dTDP-beta-L-rhamnose + NADP(+) = dTDP-4-dehydro-beta-L-rhamnose + H(+) + NADPH
Sequence Length: 375
Sequence Mass (Da): 39853
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B4L8S8 | MRDYRIDQVLHFSLRCYQLMGMHGLPLPCDAHPRRKARLLHVWTGCLLMGFSGVAYMCLTSDDEFLYKGDDFSCFNDAMKFGFAEMAILGIYWETLSSQRAYLGRFWQLYEALAATQTATTTPSGLTLRQQLVQHWRFLAIFYGTFLLELALLCVYVALQEGSRHLVLFWITFQPFILVVHLRNTQFVLHMDLLRQKLLQLECELILLVEYSSFANSSASFFGFNEYLRRRVREMQMIYARIHELCTCYRRGFSYSMLTVLLMIYIRITVDCYFFLYTKLSNITNLDYYLLLPAVLHIPAFLYTCQSFMQIVPRIAYRLHNIATSCSPVSLQIQNFSLQILHEQMRIDCMGIVILDNHLLTQIAYAVCTYMIFTVQLMPKLNGAYL | Function: Gustatory receptor which mediates acceptance or avoidance behavior, depending on its substrates.
Subcellular Location: Cell membrane
Sequence Length: 386
Sequence Mass (Da): 45158
Location Topology: Multi-pass membrane protein
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A0A520Y4T0 | MAAADSAAPTTTAATTTTTTTTTTTTTTTPPPEPLELIGRGDYTVGVTTVEVLAESDRPLTVDIWFPLEPGSTGDPQQYTLLPGVYYESPLAVAATPDTIAGSDPYPLVIYSHGSGGLRYIHSDYTEAIASHGYIVAAADHTGNTAVDQLLSSSDEPATIAFNRPNDVSNLIDEMLDTTSEITSPFAERIDSENVAVTGHSFGGFTSFAMASGYENEIGSFAADERVDAIITLAPFTSPILSDEALSAVSVPSLMIVGTDDKTTPVDPNVTRPWDLMTSDISYRVELSAAEHQTFTDVCDYQDYLPTLDAVPEPITTTIDSFAEAGCQPGDMPIDRAQELTNTFAIRFLNEVLRGGPGFDPETAMPEDVVFLMR | Catalytic Activity: (ethylene terephthalate)(n) + H2O = (ethylene terephthalate)(n-1) + 4-[(2-hydroxyethoxy)carbonyl]benzoate + H(+)
EC: 3.1.1.101
Subcellular Location: Periplasm
Sequence Length: 374
Sequence Mass (Da): 39861
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A0A968XUQ7 | GQSKWRGEQAVVAALPKHIILRTAWVVSPYGHNFVKTMLRLSASKPELGVVDDQIGSPTYAPHLADAILTIAARLRDVGADQMSWGLYHATGAGEATWCALARETFRLSAERGGTSAHVSRHHIR | Pathway: Carbohydrate biosynthesis; dTDP-L-rhamnose biosynthesis.
Function: Catalyzes the reduction of dTDP-6-deoxy-L-lyxo-4-hexulose to yield dTDP-L-rhamnose.
EC: 1.1.1.133
Catalytic Activity: dTDP-beta-L-rhamnose + NADP(+) = dTDP-4-dehydro-beta-L-rhamnose + H(+) + NADPH
Sequence Length: 125
Sequence Mass (Da): 13596
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A0A7L4EQW4 | ALFFATELTDEQKEFQATARKFALEEIIPVAAEYDRTGEYPVPLIKRAWELGLMNSHIPESCGGLGLGTFEACLITEELAYGCTGVQTAIEANSLGQMPVIIAGNEQQQKKYLGRMTEAPLMCAYCVTEPGAGSDVAGIRTRAERKGDEYVINGQKMWITNGGKANWYFLLARTDPDPRAPASKAFTGFIVEADSPGIQIGRKELNMGQRCSDTRGIVFEDVRVPKENVLIAEGAGFKIAMGAFDKTRPPVSARKKGLFTKQTRNSCRSPRTVPTQVAAGAVGLARRALDEATRYALERKTFGKPIVEHQAVAFLLAEMAMKVELARLGYQRAAWEVDAGRRNTFYASIAKAFAGDVANQVATDAVQIFGGNGFNTEYPVEKLMRDAKIYQIYEGTAQIQRVIIAREHLGRFKA | Pathway: Lipid metabolism; mitochondrial fatty acid beta-oxidation.
Catalytic Activity: H(+) + hexadecanoyl-CoA + oxidized [electron-transfer flavoprotein] = (2E)-hexadecenoyl-CoA + reduced [electron-transfer flavoprotein]
EC: 1.3.8.7
Subcellular Location: Mitochondrion matrix
Sequence Length: 414
Sequence Mass (Da): 45439
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A0A143T2I6 | SAVPYMGDMLVQWIWGGFSVDNATLTRFFAFHFLLPFIIAAATVIHLLFLHETGSNNPIGLNSDADKISFHPYFSYKDLLGFVIMLLALTLLALFSPNLLGDPENFTPANPLVTPPHIKPEWYFLFAYAILRSIPNKLGGVLALLFSILVLMVVPLLHTSKQRGLTFRPITQFMFWTLVADMIILTWIGGMPVEHPFIIIGQIASVLYFALFLVFFPLAGWLENKALKWA | 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: 230
Sequence Mass (Da): 25886
Location Topology: Multi-pass membrane protein
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A0A7T4YKY3 | YKDIGTLYFIFGIWSGMIGTSLSLLIRAELGNPGSLIGNDQIYNTIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLISSSIVENGAGTGWTVYPPLSSNIAHGGSSVDLAIFSLHLAGISSILGAINFITTIINMRLNNLSFDQMPLFVWAVGITAFLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGH | 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: 229
Sequence Mass (Da): 24896
Location Topology: Multi-pass membrane protein
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A0A1F7I5M4 | MKLDELKQYKKILILGYGVEGQATEKYLQKFYPEAEIGRADKMDGEDYLQRQNDYDLVIKTPGIPPRLVTKPYTTATNIFFANVTNQIIGITGTKGKSTVSNLVNSVLNGAGQPATLAGNIGRPMLELLTEGLDEKAIVVLELSSYQLEDIQFSPHIACILNIYQELHNHQTLENYFQAKAQIVHHSLENDYYVYNQSFVPLHNLTKKTKAQATAYSEKDEEPIGAIYRSNVAAVAAITSLYGINREVVREIIAQTPQLPHRLVNMGTYEGITFYDDSASTHPEATVHALSLIPNVSTAIIGGQNRGYDFSVLVKKLASVHVDNIVLFPDTDNVINKLIAESGNYQPQVLVTKSMVEAVAFAFSKSRRGSVCLLSPGAPSYTMFTNFSERGDTFTKLVNTHEKETASSKTATAK | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Catalytic Activity: ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate
EC: 6.3.2.9
Subcellular Location: Cytoplasm
Sequence Length: 414
Sequence Mass (Da): 45763
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A0A7L7S0W6 | MMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPPMNNMSFWLLPPALILLLVSSMIETGAGTGWTVYPPLSANTAHSGPSVD | 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: 81
Sequence Mass (Da): 8714
Location Topology: Multi-pass membrane protein
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A0A2E5MVF4 | MIILKTTFLLISILGLCVGFSVSQAQAAGLPQLDIATYPPQLIWLVITFAALLTLMSRVSLPRISQVLEERQHKIEDNLKKAESYREDAAIAAKSYAKAQEEARTNAYAIIIETHKRIAMDIAEKQEELSEKLEKEINVAEDRIQAAKEVAMAAIDKVATDVALNTTEKILGETLNKKDVSKVISEVLEDRQ | Function: Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0). The b'-subunit is a diverged and duplicated form of b found in plants and photosynthetic bacteria.
