ids stringlengths 6 10 | seqs stringlengths 16 1.02k | texts stringlengths 117 4.4k |
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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... |
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-riba... |
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 | MYARYVPPARDKASSAEATQSTAAPSTGATTPQAQAPYARYTPSLPKPQPATAVLGATPQPRKIVFNYGDDGPAATPTPKSKLTPYNSSVVGGEDDEPRRKKAKHPAKPDETSDKAPNSAKSKRKPVKDGVKDGGEEPSRLKEKKKRKSEPKDYAAQIEEDARSPKPEKRERKNKKERAKLADQGDGDGDVKMRDQPDVEEDEADTDPVDSRHKSVLKKKELALRRARNAPVEADEPDGPLAHLEHDGSGVHGLEPLPQPAFAVLDTSEPTYDTLPPWLGNPIHVSQSTRADWTTLGLKPELGISTEIASFLESKGYEKA... | 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)-pant... |
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... |
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 transp... |
J3NXP3 | MGAFASIWQTVAYVVSFWYIKLFGWWRSQPPKALWMARLRNATTYEDWEAAALQLDKLHGFDLWREMSQSKHYDWALIKDRLQLLHDTRVDPTQHHRLPNLIRSGLVRNLGNITSPKLYNCSFAGTKLIIEEYIAQVIFAIDDFLAAPITATATSPSRQQPTSPAVDEESCDQPTDDQPSRAPGAAAVSTGGHAASANAAAPRPAPTSPALSMQAKMTFIHDTRQAFGRTSLILQGGSIFGMCHLGVVKALFLRGLLPQVITGTAVGALIAALIAVHTDEELPGVLSGEAIDLSAFTPTSGKSTPPAADADSSSSVAGSI... | 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 L... |
A0A0B6CY85 | MEHLKKFFYVFLAHIYSSIFITLIPILYLKKFKRSFKNINYRKRWAERFAQIPIRLNSSIWIHSVSVGEAVSAEPLVKELLKNFPNENFVITTTTPTGSDVVNSLYSNYPNVHHMYIPYDVIPFINSFFAKTNPKIFIIVETEIWPNILNKCFAEKVPVVITNARLSKKSMRNYTKIPFAKEFLFKNISHINAQTEKDAKRFYSLAVDKNNISVTGNLKYNLITPENLENKMYSLKDSLKGRPVWIAGSTHQGEEEIILEAHKQILKIHTDCLLILVPRHKERFQKVEKLIVYNSLKYQKRSSFECQIFSDTQVYLGDTM... | 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... |
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 menaquino... |
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 | MGKKLLRNYDYVLLLTIVLISAFGVIMVGSSSVSGEISISALFSNRTFVKQLVWAVGGLVGMALLSFIDYSEWQRLKLPIYFFSLALLILVIFKGTSAGGAQRWIAIGKLFNLQPSELAKIAIIITLSATMAKEGRSLERWSGLIVPLLHVAVPMLVIFLQPDLGTSLIFMAITGAILFVAGMRWLHLAVMGVGGIIGSVLAFLFVLKPYQKSRLIIFRDPWQDPFDDGWQIIQSKVAVGSGQFRGRGLFKGTQTQLDFLPEKNTDFIFSVIGEELGFLGASIFLLVYVFLIWRVLKVAMEAKDSFGRYLCVGVAAMLSF... | 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-... |
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-cytochrom... |
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 i... |
