ids stringlengths 6 10 | seqs stringlengths 16 1.02k | texts stringlengths 117 4.4k |
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A0A1F6QPG0 | MTSLIKSIQDIKNVIAKSAKPLALIPTMGSLHAGHISLIQTAKSECKTIIVYIFVNPLQFGPNEDFSEYPKDLASDLKTCEENNVDFVFAPEINEIYPDIESVKRNLITPPCELADILCGKTRENHFSGVATVIKRFFDIIEPDFAYFGEKDLQQLYIIKWLVKEFNLPVTVQSCPIVREHTGLAYSSRNKYLSADEKNIAASLYKALKLARGNTRSGIFPLNKAILESLIFLSHFPEIKVEYFEAKDKTNLANVHNDTKHGFYYLIAAKIKKVRLIDNIEVP | Pathway: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantothenate from (R)-pantoate and beta-alanine: step 1/1.
Function: Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate.
Catalytic Activity: (R)-pantoate + ATP + beta-alanine = (R)-... |
A0A2R8BWP1 | MGAILLTIICILGVGLGIGLYVSVTIGFTALGVGLIFSDRPVWDALSYLPYNAVTTVTLLALPLFILMGELLLRSGITERMYDTVSKWLNWLPGGLLHTNIVASGLFACVSGSSPATAATIGGVAIPYMSKRGYDQRMMLGSIAGGGTLGILIPPSIVMIVYAVLAGESIGQLYIAGVVPGLILLGLCLGVILIAARVRPALAPKEASTSWAEKLAGLVWLLPILGLIVAVLGSIYAGVATPTEAAAFGVTGALIIAAMTGRLSLSMLRETLLATAATTSMIMLILVGAFLLQFVMAFLGLPVAMARAIAAWDLSTLQIV... | Function: Part of the tripartite ATP-independent periplasmic (TRAP) transport system.
Subcellular Location: Cell inner membrane
Sequence Length: 434
Sequence Mass (Da): 45589
Location Topology: Multi-pass membrane protein
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A0A174FS72 | MRKRTRKHRGTAGKMVGGFLAFFCLILLTAGMFWAIQGYVSYQKAVKEKPLAQAVEEARSGAQWASLEQVPDLYKKAVLAVEDHRYYTHHGIDWISMARAVVHDIRVMKPEQGGSTITQQLVKNMYYDQNKTFARKAAEAWTALYVERQLSKEEILELYINTIYFGDGYYGLKEASLGYFGKEPQELTDSEAVLLAGIPNAPSAYAPSRHADLALQREKQVLAAMVKYGYLEQSETDSLLWDAAADPVLAR | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
EC: 2.4.1.129
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 = [... |
A0A498K3H7 | MALSDQTFFHNCLIALYLIAPPTFISLRFLQAPYGKHRRPGWGPTMSPPLAWFLMESPTLWLTLLLFPSGRHSSNPKALLLITPFLFHYFHRTCLYPLRLHRDTASSKSSAGGFPVSVAAMAFGFNLLNAYLQGRWISEYKDYESDGWFWWRFMGGLAVFGYGMGVNIWSDSVLVGLKKEGGGYKVPKGGWFELVSCPNYYGEIVEWAGWAVMTWSWVGLGFFLYTCANLVPRARANHRWYLEKFGEDYPKGRKAVLPFLY | Pathway: Plant hormone biosynthesis; brassinosteroid biosynthesis.
Function: Involved in a reduction step in the biosynthesis of the plant steroid, brassinolide.
Catalytic Activity: a 3-oxo-5alpha-steroid + NADP(+) = a 3-oxo-Delta(4)-steroid + H(+) + NADPH
EC: 1.3.1.22
Subcellular Location: Membrane
Sequence Length: 26... |
A0A8H4SME8 | MANAQKSFKLSTGAEIPAIGLGTWQDEAAQEAAVLVALQAGYRHIDTARCYGTETAVGKAIKQSGVPRSEIFVTSKLWNNKHYPDDVEQALQMTLDDLGLEYLDLFLMHWPVAFKRGDDPFPSDKDGNLITDDIDYVDTYKAMEGLVKSGKAKAIGIANFSRKEVERLLANATIKPAVHQMELHPWLQQEEFHKFHQAQGIHVTQYSPFGNQNEIYGSREKHGQLVNDKTLVEIGKKVWKNFQSSRPRYVLPYFSMVIKLILIAAWGIAHGRSVIPKSKSPERIMQNFDIAFELAPTDIQKIDSIHKKLRFNDSSKDFGY... | Function: Catalyzes the initial reaction in the xylose utilization pathway by reducing D-xylose into xylitol. Xylose is a major component of hemicelluloses such as xylan. Most fungi utilize D-xylose via three enzymatic reactions, xylose reductase (XR), xylitol dehydrogenase (XDH), and xylulokinase, to form xylulose 5-p... |
A0A2T2QZ35 | MLKQPNRLRRQKDFARVFKHGDTVHMPAFSVKYHANHHPSRTRVAVVISSKVAKRAVIRNRTRRRFYGQIQLFWPRIRPGMDVVILLRRQATDLRGAQLAEQLRSCFHKAGILH | 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... |
A0A934MUS7 | MKTTSLKGKITVQYSLLFLACMSIVGLLVYQVVADIVQNIAINYIHETIKQTNEKIDQTLTEVENSSSTTISNWYIQTLLNRHEKYLPLRDRVQVSEMVTSAANQNSYLKSLELYSPKFGFFGFNDSVLQAADINLHIMERRLPNTKLMNKMVWMTTEQGFDQQRYILGARTIPNFISDDNLGYVMAVLDGTLIEEDFRDIDIGQGGIIFLMNEEGQIVFASSSIQPQQKKLFSATLTKLKNEALDHDIFQVDGVRSLITYSHSNKSGWMTGAVLPVSSLTRQMAYIQKIIIWTNVVAIFFILLSAGVLSSRITKPIRKM... | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Membrane
Sequence Length: 585
Sequence Mass (Da): 66938
Location Topology: Multi-pass membrane protein
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A0A498J8H2 | MTMSKQKVLLQPIILLIVIEVLLAAATSAQTQLASPPLPSPPPPSEVEVKPGCQDKCGNVSIPYPFGTKKGCYLNEDFLITCNSTHYEPPKPFFKKSYSTEVTNISVDGKLYITLYPAVICYDKSGQLTYEFTSSVNLSSFFISNTDNVYVAVGCDTYSYICGYKNEKYVYSGGCISYCAGIDDYVVNGSCNGFGCCQTRFTQGINYFEISAMSFKNHKDVYSFNPCSFSFVVQDGKFNFFSNMLGSDYLKNASLPVVLDWSVGSENCTNVVSKKNHPCKGNASCYDVENGSGYRCKCNDGFQGNPYLNGCHDIDECKVP... | Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Subcellular Location: Membrane
Sequence Length: 774
Sequence Mass (Da): 85610
Location Topology: Single-pass type I membrane protein
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A0A7X8XWS8 | MSGKKVFSLTKLNTSIGKHLNKVSGAFWIKAEIAQLNFRSGHVYLEFVEKEGDMIVAKSRATIWKGEYQVFEHRLGELLFQVLKQGAEIIAEVEISFHNVYGLSLNILDLDDSYTIGELERKRKLAIEKLYKEGKVELQGKLKLPIVPQRLAIISSAIAAGYEDFMHQLKNNQQGYKFKIDLFETAVQGDKATSMLIEQLKKIQLSNEDYDAIIIIRGGGAKMDLYAFDQYEIGKEISKASIPVITGIGHEKDETIADIVAFLNLKTPTAVAEFLINRVYTYDQNIEILLNNISDDIKDLVEDNRYSFELQVAKLFPKFS... | 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: 456
Sequence Mass (Da): 52368
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A0A831EBW4 | MFDIGFGELLLVFIIGLVVLGPKRLPVAVRTVVGWIRALRSLATTVQNELTQELKLQEFQDSLKKVEKASLDNLTPELKESMDELRQAAESMKRTYSANDAEKASDEAHTIHNPVVKDYEAQHEGVTPGVAEHQVSAPQQAPQEVPEETAPAKISLAKTAAPVSDSTPSASDKS | Function: Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes. Together with TatC, TatB is part of a receptor directly interacting with Tat signal peptides. TatB may form an oligomeric binding... |
A0A979FJK0 | MTTKVLRSLQVVKKSGSLQCVVCGSRRYSTSTNAESFSTNTSSNTSSTSTNSTNTSSTSTYSRKDAELFDIVVAGGGMAGFAMACSLGQSKVLSSLRVLVLEGGPHTDASLEALSAAPHDNRVCAIAPPSVRLLDKLGVWHDICGVRTGPVKRMQVWDSESDAMIAFGDGHRALAHIVENRVTVAALRARVPSSIEVRYGARVQSFDLPPPATDGLPLLTLRDGGHIRARLLVRGASVVRGASVVRGASVEHLEVWTVCRGGNTAARGTDSLPWWQHCSSRYGQSAVVATLQLEREENESNITAWQKFLPNGPLAILPLR... | Pathway: Cofactor biosynthesis; ubiquinone biosynthesis.