Subcellular Location: Cell membrane
Sequence Length: 192
Sequence Mass (Da): 21335
Location Topology: Single-pass membrane protein
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A0A0F7LMY6 | MECVFFSFDKDTFDVLNIATLGPSGTSSEQSAIRFGEFAIENKVAKSYQVVLCNTYEEASSHIILKNCQALVVANAYYNISEFYMDNRFNLSAAFLNYTPNYGIAIRDELTKDNIVIATHPAPKALIPELLPDNLKIADIIFKDSTSSAAKAVANSEVDAALTTEVAAKLHKLKFISHIRPIKMLWSVFTSA | 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: 192
Sequence Mass (Da): 21224
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A0A7H4P2P4 | MKRAVIDGEPLTERVVTLTGEAVSRPGNVWARLGTPVSHLLKDAGFCPSADPMVIMGGPLMGFTLPWLDVPVVKITNCLLAPSASEMGEPEEEKGCIRCSACADACPADLLPQQLYWFSKGQQHDKATSHNLADCIECGACAWVCPSNIPLVQYFRQEKAEISAIAQEEKRAAEAKIRFEARQARLERDKAARLERHKQAAVQPAAKRSGRH | Cofactor: Binds 2 [4Fe-4S] clusters per subunit.
Function: Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane.
EC: 7.-.-.-
Subcellular Location: Cell inner membrane
Sequence Length: 212
Sequence Mass (Da): 23204
Location Topology: Peripheral membrane protein
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A0A960WTX7 | MKTVRQELIDYLGNHLTGNKRDKIRAALGERTRHLTVLLEDLNQPHNASACLRSCDCFGVQDVHVIERRHPFQPDNDVAMGSNKWLSIHRYHQPESALETLRARGYHLVATSPNAEGDTPATLPIDRPIALLFGSEHKGLSDRLFSAAESTLRLPMHGFTESFNISVTLALAVSRLIERIRDSPLDWRLSEAEQEELTLKFYQRQIARHDLIEEEFWKEREE | 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: 222
Sequence Mass (Da): 25516
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B4KYG2 | MLLLQLLTSGTLRVLHLLSQLLGLTAASWQMLSGRVGVGVAPVKCERYWRLHGCLVLLFVLGFSPVAMWMVITRMDFLRQNHLLLMVGCHRYALLLGSAVLTLYRHTSRQCRLIVLANKLLWCCRQLFALLHTSRLQSSAHRLHTRDHLTIYALAVSIACSCSYTVFLLRFDVEAHRSSLFFCAVLFVYVCQLCLQLSLALYLLALLLISHLSHHCNLLLAQLLADAVHSHEALFTRCLPHRQRLLDSQQRWLALELWRLLRLHRQLLRLSLRLCSLHNVQLVLFVIFVAVESIMHSFFSYFVTFSNWWLRKFHEPAPWNVEATVFNVAVFVQLTLVIGHTHRLQQIFRKTRYIFSAGVKDVPVDCSKALSQTLHLYGLQLQVNERVFHLLACGLFKLNNSLLFGIVQTIIMYTIILIQFDKIMNR | Function: Gustatory receptor which mediates acceptance or avoidance behavior, depending on its substrates.
Subcellular Location: Cell membrane
Sequence Length: 426
Sequence Mass (Da): 49221
Location Topology: Multi-pass membrane protein
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A0A3D6DPX6 | MSIRRPVNKSLLAIPVLLLVGGCTTVPPTNIHQPMTARPQQRSDALAANLAATGSIYQAGASRTLFEDRRARYVGDTITVSITENTTAATKSNTSVSKTGSISASAGPFVGSPANWFRPAELNASSSNVAAGKGDAAANNVFTGFITVTVIEVLPNGNLLVSGEKQVAIGHGQEYIRLSGIVNPYFVNAANTIPSSQIADARIEYKESGTISEAQVMACPSFGYATQNH | Function: Assembles around the rod to form the L-ring and probably protects the motor/basal body from shearing forces during rotation.
Subcellular Location: Cell outer membrane
Sequence Length: 229
Sequence Mass (Da): 23941
Location Topology: Lipid-anchor
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A0A0J6AMY1 | MMGQMQETRHIVIKNEQAVMSPSWSIHSGVGTRRYTFIWGMVGENQVFGDMDHVKVSELR | Pathway: Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-gluconate from pectin: step 4/5.
EC: 5.3.1.17
Catalytic Activity: 5-dehydro-4-deoxy-D-glucuronate = 3-deoxy-D-glycero-2,5-hexodiulosonate
Sequence Length: 60
Sequence Mass (Da): 6924
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A0A411FIQ9 | QIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLSLLLMSAMTESGAGTGWTV | 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: 77
Sequence Mass (Da): 8484
Location Topology: Multi-pass membrane protein
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A0A0Q9XMI6 | MNSQYNASNRTSSFRSNHEHVQTTLNERNWEWSYLVRKCRNLELEESYDLYMRRLRIGYLSIFIFIQMLVTCTHALVLLTSSDLTYAYVDMITYLVTAVLIWLILSVNFRNELISKHGWLVYASSWLAVSILVLMDIGLNVYHATSNNDILNPIYDAYTLYAIYMFMPIPHVLQPFILGTAVTICYIINYSFVISAKEANQMHSIFNEAIYLSCVNFLGIFFRLMRDIALRTTFLDRRQYVEENLLLRYARDQERSLLLSILPAQIADRLQEDVRNRIERSKQQHHQRPGINHGCSNNSQALRRWRQPDHGTLFIEPHKDVTILYADVVNYTHLTTTLDVKKLVEALHDLFVRFDIASEEYNVLRIKFLGDCYYCVAGLASPNEDHAKCCVDLGLRMIKDIRDVREKRNLNIDMRIGVHSGDVLSGVIGASKWQFDIWSKDVDIANRLEATGATGRVHVSQQTLRLLDGEYFYEDGTEKAREDPVLQKHDIRTFLIKSLRAPMHDPRRVQRERQAKKLSEASKSNFMYNSTLQQYNQVRNQAKLEMCRELDKMPIGRIQITKICRRSTNLTQDEIEEETFRRNISSFCLLFRIRNWEIQYIREPDVMLKYSIVLAWFVYICLLSIQLLSKDPKYHYWILDGVTISVLTAMLIISWYKKIWIMYFSDTEQLLPQYKLSRMLYKMSDFMQRSIGIRLTVYILVVVSCIVVTAMQVLDCGPKRDEELIQCFHPWILTNCVTLLIGTAFLFTRIPFVVKTTVAVLITVAYTVLVVYEFEHIFDGSPPTNVNLNAKYSHFLLIFITLGIFHLMERQTEFIAKVDYNNWQLEAATDAEAGRRLNYE | Catalytic Activity: ATP = 3',5'-cyclic AMP + diphosphate
EC: 4.6.1.1
Subcellular Location: Membrane
Sequence Length: 840
Sequence Mass (Da): 98285
Location Topology: Multi-pass membrane protein
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A0A924M1Q5 | MSDLLHDSFYRFVRVESPPELAQKLEEVCSSAGLWGIILVASEGINGMLCGSQGGLQTVRDALEEDSRFSGLMYKRTSSSVQVFYRLRVRLKAEIVPLGIAGVDATRFRGTDVSPLEWRELLGREDVIVIDNRNSFEYTLGHFKGAINPGVNNFRDFAQFIDQNLPQWEDKTIAMYCTGGIRCEKTGAWLASRGIEILQLEGGILHYFQQMEDAEQDYDGTCFVFDARQELDTQCKVARTPRPPEFEGTVSQFLWRGMEPERDKVLSGDKDSGNIGNVVNDISSGLARKVLSRSRQRSG | Function: Catalyzes oxygen-dependent 5-hydroxyuridine (ho5U) modification at position 34 in tRNAs.