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 | MTRQPEGPDRYDGCGRSSAEVSIERKVYSVTEIVSLVRELLETGIGDVCVEGEISNLRLPSSGHMYFTLKDASSQLRVAMFRFRRKELSFQPADGLLVRVWGRVTMYEKQGECQLVAEGMEQGGKGALQAQFEALKKKLQAEGLFDGARKKPLPVLPATVGIVTSPTGAAIRDMLKILSSERLRIVIVPVRVQGDGAAAEIAGAVRMLNEWREADVIIVGRGGGSIEDLWPFNEEAVARAIAGSAIPVISAVGHEVDVTISDLVADVRAATPSVAAEMIVGAREARRMETAEMGARMARLVEQDVLRLRNRLISAAASPV... | 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... |
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... |
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... |
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: malony... |
A0A7I8XC14 | MELDNCNMFLFMQKWMTDGPSKFTLPQLQENPGGWGPAPLESSEPMKQFINMPFQLFNKCDRVGRIVDWLGVDRYKKSDTRERYNERMYGSSQNAGSQFDYVHDNEESNFQLVDSSKPQKPARPYRRTQLPFRKLLQKEQERRDQQFYNQSNKTKRSIAKEQNRAYKLWQRRGGMRNGQPSRGMAGRRYGDRQGGKGRQPSVQVRPDWKILWDLDFQRLAKLSLPNIEGQDIKGENYGILYYYDKALEKVTVKNAVPLQRCGGIFYNTTTTEDPVIMKLAQKNEGNVFATDIILATLMASQRSVYSWDIVAHRVADKLFL... | 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 specifica... |
A0A212EK03 | MVPTSNYTPVSDFYNGKTIFVTGGTGFLGKVLIEKLLYSCPGISKIYMLVREKRNLTATDRMKKFFDCPVFDRLKKEKPENLKKLKPVNGDLSQPCLGIDPKELQVIKDEVTIVFHFAATVKFNEPLSIAMKINVEGTEQVIDLCHSLKKIEVFVYMSTIFSNTDDKLNSVEERLYRSPKEVDEIYKMIKENDPREVFNPEVLDGRPNTYTFTKAVAENIVAQKRGNLPTIMIRPSVVTPAKEEPVRGWVANWMGPTATLLYLSRGWIRCHYGEDDFTFEIIPVDYVVNLTIISAAKFKRSDDIPIYHSCTSALHPVTFK... | 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 | MNVTKKINVPQLIFKYSKRLVSEANFTIQEPFRLHRLEKGPLTKVTLTKQDALTYYKKMSTIRRVENTSANLYMEKVIRGFCHLYAGQEAVAVGIQATMRPDDCLITAYRAHGWVLLMGGSPEQILGELCGRVIGCSRGKGGSMHTYAKNFFGGNGIVGAQIPMGTGIGLMMKLTGKPNVSFALYGDGAANQGQVFEAYNLAKLWNLPVIFVCENNKYGMGTSAERASAVPEFYTRGDYIPGIQVDGMDVLATREASLFAIAHCISNRGPILLEMVTYRYYGHSMSDPGTSYRSRNEVQDIRKNKDPITLFKDKILGANL... | 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 acetyltr... |
J3PDZ3 | MLRPALSLLVLALSSAGAAVSSSGSRLLVVLDDVADKDKYSKFLGDLTSRGFDITYSTPKAESLQLFRLGQRTYDHAIFFPTKVKGLGPNLTPNTLLQFVKENGNILLALSSEMAASSSIVSLLHELEIQLPAERTGLVVDHFNYDAASAPDLHDVVLVPAPAPVRPGVADVFAAPGEERLLAFPRGVAQTLGQSPLLNPVLRGPRTAYSYDPKEQGDSVDPDQLFAAGQQLSLVSAAQARNSARVAVVGSAEMLADKWFDAKVKPAGGAKDEVATYNREFASRISAWAFQELGVLRVNWIEHHLNEAGASNASNPSIYR... | 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 m... |
A0A0H3J1E1 | MSTVKLTTAQALVKFLNSQYISVDGKESFFVEGVFAIFGHGNVLGLGQALEENPGNLKVHQGRNEQGMAQAAIAFAKQSRRKKIYACTSSVGPGAANMITAAATATANNIPVLLLPGDTFSTRQPDPVLQQIEQTYSAAVTTNDAFKPVCKYWDRVVRPEQLMSAMLNAMRVLTNEGDTGAVCIALPQDVQGEAYDFPEYFFQKRVHRIERRCGTKEEINDAVELILKKKKPLIICGGGAKYSEAGEELKKFAQEFNIPICETQAGKSALESTFLLNLGGVGVTGNLAANLIASDADLIIGVGTRFTDFTSGSKGQFRNS... | 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 A... |