Function: FAD-dependent monooxygenase required for the C5-ring hydroxylation during ubiquinone biosynthesis. Catalyzes the hydroxylation of 3-polyprenyl-4-hydroxybenzoic acid to 3-polyprenyl-4,5-dihydroxybenzoic acid. The electrons required for the hydroxylation ... |
A0A6B9LZA8 | MFINRWXXXTNXXXXXXXXXLFGAWAGMVGXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXPSFXXXXASSMVEAGAGTGWTXYPPLAGNLAHAGASXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXYQTPLFVWSVLITAXLXXXXLPVLAAGITMLLTDRNLNTTFFDPAGGGDPXXYQHLFXXXXXXXXXXXILPGFGMISHIVTYYSGKKEPFGYMGMVWAMMSIGFXXXXXWAHHMFTVGMDVDTRAYXXXXXXXXXXPTGVKV... | 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... |
A0A1Q3RRL0 | MIIDGNAIAKKIKDKARNCCSDCYRKPNVVAIMLGENPSSEAYLRMIERTCNSVEFGYRLDRFDTTLSEQDLLEHIRALNEDEEIDGILVQMPLPKQISEEKVIMAIAPEKDLDGFHPINAGRLFKGEKATRPCTPLAVITMFKELDIDLEGKYIVVIGRSNIVGKPLAVMLMENNATVTICHSRTVDLEEHTRKADIIIVAVGIANFLKKEMVSEKAIVIDVGMNEVDGKLVGDVDFDSMKDYVQMITPVPGGVGPVTNAVLLLNVIEHFKGVK | Pathway: One-carbon metabolism; tetrahydrofolate interconversion.
Function: Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10-methenyltetrahydrofolate to 10-formyltetrahydrofolate.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate +... |
A0A498KBC3 | MATCPPYVGGQAKAPTPDCCTGFKQVVNNNKKCLCVIIKDRNDPELGLQMNVTLALGLPAVCKAPANVSKCPELLHLDPKSPEAQAFYQLEGNSTKTASSLAPSTTVEGPTIASMGSRSSSGAARQNIVGLLQ | Function: Plant non-specific lipid-transfer proteins transfer phospholipids as well as galactolipids across membranes. May play a role in wax or cutin deposition in the cell walls of expanding epidermal cells and certain secretory tissues.
Subcellular Location: Cell membrane
Sequence Length: 133
Sequence Mass (Da): 138... |
A0A1F6QPB5 | MTRKIDVQVIIGSKSDELKIKPALDTLAEFGIAYDFKVASAHRSPSYVEEIIDSAVNGGVKVFITGAGMANHLSGAVAGRTTLPVIGVPFSGSSLGGMDSLFSTVQMPPGIPVATVAVDGAKNAAVLALEILSIENKDLQKKIIEFRHKETEKIRNAI | Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate from 5-amino-1-(5-phospho-D-ribosyl)imidazole (N5-CAIR route): step 2/2.
Function: Catalyzes the conversion of N5-carboxyaminoimidazole ribonucleotide (N5-CAIR) to 4-carboxy-5-aminoimidazole ribonucl... |
A0A7R9FJH5 | MGLIFDSLYVDVAVGAATLLVLICIFYSYAYGYWRRRNITYIPAPFSIFGNVGDMIFMKKTPALVMRDLYNKLDGEPYGGIFIGATPIMLIRDPEVIKQVFVKNFTSFMDRHLDINEKVNPVEENLFFMKGEKWRWLRSKLTPTFSSGKLKMMFQVLTECASEMNTYVESIASKQESIEMRELFAQYNTEIIGSCAFGIKFNTINNPKSEFRAIGRTIFDQSFFQMMKGLIITIFPGLAKCFTFTIFDLKTSRFFRGIVEDTIAHREKNEISRNDFLQLLIQLKKKGYVTEDSTQLKEDAYLYYKIGDEGSSVRKEFDKT... | Function: May be involved in the metabolism of insect hormones and in the breakdown of synthetic insecticides.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 546
Sequence Mass (Da): 62704
Location Topology: Peripheral membrane protein
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A0A7S0WGW1 | MPPSTPLEEYLESVSGLPAKIQHNFTNLRELDEKSKKLHEELDQQVQQVWAPGPGQKRSRRTTVTDANAESKLEPFIKQCQQVTEGKVALAMQTYDLVDVHIQRLDKSLRKLEEVVKQRAEKEGVGAKDGQGSSGGSAFDAKRKGGDTDKRKKRDRLTTGGVSLQAPSYTDTGGGEKIDIDLPIDPNEPTYCVCNRVSFGEMIACDNNSCRIEWFHFECVGLSRDHKQKGKWYCPECAALKKKAKK | Function: Component of an histone acetyltransferase complex.
Subcellular Location: Nucleus
Sequence Length: 246
Domain: The PHD-type zinc finger mediates the binding to H3K4me3.
Sequence Mass (Da): 27509
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A0A834N216 | MVAHILYNFNLEPVDELDNVKIMEDVLLRSSKTLQNNLIPAGSICNISIHNLHRTPEFCPNLDVFNPGRFLPKNIKERNLYSYSPFSAGPKNCIGQKFAVLRLKIIVAYILHNFYLKPVDKLDDVKMIGDFILGSPKPPRIKFISIK | Function: May be involved in the metabolism of insect hormones and in the breakdown of synthetic insecticides.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 147
Sequence Mass (Da): 16795
Location Topology: Peripheral membrane protein
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A0A165HE29 | MAKTELQVLLENVPDPTDFPSADVAPGLRELDEALVCDVCREFYSGPMILECGHSFCSYCLRRAFSDRQECPKCRAPANEMRMKKNVELESVVSIWKSAARECILDLLKRNQELLIRLDEPAASGTDGVAEGPPQKRQRVDTEGSDDEVQFVSSPLKQPSIPSKVKVRPRNGHGRRPSGSSNSSSPGAPSSADGTNGLVNCPLCQKQVPLECINPHIDSGCQRFIGPGASSSAAASTQPGPKGKQKREWSKLLDGGNSVGQGSGVARKAKEKGKERERAGSMTPDPEYLPKEPYDIIKLSRLKELLQEHGLSTHDERNVL... | Pathway: Protein modification; protein ubiquitination.
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
EC: 2.3.2.27
Subcellular Location: Nucleus
Sequence Length: 4... |
A0A3M7SAF6 | MSRFDLIERDPKKINNFVQIFFSDVVAEPEFTRSEDTLWSASIELFKCSKNSVYKLFSAVFSIVWSLFCGCCLGLSAFYNVWLWMPCIKYQSFLLRFFKKLNSILLAVCLAPITSVLGLYLSKIGSGSEDDRTPRRFSIQLERIFLPERNSTNLSSKSSTQTKAEFLRNEQENFFN | Function: May act as a scaffolding protein within caveolar membranes. Interacts directly with G-protein alpha subunits and can functionally regulate their activity.
Subcellular Location: Cell membrane
Sequence Length: 176
Sequence Mass (Da): 20400
Location Topology: Peripheral membrane protein
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D7CUB9 | MVFPLGRPARLAVLASGRGSNLRALAAAFPPGDPLGSVVLVLSNRRDAPVLALARDLGIEARFIPFGADRARFEREATAQLTAAGIDLVLLAGFMRVLSPAFTARYAGRLVNIHPSLLPRFPGLHAQRQALEAGARESGCTVHFVDAGVDTGPVILQRRVPVLPDDTEERLAARILAQEHRAYPEAVRRVLLGEARFEAPQNQEATP | Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide from N(1)-(5-phospho-D-ribosyl)glycinamide (10-formyl THF route): step 1/1.
Function: Catalyzes the transfer of a formyl group from 10-formyltetrahydrofolate to 5-phospho-ribosyl-glycinamide (GAR), produc... |
B2V8K6 | MSKNLVVLISGRGSNLKAILEAIKSGKINAKVSLVLSNKKDAKGLEIAKEYGIKTKFIDPSFFETRRGYDIYIAELIKKENPDFVVLAGYMRILSDEFIDAFEGKIVNIHPSLVPAFQGKSAQRQALDYGSLITGCSVHFVTKELDNGPVIVQAVVPVLPEDTEESLSNRILEFEHKIYPQAIKWLVEDRVVVSGRKVIVKDAKYGTLPVNPSLEDF | Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide from N(1)-(5-phospho-D-ribosyl)glycinamide (10-formyl THF route): step 1/1.
