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stringlengths 6
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stringlengths 16
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stringlengths 117
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A0A9E0AKX0 | MAALRRNTFRKLERLVSRKSFETLVHEGQSVHHPPVRLTWQRQVLSTGFPAATAFSVPKRNFRRAVDRNRIKRLLREAFRKNKAELYTLLEERKQEVALLFVFTGRKLPDYRQVETQVMRCLQQLTGQLRSHDE | 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: 134
Sequence Mass (Da): 15930
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N1ZN17 | MTILQLFWSTVSFLTILPVPTSNKILPQEEFSKGILFYTLIGLLVGLIDYICYGAIVFFFKMPLIGAVFAVLSETIVTGGFHLDGLADTCDGFFSARKKEKMIEIMKDSRVGTNGALALLFDILLKIVFLVSMTESDGYLAVLLAPVAGKMATPILMKSNYAKEQSGLGSLYLTQKYTKYMIAAVLIGIALLAGFLQMKSILPIITVLLFGFLFREYCQHKIGGMTGDTLGAGYELSEIVFLAVMTLQGGIV | Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis; adenosylcobalamin from cob(II)yrinate a,c-diamide: step 7/7.
Function: Joins adenosylcobinamide-GDP and alpha-ribazole to generate adenosylcobalamin (Ado-cobalamin). Also synthesizes adenosylcobalamin 5'-phosphate from adenosylcobinamide-GDP and alpha-ribazole 5'-phosphate.
Catalytic Activity: adenosylcob(III)inamide-GDP + alpha-ribazole 5'-phosphate = adenosylcob(III)alamin 5'-phosphate + GMP + H(+)
EC: 2.7.8.26
Subcellular Location: Cell membrane
Sequence Length: 252
Sequence Mass (Da): 27492
Location Topology: Multi-pass membrane protein
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A0A061HYN5 | MPKPHSEAGTAFIQTQQLHAATADTFLEYMCRLDIDSAPIMARNTGIICTIGFASRSVEMLKEMIKSGMNVARLNFSHGTHEYHLTPSSTGLLLWLWKQRDLRSGLDSSNAAALQKHEVRKVLGEKGKNIKIISKIENHEGVRRFDEILEASDGIMVVRGDLGIEIPAEKVFLAQKMMIGRCYRAGKPVICATQMLESMIKKPRRTRAEGSDVAIIVLTKSGRSAHQVARYRPHAPIIAVTRNPQTARQAHLYRGIFPVLCKDAV | Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 5/5.
EC: 2.7.1.40
Catalytic Activity: ATP + pyruvate = ADP + H(+) + phosphoenolpyruvate
Sequence Length: 265
Sequence Mass (Da): 29498
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J3PCK8 | MYARYVPPARDKASSAEATQSTAAPSTGATTPQAQAPYARYTPSLPKPQPATAVLGATPQPRKIVFNYGDDGPAATPTPKSKLTPYNSSVVGGEDDEPRRKKAKHPAKPDETSDKAPNSAKSKRKPVKDGVKDGGEEPSRLKEKKKRKSEPKDYAAQIEEDARSPKPEKRERKNKKERAKLADQGDGDGDVKMRDQPDVEEDEADTDPVDSRHKSVLKKKELALRRARNAPVEADEPDGPLAHLEHDGSGVHGLEPLPQPAFAVLDTSEPTYDTLPPWLGNPIHVSQSTRADWTTLGLKPELGISTEIASFLESKGYEKAFAVQTAVIPRLLPTPARQGDLVISAATGSGKTLAYVLPMIRDVSLGSVTKLRALIVVPTRELVRQVHEVCIICAAAYARQPGRKAVKIGTAVGNQAFKREQESLVDEELRYDPRGYQSIVEARKWDNLRKRELEELEFDLLDLVDKPLPLVNHVVDVVSKVDILICTPGRLVEHIGRTPGFDLSYVRWLVVDEADKLLEQSYQQWLDVVMEKLAVEFPGARDFPLQNKSGVRKVILSATMTRNVSLLSKLRLRRPELIVLEGGEINGAPAESSSYELALPELLQESAIKIRDPEQKPMYLIDLLTGEYMRSGICQTESGKMPRAKADVETADESSDDSDDPDSSDTSSSGSESDASDTSPSGSDSDSDLSPADDTMDTVLIFTKSNETALRLSRLLEIMAPSRLASRIGTLTSTTRTSERKKVLRAFHSAKLRVLVASDLVARGLDLPNLDHVVNYDMPPSVRAYVHRVGRTARAGRPGRAWTFFTKTEAGWFFAEVASQQAGKRIGNAGGSSGPSIARSRRVETVKITARRSAEDMEGGVRGDFSEARVTEYENALESLGKEAKELREK | Function: RNA helicase.
EC: 3.6.4.13
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Length: 890
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): 97554
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A0A9E0C2W2 | MKSKGLLLAIDRGNTRVKIGVFSGGTLIYQEAFSVLSLNRLQSLSRRFEFSGAILSAVAPLPVPVLKFLKKLPGFLELTHRTPLPIRNAYKSPATLGRDRIAMAVAAVVRYPRQHVLVIGAGTCITFDLVQAGGTYMGGSISPGLHMRFEALHAFTGGLPKVKLQWDNPLLGIDTLSSMRSGVMNGAMAEIREMVNEYKKMYPRLKVLITGGDAAGLAERLKINIFAAPDLVLYGLYEIYRYHDANR | Cofactor: A monovalent cation. Ammonium or potassium.
Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 1/5.
Function: Catalyzes the phosphorylation of pantothenate (Pan), the first step in CoA biosynthesis.
EC: 2.7.1.33
Subcellular Location: Cytoplasm
Catalytic Activity: (R)-pantothenate + ATP = (R)-4'-phosphopantothenate + ADP + H(+)
Sequence Length: 247
Sequence Mass (Da): 27106
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J3P366 | MAQTPEQRRRNAKFQKDQEARRGKSETDIKQRASKELNHKSPISPIWLGLLGFVVFGGLVFEVFSRFFL | Function: May interact with target proteins during translocation into the lumen of the endoplasmic reticulum. May protect unfolded target proteins against degradation and facilitate correct glycosylation.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 69
Sequence Mass (Da): 8023
Location Topology: Single-pass type IV membrane protein
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A0A061IQ45 | MKLYSLSVLYKSEPKAVLLKAAYDVSSFSFFQRSSVQEFMTFTSQLIVERSAKGSRASVKEQEYLCHVYVRSDSLAGVVIADSEYPSRVAFTLLEKVLDEFSKQVDRIDWPVGSPATIEYTALDGHLSRYQNPREADPMSKVQAELDETKIILHNTMESLLERGEKLDDLVSKSEVLGTQSKAFYKTARKQNSCCAIM | Function: Vesicular soluble NSF attachment protein receptor (v-SNARE) mediating vesicle docking and fusion to a specific acceptor cellular compartment. Functions in endoplasmic reticulum to Golgi transport; as part of a SNARE complex composed of GOSR1, GOSR2 and STX5. Functions in early/recycling endosome to TGN transport; as part of a SNARE complex composed of BET1L, GOSR1 and STX5. Has a S-palmitoyl transferase activity.
Subcellular Location: Cytoplasmic vesicle membrane
Sequence Length: 198
Sequence Mass (Da): 22357
Location Topology: Lipid-anchor
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J3NXP3 | MGAFASIWQTVAYVVSFWYIKLFGWWRSQPPKALWMARLRNATTYEDWEAAALQLDKLHGFDLWREMSQSKHYDWALIKDRLQLLHDTRVDPTQHHRLPNLIRSGLVRNLGNITSPKLYNCSFAGTKLIIEEYIAQVIFAIDDFLAAPITATATSPSRQQPTSPAVDEESCDQPTDDQPSRAPGAAAVSTGGHAASANAAAPRPAPTSPALSMQAKMTFIHDTRQAFGRTSLILQGGSIFGMCHLGVVKALFLRGLLPQVITGTAVGALIAALIAVHTDEELPGVLSGEAIDLSAFTPTSGKSTPPAADADSSSSVAGSIAAFVASVLYACAPLSSSSTRRWMTLLRRLRRFTEKGYFLDVDVLERCVRDNVGELTFQEAFRRTGRVLNITVATAEQGGVPTVLNHITSPHVLIWTAAAASNADFPSLYGRETQLLCKRPNGEIERWGPANAINFRHWTEAAYGERNSPLRRIAELFNVNNFVISQARPYVVPFLRPDMHGPTSSSSVFGGGGGSATATASAGAGLATSTLGFFLRLAGLEARHRLRQLDQLGLLPTSIRRFLVDDRVPGGGSALTLVPEVRASDFARLLEVPTRDALGYWIHIGEKSVWPALSALEVRCAIETKLDWAYRRTRRMSTSPPLWQDAAAAAAAAAQGGTGSKGSNTDTTSVKQARAGKGSPG | Function: Lipid hydrolase.
EC: 3.1.1.-
Subcellular Location: Membrane
Sequence Length: 681
Sequence Mass (Da): 73573
Location Topology: Single-pass membrane protein
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A0A7Z7QRQ4 | MDWSTIFHEITTKHDFQAMHDFLEKEYSTQIVYPDRKNIYQAFDLTPFENVKVVILGQDPYHGPNQAHGLAFSVQPNAKFPPSLRNMYQELADDIGCQRTSPHLQDWAREGVLLLNTVLTVRQGQAHSHRDIGWEVFTDEIIKAVSEGKEGVVFILWGKPAQQKERLIDTTKHHVIKSPHPSPLSAHRGFFGSKPYSRANQYLESQGLKPIHWCEGKEKFDE | Function: Excises uracil residues from the DNA which can arise as a result of misincorporation of dUMP residues by DNA polymerase or due to deamination of cytosine.
Catalytic Activity: Hydrolyzes single-stranded DNA or mismatched double-stranded DNA and polynucleotides, releasing free uracil.
EC: 3.2.2.27
Subcellular Location: Cytoplasm
Sequence Length: 222
Sequence Mass (Da): 25548
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A0A0B6CY85 | MEHLKKFFYVFLAHIYSSIFITLIPILYLKKFKRSFKNINYRKRWAERFAQIPIRLNSSIWIHSVSVGEAVSAEPLVKELLKNFPNENFVITTTTPTGSDVVNSLYSNYPNVHHMYIPYDVIPFINSFFAKTNPKIFIIVETEIWPNILNKCFAEKVPVVITNARLSKKSMRNYTKIPFAKEFLFKNISHINAQTEKDAKRFYSLAVDKNNISVTGNLKYNLITPENLENKMYSLKDSLKGRPVWIAGSTHQGEEEIILEAHKQILKIHTDCLLILVPRHKERFQKVEKLIVYNSLKYQKRSSFECQIFSDTQVYLGDTMGELLHLYYIADITFVGGSLIDNGGHNLLEPAALAKPILSGPSLFNFSQISKELIRNKALIRIRNQQEIANNIFKILEDKQLLQQMSSGALKTFKSHSDVLEKQYNNIVKFL | Pathway: Bacterial outer membrane biogenesis; LPS core biosynthesis.
Function: Involved in lipopolysaccharide (LPS) biosynthesis. Catalyzes the transfer of 3-deoxy-D-manno-octulosonate (Kdo) residue(s) from CMP-Kdo to lipid IV(A), the tetraacyldisaccharide-1,4'-bisphosphate precursor of lipid A.
Catalytic Activity: CMP-3-deoxy-beta-D-manno-octulosonate + lipid IVA (E. coli) = alpha-Kdo-(2->6)-lipid IVA (E. coli) + CMP + H(+)
EC: 2.4.99.12
Subcellular Location: Cell membrane
Sequence Length: 431
Sequence Mass (Da): 49861
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A0A0H3J631 | MTSEKSNVQNIFSSIAEKYDILNTVLTLNIDSLWRKKAINISNINEDSKVLDLCCGTGKMVYYTCKKVGKNTEVIGLDFNEAMLEVGYKNLNKSIPDYKFKLLKGDVQALPFKDCSFDCVTIAFGLRNIPNKTKALSEIYRVLKPGGKAICLELSTPQIPIFKQVYGVYFNNILPIIGYLGTGDKNAYSYLRDSVNKFMSKSDLKYAFESTGFKNASYKSLSGGIASIHYGTKPIVIK | Pathway: Quinol/quinone metabolism; menaquinone biosynthesis; menaquinol from 1,4-dihydroxy-2-naphthoate: step 2/2.
Function: Methyltransferase required for the conversion of demethylmenaquinol (DMKH2) to menaquinol (MKH2).
EC: 2.1.1.163
Catalytic Activity: a 2-demethylmenaquinol + S-adenosyl-L-methionine = a menaquinol + H(+) + S-adenosyl-L-homocysteine
Sequence Length: 238
Sequence Mass (Da): 26562
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S9V0S0 | MIGADVLYSWGAVYIAMFLPAVLMLLNFVVGNCFVSEALAVHQHTSTSHHSRARLIGRGCVAAVLVSFAWQYFDYMFLARESISGREAALCNPIHFLWDVVDTLPLLKNLPMTCLVDCTWDEVIYQGSFTAFVFFFVKSVFSVPQVSEVEAKRLEKVGILISRCSKCGSCIDTMDHHCYLICNCVGRRNRHSFLLCLLSAVLNLSFLLWWCGRWAFNSHCTVTLLGLVLVIGFLSFMTVLLAFQLLLFRRGETTIAFLKRTAGLPTVRRALSLVKG | Catalytic Activity: hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein]
EC: 2.3.1.225
Subcellular Location: Membrane
Sequence Length: 276
Domain: The DHHC domain is required for palmitoyltransferase activity.