EC: 1.14.-.-
Catalytic Activity: AH2 + O2 + uridine(34) in tRNA = 5-hydroxyuridine(34) in tRNA + A + H2O
Sequence Length: 299
Sequence Mass (Da): 33564
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A0A1H3GZN8 | MNYAVIGANYGDEGKGLVTDYLTRSGRNVVIRHNGGAQSGHTVEKNDGRRFVFHELSSGSFNGAVTYWASTFYPDLYKLEEELEDFSKVGEIPQIYGCEKTNIVLLFDVAINQMKETGRGDKKHGSCGMGIWEARVRTESGFGMTLGEVKNSTPAEIVKRLEEIKENYVLKTFGKLSPDYDFDIKIYTKYLKRAIEHVNVISDETSFLGGFDNIVFESGQGLLLDSDREDLWPHTTSSCTTLANPAMLAQSYGINVDEVFYVTRTYITRHGAGPFNEDKDLNFYDETNKSNPWQGSMRFGRTDFEELLKRVSKDGAKARKISLFITHFDETNERFLSQEGNLDQEQIVEKALSHSISDIYFCKDKYGIEVTHSNK | Cofactor: Binds 1 Mg(2+) ion per subunit.
Pathway: Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2.
Function: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP.
EC: 6.3.4.4
Subcellular Location: Cytoplasm
Catalytic Activity: GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate
Sequence Length: 375
Sequence Mass (Da): 42458
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F0L8Y6 | MRGRRLSLQFSIRDAAAFLDDWSLLRHRLWPDASVAEHRAELQNLSDNDAGFIAYDLVGMAIGFADVSLRRDYVNGCDTSPVAFLEGVYVEEEFRGQGVAAALIAEVTRWAISKGVSELASDADIANVDSHRMHAALGFEETERVVYFRKLLPSHS | Function: Catalyzes the transfer of an acetyl group from acetyl-CoA to the 6'-amino group of aminoglycoside molecules conferring resistance to antibiotics containing the purpurosamine ring.
EC: 2.3.1.82
Catalytic Activity: acetyl-CoA + kanamycin B = CoA + H(+) + N(6')-acetylkanamycin B
Sequence Length: 156
Sequence Mass (Da): 17357
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A0A8C2MZ54 | MGGRRGEQEERREGELGLEYSSEETPPATQNFIIPKKEIHTVPDMGKWKRSQAYADYIGFILTLNEGVKGKKLTFDYKVSEAIEKLVALLNTLDRWIDETPPVDQPSRFGNKAYRTWYAKLDQEAENLVATVVPTHLAAAVPEVAVYLKEAVGNSTRIDYGTGHEAAFAAFLCCLCKIGVLRVDDQVAIVFKVFDRYLEVMRKLQKTYRMEPAGSQGVWGLDDFQFLPFIWGSSQLIDHPHLEPRHFVDEKAVSENHKDYMFLQCILFITEMKTGPFAEHSNQLWNISAVPSWSKVNQGLIRMYKAECLEKFPVIQHFKFGSLLPIHPVTSG | Function: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
EC: 5.2.1.8
Subcellular Location: Cytoplasm
Sequence Length: 332
Sequence Mass (Da): 37804
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A0A3D3KYE2 | METPVSAEFPFLRLGEPAAQSRAAVGSKAAALSALAAAGFRVPAGFVVTKAALLDNPAAPDLARLLRTAASGTGTGPFAVRSSAAAEDLPGASFAGMYETYLQVAAADLPAAVHRCFDSASTERIRAYQLSVPGDGPAVPPDSGMAVLVQQMVVPVAAGVAFTANPLTGARDETLISAVPGLAENLVSGVATGEEWVARSGLPGLPRGNGSALTEQSATAVAAAASAVALHFGCPQDIEWAVDHAGKVHILQARPMTALPDAVRWEAPGKGAWLRNFRMGEWLPEAVTPLFMYWAIPRIDAAYNEAVYASAGIKVPMGHAAVNGWYYVAPPTPRSLPHLLFGGKRGSLPYFFNSVVRPMFDPAGADRTVLGALEHEWRTDCLPAYRKLVDAPPADEATPSLDELRHTVEKVLEAAGAYLWYFAATGGAAWKMEAVLAAFWRRHLAGTAAGRAVSASERNAGYQVLLGGLAPVLPAPAPHAVYSLDWYHPTAGEQAGGQVRRDTLPASPPPTGGPADSRRQAESACRNVLKGTRHLHRFETLLGLAQHYALLREEQARDFTLGWPLLRRCLTAIGEHLRD | Pathway: Carbohydrate biosynthesis; gluconeogenesis.
Function: Catalyzes the phosphorylation of pyruvate to phosphoenolpyruvate.
EC: 2.7.9.2
Catalytic Activity: ATP + H2O + pyruvate = AMP + 2 H(+) + phosphate + phosphoenolpyruvate
Sequence Length: 579
Sequence Mass (Da): 61194
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A0A3D4VQZ2 | MKNTRIVTLIGIMTALSFVLYLIEIPVGFLFPSAPFLQLDFSDVPAILLSIAYGPIVGTVINLFKNVLHFIFKSQTPAASGEIANFFAGLALYLPISVYYFYIVKNKKFKLVPNLILFAVGIAMMVGVMVLINFTITLPLYGFTGDAEKWAFVSAITPFNLMKGTLLSIITMLLYPRLAKFLVK | Function: Probably a riboflavin-binding protein that interacts with the energy-coupling factor (ECF) ABC-transporter complex.
Subcellular Location: Cell membrane
Sequence Length: 184
Sequence Mass (Da): 20401
Location Topology: Multi-pass membrane protein
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A0A6P6N950 | ACLLFSSGIYRAAPMRLNPRQSQVKSVYKTHIDAIHFRKTDEKRLHGLDEDGEQKLFTKERVAALKELAAKPDVYDRLXSALAPSIYEHEDIKKGILLQLFGGTRKDFTQTGRGNFRAEVNILLCGDPGTSKSQLLQYVYNLVPRGQYTSGKGSSAVGLTAYVMKDPETRQLVLQTGALVLSDNGICCIDEFDKMSDSTRSVLHEVMEQQTLSIAKAGIICQLNARTSVLAAANPVESQWNPKKTTIENIQLPHTLLSRFDLIFLMLDPQDEAYDRRLAHHLVSLYYQSEEQIEEEHLDMAMLKDYIAFARTTVHPRLSEEASQALIEAYVDMRKIGSGRGMVSAYPRQLESLIRLAEAHAKVRFSSKVESIDVEEAKRLHREALKQSATDPRTGFVDISILTTGMSATARKRKEEVAQALKKLIQSKGKTPAMKYQQLFDDLRGQSEAAITKDMFEEALRALADEDYLTVTGKTVRLL | Function: Acts as component of the MCM2-7 complex (MCM complex) which is the replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. The active ATPase sites in the MCM2-7 ring are formed through the interaction surfaces of two neighboring subunits such that a critical structure of a conserved arginine finger motif is provided in trans relative to the ATP-binding site of the Walker A box of the adjacent subunit. The six ATPase active sites, however, are likely to contribute differentially to the complex helicase activity.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
EC: 3.6.4.12
Subcellular Location: Chromosome
Sequence Length: 479
Sequence Mass (Da): 53770
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A0A059UEZ2 | MLNFPFVSLFIFILFFSSLFSLSSMHWFGVWLGLELNLISFIPLMVQFGKTEEIESATKYFLTQAAASAMLLFSSLIMFWKEGNWELMSNSSLISSNMILFSLLMKLGAAPFHFWVPSVVSGLSWSMNSLLLTWQKVIPLLSISVFFSIDKEILLLLIFLSSMIGGIGGLNQTSIRSLMAYSSILHLGWMMAASIISTEVCCMYFFIYSFILISTFSKMMIQETKSSSQFFNILMWKNFSRVYLFSMIMSMGGMPPMLGFFGKWMILTSLVMSKMYLMSCFLILGSMISLYYYLNLSFSIIMSYEMGWKTTFSSKVEMYLVSMLSMNFSGLLLMFYFNSYM | Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor. Essential for the catalytic activity and assembly of complex I.