Function: Catalyzes the transfer of a formyl group from 10-formyltetrahydrofolate to 5-phospho-ribosyl-glycinamide (GAR), produc... |
D7CTI5 | MIVVVGSLNMDLVVRVPRAPRPGETLLGSGYETHPGGKGANQAVAAARFGAPVRMVGRVGRDAYGDPLAHRLAAEGIDLGFLEQTDDKTGVAFITVDEAGQNSIIVAPGANAALRPEDLTERVFEGAEVVLVQLEIPLKTALRAAALGRAAGARVLLNLAPAQALSAAQLGDVDLLLVNEHEAATLLGAPEVLGDLGAALAGLRRFVPAVVLTLGGRGAAWAGPEGSGLEPAHRVRVVDTTAAGDAFAGALAAELARGATLEAAVRYAGAAGALAVSRSGAQPSLPTREEAERLLRGAG | Cofactor: Requires a divalent cation, most likely magnesium in vivo, as an electrophilic catalyst to aid phosphoryl group transfer. It is the chelate of the metal and the nucleotide that is the actual substrate.
Pathway: Carbohydrate metabolism; D-ribose degradation; D-ribose 5-phosphate from beta-D-ribopyranose: step ... |
A0A932R599 | MLLTLKVGNTTIAAGIFAGEKLVADWSISARRDYTPDELGMILLNFLAAHKIKASQIEGFIVNSVVPPLNWAISKAAHKYFSTEAIFLNNRFGLVPLDVKEPESVGADRIADCIAGFRLYGGPLLIIDFGTATTFNLLSREGHFLGGAIAPTMELAAESLVKTTAQLFKVELSPPRSVIGKDTAENLQAGIVLGFLELVEGLIDRFEEEYPEGLRIISTGGRGSFFKDQIPAIEIHDEHLALKGLRIAWEERNREQKSL | 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... |
R7Y090 | MSERLRPRDLAFLATESSRTPMHNATVEIFDPGESGFDYARLVELIADRIAFVPRYRQRLQWIPGRLATPVWVDDPEFELSYHVRRSALPRPGGHDQLRELVARIASRPLDRSRPLWETYFVEGLAGGRVAVLTKSHQILVDGRETVDIGQVLLDTEPDRPELGHDEWHPRGRPDALSLTLGAITDSIERPSTLVKTVQANTQSIVRTASSARHRASDVAGALAGRKPVASSPINGPLSRQRRFLMIHTQLDDYKRIRRVHGGTINDVILATLTGGLRGWLMTRTESMAGLKTIKAIVPMSVIDDELEPTSLGTQVAGHL... | Pathway: Glycerolipid metabolism; triacylglycerol biosynthesis.
EC: 2.3.1.20
Catalytic Activity: a 1,2-diacyl-sn-glycerol + an acyl-CoA = a triacyl-sn-glycerol + CoA
Sequence Length: 485
Sequence Mass (Da): 53248
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A0A089K729 | MARVRSTAEKLKRWLADLSIQIKLIGAYIVIILVPVIVISNYLFTGFYQNTIKDIIKENRYQTDNEKQEIMSRIGVMEQSIGLLVSDRQLREYVTVESEPGLNDIKRFQEYSFTYLQTVLFNNSDIANIHFFVNNPWISELWPIIYHEERIKDKPFYTKMLNQTGNVLWEIQSEDAILQDSNAAVNQSLSSIVSLMAGVNQMNSQNLFQHLGIVKVDMPIGNFFKKAYNNSSDRDSRFYILDQQGNLHANSTDPLAGLDEADIQPAVAKYKEAGKSSLLLSHKGEDFLYLVEHIDKINAELINVISLHTTYSKIDQTRNT... | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Membrane
Sequence Length: 636
Sequence Mass (Da): 72420
Location Topology: Multi-pass membrane protein
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A0A5C5VEK7 | MSEADHPDRAPLVDSFGRRHTSLRLSVTDRCNIRCVYCMPDEQLRFLPRQEVLTFEEIERFTRVAAWLGVRKVRLTGGEPLVRCDLPALVRRLAGIHGIDEVALTTNGVLLERHAAALQDAGLTRLNVSLDSVRQETFVRLTRRDVLPEVLAGIEAAQHAGFEPIRLNAIAMRGVTEEEVVPLGRFARERGLELRFIEYMPLDADANWRRDQVLSGDEILSRLEQAFGALEPTHREDPSQPARDYRFVDGGGVVGFINPVTQPFCGDCNRLRLTAEGQIRNCLFSTEEWDARAVMRSGGTDTQLAQQVRDAVAAKRAGHG... | Cofactor: Binds 2 [4Fe-4S] clusters. Binds 1 [4Fe-4S] cluster coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine and 1 [4Fe-4S] cluster coordinated with 3 cysteines and the GTP-derived substrate.
Pathway: Cofactor biosynthesis; molybdopterin biosynthesis.
Function: Catalyzes the cyclization of GTP... |
A0A834JJN1 | MRNYVQTRDATCTLYSRCFEDNATSDARTDDASFIAENVTDVNVDWGMVFRGMVVSSSQLFSVDNVVAGAVIYLAVLIYSPATAGFSFAGVFIGLELGAPHKEVFTGLWGFNCFLTGAALGGNLFVINVQTAAATLVAIVYTVVLQYVLRIIFGKIGLPFLTLPFVISTSLFLKLRSASSSAVFPKPLQSSYPEKQRHDYLINRKRILQENVDGGSGGGSGSGSSGRRCGVKCGGGRQAVVGRGACIRGGEELNASLPKRLPAQRTSLSATRQYSPQDTFYPVVTNNVLQRGGGFPRPLPPNDQKDKENKEENEVSRPGS... | Catalytic Activity: urea(in) = urea(out)
Subcellular Location: Cell membrane
Sequence Length: 322
Sequence Mass (Da): 34598
Location Topology: Multi-pass membrane protein
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A0A351JX75 | MAQGSRGEDRGRGSGGRGGGGQGSVRDRVPVPRDARPGPRGRRPNYPPGRADRLPEGGVRTVLHAALGRIRYGPALAIQHRLHALRREGKVGDVVLSLEHESVITIGRRGDEVHILASREDLERAGVEVFPVERGGDVTYHGPGQLVLYPILDLRERGKDLHRYVGEIEETMVVTARTFGVEAVRREGFPGVWHARGKLGSVGIHVRDWVTMHGLALNVDLDPDGFRWIVPCGIVGANAVSIADLAGVRISVAAARDAACAAFANVFGVELLPVDGEVIAGWTRESRTG | Pathway: Protein modification; protein lipoylation via endogenous pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-protein]: step 1/2.
Function: Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate-dependent enzymes. Lipoyl-A... |
A0A3D0DVF7 | IDAAVAAATAGSGAAPGPKATHVVPPKAELLIYPVMKIDRVPEAAGKQESELNALDVVEVVDHYELAYHVRTRMQRANKPLYFDTIVSAKDAHIIDRWSMLQTVIGVGKSQYNGEVPISTTQVGDTFQMRDPERGTGGAYGAMAITNANNTSNAGKMYTHTTNTWGDGKQYVRGGSTTDANGQTAAVNAMWGLMNTYDSLKNVLGWQSLDGHNTASYIAVHVNTAYDNAYYSDTCRCMFIGDGSTFSSLGAIDVIGHEMGHGVTAATSNLVYSGESGGLNESSSDIGGEIAEAYARAGGKGEAIPNGGNDWMLGSEIGRN... | Function: Extracellular zinc metalloprotease.
EC: 3.4.24.-
Subcellular Location: Secreted
Sequence Length: 456
Sequence Mass (Da): 48664
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A0A0H2XST3 | MRRSGRPSQTETCSTSFSSPPEIPPNTGNVIRLCANTGAHLHLIEPLGFPLDDARMRRAGLDYHEYAQMRVHRDWDAFVAAETPDPARMFAFTTRGSGRFHDHAFLSGDWFVFGSETRGLPAELLERFPNEQRVRLPMRPDNRSLNLSNTVAVVVFEAWRQAGFEGGA | Function: Methylates the ribose at the nucleotide 34 wobble position in the two leucyl isoacceptors tRNA(Leu)(CmAA) and tRNA(Leu)(cmnm5UmAA). Catalyzes the methyl transfer from S-adenosyl-L-methionine to the 2'-OH of the wobble nucleotide.