Sequence Mass (Da): 30996
Location Topology: Multi-pass membrane protein
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A0A354HSW0 | MGKKLLRNYDYVLLLTIVLISAFGVIMVGSSSVSGEISISALFSNRTFVKQLVWAVGGLVGMALLSFIDYSEWQRLKLPIYFFSLALLILVIFKGTSAGGAQRWIAIGKLFNLQPSELAKIAIIITLSATMAKEGRSLERWSGLIVPLLHVAVPMLVIFLQPDLGTSLIFMAITGAILFVAGMRWLHLAVMGVGGIIGSVLAFLFVLKPYQKSRLIIFRDPWQDPFDDGWQIIQSKVAVGSGQFRGRGLFKGTQTQLDFLPEKNTDFIFSVIGEELGFLGASIFLLVYVFLIWRVLKVAMEAKDSFGRYLCVGVAAMLSFQLLVNVGMTISIMPVTGLPLPLISYGGSSFLTTMISLGLVLSVAAHKDTSIF | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Peptidoglycan polymerase that is essential for cell wall elongation.
Catalytic Activity: [GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)](n)-di-trans,octa-cis-undecaprenyl diphosphate + beta-D-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-di-trans,octa-cis-undecaprenyl diphosphate = [GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)](n+1)-di-trans-octa-cis-undecaprenyl diphosphate + di-trans,octa-cis-undecaprenyl diphosphate + H(+)
EC: 2.4.1.129
Subcellular Location: Cell membrane
Sequence Length: 372
Sequence Mass (Da): 40692
Location Topology: Multi-pass membrane protein
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A0A3D3NH94 | MEIYKADVVIVGGGGAGLRAAIAVAEADPLLRIALVSKVYPMRSHTVAAEGGSAGVKQASDSLEYHFNDTVHGGDWLCEQDVVEYFVAHCTEELTQLEHWGCPWSRTPDGHVNVRAFGGMKIERTWFAADKTGFHMLHTLFQTSIKYPSIKRFDEHFCVDLIVEDGRVQGVVAIEIASGEFTLVEARSVVIATGGAGRVFRENTNGGVVTGDGMALAYRHGVPLRDMEFVQYHPTCMPGTGLLFT | Catalytic Activity: a quinone + succinate = a quinol + fumarate
Subcellular Location: Cell inner membrane
Sequence Length: 245
Sequence Mass (Da): 26687
Location Topology: Peripheral membrane protein
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A0A212EME5 | MFPSKVLMDKVFGNLAHVRGLLTYRLSPHELKPFAGAFSKGGPNVIPRTTSTLMTWLPVLITSILIYVTVEESHKKSQRKNPNDFLNEVDPNTVSD | Function: Component of the ubiquinol-cytochrome c oxidoreductase, a multisubunit transmembrane complex that is part of 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. The cytochrome b-c1 complex catalyzes electron transfer from ubiquinol to cytochrome c, linking this redox reaction to translocation of protons across the mitochondrial inner membrane, with protons being carried across the membrane as hydrogens on the quinol. In the process called Q cycle, 2 protons are consumed from the matrix, 4 protons are released into the intermembrane space and 2 electrons are passed to cytochrome c.
Subcellular Location: Membrane
Sequence Length: 96
Sequence Mass (Da): 10753
Location Topology: Single-pass membrane protein
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A0A0P0M0S1 | MTLQLIVFIVLALFIAVCSVLAVTTSRILRAATYLLFVLFGTAGIYFQLNYSFLGAVQLLIYAGGITVLYVFSILLTSSQGDKAERLKNGKMVAGAISTIAGLAICLFVMLKNEFLPSHFVHGELDVRTIGHALMGMEKYQYILPFEVISVLLLACIVGGILIARKR | 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: 167
Sequence Mass (Da): 18223
Location Topology: Multi-pass membrane protein
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A0A1X7GEE5 | MTEGKRQGDNIYQVSTFSALLDGVFEGEVPFSIVKKHGDFGIGTFNKLDGEMLAVDGEFYRLQGDGTIREVKEDEKTPFAAVTFFNPSLTYRIQENGTKEQIEQFISSILPSENLFYSIRITGSFRSMKTRTVSKQEPPYSSMTDVVEEQDVSTFKDCKGTIVGFYTPRYVQGLAVAGYHLHFISEDKQGGGHIFDFEIESGTVEIGEHANLQFVLPKTKEFLEADLMHGKMAEEIEKTEG | Pathway: Polyol metabolism; (R,R)-butane-2,3-diol biosynthesis; (R,R)-butane-2,3-diol from pyruvate: step 2/3.
EC: 4.1.1.5
Catalytic Activity: (2S)-2-acetolactate + H(+) = (R)-acetoin + CO2
Sequence Length: 241
Sequence Mass (Da): 27060
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A0A7C5AH93 | MTRQPEGPDRYDGCGRSSAEVSIERKVYSVTEIVSLVRELLETGIGDVCVEGEISNLRLPSSGHMYFTLKDASSQLRVAMFRFRRKELSFQPADGLLVRVWGRVTMYEKQGECQLVAEGMEQGGKGALQAQFEALKKKLQAEGLFDGARKKPLPVLPATVGIVTSPTGAAIRDMLKILSSERLRIVIVPVRVQGDGAAAEIAGAVRMLNEWREADVIIVGRGGGSIEDLWPFNEEAVARAIAGSAIPVISAVGHEVDVTISDLVADVRAATPSVAAEMIVGAREARRMETAEMGARMARLVEQDVLRLRNRLISAAASPVFSRPAHLVQTYSQTIDHLQGNMRRCVLKVSGEMRARLENGAVMIFRAARLSRQRAAERAGRAAIRLRMLNPMAVLQRGYSLTTDEKGRVITSSDGLLPGRRVKTLLAKGSFESEVKEVHGDEKERVPGG | Function: Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.
Catalytic Activity: Exonucleolytic cleavage in either 5'- to 3'- or 3'- to 5'-direction to yield nucleoside 5'-phosphates.
EC: 3.1.11.6
Subcellular Location: Cytoplasm
Sequence Length: 449
Sequence Mass (Da): 48965
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A0A354HTP9 | MSATLNLLAPAKINLSLDVLGRRDDGYHMVEMIMQTIGLCDSISLQARSDGHIQVLCRHPFVPEGQENLAYKTANLLKQLSGKSSLGVTITIAKGIPVAAGLGGGSADAAAVLKGLNRLWDLDLSSDQLAQAGLKLGADIPFCLMGGTALARGIGEELTKLPPPPKLWVVLLKPNVGVSTAEVYKKYNDSAVHRRPDTNRLIAALAAGSLEAISQAMANVLESVTFPRLPVLRHLKQKALEFGALAALMSGSGPTIFALTPDYRRADAIFNGLRHQVEFAYITTFKEVAKK | Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 3/6.
Function: Catalyzes the phosphorylation of the position 2 hydroxy group of 4-diphosphocytidyl-2C-methyl-D-erythritol.
EC: 2.7.1.148
Catalytic Activity: 4-CDP-2-C-methyl-D-erythritol + ATP = 4-CDP-2-C-methyl-D-erythritol 2-phosphate + ADP + H(+)
Sequence Length: 291
Sequence Mass (Da): 31076
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N1ZE70 | MEEIRLKARAKINLTLDVTGKQSNGYHTVRMIMQTLSLYDSIYIKKIDKPVIRVKSNLDWLPTDERNLAYKGAELLKNTFHIQQGIFIQLNKKIPVAAGLAGGSADCAAVMVGINKLFNIGLSKKKLMKLSLQLGADIPYCILQGTALAEGIGEKLMPIKTGCPFCYVLLAKPNINISTASVYQSLELDKITQHPNTEEMLSQMQQKNITEMGKLLCNVLETVTISKYHEIALLKQKMMTLGASGALMSGSGSTVFGLFLDKQKAIEAEKIIKNEFTLRDVFVTEIWNKKQHRRRG | Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 3/6.
Function: Catalyzes the phosphorylation of the position 2 hydroxy group of 4-diphosphocytidyl-2C-methyl-D-erythritol.
EC: 2.7.1.148
Catalytic Activity: 4-CDP-2-C-methyl-D-erythritol + ATP = 4-CDP-2-C-methyl-D-erythritol 2-phosphate + ADP + H(+)
Sequence Length: 296
Sequence Mass (Da): 33005
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A0A2P5L9F1 | MAQIGKNLAIDKLKVRQSFSLACNTYDAAAGLQRIIADRMINAFNDCDGKINHVLDLGCGTGYLTKALQNSLTFDHLFAVDIALPMLVFCREKNLQRSNFSPICADAANLPFRSGSIDLITANLVLQWLSDLHGALMEIKRLLKPCGQLLFSTFGPQTLQELKQAWAQVDQFSHVNEFYHLEAIRSFLLSCGFKDIVITSQNHVMHYDSVFALMRELKDLGAHNVTSGRNKQFTSPGKLNTMIAAYEAANQSSAGIKATYEVILVSAKN | Pathway: Cofactor biosynthesis; biotin biosynthesis.
Function: Converts the free carboxyl group of a malonyl-thioester to its methyl ester by transfer of a methyl group from S-adenosyl-L-methionine (SAM). It allows to synthesize pimeloyl-ACP via the fatty acid synthetic pathway.
EC: 2.1.1.197
Catalytic Activity: malonyl-[ACP] + S-adenosyl-L-methionine = malonyl-[ACP] methyl ester + S-adenosyl-L-homocysteine
Sequence Length: 269
Sequence Mass (Da): 29776
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A0A7I8XC14 | MELDNCNMFLFMQKWMTDGPSKFTLPQLQENPGGWGPAPLESSEPMKQFINMPFQLFNKCDRVGRIVDWLGVDRYKKSDTRERYNERMYGSSQNAGSQFDYVHDNEESNFQLVDSSKPQKPARPYRRTQLPFRKLLQKEQERRDQQFYNQSNKTKRSIAKEQNRAYKLWQRRGGMRNGQPSRGMAGRRYGDRQGGKGRQPSVQVRPDWKILWDLDFQRLAKLSLPNIEGQDIKGENYGILYYYDKALEKVTVKNAVPLQRCGGIFYNTTTTEDPVIMKLAQKNEGNVFATDIILATLMASQRSVYSWDIVAHRVADKLFLDKRDTGGISNPVDALTVSETSMDPPTWDPSVPQNNAQDLATEALFINQNFRRQCLKRSEKPLSFDHARAPFEDDSPDARAECLYKYRKWNLGTTEQGKPITLVARTELDGALAPPSKDKEPQKLTIKAFNEWDSAQAGGVRWRAKLDTQKAAVLATEIKNNGCKLAKWTLQAILANADYLKFGYVSRVNTRNSAQHEILGMQQFRPQDFANNISLNLDNSWGVLRVICEFLLKQEPGKYLLLKDPLQPVVRIYSLPEGTFESDDEGDSEEEEDDDDN | Function: mRNA cap-binding component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is involved in protein synthesis of a specialized repertoire of mRNAs and, together with other initiation factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S ribosome. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation. In the eIF-3 complex, eif3d specifically recognizes and binds the 7-methylguanosine cap of a subset of mRNAs.
Subcellular Location: Cytoplasm
Sequence Length: 597
Domain: The RNA gate region regulates mRNA cap recognition to prevent promiscuous mRNA-binding before assembly of eif3d into the full eukaryotic translation initiation factor 3 (eIF-3) complex.
Sequence Mass (Da): 68509
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A0A212EK03 | MVPTSNYTPVSDFYNGKTIFVTGGTGFLGKVLIEKLLYSCPGISKIYMLVREKRNLTATDRMKKFFDCPVFDRLKKEKPENLKKLKPVNGDLSQPCLGIDPKELQVIKDEVTIVFHFAATVKFNEPLSIAMKINVEGTEQVIDLCHSLKKIEVFVYMSTIFSNTDDKLNSVEERLYRSPKEVDEIYKMIKENDPREVFNPEVLDGRPNTYTFTKAVAENIVAQKRGNLPTIMIRPSVVTPAKEEPVRGWVANWMGPTATLLYLSRGWIRCHYGEDDFTFEIIPVDYVVNLTIISAAKFKRSDDIPIYHSCTSALHPVTFKETASYLIKESCKKKLVDIPFPWITFSRSLWFLGIISFFMQLLPAYIADLYLFICGHPTRYVKMLKKYSQNMSALHYFSSRTWYMTANRSQELIDGLSAEDQKIFPCSPASIDWSEYMATYLHGVYRFLLKSHY | Function: Catalyzes the reduction of fatty acyl-CoA to fatty alcohols.
EC: 1.2.1.84
Catalytic Activity: a long-chain fatty acyl-CoA + 2 H(+) + 2 NADPH = a long-chain primary fatty alcohol + CoA + 2 NADP(+)
Sequence Length: 453
Sequence Mass (Da): 52170
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R4FK33 | MNVTKKINVPQLIFKYSKRLVSEANFTIQEPFRLHRLEKGPLTKVTLTKQDALTYYKKMSTIRRVENTSANLYMEKVIRGFCHLYAGQEAVAVGIQATMRPDDCLITAYRAHGWVLLMGGSPEQILGELCGRVIGCSRGKGGSMHTYAKNFFGGNGIVGAQIPMGTGIGLMMKLTGKPNVSFALYGDGAANQGQVFEAYNLAKLWNLPVIFVCENNKYGMGTSAERASAVPEFYTRGDYIPGIQVDGMDVLATREASLFAIAHCISNRGPILLEMVTYRYYGHSMSDPGTSYRSRNEVQDIRKNKDPITLFKDKILGANLVSEEEIKQLDNETKKIIEEATAKVRAAPVPGPEELVADVYKKPVTPNVRGVNPWRTLKHIQITKPK | Function: The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2).