Catalytic Activity: a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) + NAD(+)
EC: 7.1.1.2
Subcellular Location: Mitochondrion inner membrane
Sequence Length: 341
Sequence Mass (Da): 39146
Location Topology: Multi-pass membrane protein
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A0A8N1S8L1 | MRGDWRIVYYFGHVKCEHAVINLVRHIHILLGVNGIFVELPLLASVIPEGTYCIDKTQKVDHTLTKKQNKTTNSSAFDTTNDLSVFEKIFFLYVLIVIXCFFSNGFLPNIQSYSCLPYGHLAYRLSIVCVQFVTPFACXIVEIMMSNIKIIICWLSLVDLIIGSYVTCLILLSDFISPTPPLQKSMVGVGLIILTWRGVISYLKLVIIXLLKHISSSKTLFNIGVVMQAGSASGAIISLVLLNFTDRFKAINSCQLLSE | Function: Plasma membrane transporter mediating the uptake by cells of the water soluble vitamin B2/riboflavin that plays a key role in biochemical oxidation-reduction reactions of the carbohydrate, lipid, and amino acid metabolism.
Catalytic Activity: riboflavin(in) = riboflavin(out)
Subcellular Location: Cell membrane
Sequence Length: 259
Sequence Mass (Da): 28950
Location Topology: Multi-pass membrane protein
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A0A1D2SHK7 | MNVRSLPRVVAAMLAAVLLAAAPARAADTVSRPPSPAASAALLELGRHLFFESRLSGDGSRSCASCHAPARGFSEGVALSRGYNHSGHFRNAPGLLGLRLKERLAWDGRYRIDELPKLVEEMLTSPITMNGNPGIIAERVRQVPQLLQLWQRAFGERTPPSFDGVARAIAAWSAAHDGGDTAVDAALRGDASALSPRAAEGMRLFTGKAGCSGCHSGPAFSDGLAHRLGVPESPQILRDPERTVALLAHHASHGSADPMSERSDTGVHALTRRASDRGRFFTPGLRGVAQTAPYMHNGTLPDLAAVVAFYDRGGGRGSETKPLGLSASEREALVAFLEALTPRTALAVAPPPAFDYATQAGAGR | PTM: Binds 2 heme groups per subunit.
Cofactor: Binds 2 heme groups.
Subcellular Location: Periplasm
Sequence Length: 364
Sequence Mass (Da): 38267
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A0A0G1FU84 | MGNPTILITGGHYTPALAVIEEMQEIHPTWKILWVGRKYAFEGSRVPSSEYTWIRLMGIPFINLTTGRLQRSFSVYTIPSLLRFPIGIMQSLGILWKYKPSLIVSFGGYIALPVAIGAFVFGIPVITHEQTHALGLANSIIARIAKKICVTFPETLSLFPKKKGVLTGLPIRSQLFAPPRAPTFGIPKETLPILYITGGSTGARSLNDKLFPIIPKLLNTMMVIHQTGDVSSQKADGVKKQLKEKTNRYIIAPFFDVKDISWIYQNADVVVGRAGANTVAEVSALNKRAIFIPLPWAGGNEQMKNAEQYQSTGNAIVIKQDAVTDVSVIQAVNTLLGRVKTSSLFSAKNKNTGTSNMVRVIESLLSSYAR | 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-trans-octa-cis-undecaprenyl diphospho-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine + UDP-N-acetyl-alpha-D-glucosamine = di-trans-octa-cis-undecaprenyl diphospho-[N-acetyl-alpha-D-glucosaminyl-(1->4)]-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine + H(+) + UDP
EC: 2.4.1.227
Subcellular Location: Cell membrane
Sequence Length: 370
Sequence Mass (Da): 40588
Location Topology: Peripheral membrane protein
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A0A0U2LQF6 | LDRMPLFVWSILITAFLLLLSLPVLAGGITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFGHPKVYILILPGFGMISQIIPTFVAKKQIFGYLGMVYAMLSIGILGFIVWAHHMFTVGMDVDTRA | 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: Membrane
Sequence Length: 126
Sequence Mass (Da): 14127
Location Topology: Multi-pass membrane protein
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G3IE58 | MEQGLSRTWACDLDKFIEAHLLPNTSFRTEVKAAIKIICDFLKERCFRDAAHPVRVSKVVKGGSSGKGTALKGRSDADLVVFLNNLTSFEDQLKRRGEFIQEIKKQLYELQHRSHIKVKFEVQSSKQSNLRALSFKLSSYQLQQEVEFDVLPAYDVLGQLNCSKPNPGIYSRLIRECTSLGKEGEFSTCFTELQRNFLKHRPPKLKSLIRLVKHWYQLCKEKLRELLPPQYALELLTVYAWERGSGVTEFNTAQGFRTVLELVTKYRQLRIYWTEYYDFQDQEVSNYLRRQLRKNRPVILDPADPTGNVAGLNSDGWKLLAEEALASLQYPCFKCCGGSPVRSWDVLPELTLVERKRTLWIQAAALSGDFKLSSFQHQQEVEFDVLPAYNVLGQLNYIKPHPQIYADLIRECTSKKMEGEFSTSFTELQRNFLKRHPPKLKSLIRLVKHWYQLCKEKLGKPLPPQYALELLTVYAWERGSGFTEFNTAQGFRTVLELVTNYRQLRIYWTVYYDFRYEYVSNYLHNQLSRPRPVILDPADPTRNTAGLNSDGWCLLAEEAMAWLKYPCFENWDGSPVRSWDVPVRPCHHPVPLHTALVTPTISRIFKQKCGLSKGTQVVGCPATLLALQAL | Catalytic Activity: 3 ATP = 5'-triphosphoadenylyl-(2'->5')-adenylyl-(2'->5')-adenosine + 2 diphosphate
EC: 2.7.7.84
Subcellular Location: Cytoplasm
Sequence Length: 630
Sequence Mass (Da): 72770
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A0A345DCW3 | MSRALHSPWQWHVPRIDLSHTHWLTDSGSLTQKLKNHCQHFSVQRINQLSSPLSLSETIPMQLPRGRSVLQRQVLLICNGVPAVFAHTVTPIERVGRDWPFFNQLGNRALGVALFSNPLIRRDSFEYTRLCSQDDLYQMAQRALNGHGFDIALPSHLWARRCVFTHTRHANSRMMVTEVMLPSVYALQPTP | Pathway: Cofactor biosynthesis; ubiquinone biosynthesis.
Function: Removes the pyruvyl group from chorismate, with concomitant aromatization of the ring, to provide 4-hydroxybenzoate (4HB) for the ubiquinone pathway.
Catalytic Activity: chorismate = 4-hydroxybenzoate + pyruvate
EC: 4.1.3.40
Subcellular Location: Cytoplasm
Sequence Length: 191
Sequence Mass (Da): 21913
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A0A1Z9D928 | MKQLIKRGKFFLIAGPCVIENEKDTIEIAEKIKKITDELNIPFVFKSSYKKANRTK | 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: 56
Sequence Mass (Da): 6515
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A0A7K2WLQ1 | EALPPHLAAARVGRAAQGPLAGLTVYEGLHDPRVAELLLERLRNPGSWGPLRFERARPIPAALSGKLLDAEQSNSSLVYGDARGEAVHGDAYILKILRRVFPGPHPDLELPLALAAEGCDRVPAPVAWFEADDPTGSDDTLTLGVLQPYLRGSRDGWQLALAALGADREFTSEARALGRATAEVHLALAAALPTVTLGRAQTAQFADAMTARLDVAAQAVPALMPYVPGLRTAFDALAGLDEAARGPRSAAGTPRPPPYRRRCFSRRPPSLTCPQRR | Pathway: Glycan biosynthesis; glycogen biosynthesis.