Catalytic Activity: 5-carboxymethylaminomethyluridine(34) in tRNA(Leu) + S-adeno... |
A0A7S0RYH0 | MNEENCLLAQNLVSKAYISQGSDALARRNKLIKRLLSNRRLPPEGWDDATIEMFIQDCALMDSNNFVDVVGVGEREGRVASNLVAQRHYRLAHGIGRSGDLVAEQPKAAGSSLLAKLSNLLVMDALRVAGMEDLGAATILPMATGMAVTMVLLALRAKRPPTARYVLWPRIDQKTCAKAVATAGFELIAVPMCLEGDLLVTDVAALENEIHTRGADNILCVLTTTSCFAPRGPDDVIAVAKLCAKHGVGHVINHAYGVQARPLNAQVAAAWRRGRVDAVVQSTDKNFMVPVGGAVVAAGQSDPSLVQTVAQMYPGRGALT... | Pathway: Aminoacyl-tRNA biosynthesis; selenocysteinyl-tRNA(Sec) biosynthesis; selenocysteinyl-tRNA(Sec) from L-seryl-tRNA(Sec) (archaeal/eukaryal route): step 2/2.
Function: Converts O-phosphoseryl-tRNA(Sec) to selenocysteinyl-tRNA(Sec) required for selenoprotein biosynthesis.
EC: 2.9.1.2
Catalytic Activity: H2O + O-ph... |
B9XP92 | MILLAVETSCDETSVAIIRNGKVLSTIVSSQIKLHAEYGGVVPELAAREHLANLIPVANAAMTAAEVQSDQVDAIAATQGPGLPGALVVGLKAAQGMAFALNKPFFGINHHEAHLYSPWITGSPPVADFDSFQPNISLIVSGGHTMLIHVESELKHHVLGSTIDDAAGECFDKVAKLIGLPYPGGPEIDRLASAGNPKAYDFPRPMLRDASDDFSFSGLKTSVRYFIRDNPAVLDSLQKLQDLCASVQEAIVEVLVTKTVRAANRLQVKCVTASGGVTCNRALRSALETACKRKHLTLRLAEKSLCTDNAAMIGVLAERK... | Cofactor: Binds 1 Fe(2+) ion per subunit.
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. Is involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, togeth... |
A0A2R8C282 | MSVEAGVVTLEGRVADPAVSQDVAGIAERLEGVVAVDHALAASDDISQQINPAFERFRARADQFFARLPLFFLAAAAFAAIVVLGILLTGLRFWDRIAPNAFIAGIYRQAFRVLCGIVGIVVALDLLGAAALLGTILGAAGIVGLAIGFAVRDTVENFVASIMLSLRQPFRPNDLVEIEGDVGRVIRLTSRATILLSLDGNHIRIPNALVFKGRIVNYSQNPARRFSFDIGIDPDADPEATRVLAQAALKAQSFVLDDPEELVWIENITESGAILRVTGWIDQNETGFVTARGDAIRLVKAAIEAAGVSIPDTTYRIRLE... | Function: Mechanosensitive channel that participates in the regulation of osmotic pressure changes within the cell, opening in response to stretch forces in the membrane lipid bilayer, without the need for other proteins. Contributes to normal resistance to hypoosmotic shock. Forms an ion channel of 1.0 nanosiemens con... |
D7CY84 | MNVLVYGLGRSGGAVARLLRRQGHAVWTFDAQHPQGEDLAALGCRATSAPLEVPAELCIAAPGVPWDAPDLAALRARGVETIGEVEWVYRTVDAPILGITGTAGKTTVTRWLSHTLTLAGLDAPAGGNVDPALAAVAAPGRVLVTELSSFQLERCPSLHPRVAVVLNLGRDHLDRHGSLAAYHAAKKRLIAHLTPEDTFVYNHDDPLVRAWAEASPARTWGFSAAPTPGSAAHLADGMLTLHGRPLVAVRALQLTGQHHRLNALAVALAAAAWGLGDEAIRAGLESFSGVPGRYSVVGEVAGVRFVEDSIATRTLAVQAA... | 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-... |
A0A3B0PG01 | MNNNQQKTNNNNQKNSVDKSENDNNKKKSEANQKQENLNPNNNNKKKEDSKNESNNIPLINKNISDQQIVKISNYIKDNYPVIYADLKEKNRLGFNSNLDDDKLIVYANYEDKDLELLLKKFKVVTNNIGLYEEALTHNSYANEMHLKYNYQRLEFLGDAIINKIVAEYLFNHSDSSEGEMTKDRIKIIQSNTLIKAATQLELINYIRVGEGLKIAPLSPKILEDIFEAFIGAMYLDQGEYAVRKILNYTIIGYYQKGQLTENTDYKSIFQEIIHSTGLNMKIHYERTYDRQKNLHTVSLYAGGIMYGEGKDSSTHKAEI... | Function: Digests double-stranded RNA. Involved in the processing of primary rRNA transcript to yield the immediate precursors to the large and small rRNAs (23S and 16S). Processes some mRNAs, and tRNAs when they are encoded in the rRNA operon. Processes pre-crRNA and tracrRNA of type II CRISPR loci if present in the o... |
A0A7V1KMZ7 | MSWLNLLAVAALGYLVGGIPTAYLAGRLRGIDIRTQGSGNVGGTNALRVMGWRWGLPVMAVDVGKGYLATRLLPALSFSPLEGVHLAIAAGVGAVLGHIFSPYLAFRGGKGVATGAGMLLALIPGPVGICAVIFLAVAFGTGIVSLGSLSAGAALPLVTWLWGRGVTPVPPAVHWLTVALALLVFWTHRSNIRRLLQGRENRFRRPWERRS | Pathway: Lipid metabolism; phospholipid metabolism.
Function: Catalyzes the transfer of an acyl group from acyl-phosphate (acyl-PO(4)) to glycerol-3-phosphate (G3P) to form lysophosphatidic acid (LPA). This enzyme utilizes acyl-phosphate as fatty acyl donor, but not acyl-CoA or acyl-ACP.
Catalytic Activity: an acyl pho... |
D7CWV7 | MTQRSFTGILVLGALLAAVLYLWQPWNTTGLPPLRLGLDLQGGLRVVLQSTTPNPAPEDLQAARRVIENRVNEFGVAEPLVQTAGGDRIIVELPGLSADEQDRAQDLIGQQAVLEFRLVRPQSVGMPVEAMTEADLEPPAFTGEILSGAQTGYDELGRPVVNFQVRGADAQAFGQFTGANVGRSMAIVLDGNVVSAPTINQRIDASGQISGRFTLEEASDLALVLRSGSLPIALQVQEIRAIGPTLGADSVAAGTRAGLIGAVAVVVTVLLFYGPLFGSVLTVGVLFALVLIFGMLAGLGAALTLPGLAGLVLTIGAAVD... | Function: Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. SecDF uses the proton motive force (PMF) to complete protein translocation after the ATP-dependent function of SecA.
Subcellular Location: Cell membrane
Sequence Length: 740
Sequence Mass (Da): 77357
Location... |
A0A830GDC3 | MHVGVLGAGSMGSLFAGLLAADGAATTLLAHEGPHVDAIRERGLRIECVDGSSDAVGVEVVTDPAAAPSLDAALVFVKSHATADAADEWRGALADAHVATLQNGLGNAETLAGRFESVLAGTTSHGAVVADPGVVRHAGVGDTRLGRWDGPTDDAPARLAATLSVAGIDTAVVTDPRTALWHKVLVNVGINASTALARVENGALAEHASGSRLLRRAVAEAARVARAEGVDVGDPIAEAVTVAERTASNVSSMRQDVEAGRETEIEALHGAVVARAAEHDLPAPVNRTLADLVRLAQAASERGHP | Pathway: Cofactor biosynthesis; coenzyme A biosynthesis.
Function: Catalyzes the NADPH-dependent reduction of ketopantoate into pantoic acid.
EC: 1.1.1.169
Catalytic Activity: (R)-pantoate + NAD(+) = 2-dehydropantoate + H(+) + NADH
Sequence Length: 305
Sequence Mass (Da): 30980
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A0A3P1Y3L1 | MQNDDVKRIKERLDILEVIGDRVRLHRAGRGYLGLCPFHDEKTPSFHVSQERQNYHCFGCGRGGDVFTFVMETEGLEFRQALELLADRAGVALTRPEGRRRTSGNLYEVMDLAEKFFRSLLTAPEGTAVRAYLTRRGLSLDDAARFGLGWSANSWDSLSRHLRGAGVTDREALDAGLVLEGQRGGVYDRFRGRMTFPIRDVAGRVIAFGGRLVDGEGAKYINSPEGAIYSKRRNLYLLHEARGSIRERGRSILVEGYMDAIRLHLNGYTETVASLGTSLTEEQARLLKRFGDRCYICYDSDTAGQEATLRGMYTLQGLGL... | Cofactor: Binds 1 zinc ion per monomer.