EC: 1.2.4.1
Catalytic Activity: (R)-N(6)-lipoyl-L-lysyl-[dihydrolipoyllysine-residue acetyltransferase] + H(+) + pyruvate = (R)-N(6)-(S(8)-acetyldihydrolipoyl)-L-lysyl-[dihydrolipoyllysine-residue acetyltransferase] + CO2
Sequence Length: 386
Sequence Mass (Da): 42832
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J3PDZ3 | MLRPALSLLVLALSSAGAAVSSSGSRLLVVLDDVADKDKYSKFLGDLTSRGFDITYSTPKAESLQLFRLGQRTYDHAIFFPTKVKGLGPNLTPNTLLQFVKENGNILLALSSEMAASSSIVSLLHELEIQLPAERTGLVVDHFNYDAASAPDLHDVVLVPAPAPVRPGVADVFAAPGEERLLAFPRGVAQTLGQSPLLNPVLRGPRTAYSYDPKEQGDSVDPDQLFAAGQQLSLVSAAQARNSARVAVVGSAEMLADKWFDAKVKPAGGAKDEVATYNREFASRISAWAFQELGVLRVNWIEHHLNEAGASNASNPSIYRVKNDVTYTISLSQYDGKAWGPFTVPAADELQLEFSMLSPFHRLPLKAAALQPAPKEATAYSVSFKTPDQHGIFNFKVNYKRPFLTNIDTKDTVSVRHMAHDEWPRSYVISGAWPWITGIGATVTGWLAFVIVFMFSAPAKKASAAKKTQ | Pathway: Protein modification; protein glycosylation.
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).
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 469
Sequence Mass (Da): 50869
Location Topology: Single-pass type I membrane protein
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A0A0H3J1E1 | MSTVKLTTAQALVKFLNSQYISVDGKESFFVEGVFAIFGHGNVLGLGQALEENPGNLKVHQGRNEQGMAQAAIAFAKQSRRKKIYACTSSVGPGAANMITAAATATANNIPVLLLPGDTFSTRQPDPVLQQIEQTYSAAVTTNDAFKPVCKYWDRVVRPEQLMSAMLNAMRVLTNEGDTGAVCIALPQDVQGEAYDFPEYFFQKRVHRIERRCGTKEEINDAVELILKKKKPLIICGGGAKYSEAGEELKKFAQEFNIPICETQAGKSALESTFLLNLGGVGVTGNLAANLIASDADLIIGVGTRFTDFTSGSKGQFRNSEVEFLTINASRYNAEKMDAVKIVGDAKVSLKALYENLHLKGYKSGYTSEIEEAKDRWEQEVKRLYAIEFNDKDFKPEVAGHNDDSAKELYDLYNEAMPQTTVIGEINKFLQKDYVIVGASGSLPGDLQRLWRSNEKYSYHMEYGYSCMGYEVSGALGVKLAEPDKEVYAMTGDGSYMMLHSELISSVQEHKKINVLLFDNCGFGCINNLQMSNGMGSFGTEFRRRNEETGHLDGEYIPIDFAKSAEGYGVKTYSVKNIKELREALADAKNQTASTLIDIKILPKTMTNGYESWWHVGVAEVSNKESIQKAYDSMKENLSKARQY | Cofactor: Binds 1 Mg(2+) ion per subunit.
Pathway: Polyol metabolism; myo-inositol degradation into acetyl-CoA; acetyl-CoA from myo-inositol: step 3/7.
Function: Involved in the cleavage of the C1-C2 bond of 3D-(3,5/4)-trihydroxycyclohexane-1,2-dione (THcHDO) to yield 5-deoxy-glucuronate (5DG).
EC: 3.7.1.22
Catalytic Activity: 3D-3,5/4-trihydroxycyclohexane-1,2-dione + H2O = 5-deoxy-D-glucuronate + H(+)
Sequence Length: 644
Sequence Mass (Da): 71223
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A0A350NRP4 | MNVLQGVVIASLSGFCYVRTDDEVADAVESLECKPRGKVKSADRIIVGDRVAVTRIDEKTGIIEKIFPRKNQLLRPVIANVDQVVIVMAIKNPDLNLYLADRFLLQAETQHLDVLVCLNKCDLAAPKEVKAAARHFEAAGYRVLATEAVHNVGQRRLRALLAGRISVVAGPSGAGKSALLNMVEPGFGLRTGSISEKIGRGKHTTRHTSLHALKAGGFVADTPGFTQLDIVGVSAVDLASYFREFAGMADQCRFRGCVHVSEPNCAIKAAVADGTIRSERYEHYTHFYQELIDQEKRRFH | Cofactor: Binds 1 zinc ion per subunit.
Function: One of several proteins that assist in the late maturation steps of the functional core of the 30S ribosomal subunit. Helps release RbfA from mature subunits. May play a role in the assembly of ribosomal proteins into the subunit. Circularly permuted GTPase that catalyzes slow GTP hydrolysis, GTPase activity is stimulated by the 30S ribosomal subunit.
EC: 3.6.1.-
Subcellular Location: Cytoplasm
Sequence Length: 300
Sequence Mass (Da): 32879
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A0A942EJM3 | MATALKDTSGYLSSEDNSRANLATLSTLQNTRMRLLQNIEEISKRLAGDSPPTNPGFFETRMISMRSEISLLDTKIQGLQKVIASLDSKLELPSPKSKSHEETLLLGLRKTRSEITLLQKAIKNLQALSETETRKGRAILDNLISEIPSLASQLTDIEGDPKSTLPSLKSSELTLQQNYDTFKKALSPYFVNKSQNFTQKVESDEFNYKTLNALYESLEPEVKELVHYTPNLFYGRGLNTRLYDERGAQLQPNGSVRFSVFAPNAKDMTLCLTSIGDDELEEPLRFPMESDPITGVWTTIVGSFEDATFKGSRYHYELTTQTGNTRKKIDPMATGYIRRPDDQEILFDSVVCDYKSFKWTDQHWMDTRQLNTKRPVNIYEVHPSKWNPERVKNWRHLAPLLAEHCKKFGYTDIELFAVLEHPGNTSFSGYQVSGFFAPNSRLGTIEDFQYFINYMHAQKIAVILDWIPAHFCIDSWGLEQFGSPVYERRYVEHDQERVFDTRLEKLSNSAKKDSTQNPLRKSLHPSWGTYEFDFSKAPVREFLTSSAIFWLRELHLDGLRLDAVASMIHLGYDRERTDLLVLPSDHGDKINHDALHFMRNLNAYIRREIPRACIYAEESSGHAKVIDPVEEGGVGFLTSWNMGWMNDTFEWAKTSRFKWLAKGFQLRRNEHTVYEISHDEVRGGDKPTLIQRMGGSFSKARNIMAYQMCMPGPKLTMMGSEYAQDLPWSKSDGDRVSKKTGFEAGVFWDEIGDDHRKSFSKMLQDLGQLYQREDALWFNDGKPDSLLQENIDHDNEIISYHRKGSNDQRQLLCIHNFKSSPYKHYRIQLPNQAPYTQIENVRVLFNSDDSRWGGKDLDTAVRVDKTKPHEPFIYITLPPMTTMILEESFTN | Function: Catalyzes the formation of the alpha-1,6-glucosidic linkages in glycogen by scission of a 1,4-alpha-linked oligosaccharide from growing alpha-1,4-glucan chains and the subsequent attachment of the oligosaccharide to the alpha-1,6 position.
EC: 2.4.1.18
Catalytic Activity: Transfers a segment of a (1->4)-alpha-D-glucan chain to a primary hydroxy group in a similar glucan chain.
Sequence Length: 891
Sequence Mass (Da): 102511
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A0A1I7RM75 | MNRLAGLPPKRVATAVRLFSAAATSPSTSRADPDEIRRFDSLASEWMNENGPMKPLHSMNRIRVPWITNELNERIQRSGIDPTQPLKGIKVADIGSGAGILTLPLARLGATVDGIEATEECVRVADRLADNVLDAGTRKRINFVNSSVEELAETKVEAYDAVIASEILEHVADQADFVRAAVRLAKPGAPLFFTTLNRTALSRVVGIWLAEGLGFLPSGLHQWDKFVTPDELRSHLLLNDCQVIYKRGLIYDPLLNEWDWFFGEQINYALLAKKL | Pathway: Cofactor biosynthesis; ubiquinone biosynthesis.
Function: O-methyltransferase that catalyzes the 2 O-methylation steps in the ubiquinone biosynthetic pathway.
Catalytic Activity: 3,4-dihydroxy-5-all-trans-polyprenylbenzoate + S-adenosyl-L-methionine = 3-methoxy,4-hydroxy-5-all-trans-polyprenylbenzoate + H(+) + S-adenosyl-L-homocysteine
Subcellular Location: Mitochondrion inner membrane
Sequence Length: 275
Sequence Mass (Da): 30471
Location Topology: Peripheral membrane protein
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A0A9J7H5K8 | MAEAVFRAPKRKRRVYERYESPLPIPFGQDQGPRKEFRIFRAEMISNNVVVRDAEDMEQLYGKLTAEAFVHSVQDGMRLVICWGYFGKGILSRSRPNFTISNPKLAARWKGVQTDMPIITSEKYQHRVEWAMDFMRRQGQEESTVQKILTDYTEPLELPCRKGKEEVPQHDPLNSEANSTLEGRVGKDELSVTTGGAGQSDDLQGLNTHSDCLQEGPGQATLTVASPSSFNGHVIEDTTVLPQVPCRIAQDGLWPEDSSQAAGEKRAAHEYVLVEEELCDVQEEDEAPDEKLLQRKRLVCRRNPYRIFEYLQLSLEEAFFLTYALGCLSIYYEKEPLTIAKLWQAFTAVQPTFRTTYMAYHYFRSKGWVPKVGLKYGTDLSILSSLS | Function: Constitutes one of the two catalytic subunit of the tRNA-splicing endonuclease complex, a complex responsible for identification and cleavage of the splice sites in pre-tRNA. It cleaves pre-tRNA at the 5'- and 3'-splice sites to release the intron. The products are an intron and two tRNA half-molecules bearing 2',3'-cyclic phosphate and 5'-OH termini. There are no conserved sequences at the splice sites, but the intron is invariably located at the same site in the gene, placing the splice sites an invariant distance from the constant structural features of the tRNA body.
EC: 4.6.1.16
Subcellular Location: Nucleus
Sequence Length: 387
Sequence Mass (Da): 44095
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A0A7W4DTZ4 | MVDRSPWTGEKVKDSDRLMLITLHDSPYPVREQAEAFLLGGGRVLQYRAKGVAREQMLREATALASLCADFEATLIINDFVEVAKIVDADGVHLGLDDAPPQRARVALGGEAIIGATAHSEKELRALAAQPIDYIGLGPYRMTQTKRNLPPPHGAAGVARLVSIARSAGVNVPIFAIGGIDDMDIRDVLNAGCMGVAVSASIALASDPQRTTTRFLERINRNVR | Cofactor: Binds 1 Mg(2+) ion per subunit.
Pathway: Cofactor biosynthesis; thiamine diphosphate biosynthesis; thiamine phosphate from 4-amino-2-methyl-5-diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)-thiazole: step 1/1.
Function: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate (TMP).
EC: 2.5.1.3
Catalytic Activity: 2-(2-carboxy-4-methylthiazol-5-yl)ethyl phosphate + 4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine + 2 H(+) = CO2 + diphosphate + thiamine phosphate
Sequence Length: 224
Sequence Mass (Da): 24064
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A0A5H2CMZ3 | PLSSIWCLSRNSRYALSLLIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPILIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTTINMKPPAISQYQTPLFVWAVLVTAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLF | 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: 218
Sequence Mass (Da): 23406
Location Topology: Multi-pass membrane protein
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A0A977JKX9 | SLYFLFGMWAGMLGTSLSIIIRLELGNPGALIGDDQIYNVIVTAHAFIMIFFMVMPVMMG | Pathway: Energy metabolism; oxidative phosphorylation.
Catalytic Activity: 4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-[cytochrome c] + 4 H(+)(out) + 2 H2O
Subcellular Location: Mitochondrion inner membrane
Sequence Length: 60
Sequence Mass (Da): 6629
Location Topology: Multi-pass membrane protein
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A0A343URJ5 | MINLPEPIHEAIFVSLELGPILGGPGVVSLTNIVYSAPLSGSVFACISLPYLLPNADFVAAVQISIYVGAVNVSIVSAVTSTNEPQSFHLSTYRTAGDGITLALCISLFFLPIIMILDTSWSRVSLIVLPGGIVEEPLTDDVQRIGSHLLTDSLLPFEPLSIVLLVALVGAITTARRDKMVKLEESEVLQAKDDFFVS | Function: NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient.
Catalytic Activity: a plastoquinone + (n+1) H(+)(in) + NADH = a plastoquinol + n H(+)(out) + NAD(+)
EC: 7.1.1.-
Subcellular Location: Plastid
Sequence Length: 198
Sequence Mass (Da): 21151
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A0A7R9QME6 | MDQFTLLMLLSFSMLFGSYFSGTIPLVFTFSEDKLRLLSVLGSGILVGTALSVILPEGVNTLYTSSHEFHSHLKTISTQKTTNETTKSEDNPHSVIVLHLKTISTQKTTNETTKSEDNPHSVIGLTLVIGFVLMLLIDQFSNRHTGANSYSVALQSDSAENGESLSTCVPKRSSKMTATIGLVVHSAADGIALGAAATTSHTDVEMIVFLAIMLHKAPAAFGLVTFLMHEGVERSRLRKHLLAFALSAPIAAFITFFGISQGTKEALSDYNATGIAMLFSAGTFLYVATVHVLPEITQHQHLNLKELLALVGGTFIPSLLTVKHHH | Catalytic Activity: Zn(2+)(in) = Zn(2+)(out)
Subcellular Location: Golgi apparatus
Sequence Length: 326
Sequence Mass (Da): 35195
Location Topology: Multi-pass membrane protein
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A0A212EUU2 | MFLTNFNEFVANLAVITTIIQFLSGILVCRQYVVNRTTAEASPLPFICGFLSSGLWLLYGICKPDSKIIIVNVVGVLLMLSYSIVFYVYTFKKSSVLKQSLVAIILYLVMVVYMSTEIDNEILLVRLGYSACLLTLLTISAPMSKLFYVIRTKCTDCLPFPMIFMSFIVSSLWFIYGCIVQDVFLSIPNFIGASLAVAQLSLFVVYPSVPQTPLLLKMTEA | Function: Mediates sugar transport across membranes.