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 catalyz... |
A0A942EJM3 | MATALKDTSGYLSSEDNSRANLATLSTLQNTRMRLLQNIEEISKRLAGDSPPTNPGFFETRMISMRSEISLLDTKIQGLQKVIASLDSKLELPSPKSKSHEETLLLGLRKTRSEITLLQKAIKNLQALSETETRKGRAILDNLISEIPSLASQLTDIEGDPKSTLPSLKSSELTLQQNYDTFKKALSPYFVNKSQNFTQKVESDEFNYKTLNALYESLEPEVKELVHYTPNLFYGRGLNTRLYDERGAQLQPNGSVRFSVFAPNAKDMTLCLTSIGDDELEEPLRFPMESDPITGVWTTIVGSFEDATFKGSRYHYELTT... | 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... |
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(+) +... |
A0A9J7H5K8 | MAEAVFRAPKRKRRVYERYESPLPIPFGQDQGPRKEFRIFRAEMISNNVVVRDAEDMEQLYGKLTAEAFVHSVQDGMRLVICWGYFGKGILSRSRPNFTISNPKLAARWKGVQTDMPIITSEKYQHRVEWAMDFMRRQGQEESTVQKILTDYTEPLELPCRKGKEEVPQHDPLNSEANSTLEGRVGKDELSVTTGGAGQSDDLQGLNTHSDCLQEGPGQATLTVASPSSFNGHVIEDTTVLPQVPCRIAQDGLWPEDSSQAAGEKRAAHEYVLVEEELCDVQEEDEAPDEKLLQRKRLVCRRNPYRIFEYLQLSLEEAFF... | 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 bearin... |
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-met... |
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-cytoc... |
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 prot... |
A0A7R9QME6 | MDQFTLLMLLSFSMLFGSYFSGTIPLVFTFSEDKLRLLSVLGSGILVGTALSVILPEGVNTLYTSSHEFHSHLKTISTQKTTNETTKSEDNPHSVIVLHLKTISTQKTTNETTKSEDNPHSVIGLTLVIGFVLMLLIDQFSNRHTGANSYSVALQSDSAENGESLSTCVPKRSSKMTATIGLVVHSAADGIALGAAATTSHTDVEMIVFLAIMLHKAPAAFGLVTFLMHEGVERSRLRKHLLAFALSAPIAAFITFFGISQGTKEALSDYNATGIAMLFSAGTFLYVATVHVLPEITQHQHLNLKELLALVGGTFIPSLL... | 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 | MIVGIRRNLRLQNKKLKMGLISLGCAKNLVDSEVILGFFEQADFTRTTNPEEADILVVNTCGFIEAAKQESIDAILEMAQYKDRGRCRVLAVAGCLSRRYADELTQEIPEIDVLVGVAEYPLLPDLVKKALNGGKHSLVQQCGFIYNENMPRVLATPPFMAYVKIAEGCANRCSYCAIPLIRGPLNSRPIASITAEVRQLCAKGVAEINVIAQDTTAYGLDLYGKPSLADLLEQLVAIPDVQWLRVLYAYPNLIDDRLLEVFATHPQICRYLDLPLQHADSELLSAMRRRGRPEQYLDLLGKIRAAVPGIALRSSFIVGF... | 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 uS1... |
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-... |
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-p... |