Function: RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication.
EC: 2.7.7.101
Catalytic Activity: ssDNA + n NTP = ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate.
Sequence Length: 576
Domain: Contains an N-termi... |
A0A1Q3RDJ9 | MDFHTHTNYSPDSKTDMKKSILTAIEKNITDLAFTDHVDFDADIDSGIGDWDFDRNKYEEEIKFYQAKFEDQINLYHGLEIGVQPHLTDRNRDVVKMNQYDFVIASLHSVERRDLYHKKYFENHSDIDAIRIYFESYFESVKTFKDYSVLGHLDLYVRYKEELENVAFHKYNDHVEALLRMVIEDGKGIEINTGGYRYGLKYANPNRSFLELYKELKGEILTIGSDAHTPDFLGHKYDETVHLLKEIGFKYVSIFEQLKPKFIKL | Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 8/9.
EC: 3.1.3.15
Catalytic Activity: H2O + L-histidinol phosphate = L-histidinol + phosphate
Sequence Length: 265
Sequence Mass (Da): 31326
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A0A2N7WPE5 | MKIAAIETFEIRIPYRRNHTLSSGPLYGAHSVIVRLQTDEGLIGAGEASIPGGPVWSEESVSSVRAVIEEYLAAAVIGRDPLQCSDIAAVMSKAVRGNPFARAAIEMACFDVAGQALGVPVAQLVGGRRRSSVPMVWSLASGVVEQEIEEAQGVNQRFGISRFKVKVGHVDAAADLERVRTLMRNVPENFQIRLDANQGWNEMTANWALPRLQDLGVTILEQPLPKGDLAGMARLKQQGRVAIMADESAMNANDVINIIRNASADMIALKLAKAGGILGTLQSASVADAAGLPYYMGCMMDTGLGTAAYLQTASALKDMS... | Pathway: Aromatic compound metabolism; 3-chlorocatechol degradation.
EC: 5.5.1.7
Catalytic Activity: (2R)-2-chloro-2,5-dihydro-5-oxofuran-2-acetate = 3-chloro-cis,cis-muconate + H(+)
Sequence Length: 371
Sequence Mass (Da): 39483
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A0A5C6MBV9 | MSVAADCDRDTLLIQVLPRGPVCHLGTTTCFGDDSRSNFSAISQLEQTIEQRRKAGADNSYTAKLFIEGRDRITQKVGEEAVEVLIASKNPDDRQFIGECTDLIFHLTVLLVEHGLSWDSIYSELNKRSK | Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 2/9.
Catalytic Activity: 1-(5-phospho-beta-D-ribosyl)-5'-AMP + H2O = 1-(5-phospho-beta-D-ribosyl)-5-[(5-phospho-beta-D-ribosylamino)methylideneamino]imidazole-4-carboxamide
EC: 3.6.1.31
Subcellular ... |
A0A5C6M538 | MVAVIDYGMGNLRSVFNAIEILGFSAELVKDPEKLQLYDHVILPGVGSFRVCMDNLQKTGFDQSIKEYVQTGNALMGICLGMQILATRGFEDGESLGLDIIPGVVEKINPLDAKIKIPHVGWNDVTFNSIGNPLIKSMKNSETFYFTHSYILKCDNLNYVFGETIYEKSFTSAVLKENVFATQFHPEKSQDVGLKLFKNFINWTP | Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 5/9.
Function: IGPS catalyzes the conversion of PRFAR and glutamine to IGP, AICAR and glutamate. The HisH subunit catalyzes the hydrolysis of glutamine to glutamate and ammonia as part of the synthe... |
A0A5C6MCQ3 | MSTDPANPTRRELLSAFRTRTAAPSESARIAGPAPNGGATVRLTARLMGCDFTVVLNPGPEQVEVAGEALERISAVEAWLSHYRDDSQLSRLNQTGWPGPASISAELRDFLEFCRHCWQLTDGAFDVAAGALSQLWRHCRKAGRIPDDAAVAAAKACSGHSLVNMNPVGNTVCFSAAGISLDPGAVGKGWGLDDAAAWLLDRAEPLQNFLLSGGHSSLLAAGSHNGTGGWPVGLGNPLFTEKRIATILLMYQAMGTSGSNIQFFRHAGRRYGHVLDPRTGWPAEGMLSATVLADSAALADALSTAFFCDGSGKGG | Cofactor: Magnesium. Can also use manganese.
EC: 2.7.1.180
Catalytic Activity: FAD + L-threonyl-[protein] = AMP + FMN-L-threonyl-[protein] + H(+)
Sequence Length: 315
Sequence Mass (Da): 33073
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A0A1W1UVF9 | MKVNHLDYHVEVQGAGEPVLVLHGFSGSSKSFSKFSDLWSQDYQVILVDILGHGNSAKPADYRRYEMDKVAEDLKVILKNLNIAKTHLFGYSMGGRLALNFVFKYPQMIASLILESSSPGLENEEERELRREQDYELATFIEEKGIAEFVSYWDSLPLFNLKEIAKEKKNALHQERLNNDTKGLANSLRGMGTGRQKPLWHALQEIKVPVLLIVGEKDKKYCKIAAEMAKRLPNAQKEVVQEASHIVHLEKPHIFSNLILEFLQGRYKNDN | Pathway: Quinol/quinone metabolism; 1,4-dihydroxy-2-naphthoate biosynthesis; 1,4-dihydroxy-2-naphthoate from chorismate: step 3/7.
Function: Catalyzes a proton abstraction reaction that results in 2,5-elimination of pyruvate from 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate (SEPHCHC) and the formation... |
A7SRZ2 | RKSNFKITSWNVNGLRAWLKNNSKSFVSKEDPDVFCIQETKCALADIPKEAKLAGYHCYWNSAEQKGYSGVGLCSKKEPIKVSYGMGNKEHDKEGRVITAEYEDFHLVTSYVPNSGRGLPRLGYRQQWNKDFLSYLKKLDEIKPVILCGDLNVAHKDIDLANPKTNTRTAGFTKEERADFTTLLGEGFKDTFRELYPDKKSAYTFWSYMGGARAKNVGWRLDYFVVSDRLVPKVCDSIIRSRVMGSDHCPLSLLLSI | Cofactor: Probably binds two magnesium or manganese ions per subunit.
EC: 3.1.-.-
Catalytic Activity: Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleoside 5'-phosphates.
Sequence Length: 257
Sequence Mass (Da): 29231
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A0A1C4IA83 | MRQPAYPQGQDPYATPEAYPPPQPPGERGPQPPQAPTAQVAQAQTQAPAPERGEWDPDPDEPEHPFFASDGDAGRATGRRTKGRDDDRDDLADDEDGDGDGRAGRRGGERPKKRRGGCACLVVAVVLIGGGGGAAYYGYGLYQDRFGPPPDYAGEGSGTVVIEIPDGSTGIAMGNLLKDKGVVKSVEAFTAAQKANDKGTTLQSGFYTLHKGMSGKSAVELMLDPKSRKTLVIPEGYRNAWIYAQIDGRLGLKKGTTADVAKSDRKKLGLPKWADDDKDIKDPLEGFLYPSTYSVSKGQKPADVLRKMVAQANKQYEKID... | Function: Functions as a peptidoglycan terminase that cleaves nascent peptidoglycan strands endolytically to terminate their elongation.
EC: 4.2.2.-
Subcellular Location: Cell membrane
Sequence Length: 469
Sequence Mass (Da): 50612
Location Topology: Single-pass membrane protein
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A0A6A2ZCF9 | MRTGWADGPEFVTQCPIRPGGSYTYRFTVQGQQGTLWWHAHSSWLRATVYGALIIRPRDGESYPFPKPKRVTPILLGEWWDANPIDVAREATRTGATPNVSDAYTINVQPGRDLFKCSSEETTIVPIDFGETNLLRVIDAALNQPLFFKVASHKLTVVGADASYTKPFTTSVLMMGPGQTMDVLIQGDRPPSRYYVAARAYQSAQNSPFDNTTTTAILEYKSATYAAKNCKATTPVMPSLPAYNDTNRVTAFIQSFRSQQKVEVPTDIDESLFFTVGLGLNCPPNFHKRRCQGPNGNRFTASMNNFSFVLSRNFSLLQAH... | Cofactor: Binds 4 Cu cations per monomer.
Function: Lignin degradation and detoxification of lignin-derived products.