Subcellular Location: Cell membrane
Sequence Length: 221
Sequence Mass (Da): 24690
Location Topology: Multi-pass membrane protein
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A0A0H4KC89 | MLKNSIAVAVGGALGAYLRFVTTLWIPHSSFPYHTLFQNIVGSFVLGALTAYFSLRTRREWIKVGLGTGVCGGFTTFSTLAFDAVFLKSTEAFLLYISISLGFGLLAVFLGTRFVRTFVKERGVRK | Function: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Subcellular Location: Cell membrane
Sequence Length: 126
Sequence Mass (Da): 13854
Location Topology: Multi-pass membrane protein
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A0A351J8B2 | MIVGIRRNLRLQNKKLKMGLISLGCAKNLVDSEVILGFFEQADFTRTTNPEEADILVVNTCGFIEAAKQESIDAILEMAQYKDRGRCRVLAVAGCLSRRYADELTQEIPEIDVLVGVAEYPLLPDLVKKALNGGKHSLVQQCGFIYNENMPRVLATPPFMAYVKIAEGCANRCSYCAIPLIRGPLNSRPIASITAEVRQLCAKGVAEINVIAQDTTAYGLDLYGKPSLADLLEQLVAIPDVQWLRVLYAYPNLIDDRLLEVFATHPQICRYLDLPLQHADSELLSAMRRRGRPEQYLDLLGKIRAAVPGIALRSSFIVGFPGETEQQFQTLLDFMAEAAFDYAGVFQYSAEENTPAADLPGQVSGTVKEERYHRAMRQQAAITRKALAGRIGSESAFLCTGQRQQNGDNLITGRVEWQAPDVDGITLLEGSRVKSGELINVKITGSGDYDLRAARANENPKKE | Cofactor: Binds 2 [4Fe-4S] clusters. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalyzes the methylthiolation of an aspartic acid residue of ribosomal protein uS12.
EC: 2.8.4.4
Catalytic Activity: [sulfur carrier]-SH + AH2 + L-aspartate(89)-[ribosomal protein uS12]-hydrogen + 2 S-adenosyl-L-methionine = 3-methylsulfanyl-L-aspartate(89)-[ribosomal protein uS12]-hydrogen + 5'-deoxyadenosine + [sulfur carrier]-H + A + 2 H(+) + L-methionine + S-adenosyl-L-homocysteine
Subcellular Location: Cytoplasm
Sequence Length: 463
Sequence Mass (Da): 51125
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A0A7Z7QQL0 | MVKLAVDMMGGDDAPNIVLEGVEKAVNDFEDLEIILFGDEKQCHIQHPRVEVRHTTEEITMEDEPVRAIKRKKDSSMVRMAEAVKNGEADACVSAGNTGALMSAGLFIVGRLPGVARPALVVTLPTVKGKGVVLLDVGANADAKAEHLYQNAVLGHIYAQKLRGIETPKVALLNIGTEAKKGNSLTKEAFNLMSKN | Pathway: Lipid metabolism; phospholipid metabolism.
Function: Catalyzes the reversible formation of acyl-phosphate (acyl-PO(4)) from acyl-[acyl-carrier-protein] (acyl-ACP). This enzyme utilizes acyl-ACP as fatty acyl donor, but not acyl-CoA.
Catalytic Activity: a fatty acyl-[ACP] + phosphate = an acyl phosphate + holo-[ACP]
EC: 2.3.1.274
Subcellular Location: Cytoplasm
Sequence Length: 196
Sequence Mass (Da): 21056
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A0A350BDH1 | MNRKVMIFSLTSSKKLATQVAFILGLPISNVEVMHFADGEIMVRSLESVRDSNVYIIQSTCPPVTENLMEVLIFTDALKRSSAHEINVVIPYFGYARQDRMARPREPITAKLIADLLTAAGIKRIITVDIHTLQIQGFFAVPVEIMSVLPMFGHHLRQRLENENIPLDQVVVVSPDHGSAIRARDLASLLPNSQIALIDKRRPAPNKAEVSSLIGDVYGKIAIIVDDIVDTGGTMIAASDLLKKHGAKRILACATHGVFSQNALELLKQSPIDLLTITDSIEHDNLQGIEVISVAPMLGQVIDHIEKGLPLSPIYDAYNL | Cofactor: Binds 2 Mg(2+) ions per subunit.
Pathway: Metabolic intermediate biosynthesis; 5-phospho-alpha-D-ribose 1-diphosphate biosynthesis; 5-phospho-alpha-D-ribose 1-diphosphate from D-ribose 5-phosphate (route I): step 1/1.
Function: Involved in the biosynthesis of the central metabolite phospho-alpha-D-ribosyl-1-pyrophosphate (PRPP) via the transfer of pyrophosphoryl group from ATP to 1-hydroxyl of ribose-5-phosphate (Rib-5-P).
EC: 2.7.6.1
Subcellular Location: Cytoplasm
Catalytic Activity: ATP + D-ribose 5-phosphate = 5-phospho-alpha-D-ribose 1-diphosphate + AMP + H(+)
Sequence Length: 320
Sequence Mass (Da): 35149
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A0A8J8CEP1 | MDFKTEKLRGFRDFLPEDMKIRNYVRKAIEKKFKLYGFDEILTPTVEYTGIFTLKSGEEITESMFAFKDKGNRDVCLKPEQTVSTARFFIENFKNFAMPLKFYYFCPVFRYDEPQHARYREFWHLGVELIGSNTPESDAEVISLAYCGLKQLNLNFELELSNIKVIKGVLNSTNLSRGDKEKILHYIDKHNDEGINEILKRTDNGEILNKVLSFKGKRGNLNELKNIVRNCPEAIEGIEELENILNFVEMFNNDYVINFNIVRGLDYYTSNVFEIHANDMQICGGGRYDNLIGLFSDKDSKNDKNKGVPAVGFAYGFDRVIEALKAQNLIPKFENNKILITYVSEEFLPYCIKVAGELRERNITADLDIMKRKVKKAMEYANNKYRYVIVVGKKEFEEGRITLRDMESGGQKFLDVGEIEPLC | Catalytic Activity: ATP + L-histidine + tRNA(His) = AMP + diphosphate + H(+) + L-histidyl-tRNA(His)
EC: 6.1.1.21
Subcellular Location: Cytoplasm
Sequence Length: 423
Sequence Mass (Da): 49035
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A0A352W9B0 | MQRLGILGGTFDPIHLAHLMLASEAQHQLSLDRVLFIPSSIPPHKKNGTFADVQQRLRMTELAIKVEPAFQVCDIELQRSGPSYSVDTVAAIRATLAEQDEVYFIIGWDAFSQLDSWHNPSRLAELCFFAVAGRPGAGDMVHSRYPESCPPERVYHINTPQFSISSTDIRNRIETGRPYHYMLPEAVYRYIKANGIY | Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; deamido-NAD(+) from nicotinate D-ribonucleotide: step 1/1.
Function: Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
EC: 2.7.7.18
Catalytic Activity: ATP + H(+) + nicotinate beta-D-ribonucleotide = deamido-NAD(+) + diphosphate
Sequence Length: 197
Sequence Mass (Da): 22277
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Q6F3N5 | FACDVSEDLLLGTSEKIVKWGLKDLGYNYVILDDCWSEGRNSSDYLIPDSKKFPRGMKHVADSLHDEGLLFGMYSSAGEYTCAGYPGSLGHEEADAASFASWDVDYLKYDNCYNQGNYGTAQLSYERYKAMSDALNKTGRPIYYTLCNWGEDSPWHWASAIANSWRISGDIYADFDRPDSRCPCNGDEYYCHLAGFHCSIMNILNKAAPLGQKAGPGGWNDLDALEVGVGNMTDEEEKTHFSMWAAVKSPLVIGANLNTLDAKSFSIYVNPAIIAVNQDAAGAPVMRVWRYYVSDTDEHGQGEIQLWSGPLDNGDQIVALLNAGSKDRPMNATLEDIFIDSGADSEKLSSSWAIYDLWANRLDEDTAKDIINGNSTAEGKLYNATELPYTEGIAKNDTRLFGTKVGTVKPFGSIET | Catalytic Activity: Hydrolysis of terminal, non-reducing alpha-D-galactose residues in alpha-D-galactosides, including galactose oligosaccharides, galactomannans and galactolipids.
EC: 3.2.1.22
Subcellular Location: Secreted
Sequence Length: 416
Sequence Mass (Da): 45841
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A0A109RDF3 | MSFIKGVFHEMRMVEWPSGKQLMRDTGIVLITILIAAIYLGVVDELVTMLFGWFIQL | Function: Essential subunit of the Sec protein translocation channel SecYEG. Clamps together the 2 halves of SecY. May contact the channel plug during translocation.
Subcellular Location: Cell membrane
Sequence Length: 57
Sequence Mass (Da): 6559
Location Topology: Single-pass membrane protein
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A0A174WVR7 | MMLEPPMNQLLKQVPSRYMLVNVVAQRARQVASEAEDAGIPLDDKPVTIAIREVAEGKVELNDEE | Function: Promotes RNA polymerase assembly. Latches the N- and C-terminal regions of the beta' subunit thereby facilitating its interaction with the beta and alpha subunits.
EC: 2.7.7.6
Catalytic Activity: a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1)
Sequence Length: 65
Sequence Mass (Da): 7247
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A0A7R9M6A7 | MLRSDDSNTISKSAVIFRCIDYILCLEKHLSFLMIMMTWLLFVTKLGPMFMKNRKPFVLREIIMVYNLILVLTNAYYIYASLKWLEFGRKSLDPKLPGYCTDGYIYYWIYEYWEQGIDTRTRGYFLVDMSPLTLCCILAMYIIHVKLLIPYLMKNRKPFDLKKIIIGYDVLLVAINAYFWFYSLAHITDMWDFKKELASHVGWLLCRKHPEVLEKGKTIDMSDLDRDPLIKFQRRFYIPLVALIWGAFPTYVPYYLWGESLWNSYFLCVMFRYALILNITWCVNSAAHLWGKKPYDKSINPVECVIRHVMFGEGFHNYHHTFPWDYSASELGAFDVFNPATMFIDFWAYFGQAYDLRKASDDVVKSRQKRSGDMNWKGSTKVFEIATCLATIGLMTQSTATETETGNNNNEIGFQNGTEIDAKPKPEYKLELVWRNIILMTIVHLSAIYGLYRGVFYAKPMTIYFMYLLGLLSSFGVQCGAHRLWCHRTYKAKLPLQILLAFMHILALENDIYEWSRDHRVHHKYSETDADPHNAKRGFFFAHVGWLLCRKHPEVLEKGKTIDMSDLDKDPLIKFQRRFYIPLV | Subcellular Location: Membrane
Sequence Length: 584
Domain: The histidine box domains are involved in binding the catalytic metal ions.
Sequence Mass (Da): 68787
Location Topology: Multi-pass membrane protein
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A0A212FCC4 | MKNLIILGLLGYLSIAFADKETLVLVDNLNIRETHSLFFKSLQERGYSLTFKLADDANLVLSKYGEYLYKNLVVFAPSVVEFGGQLDTEAITRFIDDGGNVLIAGSSAAGDVYREIASECGFEMDEESAAVIDHFNYDSLDEGDHTRIVVSPKNLIDAPTIVGTHNTQPLLFDGTGLILDKDNSLVLPILTADSTAYSYNPKNQVKEYPHAVGRKTVLIAALQARNNARIVFSGSLFFFSDEAFNSPVSKVHGDKIKSALSGNKQLSIHLSQWVFGERGQLRVQSVHHQRQGDKKSSNTYTITDTVVYRIEIEELKNGKWQPFEASDVQLEFVRIDPFIRTTLQKKPNGIYEAIFKVPDVWGVYQFKVDYDRVGYTRLYHSTQVSVRPLQHTQYERFIPSAYPYYVSAFSMMVGVFLFSFVFLYYKEESPKSKAE | Pathway: Protein modification; protein glycosylation.
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).
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 435
Sequence Mass (Da): 49115
Location Topology: Single-pass type I membrane protein
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A0A7R9QXR6 | MQTFSCLNRIQWPSLVFLVLCLMNAIHCRELSYVVNPGCDQSCEQWTAAKKSLNLVHISSKDTSDTIHFLWSSITSIPPTLLIVKTPSDATLTIDYAKLLQTKSTSPDGGISFSKEPLNAIGVQFSRLFFFNDINKSGSYDEKDPIFEVMWKDFHWTPVANGSAKDSIELHLKNSDEIETNESAIKGTIEFVLRVDSSDGRGEELPHLAFTDNSVSLSLNVMDVEYDKTEAFNKSLHDQILPRVMTSIFVINDIKDNTTKSDPSIETLTSIDDEYTPGAFDLIHMKVDSNKGSKSENENKAFIQWKPIAYNSDDRIIANTLDVIHKGFDSINGTDLAKNNSLFLESFFNTRTKSSHSFNLTFGASDDEKYYDDKKYIGYSFVVGLGAAPEDSLSTLVKMIILVGFGLPALVTC | Function: Required to protect lysosomal transporter MFSD1 from lysosomal proteolysis and for MFSD1 lysosomal localization.