A0A8J8CEP1 | MDFKTEKLRGFRDFLPEDMKIRNYVRKAIEKKFKLYGFDEILTPTVEYTGIFTLKSGEEITESMFAFKDKGNRDVCLKPEQTVSTARFFIENFKNFAMPLKFYYFCPVFRYDEPQHARYREFWHLGVELIGSNTPESDAEVISLAYCGLKQLNLNFELELSNIKVIKGVLNSTNLSRGDKEKILHYIDKHNDEGINEILKRTDNGEILNKVLSFKGKRGNLNELKNIVRNCPEAIEGIEELENILNFVEMFNNDYVINFNIVRGLDYYTSNVFEIHANDMQICGGGRYDNLIGLFSDKDSKNDKNKGVPAVGFAYGFDRV... | 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... |
Q6F3N5 | FACDVSEDLLLGTSEKIVKWGLKDLGYNYVILDDCWSEGRNSSDYLIPDSKKFPRGMKHVADSLHDEGLLFGMYSSAGEYTCAGYPGSLGHEEADAASFASWDVDYLKYDNCYNQGNYGTAQLSYERYKAMSDALNKTGRPIYYTLCNWGEDSPWHWASAIANSWRISGDIYADFDRPDSRCPCNGDEYYCHLAGFHCSIMNILNKAAPLGQKAGPGGWNDLDALEVGVGNMTDEEEKTHFSMWAAVKSPLVIGANLNTLDAKSFSIYVNPAIIAVNQDAAGAPVMRVWRYYVSDTDEHGQGEIQLWSGPLDNGDQIVAL... | 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 | MLRSDDSNTISKSAVIFRCIDYILCLEKHLSFLMIMMTWLLFVTKLGPMFMKNRKPFVLREIIMVYNLILVLTNAYYIYASLKWLEFGRKSLDPKLPGYCTDGYIYYWIYEYWEQGIDTRTRGYFLVDMSPLTLCCILAMYIIHVKLLIPYLMKNRKPFDLKKIIIGYDVLLVAINAYFWFYSLAHITDMWDFKKELASHVGWLLCRKHPEVLEKGKTIDMSDLDRDPLIKFQRRFYIPLVALIWGAFPTYVPYYLWGESLWNSYFLCVMFRYALILNITWCVNSAAHLWGKKPYDKSINPVECVIRHVMFGEGFHNYHH... | 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 | MKNLIILGLLGYLSIAFADKETLVLVDNLNIRETHSLFFKSLQERGYSLTFKLADDANLVLSKYGEYLYKNLVVFAPSVVEFGGQLDTEAITRFIDDGGNVLIAGSSAAGDVYREIASECGFEMDEESAAVIDHFNYDSLDEGDHTRIVVSPKNLIDAPTIVGTHNTQPLLFDGTGLILDKDNSLVLPILTADSTAYSYNPKNQVKEYPHAVGRKTVLIAALQARNNARIVFSGSLFFFSDEAFNSPVSKVHGDKIKSALSGNKQLSIHLSQWVFGERGQLRVQSVHHQRQGDKKSSNTYTITDTVVYRIEIEELKNGKW... | 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 m... |
A0A7R9QXR6 | MQTFSCLNRIQWPSLVFLVLCLMNAIHCRELSYVVNPGCDQSCEQWTAAKKSLNLVHISSKDTSDTIHFLWSSITSIPPTLLIVKTPSDATLTIDYAKLLQTKSTSPDGGISFSKEPLNAIGVQFSRLFFFNDINKSGSYDEKDPIFEVMWKDFHWTPVANGSAKDSIELHLKNSDEIETNESAIKGTIEFVLRVDSSDGRGEELPHLAFTDNSVSLSLNVMDVEYDKTEAFNKSLHDQILPRVMTSIFVINDIKDNTTKSDPSIETLTSIDDEYTPGAFDLIHMKVDSNKGSKSENENKAFIQWKPIAYNSDDRIIANT... | 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 | MVDYPLETVVEGKTKILVPDVEAFRKSPSSYPPSDAPVFYNKVMELNRDFALATLRVYIDLLSKKESLFYCEPMAGSGIRAVRIANELENISVVINDRNPHAVELIKENVKQLKLTEKTSVHMDDACELMIRHAASGNRFDVIDVDPFGSPSVFMDSAAQALGYNGFLAVTSTDMATMCGVYPKACIRKYASKPIHSSIGHEVAVRMLIGFIATNLARHGKGTKPIFAHSTEHYIRAYVVAEKGITKAKESMNTLGYIAHCLKCYAIESRKGLINSLTKECPDCQNKHRLLGGPVWLGDLYDEQFVNKLKSEVEDNKTNY... | 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... |
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 acyltran... |
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... |