EC: 2.7.1.175
Catalytic Activity: ATP + D-maltose = ADP + alpha-maltose 1-phosphate + H(+)
Sequence Length: 277
Sequence Mass (Da): 29502
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A0A6F8PRK9 | MHTLADPDAFLKAHLATLARNRHRDLVILQGSTDWAWQIITPHLPTNSLIIGNAPSDSARTSANPQNLKHQLGKEFAGAAIDLNDGLSANTLGIVAGLLQAGSGLFLIMPPTWPEIANPQDSRFLNTPLQPQQLEPWFYRHLASSWQKQSTWLKQHGEQTQLICQTTSVQSENALTEFDSGAATREQNQAITQILKVAFGHRKRPLVLSADRGRGKSAALGLAAVQALLQGKAHIAISASLPEQAHNAFFHAQRWLEQNISEQISTISTHGDCLSFEYQGETKQLKFYAPDYLNLNRVECDLLLIDEAAQIPTPLLTSLLQSYHRMVFATTLHGYEGSGRGFELRFTKTLNQLTPDWKRLHIKQPLRWNNQDPLEAAINQALLLQADNDAPTLPDCPQAALMQLEINELSKTQRLADLDAIFGLLVKAHYQTSPNDLQQLLNSPNRIWVTRYQKQTIGVLLSQEEGGLTGNESKIHGHLVPQLLDRQYAFSDALSMQSWRLMRIAIEPEWQSLGIGSMLVEKWQKQAQTEQIDFISSSFGAENDLTRFWIQQGMQPLHLGCKRDKASGTYNLVVYQALSEQAESLKQIQQQFQQQLPMLLNDELKQLDSRLLTLITSNFANSETEINTAEIIQDYLNGKRPFTTSSYFLKQFLLQNPALLSNLESKQASLLTDKLLKQLSWAELVETHKLIGKKQAEQGFQDALKRLQINA | Function: Catalyzes the formation of N(4)-acetylcytidine (ac(4)C) at the wobble position of tRNA(Met), by using acetyl-CoA as an acetyl donor and ATP (or GTP).
Catalytic Activity: acetyl-CoA + ATP + cytidine(34) in elongator tRNA(Met) + H2O = ADP + CoA + H(+) + N(4)-acetylcytidine(34) in elongator tRNA(Met) + phosphate
EC: 2.3.1.193
Subcellular Location: Cytoplasm
Sequence Length: 711
Sequence Mass (Da): 79871
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A0A2T1C697 | MTETTKNHLLEIKEIGQSIWMDNLTRDLIESGELKKMIESRGLRGITSNPAIFEKAIAGNVIYDADIEAGIRAGKSVLEIYESLVFEDIRNACDIVAPVYAESKGLDGYISIEVPPTIANDTESTISEALRYYQAIGKPNVMIKIPGTAQGWPAVERVISEGINVNVTLLFSVDSYVETFWAYIRGLEARAAKGLDVSNIASVASFFLSRIDINIDGQIDAKLKGVTDVATKAKLEAVKGKIAIANAKVAYQKYKEIVASDRWQALAAKGAEVQRLL | Pathway: Carbohydrate degradation; pentose phosphate pathway; D-glyceraldehyde 3-phosphate and beta-D-fructose 6-phosphate from D-ribose 5-phosphate and D-xylulose 5-phosphate (non-oxidative stage): step 2/3.
Function: Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway.
Catalytic Activity: D-glyceraldehyde 3-phosphate + D-sedoheptulose 7-phosphate = beta-D-fructose 6-phosphate + D-erythrose 4-phosphate
EC: 2.2.1.2
Subcellular Location: Cytoplasm
Sequence Length: 277
Sequence Mass (Da): 30271
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A0A6I9WKL8 | MTARIAISMQERDNKVAITSGDCDKLRTPGHVINKQHGRRSRILTRRVLLFTNERLGRVDDTLTPSVAWSVLPWHRQRSTCRRNPAVLRRRTRTRIPRKRKGVANQSKRCPMCRQEIPPDFLERPQLVEIEEPQKESEHPEEEYQWFYEGRNGWWQYDQRTSIELETAYKQGKRTCELLIAGFLYIADFGSMLQLRRNDPSRRRRIKRDLYNVPRKGVAGLRLNVQDEEIVREIRGAERPASPASDSMGTGDGTNTPIPPSNTPQTPAGGTASGDATPLNDRIDQRSDSLHQVLEQMRSLVLREHLSLNSDNEFEEDTEDATISDHPTLS | PTM: Ubiquitinated; autoubiquitinated.
Pathway: Protein modification; protein ubiquitination.
Function: E3 ubiquitin-protein ligase that specifically binds poly-ADP-ribosylated proteins and mediates their ubiquitination and subsequent degradation.
EC: 2.3.2.27
Subcellular Location: Cytoplasm
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: 330
Domain: The WWE domain mediates non-covalent poly(ADP-ribose)-binding.
Sequence Mass (Da): 37973
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A0A1H3CYZ0 | MTETHVTVKADSRVARKIMLRRIAACAILTAMAVLLMYLEIPLPFMPSFLKFDFSELPVLIGSFALGPVWGIVIELLKNLIHLPVTQTMGIGELSNFITGVIYVGTAGIIYRIFVSKKGAAIAMIIATLVLAAVSVPVNAFLTLPLYGSVMGFPLEAIIGMSAAVNPLVKDKLSLLLAVFVPFNLFKGFIVAGITYFVHLPLSKLINKTYNATHDPATT | Function: Probably a riboflavin-binding protein that interacts with the energy-coupling factor (ECF) ABC-transporter complex.
Subcellular Location: Cell membrane
Sequence Length: 219
Sequence Mass (Da): 23665
Location Topology: Multi-pass membrane protein
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A0A7H4P792 | MTGIRFIVPVKNGQNIRRLGEDIAHGAVVFPAGTRLTAAELPVIASLGIAEVDVVA | Pathway: Cofactor biosynthesis; molybdopterin biosynthesis.
Function: Catalyzes the insertion of molybdate into adenylated molybdopterin with the concomitant release of AMP.
EC: 2.10.1.1
Catalytic Activity: adenylyl-molybdopterin + H(+) + molybdate = AMP + H2O + Mo-molybdopterin
Sequence Length: 56
Sequence Mass (Da): 5825
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A0A6I9WDV6 | MSTSSFRVFLKVLTLLVVNINAQYQSSRTECRVDGQPGKCINARDCTLVANILQQSREQAINYLRQNHCGFDGSNPLICCINSTNVETRPGSSLVNPGTTQTSYAETTPTEIRVNLANNPLLPEECGIDLSQKLLGGERTELNEFPWMALLEYQKPNGRTTACGGVLISKRYVLTAAHCIKGKDLPTTWRLTGVRLGEYDTDTERDCVPDGDDTIVCADDPITVGVEEKIAHEEYRPQSRDQRYDIALLRLSHDVQFTTYIKAICLPSSSASLNGKLFVAGWGKTENRSASNVKLKLGLPLADMEQCDQTYNIAGVRLGYGQICAGGQRGKDSCRGDSGGPLMAVERLPNGDGRWTAVGVVSFGPSPCGMQGWPGVYTKVMDFVPWILSKMRP | EC: 3.4.21.-
Subcellular Location: Secreted
Sequence Length: 393
Domain: The clip domain consists of 35-55 residues which are 'knitted' together usually by 3 conserved disulfide bonds forming a clip-like compact structure.