Subcellular Location: Lysosome membrane
Sequence Length: 413
Sequence Mass (Da): 46077
Location Topology: Single-pass type I membrane protein
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A0A843C4F6 | MVDYPLETVVEGKTKILVPDVEAFRKSPSSYPPSDAPVFYNKVMELNRDFALATLRVYIDLLSKKESLFYCEPMAGSGIRAVRIANELENISVVINDRNPHAVELIKENVKQLKLTEKTSVHMDDACELMIRHAASGNRFDVIDVDPFGSPSVFMDSAAQALGYNGFLAVTSTDMATMCGVYPKACIRKYASKPIHSSIGHEVAVRMLIGFIATNLARHGKGTKPIFAHSTEHYIRAYVVAEKGITKAKESMNTLGYIAHCLKCYAIESRKGLINSLTKECPDCQNKHRLLGGPVWLGDLYDEQFVNKLKSEVEDNKTNYGSQKKMGKMLVLIEEEVKAQQTNAGICFFDLHQISDKLNIPSPKVEAVMEELAKGGYSATRTHFRTNSIKTDAPIDKIVSAMKKVLNI | Function: Dimethylates a single guanine residue at position 26 of a number of tRNAs using S-adenosyl-L-methionine as donor of the methyl groups.
EC: 2.1.1.216
Catalytic Activity: guanosine(26) in tRNA + 2 S-adenosyl-L-methionine = 2 H(+) + N(2)-dimethylguanosine(26) in tRNA + 2 S-adenosyl-L-homocysteine
Sequence Length: 408
Sequence Mass (Da): 45345
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A0A1I7RQW6 | MAWLVWLATVLVVFITLLQVSNVFRFYFKCVLFGATVIGASFIGSFLCLLNGTTTKNHYVIFNVFHKLGVWMNIEYTVENPELLVSEEPYVIIANHQAALDVFTMSKIWPDNCVVMLKNSLKYVPFFNICAWKCNAIFVDRFSKDKAHQTIDHAREGMEKDKKKIFIYPEGTRNNREELLPFKKGAFIISKGVNVPIVPCVFSSYKPFYDYDKKMWLSSGKVTIRVLPKVYPGDKDVEQLAEECRDLISKNFKELSGFSKKE | Pathway: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-diacylglycerol from sn-glycerol 3-phosphate: step 2/3.
EC: 2.3.1.51
Catalytic Activity: a 1-acyl-sn-glycero-3-phosphate + an acyl-CoA = a 1,2-diacyl-sn-glycero-3-phosphate + CoA
Sequence Length: 262
Domain: The HXXXXD motif is essential for acyltransferase activity and may constitute the binding site for the phosphate moiety of the glycerol-3-phosphate.
Sequence Mass (Da): 30203
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A0A7R9MVQ7 | HSFALYGINIAIFKAKWTTIVFVHIIAILSSMGVQSGAHRLWSHRAYKAKLPLRIILAFFHIMAFQNDIYEWCRDHRVHHKYTETDADPHNAKRGFFFSHVGWLLVKKHPDIRAKGKNVDLSDLMADPVVRFQRKFYIPLLLAIWGVIPTVIPHLFWSESLWNAFFTC | Subcellular Location: Membrane
Sequence Length: 168
Domain: The histidine box domains are involved in binding the catalytic metal ions.
Sequence Mass (Da): 19656
Location Topology: Multi-pass membrane protein
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N1ZQM1 | MAKKKMTFEQAIQRLEEIVEILETEEIALEKSVDLYKEGMELAEFCQTKITKAETEVVLLQKNISGEIEQTHFEVEEGE | Function: Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.
Catalytic Activity: Exonucleolytic cleavage in either 5'- to 3'- or 3'- to 5'-direction to yield nucleoside 5'-phosphates.
EC: 3.1.11.6
Subcellular Location: Cytoplasm
Sequence Length: 79
Sequence Mass (Da): 9148
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A0A7R9MPZ5 | CDPGVVAKDHDQRYRVSFHACEPVTIIELAERDGFDPQWFCSTCLIRKPLRSKHCSICNQCVARFDHHCPWVANCVDYEHHIHFGDDTNVWTFIANAWTYNGWITWCALNAAVHSRLVRNDYKRAHELSAL | Catalytic Activity: hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein]
EC: 2.3.1.225
Subcellular Location: Membrane
Sequence Length: 131
Domain: The DHHC domain is required for palmitoyltransferase activity.
Sequence Mass (Da): 15243
Location Topology: Multi-pass membrane protein
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A0A060NCY3 | VKDYKLNYYTPDYETKGTDILAAFRVTPQPGVPPEEAGAAVAAESSTGTWTTVWTDGLTSLDRYKGRCYHIEPVAGEENQYIAYVAYPLDLFEEGSVTNMFTSIVGNVFGFKALRALRLEDLRIPPAYVKTFQGPPHGIQVERDKLNKYGRPLLGCTIKPKLGLSAKNYGRAVYECL | Cofactor: Binds 1 Mg(2+) ion per subunit.
Catalytic Activity: 2 (2R)-3-phosphoglycerate + 2 H(+) = CO2 + D-ribulose 1,5-bisphosphate + H2O
EC: 4.1.1.39
Subcellular Location: Plastid
Sequence Length: 177
Sequence Mass (Da): 19663
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A0A345UFH4 | LYLVFGAWAGMVGTALSLLIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGISSILGAINFITTIVNMKPPAISQYQTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHL | 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: 217
Sequence Mass (Da): 23119
Location Topology: Multi-pass membrane protein
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A0A0C4F041 | MQGVLCYSPGTIQSAAEVIRSEDVVAFPTETVYGLGASALSSTAVSKIFRAKGRPSDNPLIVHVCSLDLLKTFLPPDWAFPATYEALIERFWPGPLTLLVPTTSPAQPTSPISSLVTCGLPTVAVRMPAHPISRALIAASGVPIAAPSANLSGRPSPTTAEHVARDMKTKISMILDGGPCQVGVESTVVDGLNPDGRLRILRLGGLSVEDIEACLIGAGLSHCDGTPILAGVYNRDYRDKELEVKPTTPGMKYKHYAPHAKVVILDPVSPPSSSTDGHQSLSGVNELVSGLCGDNSDSSKGLRIGLMLIDDSQLHKSFIRCANSKTYYHHQFCYSNLGPETQPVISAQRLFAALRHLDEDLRVDIIYVERLAEVGLGATVMERLRKASGQSSLVSISVSNP | Function: Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine.
Catalytic Activity: ATP + hydrogencarbonate + L-threonine = diphosphate + H2O + L-threonylcarbamoyladenylate
EC: 2.7.7.87
Subcellular Location: Cytoplasm
Sequence Length: 401
Sequence Mass (Da): 42744
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A0A5S9NQX8 | MSENIPCGVILIGMPGAGKSTIGRALASRCGKSFVDTDHLIEARERLSLQILLDTNGYEYLRAIEAEVLLEHDFSNKVVATGGSAVYSHDAMEHLQRFGPCLFIDIPLDSLIKRVQNFSERGIAGPIGQDFHAVYQERLPLYRRYADITVNGAGLNEAELLAAVQRALSETTFFGVSG | 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: 178
Sequence Mass (Da): 19456
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A0A354HQD1 | MKVIPKIPLLVIAGPTASGKSAAAVELAQIFDGEIVSADSMQVYKYMDIGTAKVDLATRAQVPHHMLDVVEPDEDFSLAQYKEQADKIIQDIWRRQHLPILTGGTGLYIKAVTENYPLQQLPFDPHCRAELNRLWDERGREYMVSRLQQVDPETAAKANDRRRIIRALEIYQLTGRGPAEIHRQAKAESPFNALIFALTLPRPQLYECIEARAEAMVIQGLIGEYIKLIERGYSPAAKAMQGLGYYHAGMCVAGNWTREEMIANLQRDTRRYAKRQLSWFRGMQDVIWLDHSNPQASMEKISAETAGKLQLYSELVINIDI | Function: Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A).
EC: 2.5.1.75
Catalytic Activity: adenosine(37) in tRNA + dimethylallyl diphosphate = diphosphate + N(6)-dimethylallyladenosine(37) in tRNA
Sequence Length: 321
Sequence Mass (Da): 36339
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A0A7C4NNP5 | MKSVFEELLNLDYSAVTRYLISRIRNKVSETGFDKVVVGLSGGLDSSVTVKLLTEALESSRVLALIMPDSRVTDKADVEDAVNLAESLGVNYRILNIDGIVDEYAKILGVDNYESIPIGNLRTRIRMSILYYYANTTKALVAGTSDKSEILIGYFTKYGDGAADFYPIACLYKSQVRRLAEYLGLPSRIIRKPSSPGFWRGHLAEEEIGLKYEVIDSILYLLFDKKLSIDEIITNYNFDRDVVVKVLSMFRRSMHKRVLINEEDLYLPNPPI | Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from deamido-NAD(+) (ammonia route): step 1/1.
Function: Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses ammonia as a nitrogen source.
EC: 6.3.1.5
Catalytic Activity: ATP + deamido-NAD(+) + NH4(+) = AMP + diphosphate + H(+) + NAD(+)
Sequence Length: 272
Sequence Mass (Da): 30757
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A0A351J4A7 | MLQKIRVLIADNNRDLCAALAEHIELQQDMELAGVAYDGLEALEKIRDTHPDVIILDITMPYLDGIGVLEQMPAFEDGTYPRVIVLTAFEQENMIQRLISLGADYYMVKPFDMNTLFERLRQFSRGTQPASPQSREHSADYLSTPKASRPKNNPTPSDVELEITRVFHEMGIPAHFRGYVYLREAILMSVHEVELLGNITKNLYPRIAEKFKSTPSGVESAIRHTIEIGWQRGNVDYMCDFFGYGDAGKSRFPTTASFIAKVTDKIRLETRFVS | Cofactor: Binds 1 Ca(2+) ion per subunit.
Function: May play the central regulatory role in sporulation. It may be an element of the effector pathway responsible for the activation of sporulation genes in response to nutritional stress. Spo0A may act in concert with spo0H (a sigma factor) to control the expression of some genes that are critical to the sporulation process.
Subcellular Location: Cytoplasm
Sequence Length: 274
Sequence Mass (Da): 31138
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A0A212FH64 | MVWPTEFDVKLDEYDAMDLPGQQLQSAQASTTLDHILNLNISAPAGCQRLTGIISFMGKSTYDVEVMQKMIAAGMNIALLNLSFGNKEEHMETIKNLREAVKNYSVKCGKKYPLAIGARLPGRKIRTGCIADTFGETVELKTGEVVRLTTDETYRDRCSNYTVYIDFMHFAEQMDKGNLVLLDNETIKLKVEMISATTLTCKIERGGFLGSYKDVFVPNVTFDMPNYSEHDKEYIDMAIHMQLDILVASFVNSSNTITELRLLMGEKGKKIAIVANIQTIQGFHNFDDILSAASGIMITRQELGSDITPKKLVIAQKNMIARANMANIPICVSAHLLSSMRHNSIPLRAELLDIANCILDGADALVLSAETAVGDYPVDTVECMATTCKEAEACVWTKQVFHDMFDKTPQPCDQATGTALAAVIAAQRCLAAVIVVITTSGKSAQIVAKYRPRCPIIALTRYAAIARSLHMWRGIIPLIYEAGPAVDWQMDLENRVHFCTKWAMEQGFLRIGDAVVVVSGWRQGSGFTNTTRIIYTTADTAN | Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 5/5.
EC: 2.7.1.40
Catalytic Activity: ATP + pyruvate = ADP + H(+) + phosphoenolpyruvate
Sequence Length: 542
Sequence Mass (Da): 59884
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A0A0C4MP81 | YKLSTTGNWMNNDENYNKIIASYAFVMILFMVMPFMIGGFGNWLIPLMIGAPDMAFPRMSNTSFQLLMPSMFMLLLS | 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): 8829
Location Topology: Multi-pass membrane protein
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A0JC78 | MTTQGSRPTGDVVVQKYGGSSLATVSQVRQVADRVGALARSGRRVVVVVSAQGDTTDELVGRAEAVNPRPAGHELDQLLATGETASAALMAMALQRGGLAATALSGARSGVLATGPHGAGVIVAVDTDQLRTLLDAGRTVVLAGFQGVTAEGDIITLGRGGSDTTAVAVAAELRSGHCEIYSDVPGVFTADPRVVPDARLMPDIDIDVMTEMAFAGARVMHARAVELAALYDVDILVGRSTATRTGTRIHRRDGNDMLEDRTAVSAVVHDADIARITLRTHDTPDPSADVFRFLAKESIPADMTTVSSAPDGGFSLGFTVRRSHAADVGRSFSDLMAPRPHGVEVEDQVAKVSIVGQGLLSRPEYASRMLASLVGSGISARSLTASQLRVSVTVPRSDAVRAVGLLHSEFGLGAEAGAVPASLTPRP | Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 1/4.
Function: Catalyzes the phosphorylation of the beta-carboxyl group of aspartic acid with ATP to yield 4-phospho-L-aspartate, which is involved in the branched biosynthetic pathway leading to the biosynthesis of amino acids lysine, threonine, isoleucine and methionine.