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-cytoc... |
A0A0C4F041 | MQGVLCYSPGTIQSAAEVIRSEDVVAFPTETVYGLGASALSSTAVSKIFRAKGRPSDNPLIVHVCSLDLLKTFLPPDWAFPATYEALIERFWPGPLTLLVPTTSPAQPTSPISSLVTCGLPTVAVRMPAHPISRALIAASGVPIAAPSANLSGRPSPTTAEHVARDMKTKISMILDGGPCQVGVESTVVDGLNPDGRLRILRLGGLSVEDIEACLIGAGLSHCDGTPILAGVYNRDYRDKELEVKPTTPGMKYKHYAPHAKVVILDPVSPPSSSTDGHQSLSGVNELVSGLCGDNSDSSKGLRIGLMLIDDSQLHKSFIR... | 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 Len... |
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
S... |
A0A354HQD1 | MKVIPKIPLLVIAGPTASGKSAAAVELAQIFDGEIVSADSMQVYKYMDIGTAKVDLATRAQVPHHMLDVVEPDEDFSLAQYKEQADKIIQDIWRRQHLPILTGGTGLYIKAVTENYPLQQLPFDPHCRAELNRLWDERGREYMVSRLQQVDPETAAKANDRRRIIRALEIYQLTGRGPAEIHRQAKAESPFNALIFALTLPRPQLYECIEARAEAMVIQGLIGEYIKLIERGYSPAAKAMQGLGYYHAGMCVAGNWTREEMIANLQRDTRRYAKRQLSWFRGMQDVIWLDHSNPQASMEKISAETAGKLQLYSELVINID... | 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)-dimethylall... |
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(+)
Sequ... |
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 s... |
A0A212FH64 | MVWPTEFDVKLDEYDAMDLPGQQLQSAQASTTLDHILNLNISAPAGCQRLTGIISFMGKSTYDVEVMQKMIAAGMNIALLNLSFGNKEEHMETIKNLREAVKNYSVKCGKKYPLAIGARLPGRKIRTGCIADTFGETVELKTGEVVRLTTDETYRDRCSNYTVYIDFMHFAEQMDKGNLVLLDNETIKLKVEMISATTLTCKIERGGFLGSYKDVFVPNVTFDMPNYSEHDKEYIDMAIHMQLDILVASFVNSSNTITELRLLMGEKGKKIAIVANIQTIQGFHNFDDILSAASGIMITRQELGSDITPKKLVIAQKNMI... | 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-cytoc... |
A0JC78 | MTTQGSRPTGDVVVQKYGGSSLATVSQVRQVADRVGALARSGRRVVVVVSAQGDTTDELVGRAEAVNPRPAGHELDQLLATGETASAALMAMALQRGGLAATALSGARSGVLATGPHGAGVIVAVDTDQLRTLLDAGRTVVLAGFQGVTAEGDIITLGRGGSDTTAVAVAAELRSGHCEIYSDVPGVFTADPRVVPDARLMPDIDIDVMTEMAFAGARVMHARAVELAALYDVDILVGRSTATRTGTRIHRRDGNDMLEDRTAVSAVVHDADIARITLRTHDTPDPSADVFRFLAKESIPADMTTVSSAPDGGFSLGFTV... | 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 t... |
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-cytoc... |
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 To... |
A0A2P6N0M2 | MGKESEHQGSDYAEYYTGQDGREYTNQPAPVMHQTYARHYDEESPINNRNSDDKFKPANHRRDPAWTIVFLVHLVAFFVLFVFAAVKYQAVMKDQQTTNTGNNTGNNEPYSDSTNLRKLLFSCMGMVALSLIFAGVWLQVIKTFATQIIYITLVLSSALWIAFSIYLFSIHSIFGGIITLLAALLHIFLWFSWRSRIPFASLMLRTVSGVTQRYHGMTVISYLSLFVSIFWIVLWVLTVIFLDQGLSSKVVDQNGQSHIERPTAVYVLYVFLLLSFYWVAQVIKNVVHVTTSGTVASWYFLYGTEAMPVNPSIASFKRAT... | 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 | MEGRIPPHNLEAEQSVLGAILLDSDVLDELEGLLPSPEAFYAEAHRKIYAAMQTLRSQGKPVDLVTLAEELSRRGELEALGGVSYLVQLSEATPTAAYAEHYARIVAEKWTLRKLIQAAGEAMRLAYEEAGSLDEILDTAGKKILEVALTQTETEARSIRELVHETFEHIEALFQNKGEVSGVRTGFKELDQLIGTLAPGSLNIIAARPAMGKTAFALTIAQHAALKEGIGVGIYSLEMPASQLTLRLMCSEARIDMNRVRLGQLTDRDFSRLVDVAGRLSEAPIYIDDTPDLTLMELRARARRLRSQYEVGLLIIDYLQ... | 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 | MENVGQFAVTISREGDLKPTVCVDFKTEDGTANAGSDYEPIEGTIIFRPNEMHKQVFITVIDDDLFEEDEHFYVRLSNPRYLSHDGCTPMNGAISNTNKSPPLLQLATPAIATVMILDDDHSGVYSFAESQYEVSESVGEYHLKVNRFSGARGKVSVPYHTCEGTAKHGVEFEMTEGVVFFDNNQTSQEIVIHIMDAESYEKDAVFYVELGEPVREEDSIEEFDDQKDPNHQSFDEKIALLGKPKLGEIYKCSVRIKESKEFKNTVDKLISKANTKILMGTSSWRDQFIDAITVSAGDDDNADEDGEEGEREEKLPTCSD... | 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)-dimethylall... |
J3NY35 | MSPPFPVIYLLSTHLNTDRLRALEAQITTITYNAQEAEVVLGNISKKQRAMFELRRLGLWTSEVPTSNVATEPPKKRPRHTSSANNNDEAWLLGSQPVGTDNQGIRGTVPGSGKVTVVKLTWFTESTKLGQVLPFGDHLLYEGIKLAGSYEVNDPRSPPSNLPPIPQRSRSGVVGASSQQPTAKTSTATHRSSQVPSLLRQSTSEHEAARHMPTMPDFLRTVYSCQRPTPIHPPNEAFINQLAKIKTTRLLAGDRIGVRAYSSAMASLAAYPYVLASPEEVDRLPNCGPKFAVLFQEFQRQGGVIREAQEAELDPKLSVI... | 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... |
A0A353N5T5 | MWERKYFKNIDYYLLGSVLLLVLIGLVMIYSATRNNQALTGGEPFMLVKKQLVAVIIGVLGMILIMFSDYRLPDLMYQIIYGFNLFLLLIVLSPLGLEIKGAKSWLNVGGPFSLQPSEFAKLMMILTLAKHLAGKEEIDSFWDLWSPFFHIMPPLILILIQPDLGTTLVFFFFFFIMLYIAGYNGRFLLGLILTGVIILTLIFLSHYYFGTPLPFKEYQIRRMTIFLNPESDPTGSGWNVRQAIITVGSGRFSGKGLFQGTQGRLGFLPENHTDFIFAILCEEWGFLGGFVLLSLYFTMIWRCLVITQHSKDKYGTLVAA... | 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-... |
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
|
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 Topolo... |
A0A212ENP8 | MRWKCKSSKGRWLYVLLMLIVLPVVVAQKIGDPYKILGINQRATLPEIRKAYRQLAKEWHPDKNENPNAEARFVEIKQAYELLSDTERRQAYDLYGITNEDDHMYKQRHDYSQYARFSNDPFEFFSTHFRAQDQDITLFHKLSVTTRHFENNILEKSVHTPALVLFYTDWCFDCVRSAASWRKLVDSLQPLGVTLATIHAGHEASLARRIGVHSVPCLTLILDKQIYIYKDGLNSLPKILEFMRWKFPYKLVRGINDGNVDSFVTDFEDNKVKALIFEERQTIRLRYLITAFHYRDRLSFAFVDISARDTANVTSRYKVQ... | 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
|
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... |