EC: 1.10.3.2
Catalytic Activity: 4 hydroquinone + O2 = 4 benzosemiquinone + 2 H2O
Subcellular Location: Secreted
Sequence Length: 451
Sequence Mass (Da): 49830
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A0A932R794 | MKNNSLGVVILAAGRGTRMGQITPKAFLLLEHKPVLLYSIDLLARVEYVDEIIIVVHPEDRQHLENKVLSSLSVKKRIHVVEGGAQRQDSSLSGVRATTSSWVAVHDAARPLFSSQLLDRVYRAAQEAQAAIPTLPVTESLRLVSKESLITTDVNRENLHLVQTPQCFARELLLRSLEQVCAERRYFTDEAGAVLAISGVRAKAVPGERANLKITLPEDLEWAEALLKIKSRAA | Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 2/6.
Function: Catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP).
EC: 2.7.7.60
Catalytic Ac... |
A0A3A9JDS4 | MRQKVMRRLPRRHLSMPRRYGLAALMVLAAGGIRLALPVIGPPYLFFIPPVMAVAFLLGNGPGLFATALATLLAVGLFIPPYYTLQIPFEQWTATALFALVAAALALVCSAFRRTLDARDADLAQLRQALADAADGRAAADASNAFLSGVLASSADCITVLDLDARLTFMSEGGRRSMEVANFATIHHAPWPELWQGEARAEAEAAVAEARAGRAARFQGLAHTMRGRPLWWDVAVTPMLDGDGQPERLLCVARDITAQRRLEEQQQLLNQELKHRLKNTLAMVQAVMNQTLRQSRSLPEAQEALEARLVALSGAHGGLL... | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Membrane
Sequence Length: 470
Sequence Mass (Da): 50987
Location Topology: Multi-pass membrane protein
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A0A1F3ITE7 | MVRLFRKKIANELSKSIKNIFGFRPGNIFLYELAFMHKSAHAERNGREISNERLEYLGDAVISVIVADFLFKKFPFADEGNLTEMRSRVVSRNSLNKIAEKLGVGRLVTMSSVPVSNAYTGNALEAFFGAVYLDKGYSFAQNLLINFIFGRRIDVDAFINTETNFKSKLIEFCQKEKSSLDFSIVEEIQAGRKKQYVCEARINGEARSRGIDYSIKGAEQNAAEKALEVLRNGAE | Function: Digests double-stranded RNA. Involved in the processing of primary rRNA transcript to yield the immediate precursors to the large and small rRNAs (23S and 16S). Processes some mRNAs, and tRNAs when they are encoded in the rRNA operon. Processes pre-crRNA and tracrRNA of type II CRISPR loci if present in the o... |
B9XIP2 | MKVLVIGGSGLVGSHVLKAALAAGHQAIGTYRRSPLSGLVPLDAGDAAAAGKLLDQEKPDAVVHAAGWTWVDGCEDDPKRAFAENAEQPANLARLCQKRGIHFTYFSTSYIFDGLDGPYDEDAKPNPINVYSQSKWEGEQRVQQETDGTALLPRIICVYGAEVQKKNFAYQVWNALREGKALTLPSDQCGNPTYAGDIARWLITLLEKRERGPWHLGGPWPTCTRPEWAEKLIAAFKAEGIISHPNFAVKTLPTADLRQKALRPLRAGMISMKAFGGEFESTEFNQTIRELVANSI | Pathway: Carbohydrate biosynthesis; dTDP-L-rhamnose biosynthesis.
Function: Catalyzes the reduction of dTDP-6-deoxy-L-lyxo-4-hexulose to yield dTDP-L-rhamnose.
EC: 1.1.1.133
Catalytic Activity: dTDP-beta-L-rhamnose + NADP(+) = dTDP-4-dehydro-beta-L-rhamnose + H(+) + NADPH
Sequence Length: 296
Sequence Mass (Da): 32417
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A0A178MXK6 | MFVLSAVGILLISAATVGYISFANSRDAIAVLASEFRRELANRVVDHLRVFLEAPQNILRENAANLAEGILPTDDPGAISRHFLRQSLIHPSLSSLYFGNTSGGLAVGGHDGRREVLYTITTDGFVAGRFNKYRADPDGSRQGLIQSLPNYDARTRPWYRSAMASGDGVWGPIYILFTGDDMALPPSRAVRDTSGRLLGVVGADLFVAQLSRFLSDLHSRAPGQTFIMEADGSLVASSTGEPPFTRSQEGQPGHRLKATASSNRLTAEAASLVLTEDKRSGHSLRLDSAQGRHFVEVTPFHDPRGIAWTIATVVPEHHYM... | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Membrane
Sequence Length: 804
Sequence Mass (Da): 88012
Location Topology: Multi-pass membrane protein
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A0A2H6K5L7 | MHLIVGLGNPGSEYEGTRHNAGFMAADRFRVTRELGRTRRRYQGRWCEGRVCGRDVALLMPHTYMNNSGEAVRAAAVRKHISPEEIIVIHDDMDFPFGTVRVRAGGGTGGHKGLESIAALLGTTGFARVRIGIGRPENPFIAARDWVLSDMGVSGDELVAVLDTAADCAEAIIIDGMEAAMTRFNRRNDDKV | Function: The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis.
Catalytic Activity: an N-acyl-L-alpha-aminoacyl-tRNA + H2O = a tRNA + an N-acyl-L-amino acid + H(+)
EC: 3.1.1.29
Subcellular Location: Cytoplasm
Sequence Length: 192
Sequence Mass (Da): 20953
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G9PE34 | MLPPQPPVAGRQSASADPWRIWTIPNALSALRLAFIPVFALSIWQGHMLSAAIILVLASVTDFLDGVIARAFNQRSRLGRLLDPAADRLYIATALIMLAVVGALPWLVMVLLLARDVILAVHVPIFAHYGYAPISVNAAGKVGAFMLMSAFPLLLVRFAWVSTSIWAQITYSAGVATLIWGAGLYCWSAFIYLKQITRVLSEAVK | Pathway: Lipid metabolism; phospholipid metabolism.
Subcellular Location: Membrane
Sequence Length: 205
Sequence Mass (Da): 22301
Location Topology: Multi-pass membrane protein
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A0A809RDA7 | MNSIRQRLLLWLIVGMLISTGIAGLSMYLLAQDEANELFDYQIKQIALSLPGSSQLPVVTADDEDPEEDNVIQVWDAQGKPLFVSYPSRALPRYVATGLHTVNYRQQPWRLYNTQRRGQFIQVAQPMTVREELAAALALRMLMPFFVLIPLLAGLIWWSVGRSLRPMQDVTTALATRHADAMQPLDETDLPQEIKPMVIALNQLLMRLDQAMQSQRAFVADAAHELRSPLTALKLQLQLTERTSGDEQRTIAFTKLNQRVDRSIHLVQQLLTLARSEPRLEQAQFTDVDLSALAYEVAQDFMPLAEAHQTELRLELQPDV... | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Cell inner membrane
Sequence Length: 432
Sequence Mass (Da): 48362
Location Topology: Multi-pass membrane protein
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A0A6A2ZVH8 | MPMATDVIASLDISFVSCCSLFRRGCRQRRVGGVVFYVLGVTSTSSCHRVAAWSNGVGKALSMQAHPDKEMAKELHKMNSNLYKDDNHKPEMALAVTTFTALCGFISLHELKQVLEGVHEIVQVVGIASAKQVMDIHDRGGAPTDEVKSALRSVFTQLMSASKEMTTTVISKLKSRLLVESQAGEALCLAANEPHAYLSGDCIECMATSDNVARAGLTPKHRDVQTLCSMLTYNQGYPEILSGLPLSPYITRYLPPFDEFEVDRCVLPTGSSAVFPAIPGPSVFLAFAGEGTLKTGSCGGIVTEGDVMFGPANTEITITA... | Cofactor: Binds 1 zinc ion per subunit.
Pathway: Nucleotide-sugar biosynthesis; GDP-alpha-D-mannose biosynthesis; alpha-D-mannose 1-phosphate from D-fructose 6-phosphate: step 1/2.
EC: 5.3.1.8
Catalytic Activity: D-mannose 6-phosphate = D-fructose 6-phosphate
Sequence Length: 342
Sequence Mass (Da): 36736
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A0A931LLF3 | MNPTQIQREKKPWLSLLLALLAGTLTALSQPGYGLDWLSAFSLIPLFFALDNSRAKAAFFSSWLAGFVFFAILLYWLFFLSDWAGPWIALGYLVLCSYLALYWGVFGWLYSVLQKSVRGLHWLAVPALWVSLEFVRSLTHYGFTWGYLSDSLYAQPKLIQIASITGAWGVSFLIALVNLLFFWALKHRQVRFVLAGLGVITLALLTGYFLVNSEATQTVRSLEIAIVHSHVNQLDRSSPSQTDRLVELYASQVEQSVQGPVDLIVLPETILPAFILRNPEVFSRFSSLAIAKRAWMIVGTIDYRLDHPGALYNTAALLSP... | Pathway: Protein modification; lipoprotein biosynthesis (N-acyl transfer).