EC: 2.7.2.4
Catalytic Activity: ATP + L-aspartate = 4-phospho-L-aspartate + ADP
Sequence Length: 427
Sequence Mass (Da): 44208
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A0A1P7ZNU5 | VYILILPGFGLVSQMISNESMKKETFGVMGMIYAMISIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLASMNGMKIKFNVSNLWLLGFIFLFTVGGLTGIILSNSSIDIVLHDTYYVVAHFHYVLS | 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: 140
Sequence Mass (Da): 15606
Location Topology: Multi-pass membrane protein
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A0A940HTG0 | MANKLIKIALIGNTNAGKSTLMNSMIDKTVSIINKKINTTQNIIMGIVNIDDTQIIFYDTPGSNFLNSSVSSQKRLKIDIWTAIDEVECILYIIDVSKYNYNSVCSDIKKINEVKKPIIVIFNKTDLIDNKLILPYIESLNNLNIVEAFFNISAKYRKGLNKLSIFIKSKAKNNKWIFNKGEVSNKDPIFMANECTRNAILKYLHKEIPYNITVRNLLFKSLNNNDIKIKQSIDLTNMRYKPIILGNKGETIKKIRECSQNEISNIMKSKIHLYLQVNKLND | Function: An essential GTPase that binds both GDP and GTP, with rapid nucleotide exchange. Plays a role in 16S rRNA processing and 30S ribosomal subunit biogenesis and possibly also in cell cycle regulation and energy metabolism.
Subcellular Location: Cytoplasm
Sequence Length: 282
Sequence Mass (Da): 32345
Location Topology: Peripheral membrane protein
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A0A2P6N0M2 | MGKESEHQGSDYAEYYTGQDGREYTNQPAPVMHQTYARHYDEESPINNRNSDDKFKPANHRRDPAWTIVFLVHLVAFFVLFVFAAVKYQAVMKDQQTTNTGNNTGNNEPYSDSTNLRKLLFSCMGMVALSLIFAGVWLQVIKTFATQIIYITLVLSSALWIAFSIYLFSIHSIFGGIITLLAALLHIFLWFSWRSRIPFASLMLRTVSGVTQRYHGMTVISYLSLFVSIFWIVLWVLTVIFLDQGLSSKVVDQNGQSHIERPTAVYVLYVFLLLSFYWVAQVIKNVVHVTTSGTVASWYFLYGTEAMPVNPSIASFKRATGTSFGSICLGSLIIAALQTIRTLLRGLRGNHDILNAIIDCFLSIIENLVRYFNKYAFAQIAIYGKSYCEAAKDTWAMFEQHGFMAVVNDDITGTVLGMSTLLGGVLNGVLGAILSVILFPQNSNALAAMIIFGFLIGLLLCSQVMEVLESGITTIFVSFVMDPAVLARNSPELYAQFQERYSEEDTQGGRSLLYPTTLHTPTRRSSQMKSSMKRSNPLSDSDAELGKKRIRVARPPNSFLLFSNATRSALKRQNPHLNNAQLAKLLGTTWKTLHPDEKKRFTERADRIKTNYFKINPIPITEDADTIQPESVRPQSALELLEAALHTGPSPPEPDYQETLDFIEGYMTERKITGYSEEDIDSFTTVSSTLTPNTSLPSTPSSQFSLGERHESQGGQRKKGNSSSG | Function: Choline transporter.
Subcellular Location: Cell membrane
Sequence Length: 725
Sequence Mass (Da): 81070
Location Topology: Multi-pass membrane protein
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A0A0N0IQ38 | MEGRIPPHNLEAEQSVLGAILLDSDVLDELEGLLPSPEAFYAEAHRKIYAAMQTLRSQGKPVDLVTLAEELSRRGELEALGGVSYLVQLSEATPTAAYAEHYARIVAEKWTLRKLIQAAGEAMRLAYEEAGSLDEILDTAGKKILEVALTQTETEARSIRELVHETFEHIEALFQNKGEVSGVRTGFKELDQLIGTLAPGSLNIIAARPAMGKTAFALTIAQHAALKEGIGVGIYSLEMPASQLTLRLMCSEARIDMNRVRLGQLTDRDFSRLVDVAGRLSEAPIYIDDTPDLTLMELRARARRLRSQYEVGLLIIDYLQLMSGPGAGKQGENRQQEIAAISRGLKALARELNVPVIALSQLSRAVEARPNKRPMLSDLRESGCLAGDTLVQLADGSRKPIRELVGRSGFHVLALNEATMKLEAAMVSRAFATGVKPVFALTTQLGRQIRATANHKFLTSKGWKRLDELRPGDWVALPRRLDVATQQTLGDEELALLGHLIGDGCALPRHTLQQASGLSQRELYRAVGMAYAGSTLFRQNLSRDRAVRMAHAVKSVALSQMATSDVYWDKVASIQPDGIEEVFDLTVPGLHNFIANNIIVHNSIEQDADLVMFIYRDEYYNPHSEKAGIAEIIVGKQRNGPTGTVELQFHAAHVRFNDLAREP | Function: Participates in initiation and elongation during chromosome replication; it exhibits DNA-dependent ATPase activity.
EC: 3.6.4.12
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Length: 663
Sequence Mass (Da): 72893
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A0A7R9LXL9 | MENVGQFAVTISREGDLKPTVCVDFKTEDGTANAGSDYEPIEGTIIFRPNEMHKQVFITVIDDDLFEEDEHFYVRLSNPRYLSHDGCTPMNGAISNTNKSPPLLQLATPAIATVMILDDDHSGVYSFAESQYEVSESVGEYHLKVNRFSGARGKVSVPYHTCEGTAKHGVEFEMTEGVVFFDNNQTSQEIVIHIMDAESYEKDAVFYVELGEPVREEDSIEEFDDQKDPNHQSFDEKIALLGKPKLGEIYKCSVRIKESKEFKNTVDKLISKANTKILMGTSSWRDQFIDAITVSAGDDDNADEDGEEGEREEKLPTCSDYVMHLFTLFWKILFAFVPPTEMGDGWACFVISIIWIGILTAVVGDLASHFGCTVGLKDSVTAISFVALGTSIPDTFASKVAAQNDQFADSSIGNVTGSNAVNVFLGIGIAWTLAAIVHAYRGTQFRVDPGSLVYSVTLFSICAFLTCIVLMIRRRLGGELGGRMLYKLPAVILFVCFWLFYVLMSSLEAYKMIPGF | Catalytic Activity: Ca(2+)(in) + 3 Na(+)(out) = Ca(2+)(out) + 3 Na(+)(in)
Subcellular Location: Cell membrane
Sequence Length: 516
Sequence Mass (Da): 57196
Location Topology: Multi-pass membrane protein
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A0A0X8FCB8 | MTKEKLIVICGPTGVGKTALSLDLAQKFSGEVVNGDSMQVYRHLDIGTAKISPEERGSIPHHLFDLREVHESYSVADFKRDATEVITKIHERGHLPLLVGGTGLYLEALLYDFDLGSEVAEHPAFREAMAGYADQYGALALHQKLQTVDPKAAEAIHPNNQRRVIRALEVCQFSSGKFSDQKQSRHQDSPYDLLIIALVRDRQKLYEQINQRVLEMVDQGLLEEAKWLYQQDLPPDAQSMKAIAYKELFPYLSGQESLEAGIQRLQKNTRHYAKRQLTWIRHRLPAAQTYDLVDDPQATDYQRLVEEVKRFLKT | Function: Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A).
EC: 2.5.1.75
Catalytic Activity: adenosine(37) in tRNA + dimethylallyl diphosphate = diphosphate + N(6)-dimethylallyladenosine(37) in tRNA
Sequence Length: 314
Sequence Mass (Da): 35783
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J3NY35 | MSPPFPVIYLLSTHLNTDRLRALEAQITTITYNAQEAEVVLGNISKKQRAMFELRRLGLWTSEVPTSNVATEPPKKRPRHTSSANNNDEAWLLGSQPVGTDNQGIRGTVPGSGKVTVVKLTWFTESTKLGQVLPFGDHLLYEGIKLAGSYEVNDPRSPPSNLPPIPQRSRSGVVGASSQQPTAKTSTATHRSSQVPSLLRQSTSEHEAARHMPTMPDFLRTVYSCQRPTPIHPPNEAFINQLAKIKTTRLLAGDRIGVRAYSSAMASLAAYPYVLASPEEVDRLPNCGPKFAVLFQEFQRQGGVIREAQEAELDPKLSVIKNFYDVWGVGDVTAKKWYDNGWRDLDDVVEYGWETLTRDQQIGVKFYDEFLLKIPRDEVEKIADTILEHANRLRNGFQMVIVGGYRRGNKESGDVDIMLSHPDENATRNLVTHLVVALEGSNYITHTLVLSTKNSERGQVTLSWKGEVNKVPGSGYCTLDKALVVWQDPSWAAGGNNTEKNPNPHRRVDIVVTPWKTAGCALLGWTSGTTFQRDLRNYCKRERGLKFDSSGIRSRTSGRWLDLESGEDGSPAPDMLTAEKRVFAGLELEWLSPEERCTG | Function: DNA polymerase that functions in several pathways of DNA repair. Involved in base excision repair (BER) responsible for repair of lesions that give rise to abasic (AP) sites in DNA. Also contributes to DNA double-strand break repair by non-homologous end joining and homologous recombination. Has both template-dependent and template-independent (terminal transferase) DNA polymerase activities. Has also a 5'-deoxyribose-5-phosphate lyase (dRP lyase) activity.
Catalytic Activity: a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)
EC: 2.7.7.7
Subcellular Location: Nucleus
Sequence Length: 599
Sequence Mass (Da): 66638
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A0A353N5T5 | MWERKYFKNIDYYLLGSVLLLVLIGLVMIYSATRNNQALTGGEPFMLVKKQLVAVIIGVLGMILIMFSDYRLPDLMYQIIYGFNLFLLLIVLSPLGLEIKGAKSWLNVGGPFSLQPSEFAKLMMILTLAKHLAGKEEIDSFWDLWSPFFHIMPPLILILIQPDLGTTLVFFFFFFIMLYIAGYNGRFLLGLILTGVIILTLIFLSHYYFGTPLPFKEYQIRRMTIFLNPESDPTGSGWNVRQAIITVGSGRFSGKGLFQGTQGRLGFLPENHTDFIFAILCEEWGFLGGFVLLSLYFTMIWRCLVITQHSKDKYGTLVAAGIMAMFIFHILENIGMNLGIMPITGIPLPFVSYGGSSIITNLLAVGFLENIWIRRQKLIF | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Peptidoglycan polymerase that is essential for cell wall elongation.
Catalytic Activity: [GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)](n)-di-trans,octa-cis-undecaprenyl diphosphate + beta-D-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-di-trans,octa-cis-undecaprenyl diphosphate = [GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)](n+1)-di-trans-octa-cis-undecaprenyl diphosphate + di-trans,octa-cis-undecaprenyl diphosphate + H(+)
EC: 2.4.1.129
Subcellular Location: Cell membrane
Sequence Length: 380
Sequence Mass (Da): 43092
Location Topology: Multi-pass membrane protein
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A0A977JJI5 | TLYFIFGAWAGMLGTSLSLLIRAELGNPGSLIGNDQIYNVVVTAHAFVMIFFMVMPIMIG | Pathway: Energy metabolism; oxidative phosphorylation.
Catalytic Activity: 4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-[cytochrome c] + 4 H(+)(out) + 2 H2O
Subcellular Location: Mitochondrion inner membrane
Sequence Length: 60
Sequence Mass (Da): 6524
Location Topology: Multi-pass membrane protein
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A0A3B8S8A9 | MSALSLSHRHLRIAALLLFFVTLSALAVVHTSFKNRQLFIELQALQLEATQQKIKLGRLLIEESTWSSLAAIEHTASSQLAMTVPRPEQLVVVSTLSQQGER | 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: 102
Sequence Mass (Da): 11349
Location Topology: Single-pass type II membrane protein
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A0A212ENP8 | MRWKCKSSKGRWLYVLLMLIVLPVVVAQKIGDPYKILGINQRATLPEIRKAYRQLAKEWHPDKNENPNAEARFVEIKQAYELLSDTERRQAYDLYGITNEDDHMYKQRHDYSQYARFSNDPFEFFSTHFRAQDQDITLFHKLSVTTRHFENNILEKSVHTPALVLFYTDWCFDCVRSAASWRKLVDSLQPLGVTLATIHAGHEASLARRIGVHSVPCLTLILDKQIYIYKDGLNSLPKILEFMRWKFPYKLVRGINDGNVDSFVTDFEDNKVKALIFEERQTIRLRYLITAFHYRDRLSFAFVDISARDTANVTSRYKVQRSMDTMVLLKEDSIEPAATVSTTEIQTQTMRQLIEANQMLTLPRLSSQNILDTVCPVEWRAARRVLCCVLVVRDERDVRSNAHSIQQLRDLARRAPDRIRYTYVYEHAQPDFVNALANGSGIDLSSLDHRIVVIWRRESTRIQYEWLKESWPSCGRCQGEEGVSYQDKMNRTQRALDEMLKRLLRPSEVVAYEARIQELVDESSPCGARLVMARVSEWIERAMSALRSHHALSALSILATVALVLAAGYFMAYLIRVEEESVQREKEERRRQNGGKRNNNEAQPEMRLHELRAEKYNGLVRLQKPGCRTIVLLVDSQSRVQLLSKFHRIVWPYRKNKTLVFAYLCVERNVEWFRRVLQLSLGGGGELRVNRRNCVGTVLALNPHRKYFCIYHAKHPECVKPHKRMSRMAASLGGRAPDPEAGAFIGFTTDPDSSDDDCYDPPLLLQENLLDGLENWLDRLFEGSTHRYYVNYWPDMTTK | Function: Plays an important role in regulating the size of autophagosomes during the formation process.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 799
Sequence Mass (Da): 92925
Location Topology: Single-pass type IV membrane protein
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A0A0X8FBV8 | MPELPEVDRVRQGLEDLVLGARVTGLSLSWPKIIDQPSPEEFETIMLGLRLEGLGRRGKYLIFDWGEWAWISHLRMEGKWLVLPSDQAVDKHTHLVLQLDDGRDLRYHDVRKFGRIRLFPKAQLDEELARLNLGPEPWDLDADTFYQQLQRRKLAIKLVLLDQHVVAGIGNIYADEILYRARLHPEQPANTVSRIKSNRLVHYAGKVIEEAMAKGGTTIRSYTDALGHSGGFQQTLNAYGRAGLPCPRCQTPMKKIKVGQRGTTFCPRCQVLKKERR | Cofactor: Binds 1 zinc ion per subunit.