A0A481RL18 | MGIRRHAIPRPTTSTYHVKSDNMDAWSISPKDLKPIGVAAADQQKQQQLQLQQQPLGPKKLTSDDLKKGPDTGSGGGGGSKSDVFHTLAPVYHLSKICGLLPVKFKANKAGKYEGRLDVAEVAYGIVLVAALAGAQCYGLYRDLRNGWENSTRLSSETAITVTCSDVFAVISAAFVAILGSGYRWHHLQDALNKIVDVDDKLLDVPTSERLRKVSIIVIVSSLVYIVVISSLDFVSWRASSAGKNNAHFGDKGPINYAPLYFMYIVVTVFEVQYALVLFNVGERFLKLNKSVANLTRSNMALEQLFRRYTHQPHHQQQQE... | 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 | MTQNKNIIVLGAAESGVGAAVLAKVQGYNVFVSDIGSIKEEYKKELIENEILFEENNHTVEKILSAGEVIKSPGVPDNASIIRKIKAEEIPIISEIEFAGRFTDAKMICITGTNGKTTTTLLTHFILKNAGLNVGLAGNVGHSLAMQVAKKNHDYYVIELSSFQLDYMFEFRANIAVLLNITPDHLDRYDYKIENYINSKFRITQNQTSEDAFIYCADDEILNKEITNKTIQAQSYPFSIEKEEGMTAYLNSNQLTINTQTKPLTMTIYDLALQGKHNLYNSMAAGISSKILDIKNEEIRQSFSDFKNIEHRLELVNTIH... | 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-... |
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
|
A0A256GHE0 | MTTPLVEIRNLSINFQRDDQLVKVVEGINLTIHPGETVALVGESGSGKSVTARALIGLSGPSAIVKADLFEIDGLSVLDYRDKEWRGLRGNKIGFVLQDALVSLDPLRRISQQLSDAFGVKGFFRRPDVTDRSKALLRSVGIPDPDRRLLQYPHQLSGGLRQRALIATAVARSPSLLIADEPTTALDATVQKQILDLLAERRRAGHTLLLISHDLAVVSRLADRVLVMHNGRIVEEGPTRQILSAPKEAYTRHLLEAVPSAGSRGYRLSPAQPHQPQVRVALPAKRIDESTNVLEAKGLFKHYGKANTPLAVNDVSFSLK... | 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
|
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
|
A0A256G1E1 | MTIINTLLSVEGLVVRSNETALAGPVSFTLKQGETLGIVGESGSGKTLTAMAIAGLLPQSLHADGQSYLDGAPLALGISDRGRDFRTSQIGVVFQNPTTALNPRLSVGAQLFEALSPAMRGDKAKAATICLHLLEEVGISEPVKKLTAWPHELSGGLAQRVVIAMALARQPKLLIADEPTTALDVTVQAQILDLIARLQKRHGFGVLLITHDMGVIRDRADSVAVMDGGAIVESGATLNLFTNPKSRAARSLLKASELVFATASGVLHDAASQPPLVEVKALQKTFRNGPRALGGVDILVKSGTTLGIVGESGSGKTTLA... | 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' e... |
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
|
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 ... |
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)... |
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 Loc... |
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-... |
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
|
A0A8C5ME75 | MDVPHAVTPATSASSLCFISKELILQEGHFAMKRLDPGTSLCAALLAGLVLCVLMAEALGGEVCYETLGCFTDDKPYSGTPQRPKAALPWTPKKIGARFLLFTPENPTKHQVIRADSIASIESSNFKTTRKTCIIIHGMADKAEDSWVSKMCNEIVTMDDVNCIGVDWRRGSGNIAIYVQAANNARLVGAVVAHFLKIIQENINSSYSGSSIHLIGHSLGAHAAGETGKRYSGIWKITALVDILACNHLRAIHYYTASIRHPGGFLAYPCDSYKAFKEGSCFPCPAPGCPLMGYFSNSSHSVTSPQSYYLHTSTKLNGHP... | 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
|
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 th... |