Sequence Mass (Da): 43067
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A0A960WSK2 | MERENLPLDRQLRQEILFARERVYRFGQPTPLESFSLPGGPEVWVKREDLCAVKSYKWRGACNRMAVLTPEEASRGVVTASAGNHAQGVALAAKALGIQARVYMPRSTPRVKQAAVRQHGGDWVEIRLSGDSYDEAVHAARADEEESGATYVHAYDDLRVMAGQGTLADEVVLSGHGPFDAAFLQIGGGGMASGVSTWLKTYWPGIELIGVEGAGQASMKAALAAGEPVALDQVDLFCDGTAVRKAGEWAYRVLRDTLDRVETVSNAEVSHAIRELWESLRCVSEPSGALGLAAVLKSRQELAGKKVLVIVSGANVDFLQLGLIARSQGASSQATRCLRVRIPERPGTMLHLLDTGFAGVDIIDFQYGKSDETEAWPVFTLAADDEALLRGIPSKLDAAGFEWEEMEGAVDVDFRAI | Pathway: Amino-acid biosynthesis; L-isoleucine biosynthesis; 2-oxobutanoate from L-threonine: step 1/1.
EC: 4.3.1.19
Catalytic Activity: L-threonine = 2-oxobutanoate + NH4(+)
Sequence Length: 417
Sequence Mass (Da): 45096
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A0A7H4P3C8 | MTSFPGNKSNWQQPFWSDKDMLALVISELDTLPELLSFEEISEFNKALAAVYAGKAMIFQAGDCAERIANLTRYMYGKN | Cofactor: Binds 1 divalent cation per subunit. The enzyme is active with manganese, cobalt or cadmium ions.
EC: 2.5.1.54
Catalytic Activity: D-erythrose 4-phosphate + H2O + phosphoenolpyruvate = 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate + phosphate
Sequence Length: 79
Sequence Mass (Da): 8928
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A0A1Y1S577 | MSTTQRIISLYEILDDSLAEYELYTNEETESQLFALLLNNMSAAERKREDFSFKNEVVCKIFEYLNRKIGKARTYDILNSCLIVKSSETTKEVIWAGSNATVKMEANKQFVDRSCLLNPKQTNTSYLATFKAIINTKQYHMMKEVTYNMQKTIDLIENKVREFVDKFNTLHTWQICKMCVRSSKEAEYEEMVNFLFCISKKCLKGIFTFRQFRILKGKITLFVYKNKIENMSAQECCNHIDMKNVKLFTGNRYTREENIICSAMFQNFMITLFQQFYTHLINKHFYVTEMSGRGFRLLYFNKDWYQKETKRVCEEFVSSCKIEKCSSSSQSYGSIRALRKQDGFRIITNYKKVNYPFKPIIGIFRNILRKKYDHLIFGNSDRIKELKEHLGTKTEMNYIHSFDLSKCYDRIDQQVLAECVNMLFQEIESNSDFFVNKCIKYTFDEIKQRYRHQMCYINGPISDGNNLIKEIKAIKYTKQDISEIVLSGVSNHCIKYNNEFYRFALGIPQGMTLSTYLCALYQANLVERHFGFINDGLLLNYVDDFLFITSNKKENDEFLAKIENFDYENMLLNHKKTQTNQECVTWCGYKIYNSGFNIKYSYETVHFGYNFALPTHNPGRNIKEKIKKILQVKLNKLLISKKNPKCYENIYDIFLYVFGVLGVLFGRCEFVNVGFVRKVIDEIVLQVKESIRCNSQLIDKMAEDALNKTGLLSVEPRRFQ | Function: Telomerase is a ribonucleoprotein enzyme essential for the replication of chromosome termini in most eukaryotes. It elongates telomeres. It is a reverse transcriptase that adds simple sequence repeats to chromosome ends by copying a template sequence within the RNA component of the enzyme.
Catalytic Activity: a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)
EC: 2.7.7.49
Subcellular Location: Nucleus
Sequence Length: 720
Sequence Mass (Da): 84890
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A0A2A4JXI2 | MGDSFLHLGDIVSLHAEGTVSGFLSTLGLVDDRCVVCPEAGDLTDPPKKFRDCLFKICPMNRYSAQKQFWNTAKQSANSNTDTGLLKRLHHAAEIEKKQNELENKKLLGTVVQYGSVLQLLHVKSNKYLTVNKRLPALLEKNAMRVHLDANGNEGSWFYVMPFYKLRSTGDNVVVGDKVIMNPVNAGQQVLHVSSNHELPDNVGCMEVNVVNSSTSWKVTLFLEHKENQEEILKGGDVVRLFHAEQEKFLTMDEYKKRQHVFLRTTGRSSATAATSSKALWEIEVVQHDPCRGGAGHWNSIFRFKHLATGHYLAAEACNRPPDAPVEPHEPAFQLVSVPHSSEIATLFELDPTTMTHSDAPVPQSSYVRAAMSGMMDSYQPTFQLVSVPHSSEIATLFELDPTTMTHSDAPVPQSSYVRAAMSGMMDSYQPTFQLVSVPHSSEIATLFELDPTTMTHSDAPVPQSSYVRAAMSGMMDSYQPTFQLVSVPHSSEIATLFELDPTTMTHSDAPVPQSSYVRAAMSGMMDSYQPTFQLVSVPHSSEIATLFELDPTTMTHSDAPVPQSSYVRAAMSGMMDSYQPTFQLVSVPHSSEIATLFELDPTTMTHSDAPVPQSSYVRAAMSGMMDSYQPTFQLVSVPHSSEIATLFELDPTTMTHSDAPVPQSSYVRAAMSGMMDSYQPTFQLVSVPHSSEIATLFELDPTTMTHSDAPVPQSSYVRAAMSGMMDSYQPTFQLVSVPHSSEIATLFELDPTTMTHSDAPVPQSSYVRLQHLCTHTWVHSTSIPIDKDEEKPVMSKVGCSLVKEDKEAFALISVSPSEVRDLDFANDACKVLSALSTKLQLGNIEHNERKALTCLLQDIVYFIAGFENEPNKSEALDLVVENPNRDRQKLLREQYILRQLFKILQGPFQETSDGEAFLKIEELYDPRYAAYKYIFRLCYRILRLSQQDYRKNQV | 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: 955
Domain: The receptor contains a calcium channel in its C-terminal extremity. Its large N-terminal cytoplasmic region has the ligand-binding site in the N-terminus and modulatory sites in the middle portion immediately upstream of the channel region.
Sequence Mass (Da): 106331
Location Topology: Multi-pass membrane protein
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A0A0A7C4W0 | MFYLEMFILGLEFLFLVVMILLGVAFYTLMERSVLGYSQDRSGPNSAGWMGLIQPFSDGMKLFLSEFIVPVNSNVGMYLLSPCIGFFLSVIMLMLLGWEEGFMGFKYSFVVMLCISSITSLLIISTGWSSNSCYSLLGGLRVVAQMISYEVIVALMLMSLIYSVGSMRFEDFSMFHSWGLILMGFFVMFLIWIISILAECNRTPFDLAEGESELVSGFNVEYGGGLFAFIFLAEYTSMIFMSVLSVYIFFGVTFYSLKVLLIMYLYLWMRASLPRIRYDMLMNLAWKFLLMIILMMMMFYLGFVTLYYV | 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): 35471
Location Topology: Multi-pass membrane protein
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A0A6P6MW69 | MKKPFCCQNKVEPFVPPPELDDPELSPVPEPSDCVPTNESISTRYIVQNIIGEGGYGKVYEGIRVSDGKKVAIKRIKKTVRDHYLQTTVHPKPLITEVALMLTMKQGPISPYVIQLYEWFEHPQVFTLVMENPDPCESLLDFINNNPNMNETTARLIMCQAVQAVLHCIEHGVFHNDIHPDNILLRKHTLELKLIDFGCGHLLSSNGYNRSQYRGIQAYYPPELFTCGRFYATSTNVWALGVLLYEMVNTCSPFCNITEITQAEIRFENPDLSKECRDLIVQCLNRDPTERLTLDQILQHDWCKTEDLEESED | Function: Proto-oncogene with serine/threonine kinase activity involved in cell survival and cell proliferation.