Function: Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized purines, such as 7,8-dihydro-8-oxoguanine (8-oxoG). Has AP (apurinic/apyrimidinic) lyase activity and introduces nicks in the DNA strand. Cleaves the DNA backbone by beta-delta elimination to generate a single-strand break at the site of the removed base with both 3'- and 5'-phosphates.
EC: 3.2.2.23
Catalytic Activity: 2'-deoxyribonucleotide-(2'-deoxyribose 5'-phosphate)-2'-deoxyribonucleotide-DNA = a 3'-end 2'-deoxyribonucleotide-(2,3-dehydro-2,3-deoxyribose 5'-phosphate)-DNA + a 5'-end 5'-monophospho-2'-deoxyribonucleoside-DNA + H(+)
Sequence Length: 277
Sequence Mass (Da): 31668
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A0A481RL18 | MGIRRHAIPRPTTSTYHVKSDNMDAWSISPKDLKPIGVAAADQQKQQQLQLQQQPLGPKKLTSDDLKKGPDTGSGGGGGSKSDVFHTLAPVYHLSKICGLLPVKFKANKAGKYEGRLDVAEVAYGIVLVAALAGAQCYGLYRDLRNGWENSTRLSSETAITVTCSDVFAVISAAFVAILGSGYRWHHLQDALNKIVDVDDKLLDVPTSERLRKVSIIVIVSSLVYIVVISSLDFVSWRASSAGKNNAHFGDKGPINYAPLYFMYIVVTVFEVQYALVLFNVGERFLKLNKSVANLTRSNMALEQLFRRYTHQPHHQQQQEQSMAFFSNEIGHIGRFRRVNNKISDFGPGAGTETASKTAELIGRLIGLHGILCDSVKNVNKAYGGAVVVGTISCLIHLIITPYFLYNEIFSDSISSWYVLTMQVFWTFFHVCRLLFLVQPCHMVSVEARKTGALVSQALASNWQPEAKKQLEIFSLQLLQRPVEFTACGLFFLDRGLVTSIAGAVTTYLVILVQFQNADETKGTKNLLQNATELLKNASSFKNITFKVR | Function: Gustatory receptor which mediates acceptance or avoidance behavior, depending on its substrates.
Subcellular Location: Cell membrane
Sequence Length: 549
Sequence Mass (Da): 60746
Location Topology: Multi-pass membrane protein
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A0A7Y1UA76 | MTQNKNIIVLGAAESGVGAAVLAKVQGYNVFVSDIGSIKEEYKKELIENEILFEENNHTVEKILSAGEVIKSPGVPDNASIIRKIKAEEIPIISEIEFAGRFTDAKMICITGTNGKTTTTLLTHFILKNAGLNVGLAGNVGHSLAMQVAKKNHDYYVIELSSFQLDYMFEFRANIAVLLNITPDHLDRYDYKIENYINSKFRITQNQTSEDAFIYCADDEILNKEITNKTIQAQSYPFSIEKEEGMTAYLNSNQLTINTQTKPLTMTIYDLALQGKHNLYNSMAAGISSKILDIKNEEIRQSFSDFKNIEHRLELVNTIHGVEFINDSKATNVNSTWFALESVTKPIVWIAGGVDKGNDYALLQDLVRDKVKAIVCLGKENEKLHDAFGHVVSEIVDSGSASDAVYQAFSLSDKGDTVLLSPACASFDLFKNYEDRGWQFKQAVRAL | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA).
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: 447
Sequence Mass (Da): 49783
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A0A520Y0W1 | MLVGAAAVPAAGVASQVAAGATVATPRSAHTTDEPARPFDQVLEEEDAKTEGFRQSDIRTIVEWLAVIISALVVALVIKAFVLQAFWIPSESMQTTVNEGDRILVNKVSYRLHDVRRGDLVVFKKLPGTPGPTEDLIKRAIALPGETIEVRDDGRIWIWGPGETPADAQLLVEPYLDPRNEILQAPSATDALSSDIWDDQCANQPRTPGRCTLAEGQYFMMGDNRYSSSDSRFFGPITEDLVVGRAFLRIWPLGDISSL | Catalytic Activity: Cleavage of hydrophobic, N-terminal signal or leader sequences from secreted and periplasmic proteins.
EC: 3.4.21.89
Subcellular Location: Membrane
Sequence Length: 259
Sequence Mass (Da): 28288
Location Topology: Single-pass type II membrane protein
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A0A256GHE0 | MTTPLVEIRNLSINFQRDDQLVKVVEGINLTIHPGETVALVGESGSGKSVTARALIGLSGPSAIVKADLFEIDGLSVLDYRDKEWRGLRGNKIGFVLQDALVSLDPLRRISQQLSDAFGVKGFFRRPDVTDRSKALLRSVGIPDPDRRLLQYPHQLSGGLRQRALIATAVARSPSLLIADEPTTALDATVQKQILDLLAERRRAGHTLLLISHDLAVVSRLADRVLVMHNGRIVEEGPTRQILSAPKEAYTRHLLEAVPSAGSRGYRLSPAQPHQPQVRVALPAKRIDESTNVLEAKGLFKHYGKANTPLAVNDVSFSLKAGEALGIVGESGSGKTTVAKIVLGLTEPDQGSVHIDGRLWSNLREEQRREQRAHMQLIAQDALSSFDPRYTVEKIVGESLDSVHVYGDERRKRVVEVLDAVRLGAPFLKRYPRELSGGQRQRVAIARAFAPRPKLLVADEPVSALDVSVQAQVLDLLAELQAASGTSLLFISHDLGVVHHLTDRVLVMKDGRIVESGAVERVFSQPQHNYTRALLDAVPTISAA | Function: Probably part of an ABC transporter complex that could be involved in peptide import. Probably responsible for energy coupling to the transport system.
Subcellular Location: Cell inner membrane
Sequence Length: 544
Sequence Mass (Da): 59442
Location Topology: Peripheral membrane protein
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A0A7R9MN61 | MEDVMLGNTGVKVEKGMSVEIPVYAIHHDPDHYPDPFTFSPDRFMPENRGHMKAYTYLPFGS | Function: May be involved in the metabolism of insect hormones and in the breakdown of synthetic insecticides.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 62
Sequence Mass (Da): 7101
Location Topology: Peripheral membrane protein
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A0A256G1E1 | MTIINTLLSVEGLVVRSNETALAGPVSFTLKQGETLGIVGESGSGKTLTAMAIAGLLPQSLHADGQSYLDGAPLALGISDRGRDFRTSQIGVVFQNPTTALNPRLSVGAQLFEALSPAMRGDKAKAATICLHLLEEVGISEPVKKLTAWPHELSGGLAQRVVIAMALARQPKLLIADEPTTALDVTVQAQILDLIARLQKRHGFGVLLITHDMGVIRDRADSVAVMDGGAIVESGATLNLFTNPKSRAARSLLKASELVFATASGVLHDAASQPPLVEVKALQKTFRNGPRALGGVDILVKSGTTLGIVGESGSGKTTLARIIAGLERADDGHILIDGNVRPPRTRSDHVQYVFQDPYSSLDPRISIVNTVAEPLLAKGLRKAEALRIAQGLLEEVGIHPALWHRLPGRLSGGQRQRVGFARAIAPSPKLLIADEPVAALDSTSRERVLALMEDMQRRHGTAQMLISHDLSVIARLCREVVVMRGGEIVERGETRRIFEAPAHPYTRQLLAAIPGRKPLVAPKF | Function: Probably part of an ABC transporter complex that could be involved in peptide import. Probably responsible for energy coupling to the transport system.
Subcellular Location: Cell inner membrane
Sequence Length: 524
Sequence Mass (Da): 55909
Location Topology: Peripheral membrane protein
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A0A7L9AXG2 | MDSNTITSFQVDCYLWHIRKLLSMRDMCDAPFDDRLRRDQKALKGRGSTLGLDLRVATMEGKKIVEDILKSETDENLKIAIASSPAPRYITEL | Function: Inhibits post-transcriptional processing of cellular pre-mRNA, by binding and inhibiting two cellular proteins that are required for the 3'-end processing of cellular pre-mRNAs: the 30 kDa cleavage and polyadenylation specificity factor/CPSF4 and the poly(A)-binding protein 2/PABPN1. In turn, unprocessed 3' end pre-mRNAs accumulate in the host nucleus and are no longer exported to the cytoplasm. Cellular protein synthesis is thereby shut off very early after virus infection. Viral protein synthesis is not affected by the inhibition of the cellular 3' end processing machinery because the poly(A) tails of viral mRNAs are produced by the viral polymerase through a stuttering mechanism. Prevents the establishment of the cellular antiviral state by inhibiting TRIM25-mediated RIGI ubiquitination, which normally triggers the antiviral transduction signal that leads to the activation of type I IFN genes by transcription factors IRF3 and IRF7. Also binds poly(A) and U6 snRNA. Inhibits the integrated stress response (ISR) in the infected cell by blocking dsRNA binding by EIF2AK2/PKR and further phosphorylation of EIF2S1/EIF-2ALPHA. Stress granule formation is thus inhibited, which allows protein synthesis and viral replication.
Subcellular Location: Host nucleus
Sequence Length: 93
Domain: The dsRNA-binding region is required for suppression of RNA silencing.
Sequence Mass (Da): 10617
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A0A6I9MPX2 | MKLLLLVSLLTGATAQSISPQAVWQLGNVFECNIPRSGTVLEYRFYGCYCGLVRFGDPDEDLDSCCRTRDNCLAQVDNLENCAVLIRNPYTSSYLFSCSGNEVTCSDKNNLCQSFICNCDREAAICFSKQIKGIHC | Cofactor: Binds 1 Ca(2+) ion per subunit.
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+)
EC: 3.1.1.4
Subcellular Location: Secreted
Sequence Length: 136
Sequence Mass (Da): 15103
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A0A804JRH4 | MATARVLLRRGLLPGHRPSAAAATATVRLLLAQTHSSLSESAEPKRLKTFSIYRWNPDRPDSPQMQEYEVDLNECGPMVLDALLKIKNEVDPSLSFRRSCREGICGSCAMNIDGDNGLACLTKIPAAESAAAAMITPLPHIFVVKDLVVDMTNFYSYNKDRAKLDGTHECILCACCSTSCPSCWWNPEAYLGPEALLHAHRYVLLL | Cofactor: Binds 1 [2Fe-2S] cluster.
Pathway: Carbohydrate metabolism; tricarboxylic acid cycle; fumarate from succinate (eukaryal route): step 1/1.
Function: Iron-sulfur protein (IP) subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q).
EC: 1.3.5.1
Subcellular Location: Mitochondrion inner membrane
Catalytic Activity: a quinone + succinate = a quinol + fumarate
Sequence Length: 206
Sequence Mass (Da): 22679
Location Topology: Peripheral membrane protein
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A0A212EZQ7 | MCENLSQDRIRCEACRTINLAKNVNQPKPDMQIYEKCSPTQKICSRVPELPIHPTCIKVCSKEEYKLRKSGKKLTLPVKTVPCPHGKLMYAVKAGILVGAVYFTYTQGVWGDQRDVTECIRRWQEYIRSINTRRPPVFDQCGNVIKKESSESIIAPMYLIYKRIVTTCFEGIVKFPMILKCAYIDYIKALERRQAELDQERKIRKRSI | Function: Component of the MICOS complex, a large protein complex of the mitochondrial inner membrane that plays crucial roles in the maintenance of crista junctions, inner membrane architecture, and formation of contact sites to the outer membrane.
Subcellular Location: Membrane
Sequence Length: 208
Sequence Mass (Da): 24169
Location Topology: Single-pass membrane protein
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N1ZQL6 | MKKVAILPNLEKDKQFAITKRLVNYLLYKNCEPMLTKKIAEMSNLELYGKDEEQIYQNADFLISLGGDGTLLGVGRRSAKYGKPILGINLGHLGFLTAEEKDYAECAIDRVLEGDCYIEKRMMLEASIFAEPKRIEGLLALNDVCITRGFSSKILEFNIFVNMEYVDTLRADGVIICTPTGSTAYNLSAGGPILKTDAEIIAITPICPHTLTSRPIIVSAEDKITVEVFSRANEDFIVSTDGQCSMSLKRRNVVQVKKSPYFTTIMKTNQVSFYDVLREKLGK | 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: 283
Sequence Mass (Da): 31603
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N1ZET9 | MREIINILGVPFDVVTMEQAAEKIKGFLCEKGQHIVCTPNPEIVMEAQNDDKLMNILKAADLVVPDGIGVVWASKYSEKKLTERVAGYDLVQKLFDEIKDTEHTVYFFGGAPGVSLAAAKKMEQKYANLKIVGGHNGYFDEKEEKRILNDIKKLSPSILLVGLGSPKQEKWIYENIRLTNVKVAIGVGGSFDVMSGKIKRAPDIFCKMGLEWFYRLITQPSRIVRMMKLPKFAFTVLKNRK | Pathway: Cell wall biogenesis; teichoic acid biosynthesis.
Function: Catalyzes the conversion of GlcNAc-PP-undecaprenol into ManNAc-GlcNAc-PP-undecaprenol, the first committed lipid intermediate in the de novo synthesis of teichoic acid.