Function: Catalyzes the phospholipid dependent N-acylation of the N-terminal cysteine of apolipoprotein, the last step in lipoprotein maturation.
Catalytic Activity: a glycerophospholipid + N-terminal S-1,2-diacyl-sn-glyceryl-L-cysteinyl-[lipopr... |
A0A931LMB7 | MARSKKSEWIEVFAPATVANCGPAFDTIGFSLDTLGDCLEARLVDKPGVHIAEITGTKGLSTDPTKNTAGIAAQETLKLAKSLSQGVEIRLHKQIPQGSGLGSSAASAVAGAYAVNILLGEPLSQEELLEPCLAAECAVSGYFADNVAPALLGGFVLIQNLKPLRLVRLPVPDKLIVTAVTPDYVLLTREARAVLPEKILLKQAVRQWANIGALVAALHQNDLKLLGEAMEDFIIEPVRAPLIPGFDRMKQAALAAGALGCAISGAGPTAFAITDDLTKAEKIAQRMQAGFAQVSLKSQAHIGRVSTQGARCLRGKNR | Pathway: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine from L-aspartate: step 4/5.
Function: Catalyzes the ATP-dependent phosphorylation of L-homoserine to L-homoserine phosphate.
Catalytic Activity: ATP + L-homoserine = ADP + H(+) + O-phospho-L-homoserine
EC: 2.7.1.39
Subcellular Location: Cytoplasm
S... |
C2MBE5 | MDDLVISELIALLQAHGVRDVVLCPGSRNAPLVHALSHYLTRATCHSIIDERSAGFYALGLALATHREVVVCCTSGTAVANLHPAVAEAYYQGVPLVILSADRPERWIGQWAGQTLPQPGLFGSLVRKAVQLPEPHTDEERWYCNRLINEALLVALAPLPGPVQINVPISDPSVSLLPPTPAEQQSDPSDRRPIGMQSGRHIKQCCPCGVDAQAVKPLLERLATFERKMILVGQESWTATTSAGAVFPQSLREQFLCIGESLSNRPVTICSLDALLASLSEADRRALQPDLLITLGGHIVSNKIKQYLRNYPPRETWHLS... | Cofactor: Binds 1 thiamine pyrophosphate per subunit.
Pathway: Quinol/quinone metabolism; 1,4-dihydroxy-2-naphthoate biosynthesis; 1,4-dihydroxy-2-naphthoate from chorismate: step 2/7.
Function: Catalyzes the thiamine diphosphate-dependent decarboxylation of 2-oxoglutarate and the subsequent addition of the resulting s... |
A0A418XV42 | MAKKTNKTPARSRGQAQRKKSPSRKKAAAPRRRWFSWAFVAKFSLVLLVIGAAGLAYLDAMVRERFDSHVWQLPARVYARPVELYEGRVLSREDMLKLLDLMRYRRDAAASTPGSFAVQGSRLLIHTRGFKDSDGGETPKRIRISLSGGQIRNLDAGGDGLARLEPLQIGSIHPQHAEDRVLVPLEQVPPLLVDMLVATEDQSFYEHHGISLRGLARAMVANVKAGGLVQGGSTLTQQLVKNFWLTSERTLSRKLLEMPMAILLELHYSKQEILEAYLNEVYLGQDGARAIHGMGLGAQFLFGRPLEELEPHQLATLVAL... | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Cell wall formation. Synthesis of cross-linked peptidoglycan from the lipid intermediates. The enzyme has a penicillin-insensitive transglycosylase N-terminal domain (formation of linear glycan strands) and a penicillin-sensitive transpeptidase C-term... |
A0A1I4C589 | MTAYTATVTVRLKRGVLDPEAETTKRALDRLGFELQGLRATDRYEIDLDAADADAAEERASEMADRLLANPTIHDYEVEVEEAEE | Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole from N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide: step 1/2.
Function: Part of the phosphoribosylformylglycinamidine synthase complex involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent ... |
A0A0M4FVZ8 | MEIYLDVIWLLNFCFDLLLLSLTGKILKRNVKKFRLVLGALIGSGIVLIMFTPFSWFVSHPAGKLAFSLLIVFAAFGFKRFRYFLQNWLTFFFVTFLLGGGIIGAHSLLQSDGQLENGALMTASSGFGDPISWIFVIIGFPILWIFSKKRIEDIEIRKIQFEEHVNVQVMIGGQEVFLKGLVDSGNQLYDPLTKTPVMIVYAECLKPIVGEAFLELVKTGDSVHALEQIDETFPFIDRLRLVPYRGVGQQNQFLLSIKPDDVLVYTKEEIISVEKCFVGISPSGLSSDDDFQAIVHPKMLSEKGIKHVS | Function: Probable aspartic protease that is responsible for the proteolytic cleavage of the RNA polymerase sigma E factor (SigE/spoIIGB) to yield the active peptide in the mother cell during sporulation. Responds to a signal from the forespore that is triggered by the extracellular signal protein SpoIIR.
EC: 3.4.23.-
... |
A0A7C2UHX8 | MADANARSLDIAELIRRHPAEIAEILAALREEEAVELLRRLYRRRAAAEPLGEMEPDEAARLLAELNREDAAHILSHMEPDDAVDLLAELPPNMVQDILSRLEAREAKELGELLAYPPDTAGGLMSTEVVALAEEMTAEEAIQELRARAEEAETVYYAYVVDDRGTLLGVLSLRDLVLARPDTPLRAIMKSDAVALPVTMDKEEVAHVFDKYNFLALPVVDEGRKLLGIVTIDDVIDVIREEATEDALRLGGIPAGEDHPLDPPQSSVRKRLPWLMGLVVLNMSVAGLISQFEATIAQIAFVASLMPLIADMSGNAAAQA... | Function: Acts as a magnesium transporter.
Subcellular Location: Cell membrane
Sequence Length: 438
Sequence Mass (Da): 47260
Location Topology: Multi-pass membrane protein
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A0A5C6MAB6 | MGYRFKDRAQLYQALTHRSAIMELSSSGVCSDALPWNERFEFLGDAVLGLAISRRLMDLGQGLVEGELSRIRAALVNEVSLAVVARTLDLGRFLVLGKGAAKSGGRKRDSLLADGLEAVIGAVFNDGGFAAAEAVVDVLFGNVLRGDLMHLVQTDFKTMLQELTQEKFKKVPSYEVLLETGPDHNKVFEVRVILGTEELGRGSGASKKRASQAAAQQAFSKLSNEGEGEETP | Function: Digests double-stranded RNA. Involved in the processing of primary rRNA transcript to yield the immediate precursors to the large and small rRNAs (23S and 16S). Processes some mRNAs, and tRNAs when they are encoded in the rRNA operon. Processes pre-crRNA and tracrRNA of type II CRISPR loci if present in the o... |
A0A1W1VM25 | MDIRQQRKWDHLKLSLQADKGPLKTGFDDIYLIHQALANTNFNDVNCSIEIFKKKIDFPLIINAMTGGADGLDIINKKLANIARTCNVVLAVGSQTSGVLDRRTRHTYEVVRKTNPDGLILANVSALVDVKIALEAIEMIEANAIQLHLNVAQELAMDEGDREFEKLEENILKIKEKSNVPIIIKEVGFGLSKETIQKLTQYNINYFDIGGAGGTNFASIEVKRSKNPKDDIINWGIPTAISLVEALSVSKNINLFASGGIRSTLDMVKSLTLGAKGVGIAEPILKDVYINREKEVIVFLQEMKKQLKKLMILCGAKNIP... | Function: Involved in the biosynthesis of isoprenoids. Catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its allylic isomer, dimethylallyl diphosphate (DMAPP).
Catalytic Activity: isopentenyl diphosphate = dimethylallyl diphosphate
EC: 5.3.3.2
Subcellular Location: Cytoplasm
Sequ... |
A0A1H2XLL5 | MRLSTLAARCASIAAGVFTAGRAFADDQLPELPVIGAPVPGGMHFQQPVTGTMQSAVFLDNLLLWIIVPITIFVTGLLIWCIVRYNQRANPTPARFTHNTAIEVTWTIVPILILFVIGAFSLPILFKDQTIPQADVTIKATGYQWYWGYEYVDHDVEFSSFMLAREELEENGYAQSEYLLATDTAMVIPVNKTVVVQVTGADVIHSWAMPSFGVKQDGVPGRLAELWFMAEEEGIYFGQCSELCGISHAYMPITVKVVSEGEYLAWLERQGATNMAAAPGADTLRVAAAAD | Cofactor: Binds a copper A center.