EC: 2.7.11.1
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Length: 313
Sequence Mass (Da): 35875
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B4L4A6 | MMTGEPSERQTFWERHELKFYRYGHIYASICGQVIIDYAPQRPIRAPFKLLLIAYSHVLSLLLIVVLPGYFGYNYRALTATDDRRIQLVLYVGFANTLIKYATVIVTYVANTCHFEAINQRCSLQRARLQAAFAASYRGSGWPKRSFELFMYLKFVLINLMIIVQICAIFAIARIDSDTDSDSDSDSDSAAAAQGRRLRIQFAIYAFVLWNYTENMADYFYYVNSCVLLYFRLLHMQLQEELEQLRRLGCGRLLLYGCRLCDRIGLLRERYAQIHGLYADSFRMHQFQLLGLMLTTLITNLTNLFTIFNLLATSSCAFGSFPIAVSGVYALGFYLDTYLLSLVGEYIKVEQTRLALTVRQFSESPALQPPSLNQELEQFSLLLMHCRQPMLCGVVYLDRRLIYLISVTAFSYFITLVQFDIYLRTQHNK | Function: Gustatory receptor which mediates acceptance or avoidance behavior, depending on its substrates.
Subcellular Location: Cell membrane
Sequence Length: 429
Sequence Mass (Da): 49606
Location Topology: Multi-pass membrane protein
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A0A960F8V5 | MLVTAVGTMIVAYLVGSLPIAYLIARHAGGIDIRAEGEGNVGARNVFHVVGSRWGLAAFAGDFLKGSTVAMLFRHSPLWQLAIAAVAVLIGHAFPVWLDFVGGKGLSTAGGVTAVLMPWATLIGGALAGVVWAASKSFYPTTIVAIVTAVVVAPLTGVDIAVVVLVVWLFAMAGIKRALDEPRMRAVEATTGWDRLRGMSP | Pathway: Lipid metabolism; phospholipid metabolism.
Function: Catalyzes the transfer of an acyl group from acyl-phosphate (acyl-PO(4)) to glycerol-3-phosphate (G3P) to form lysophosphatidic acid (LPA). This enzyme utilizes acyl-phosphate as fatty acyl donor, but not acyl-CoA or acyl-ACP.
Catalytic Activity: an acyl phosphate + sn-glycerol 3-phosphate = a 1-acyl-sn-glycero-3-phosphate + phosphate
Subcellular Location: Cell membrane
Sequence Length: 201
Sequence Mass (Da): 20920
Location Topology: Multi-pass membrane protein
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A0A832NDN5 | MRSSFLSDRSLRLSSRWEFSHVYSAGARVSEEGGRLLAAPPPPSFPSAASRIGLAVGRRLSRSSVRRNRAKRLLREGLAALYPCIPDGWWLVFEPRRVPPSLGDALLLLMRLLARAGLLRKVCPLA | Function: RNaseP catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5'-leader sequence and broadening the substrate specificity of the ribozyme.
EC: 3.1.26.5
Catalytic Activity: Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor.
Sequence Length: 126
Sequence Mass (Da): 13962
|
A0A849XVA0 | MPSLPPPPLLVGVAADLSTLRRVAGQGVRRRGVDVVEARFDLYPKEGLAEALRLCGKLEKTGTPTLATCRLADEGGGWDRDDAARAQLLGAAASVCAMVDVELRSLHLSAVRKAARAAKSVLVVSHHNFRRTPPAASLQRIIRQAGASGADIVKISVLVRSARDHSTLVNLMLKYRRRPLCLIGMGAAGLPLRVYLSAIGSLLAYGALGPPSAPGQPTAADLRAALRACSAAFRARTS | Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7.
Function: Involved in the third step of the chorismate pathway, which leads to the biosynthesis of aromatic amino acids. Catalyzes the cis-dehydration of 3-dehydroquinate (DHQ) and introduces the first double bond of the aromatic ring to yield 3-dehydroshikimate.
EC: 4.2.1.10
Catalytic Activity: 3-dehydroquinate = 3-dehydroshikimate + H2O
Sequence Length: 238
Sequence Mass (Da): 25039
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A0A7S0Z5K8 | ALHGTVAATALVIAWALTEVVRYPSYALGLYSQCPSWLNWLRYTIFIPLYPLGAGAEMKLMYDARAFARKANMYSFSMPNAFNFAFDYVTFLNGLLIVYPFLFYSLYSYMFTQRKKKLGHVTSVKKQK | Pathway: Lipid metabolism; fatty acid biosynthesis.
Function: Catalyzes the third of the four reactions of the long-chain fatty acids elongation cycle. This endoplasmic reticulum-bound enzymatic process, allows the addition of two carbons to the chain of long- and very long-chain fatty acids/VLCFAs per cycle. This enzyme catalyzes the dehydration of the 3-hydroxyacyl-CoA intermediate into trans-2,3-enoyl-CoA, within each cycle of fatty acid elongation. Thereby, it participates to the production of VLCFAs of different chain lengths that are involved in multiple biological processes as precursors of membrane lipids and lipid mediators.
Catalytic Activity: a very-long-chain (3R)-3-hydroxyacyl-CoA = a very-long-chain (2E)-enoyl-CoA + H2O
EC: 4.2.1.134
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 128
Sequence Mass (Da): 14741
Location Topology: Multi-pass membrane protein
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G8JUZ7 | MAVYSAPRWLHRTSLTIFCSLLVAFSLVMPIDSVVQAARSGKNALNTSVVVGAVVLTGIVFAVFATSRVLVHRSCIQDIPKRYIPITKHDILHSACRDEITKCIEFTHKSGKDLRTPMRKVVHDGLEPPPNPKFPGDDTIPPLLNYKTCLKVVADRFKFQGMFLNNLDANPRIGSTFSQYVREQFKSEDEALTRRVDEFIDLYEKIRYSDTPIRREEFLRYMDISLYFVDLSLIIGHEHPVNINELAYPASSKRTSVASSSKPGTISGECSDYNGSGDLIQNRNWTALQRTGSTGTVAIRIVSTQPPEEPEFYRNELQDASVSYIKGEHTPSSAGSYNSVIRR | Function: Required for growth under high-pressure and low-temperature conditions.
Subcellular Location: Membrane
Sequence Length: 343
Sequence Mass (Da): 38509
Location Topology: Multi-pass membrane protein
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A0A0B8P040 | MGVSSAHRDAAFASCEFIMDYLKTKAPFWKKERLNEGSRWLDARESDEESATRWDEIK | Pathway: Cofactor biosynthesis; molybdopterin biosynthesis.
EC: 2.8.1.12
Catalytic Activity: 2 [molybdopterin-synthase sulfur-carrier protein]-C-terminal Gly-NH-CH2-C(O)SH + cyclic pyranopterin phosphate + H2O = 2 [molybdopterin-synthase sulfur-carrier protein]-C-terminal Gly-Gly + 4 H(+) + molybdopterin
Sequence Length: 58
Sequence Mass (Da): 6798
|
A0A0B8PAF8 | MRVLVTGCNGQLGHCLVNQLNDKVELLAVDRAELDITDRDAVFETATEFKPNFIINAAAHTAVDKAEEEVDLSYAINRDGPLYLAEAAKMVDATILHISTDYVFPGNKKGEYVEDDETGPLGVYGKVS | Cofactor: Binds 1 Mg(2+) ion per monomer.
Pathway: Bacterial outer membrane biogenesis; LPS O-antigen biosynthesis.