N1ZPF3 | MEKFMMIDGNSIANRAYYGVPLLTNSQGTYTNAIYGFINILFKLLEEEKPDYLAVAFDLHSPTFRHKLSEQYKSNRKGMPKELREQMPLLKQILTAMQIKQYEIEGYEADDILGTLSLKAEQNNMQAVIISGDRDLLQLASDTLKIRIPKTKAGKTEIEDYFAQDVLQKYGVTPTEFIDVKALMGDASDNVAGVPSIGEKTAIKIIQQYHTIENAIQYVDDIKPKKASENLKAYYEQAMLSKTLVTIVRDIDITIDKNTLGIKNMFNEQVYAIMKQLEFKTFLYRFTQNKTQSILKNEISYQTITEPSQYDTVFHALQKN... | 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
|
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
|
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
|
A0A1A9AWA3 | MDWLSGNIMQFWASFLWPFARISSMLMTMTAIGAAFVPARVRLLLAVAVTLASLPSIPAMPQGIELFSLHSALITAQQILIGVAIGMISQFLTQIFVMLGQVVSMQSSLGFASMVDPASGQNTPLLGQIYMMLTLLVFLLLDGHLIMIEMLVRSFTTLPVGETGITAGGYHLLSQWFGILFLGSVSMSLSAIISLLTVNIAMGIMNRAAPQLNVYSLGFGLILLCGLFSLWYLLSAFPRHYDIYWRVALDDMCTLLHMTCGDGL | Function: Role in flagellar biosynthesis.
Subcellular Location: Cell membrane
Sequence Length: 264
Sequence Mass (Da): 28780
Location Topology: Multi-pass membrane protein
|
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
|
A0A7R9MD55 | VVIIFSGKELPNDLRLSDCDLGHNSVIHAINALNIKTKTKLLPFSDQLTLNQKLTNLDMNDTNEETRHELEDRNRLSRRVTTDEDKSAQKYYFFVFCNSCEQLMNGKLRVVCDKCKNGTIVVDREPREWHDVLTPNRITGVCQSQDCNGTIAQFYFKCAANTHNSAADDDRTTGADAVDRSRAVVLPLIRHNCIGVSCLACTDVKDTVLVFPCAAKHVICLHCFRDYCLSKLNERRFVTDPQIGYSVNCAVGCHESLIRETHHFKLMGQIAYEKYQRFGAEECVLSAGGVLCPQPGCGAGILLDETEPEFCTRITCSECT... | 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 = [... |
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-dihydr... |
A0A7R9MCM4 | GLYDEVVVKYEIDYSAGGSVQNALRYAQWVVGKNNPIANYIGAVGDDYFGKYLANKVKVDGLNVKYMVVDDKPTGACTVLFNNNGKYKSVCANLGASTCFDKHFLMNNFWFCERARVILTSGHLLPVSPDSVMYLAKHCHEWGKDFLLIISYRFLRPIPIGASYVIHNSTNYVMDLFPYIDFLFCSADEALAFATVKGYHTRDLKQVVKLMADEPKVSYNNPNIPNNYKSGRVVVVNQRGGKPVLLAKTDVFNTKEYPVPIMTDTEIIDTSGMGDALIGGFLAMYIDGRPFDVCVQCGIYCATECCRQSGCILPEKMKFK... | 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... |
A0A497R2X3 | MHPIIKERLKKQGYQLYGKQVAVKKCLWTHKYLKEEQYCYKNAYGIESHRCIQATPTLLCTHQCTFCWRLQEKDVGLKPVWNVPDSEFDSPEEVYKGLLWGWKRAISGYKPIVPKELFDQAMDPQHVALSLAGEPTLYPFLTELLELLHAKGLSTFLVSNGTMPESISKMITTGVRPTQLYITIPAPNKKDYLHVCKPIIQNGWDRLNKSLELLGKLGGRTVTRLTMAKELNMKNPVEYVALIKKAHPAFIEIKGYVHVGFSQYRVTRGNMPFHEEIRAFANKILEGLPEYKLVYEMEDSKVVILSNDKQPLKIDFQKIG... | 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-demethy... |
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 ... |
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