EC: 2.4.1.187
Catalytic Activity: N-acetyl-alpha-D-glucosaminyl-di-trans,octa-cis-undecaprenyl diphosphate + UDP-N-acetyl-alpha-D-mannosamine = H(+) + N-acetyl-beta-D-mannosaminyl-(1->4)-N-acetyl-alpha-D-glucosaminyl di-trans,octa-cis-undecaprenyl diphosphate + UDP
Sequence Length: 241
Sequence Mass (Da): 27170
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A0A7R9QZ14 | MTETKMNSAICETEQVHHVKTPYKRELVWRNIILMTILHLSALYGFYLAITAVQFKTIIFFNFIAFFSSFGIQCGAHRLWCHRTFKAKLPLQVILMVLQTMSLQNDIFEWSRDHRLHHKYSDTDADPHNSSRGFFFSHVGWLLCK | Subcellular Location: Membrane
Sequence Length: 145
Domain: The histidine box domains are involved in binding the catalytic metal ions.
Sequence Mass (Da): 17111
Location Topology: Multi-pass membrane protein
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A0A8C5ME75 | MDVPHAVTPATSASSLCFISKELILQEGHFAMKRLDPGTSLCAALLAGLVLCVLMAEALGGEVCYETLGCFTDDKPYSGTPQRPKAALPWTPKKIGARFLLFTPENPTKHQVIRADSIASIESSNFKTTRKTCIIIHGMADKAEDSWVSKMCNEIVTMDDVNCIGVDWRRGSGNIAIYVQAANNARLVGAVVAHFLKIIQENINSSYSGSSIHLIGHSLGAHAAGETGKRYSGIWKITALVDILACNHLRAIHYYTASIRHPGGFLAYPCDSYKAFKEGSCFPCPAPGCPLMGYFSNSSHSVTSPQSYYLHTSTKLNGHPSWRYKLSVTLRGTSGIQGALQAVVHSEEGIVEECDALTGDFFPGNIYSSFLDVGFEVISVTRVTFSWSLSHFNLFQHTLGAARIDFQRGRDGNISSFCTDGTVPEHVIQTLLPC | Catalytic Activity: a triacylglycerol + H2O = a diacylglycerol + a fatty acid + H(+)
EC: 3.1.1.3
Subcellular Location: Secreted
Sequence Length: 434
Sequence Mass (Da): 47137
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A0A6J5S951 | MNRSIVAVLWALGIFAAIHLTDKYTHIEENIMAIAKSTLSFITKEEGVRYRAYQDSKGLWTIGVGHLIKSSEPHLMTATLTQEEVDKLLESDLRWCDDAVASSVRVPLAQPQYDALYSLCFNIGETQFKKSTVVKKLNANDYQGAADAILLWNKPAVLEKRRKRERDLFLSAI | Function: Endolysin with lysozyme activity that degrades host peptidoglycans and participates with the holin and spanin proteins in the sequential events which lead to the programmed host cell lysis releasing the mature viral particles. Once the holin has permeabilized the host cell membrane, the endolysin can reach the periplasm and break down the peptidoglycan layer.
Catalytic Activity: Hydrolysis of (1->4)-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrins.
EC: 3.2.1.17
Subcellular Location: Host cytoplasm
Sequence Length: 173
Sequence Mass (Da): 19558
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N1ZPF3 | MEKFMMIDGNSIANRAYYGVPLLTNSQGTYTNAIYGFINILFKLLEEEKPDYLAVAFDLHSPTFRHKLSEQYKSNRKGMPKELREQMPLLKQILTAMQIKQYEIEGYEADDILGTLSLKAEQNNMQAVIISGDRDLLQLASDTLKIRIPKTKAGKTEIEDYFAQDVLQKYGVTPTEFIDVKALMGDASDNVAGVPSIGEKTAIKIIQQYHTIENAIQYVDDIKPKKASENLKAYYEQAMLSKTLVTIVRDIDITIDKNTLGIKNMFNEQVYAIMKQLEFKTFLYRFTQNKTQSILKNEISYQTITEPSQYDTVFHALQKNKQIAYIILHENDIIRGISLYDGGEQCYFLLCQNHQNMVYLLNSAKDFFENKCYSKIAHNAKTDMVLLRQYDIELSDVIFDASIAAYILNSTKDSYEYDDIAKEFLNEIYPCKEELLGKGKSKISLLELQQQQLTQFACNQSEVIYKAMPILLQKIKDNNQQQLYFEIELPLIRVLADMQKYGIKVNKTALQQYGAELEKSIEILTLEIYTMAGIKFNINSPKQLGEILFSTKHMALSGGKKTKTGYSTAADVLEKLSNSHPIIPKILYYRQLSKLKSTYVDGLLSVLDEKTQKIYSTFHQTVTATGRISSTEPNLQNIPIRLDLGRQLRKVFIPTDENYCFLDGDYSQIELRVLAHMAQDKTLIDAFVNGQDIHTITASQVFNVPFDQVTEIQRRNAKAVNFGIIYGIGAFRLSQELNITIKQAENYIAGYFSKYPNIKKYMDKTVLDAQKNGYVKTLFQRRRAMPELHSKTFVQRSFGERVAMNMPIQGTAADIIKIAMIQVHKKLLENGLHARLILQVHDELLLEVHKQHASEAAQLLKQTMEQAVNLSVPMFVEVHQGNSWFETK | Function: In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity.
EC: 2.7.7.7
Catalytic Activity: a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)
Sequence Length: 888
Sequence Mass (Da): 101623
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A2SNS9 | MSDDPRIGRLIGVSLGPGDPGLITRTAWALLERRDTVWAYPARSTKTPSYAFDIVQRAGLLPPTEHHCLLFPMTHDGEKLGRAWLRAAETVLPRLQAGRDVLFLVEGDASTYATFGHLARTVRSLDGRIEVQTVAGVNAFTAACATLGQPLSEQDDTVAIVPAAYGVAALDRLLADFDTLVLLKVKPLVDELFDWLQARDLLDGASFIERCGAPDERVLRGAEMLALRGSKVSYLSLMLVPNPYRVRGERIKGCLKKTSPMSAPAGPMEIEIEL | Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis.
Function: Methylates precorrin-2 at the C-20 position to produce precorrin-3A.
EC: 2.1.1.130
Catalytic Activity: precorrin-2 + S-adenosyl-L-methionine = H(+) + precorrin-3A + S-adenosyl-L-homocysteine
Sequence Length: 274
Sequence Mass (Da): 29878
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A0A977JKF0 | TLYIIFGAWSGMVGTSLSLLIRAELSNPGSLIGDDQIYNVIITAHAFIMIFFMVMPIMIG | Pathway: Energy metabolism; oxidative phosphorylation.
Catalytic Activity: 4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-[cytochrome c] + 4 H(+)(out) + 2 H2O
Subcellular Location: Mitochondrion inner membrane
Sequence Length: 60
Sequence Mass (Da): 6565
Location Topology: Multi-pass membrane protein
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A0A1A9AWA3 | MDWLSGNIMQFWASFLWPFARISSMLMTMTAIGAAFVPARVRLLLAVAVTLASLPSIPAMPQGIELFSLHSALITAQQILIGVAIGMISQFLTQIFVMLGQVVSMQSSLGFASMVDPASGQNTPLLGQIYMMLTLLVFLLLDGHLIMIEMLVRSFTTLPVGETGITAGGYHLLSQWFGILFLGSVSMSLSAIISLLTVNIAMGIMNRAAPQLNVYSLGFGLILLCGLFSLWYLLSAFPRHYDIYWRVALDDMCTLLHMTCGDGL | Function: Role in flagellar biosynthesis.
Subcellular Location: Cell membrane
Sequence Length: 264
Sequence Mass (Da): 28780
Location Topology: Multi-pass membrane protein
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A0A977JJ44 | TLYFIFGSWAGMVGTSLSLLIRAESGNAGSLIGDDQIYNVIVTAHAFVMFFFMVMPIVIG | Pathway: Energy metabolism; oxidative phosphorylation.
Catalytic Activity: 4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-[cytochrome c] + 4 H(+)(out) + 2 H2O
Subcellular Location: Mitochondrion inner membrane
Sequence Length: 60
Sequence Mass (Da): 6491
Location Topology: Multi-pass membrane protein
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A0A7R9MD55 | VVIIFSGKELPNDLRLSDCDLGHNSVIHAINALNIKTKTKLLPFSDQLTLNQKLTNLDMNDTNEETRHELEDRNRLSRRVTTDEDKSAQKYYFFVFCNSCEQLMNGKLRVVCDKCKNGTIVVDREPREWHDVLTPNRITGVCQSQDCNGTIAQFYFKCAANTHNSAADDDRTTGADAVDRSRAVVLPLIRHNCIGVSCLACTDVKDTVLVFPCAAKHVICLHCFRDYCLSKLNERRFVTDPQIGYSVNCAVGCHESLIRETHHFKLMGQIAYEKYQRFGAEECVLSAGGVLCPQPGCGAGILLDETEPEFCTRITCSECTFVFCRKCLQGYHVDDCVSDADNGVSEPNTSAFQAMSAANADHSKWDDMMTRTAIRLSTKPCPKCRTPTERSGGCMHMVCTRSQCGFNWCWICQTEWNRDCMGNHWFG | Pathway: Protein modification; protein ubiquitination.
Function: Functions within a multiprotein E3 ubiquitin ligase complex, catalyzing the covalent attachment of ubiquitin moieties onto substrate proteins.
Catalytic Activity: [E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-N(6)-ubiquitinyl-L-lysine.
EC: 2.3.2.31
Subcellular Location: Cytoplasm
Sequence Length: 427
Sequence Mass (Da): 48019
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A0A352W9N1 | MASVCRRWRESSVIACGRPAPLPGSTYNIAVAFGEGEGILTSDCVRLRNLAFYGYHGPFGAEKELGQRLEVDLELRMNLEKAARSDEPEFSTNYAEVYALVREVIEENNFCLLESIAQTIINRILDHFDVEGARVLVRKPLAPIGGLLDSVEVEIYREHPRR | Pathway: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate from 7,8-dihydroneopterin triphosphate: step 3/4.
Function: Catalyzes the conversion of 7,8-dihydroneopterin to 6-hydroxymethyl-7,8-dihydropterin.
EC: 4.1.2.25
Catalytic Activity: 7,8-dihydroneopterin = 6-hydroxymethyl-7,8-dihydropterin + glycolaldehyde
Sequence Length: 162
Sequence Mass (Da): 18224
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A0A7R9MCM4 | GLYDEVVVKYEIDYSAGGSVQNALRYAQWVVGKNNPIANYIGAVGDDYFGKYLANKVKVDGLNVKYMVVDDKPTGACTVLFNNNGKYKSVCANLGASTCFDKHFLMNNFWFCERARVILTSGHLLPVSPDSVMYLAKHCHEWGKDFLLIISYRFLRPIPIGASYVIHNSTNYVMDLFPYIDFLFCSADEALAFATVKGYHTRDLKQVVKLMADEPKVSYNNPNIPNNYKSGRVVVVNQRGGKPVLLAKTDVFNTKEYPVPIMTDTEIIDTSGMGDALIGGFLAMYIDGRPFDVCVQCGIYCATECCRQSGCILPEKMKFKY | Cofactor: Binds 3 Mg(2+) ions per subunit.
Pathway: Purine metabolism; AMP biosynthesis via salvage pathway; AMP from adenosine: step 1/1.
Function: ATP dependent phosphorylation of adenosine and other related nucleoside analogs to monophosphate derivatives.
EC: 2.7.1.20
Subcellular Location: Nucleus
Catalytic Activity: adenosine + ATP = ADP + AMP + H(+)
Sequence Length: 321
Sequence Mass (Da): 35903
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A0A497R2X3 | MHPIIKERLKKQGYQLYGKQVAVKKCLWTHKYLKEEQYCYKNAYGIESHRCIQATPTLLCTHQCTFCWRLQEKDVGLKPVWNVPDSEFDSPEEVYKGLLWGWKRAISGYKPIVPKELFDQAMDPQHVALSLAGEPTLYPFLTELLELLHAKGLSTFLVSNGTMPESISKMITTGVRPTQLYITIPAPNKKDYLHVCKPIIQNGWDRLNKSLELLGKLGGRTVTRLTMAKELNMKNPVEYVALIKKAHPAFIEIKGYVHVGFSQYRVTRGNMPFHEEIRAFANKILEGLPEYKLVYEMEDSKVVILSNDKQPLKIDFQKIGKKEEELTKKS | Cofactor: Binds 2 [4Fe-4S] clusters. Binds 1 [4Fe-4S] cluster coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Component of the wyosine derivatives biosynthesis pathway that catalyzes the condensation of N-methylguanine with 2 carbon atoms from pyruvate to form the tricyclic 4-demethylwyosine (imG-14) on guanosine-37 of tRNA(Phe).
EC: 4.1.3.44
Catalytic Activity: N(1)-methylguanosine(37) in tRNA(Phe) + pyruvate + S-adenosyl-L-methionine = 4-demethylwyosine(37) in tRNA(Phe) + 5'-deoxyadenosine + CO2 + H2O + L-methionine
Subcellular Location: Cytoplasm
Sequence Length: 330
Sequence Mass (Da): 37999
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A0A2V6UMY5 | MDSCPPPTQRSCRRSITHSGGGCAPAAAQRRARNGASASGPTTPAIYSPFGAIFPRRRWVSGYVPVAVFGVLIIAFGVVSLAVAWLLRPSRPDIVKLMNYECGAEPIGPAWVRFPVGFYLVALVFIVFDALAVFLVPWLLVLEPLGLPAFWGMAGFVGIIALGWLYAYREGVLEWK | Function: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. 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: 176
Sequence Mass (Da): 19081
Location Topology: Multi-pass membrane protein
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