Function: Catalyzes the reduction of dTDP-6-deoxy-L-lyxo-4-hexulose to yield dTDP-L-rhamnose.
EC: 1.1.1.133
Catalytic Activity: dTDP-beta-L-rhamnose + NADP(+) = dTDP-4-dehydro-beta-L-rhamnose + H(+) + NADPH
Sequence Length: 128
Sequence Mass (Da): 13974
|
Q82WS1 | MDLSSNRLAGKSILITRPLHQAGGLATWVRELGGEPWLFPVLEISDSENKQPLLDLIARLDEFDLAVFVSPNAVEKVIPLVQVSHSWPRHVLVATVGKGSARVLERYGITNVIVPEEGSDSEALLRMPQFQVMQGRHVVIFRGNDGRRLLGDTLRERGASVEYIECYRRHKPEADPLPLLKHWRDDGIQAVIISSSEGLDNLFDMIGETGQQLLKATPVFTAHERIERKARELGIRKIYRTLLGDEGTVQGLLEYFEKM | 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: 259
Sequence Mass (Da): 29138
|
A0A482GYR5 | MNNMSFWLLPPSIIMLMLSSLVETGTGTGWTVYPPLSSIIAHTGTSVDFSIFSLHIAGISSIMGAINFITTMLNMKIKYLMMGQISLFIWSILITAILLLLSLPVLAGAITMLLTDRNLNTSFYDPMGGGDP | 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: 132
Sequence Mass (Da): 14318
Location Topology: Multi-pass membrane protein
|
A0A3G2LJK5 | EMKLITVLIILAAMTKSAQIPFSSWLPAAMAAPTPVSALVHSSTLVTAGVYLLIRFSPMLNCYNYGWFLLLIGCMTMFMAGLGANFEFDLKKIIALSTLSQLGLMMSILAMGFPKLAFFHLLAHALFKALLFMCAGSMIHNLKDSQDIRFMGSIVNFMPLTSVCFNVSSLSLCGMPFLAGFYSKDLILEMVCFSWINSLIFFFYFFSTGLTASYSFRLFYYSMSGDNNFYSSFSFDDKGYYISFGMIGLLFVAVFGGSLLSWLIFPVPHMITLPFYLKFLTITVVILGSYFGYFISKFSFSHNLFSL | 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: 307
Sequence Mass (Da): 34405
Location Topology: Multi-pass membrane protein
|
A0A0B8P003 | MLSYRHSFHAGNHADVVKHIVQSLILDALKQKDKPFVYHDTHSGVGRYDLTHEWSEKTGEYKQGIAKIWQQAMPEELTSYLDSIRTLNQGEDLRYYPGSPRVARAQLRKQDRMVLTELHPSDFPLLEQEFHRDRQVRIYKEDGFKRLKASLPPQERRGLVLIDPPYELAKEYRDVVNAIAQSYKRWATGIYAIWYPVVNRYDIDDMLEGLEGLALRRFCRLN | Function: Specifically methylates the adenine in position 2030 of 23S rRNA.
EC: 2.1.1.266
Catalytic Activity: adenosine(2030) in 23S rRNA + S-adenosyl-L-methionine = H(+) + N(6)-methyladenosine(2030) in 23S rRNA + S-adenosyl-L-homocysteine
Sequence Length: 222
Sequence Mass (Da): 26132
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A0A062V9N3 | MIPVRCFTCGKVISSVWDEYKKRTQTEEPGKVLDDLGIERYCCRRMLLTHVELVDLLAPYQ | Cofactor: Binds 1 zinc ion.
Function: DNA-dependent RNA polymerase (RNAP) 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)
Subcellular Location: Cytoplasm
Sequence Length: 61
Sequence Mass (Da): 7147
|
A0A7Y3LN43 | MPSEKRARQRAARQARLAQEAAAKKKKRTIQQAVIGAVIVVIIVGALILSNSGGSPTSAHSSKSTTTKGSSRSTTSAVPGTTIPLGTTGAVPVSNACPSSISNVQRTTTFSKAPAMLINTSSTYYANFQTDIGNIKIKLEPNLSPITVNNFVFLACYHYYDGTIFHRVIPGFMDQGGDPNGHPPGTGGPGYTIPDEYPKGSSNTSPYAPGQLAMANTGAGNSGGSQFFIVDSASGATTLDQDIARPNAEVYTIFGQVVSGMNIVQKINADGAQSGTPNITHKLEKVTITSN | 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: 291
Sequence Mass (Da): 30309
|
A0A166JH41 | MANLTDNTTTTLPTGLEKPILAGITLETAIKAVVILVAMIILGRTLRKIIIRESKETSLTWIINEDTADIVFRMFVLGGITWSLFEIGLMAYPIFRPPVGNVTFAVSFFYFAYLIARKSKDYVIMSAGRRPSPDVQIKVKIFYYTFITVAFFLSLNFEGVSTKLSALLAAAGITGIVLGFSAQTVVSNFISGLFM | Function: Mechanosensitive channel that participates in the regulation of osmotic pressure changes within the cell, opening in response to stretch forces in the membrane lipid bilayer, without the need for other proteins. Contributes to normal resistance to hypoosmotic shock. Forms an ion channel of 1.0 nanosiemens conductance with a slight preference for anions.
Subcellular Location: Cell inner membrane
Sequence Length: 195
Sequence Mass (Da): 21470
Location Topology: Multi-pass membrane protein
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A0A0N7AU58 | FPXMNNMSFWLLPPSLTLLLTSSMVETGAGTGWTVYPPLXNNIAXAGASVDLAIFSLHLAGIXSILGAVNFITTIINMRSTGMTLDRMPLFAWSVVITAVLLLLSLPVLAGXITMXLTDRNLNTSFFDPMGGG | 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: 133
Sequence Mass (Da): 14171
Location Topology: Multi-pass membrane protein
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A0A0B8P085 | MTACLGIMGNVGAYVACSVIQKKPLGEMLSSIKAALIDGGKGVVVVGILLVSAQVFVAMVNLTGVGVTITNIILDFANGDVLLIAGLMSIVCLIAGMGLPTSAAYVLVSAVFAPALIQQGFEALTVHLFVLYYAALSVITPPVCISVFVAAAISKDPWHKVAGYTLRLGGTAYLLPLLFLFNLNCCLRARLSASSLCWSSPYCR | Function: Part of the tripartite ATP-independent periplasmic (TRAP) transport system.
Subcellular Location: Cell inner membrane
Sequence Length: 204
Sequence Mass (Da): 21274
Location Topology: Multi-pass membrane protein
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A0A7L4E1J0 | SSTYRSQGIEVTVKYSQGSWTGVLGTDVITMPKGLDGSYTVNIATILESENFFLPGVKWHGILGLAYDALAKPSSSVETFFDSLVRQAAIPNIFSLQMCGAGLPVSGSGTNGGSLVLGGIEPSLYTGDIWYTPIKEEWYYQVEILKLEVGGQNLELDCREYNADKAIVDSGTTLLRLPEKVFSAVVQAIARTSLIQEFSSGFWTGSQLACWDRTEKPWSLFPKLSIYLRDENSSRSFRISILPQLYIQPILVIGDNLQCYRFGISSSTNALVIGATVMEGFYVIFDRAQRRVGFAVSPCAEVDGAPVSEIEGPFTTADVASNCVSSVSFHEPVLWIASYALMSLCGIILLVLIVLLLIPPRCQHRYTDNDVVNDESSLVRHRWK | Catalytic Activity: Broad endopeptidase specificity. Cleaves Glu-Val-Asn-Leu-|-Asp-Ala-Glu-Phe in the Swedish variant of Alzheimer's amyloid precursor protein.
EC: 3.4.23.46
Subcellular Location: Endosome
Sequence Length: 384
Sequence Mass (Da): 42215
|
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