Function: Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B).
EC: 7.1.1.9
Catalytic Activity: 4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(... |
A0A6A2YRR7 | MLAEHIVQLIAAVKPPLARLRRDGLGWRWEANKSFTTKSAYHSFTQPEDSWLNWKIIWKVEAPQRSAEVWAMRLIDLLIVALIPVTKVLSVTGVGLFLALDHVYLLGPDARNHLNKLVFYVFGPSLVAINLAGTITFDSFLTLSSAFAWILIKITKLPSTFKAWSSAVVLLLPLILVPAVCEEPNNPFGDSSTCSANAGAYASLSLAVGAIFIWSYAYAIMRSYANSCKQDSLAITIDTFKETTSESFSENCRIDRRDSLAIRQLLNGADAPLRGANSCMHDLASGSKSSKGLKRTRHESFNYSAVRNILMPLFGVGVVR... | Function: Involved in cellular auxin homeostasis by regulating auxin metabolism. Regulates intracellular auxin accumulation at the endoplasmic reticulum and thus auxin availability for nuclear auxin signaling.
Subcellular Location: Membrane
Sequence Length: 391
Sequence Mass (Da): 43154
Location Topology: Multi-pass me... |
A0A1Y5L7G9 | MTAAAADRMSSLDAFFFYTEEDGVNHMHVGGFALVEGAAPTAIEVAQALLPKLDRIPRYRQIAQPVPLHLGRPVWVDASQFDVTRHVRSTVLPESSRAALRTELETFISQPLERTRPLWELLLIDAVDADHWCIAWKIHHSMVDGVSGTELLTILFDSAPSPSSPPTVLRAQEPRKLASKQAIVLSSVTDLVLGASRTVHSIRPATARKLSRVGQAYLGLVKQTIFPDLHSPLVGNIGPERSYDYCVVPFADIKEIRAGLGGTVNDVVLTAVLKGFSAVLTAHGTNVSGKSLQAMVPVALRPRDAQGRPLGDGTMETKAS... | Pathway: Glycerolipid metabolism; triacylglycerol biosynthesis.
EC: 2.3.1.20
Catalytic Activity: a 1,2-diacyl-sn-glycerol + an acyl-CoA = a triacyl-sn-glycerol + CoA
Sequence Length: 469
Sequence Mass (Da): 50533
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A0A1W1UZZ9 | MRQAKVKTYAKINMVLNCLYKRDDGYHEISSIMQAISLHDNINLKPAGEIILNSNSTLIPLDEKNFAFKAAQLVISKYPSIKGVEIYIDKKIPIEAGLAGGSTNAAGVILGMNKLFNLKMTTSEMIEVAEQIGSDVPFGIIGPTALSTGRGTNVSPIPEAPLLWVVLLKPDFGVSTPKVYSNMKEQMFEKTDNIKGFLGALERKDQDYILGNLVNTLEKSTFALYPKVQEIKDFFIRNTKHSLMAGSGPTVFALFPNEIEAINFKDSIPPDYGKAYLAQTIDSKEIHERVIIDEKEN | 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... |
A0A3M7SML3 | MFKEIKISSPGKIILCGEHAVVYGKKALACSVDLRTTLTASHTSNNFFQLILINLNKTVEIKKEDFMSIRSSPISSEPNAIINHLEKVENDKIVSSLKFFILLDPDLEWSKIAGLQVLVSSEIPIASGLGSSASYSTCLSSLFFVLGSNRVFSESDLETINRNAYYIEKFFHGNPSGLDNSVSTYGNFVVFEKGQIREKFTSDQKLNVLIINSQIPKQTLEQVKKVRSLYEKHTAVLDSLMNTVDILVDKFVQSLKEKSSLDGIKDLVTINQGLLYALQISNQSLNSIVNICEKFGFGAKITGAGGGGCCITIFDHANRL... | Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via mevalonate pathway; isopentenyl diphosphate from (R)-mevalonate: step 1/3.
Catalytic Activity: (R)-mevalonate + ATP = (R)-5-phosphomevalonate + ADP + H(+)
EC: 2.7.1.36
Subcellular Location: Cytoplasm
Sequence Length: 350
Sequence Mass (Da): 3872... |
A0A8B7PJS2 | MAGGSIPSKRPRLINKVVFWSLCLLTLLLLTLESYGPEGIVPYDSADVRFKAPEIFFELSDEIVLSSDEALKYHYNRSSTDEVANTDKIDVSYIADFDGVKPVPFNRSLLKTILVWNNGYGLPAEGLADGDERELERMGCPQPNCVIMSRKKQAQPVQTYDAIIFHFRATTPDDLPLMRTPSQRWVFRESEPASYVFQYPHTYNGLFNWTFTYRTDSDIVMSPGRYIPLSKEEISKPKSALETRPLPKPKMAAWFVSNCNAHSGRDRIARQLEKFFDVDVYGRCGPLKCGREDSVSCRRMLEENYKFYLAFENSLCKDYA... | Pathway: Protein modification; protein glycosylation.
EC: 2.4.1.-
Subcellular Location: Golgi apparatus
Sequence Length: 400
Sequence Mass (Da): 46654
Location Topology: Single-pass type II membrane protein
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A0A448MMZ9 | MTNKVIVALDYETEAEALTLVDQIDPSLCRLKVGKEMFTTLGTNFVKQLHQRDLMFSLI | Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 2/2.
Function: Catalyzes the decarboxylation of orotidine 5'-monophosphate (OMP) to uridine 5'-monophosphate (UMP).
EC: 4.1.1.23
Sequence Length: 59
Sequence Mass (Da): 6730
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A0A3M7SCX9 | MSLKRNPSRSIINFSAGPSSLPYEVLEIAQRELVAYGETGLSVMEMSHRSATFSKIINNAEQLVRELLNVPVNYSVLFLQGGGNGQFACVPLNLMNLKPKKSADYVLTGYWSERAANEAKKYGAVNLVFPKPEKYSRIPPVQEWNLDPEASYVFVCDNETINGIEFQEDITQALNGVPLVADCSSNLFSRQIDVSKYGLIFAGAQKNFGPSGVTLVIIRNDLIGHAAKECPSIFDYKIQAGNNSLYQTPPTFSIYMCGLVFEWLKKHGGMESIDKVNRMKADAVYEVIDNSNGFYYSPISPKDRSRVTIPFRLCVDGKPN... | Pathway: Amino-acid biosynthesis; L-serine biosynthesis; L-serine from 3-phospho-D-glycerate: step 2/3.
Function: Catalyzes the reversible conversion of 3-phosphohydroxypyruvate to phosphoserine and of 3-hydroxy-2-oxo-4-phosphonooxybutanoate to phosphohydroxythreonine.
EC: 2.6.1.52
Catalytic Activity: 2-oxoglutarate + ... |
A0A2T5AIY0 | MTVAVLGVGVDTVDLGAFAASLAEPGTRFAGAFSATERRQCRERAEARGAGPGTSRADGDRPGGSRSDGDRSGADRSRGATSSSSDQSTPMARHLAARWAVKEAVVKAWSAALYGTPPPISPDLLVWSEIETVCDAWGRPAVRLSGEVARQVAATVGEGTRWNVSLSHDGDSAVAFVVLEGTPTG | Function: Transfers the 4'-phosphopantetheine moiety from coenzyme A to a Ser of acyl-carrier-protein.
Catalytic Activity: apo-[ACP] + CoA = adenosine 3',5'-bisphosphate + H(+) + holo-[ACP]
EC: 2.7.8.7
Subcellular Location: Cytoplasm
Sequence Length: 185
Sequence Mass (Da): 19081
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A0A6A0HBR6 | MTETYYGRKILIADREQVEVGAGDLLQSADVQDVALLVVGDPLSATTHSDLMLRAQALGIPVQVLSNASVLTSAATTGLKLERLGEVVSIPYWEENWQPESFYDKICTNLKHGLHTLCLLDIKVKEQTVENIIKNRKLFEPPRFMRTHEAAKQLLAIIEKREQQDNSCTEGTLRRDTTCIACVRLGTERQKNLVMTLQESAEADLGEPLHSMVVCAPLSDAETRDAAALASWYQGATKPASSCAGRLHLIGMGLTISDITVKGVEILLKTNHVFLDKASRQILNVLLGSRSIREIFSDVFNPDELDRLDAAFDVNKPSVS... | Pathway: Protein modification; peptidyl-diphthamide biosynthesis.
Function: S-adenosyl-L-methionine-dependent methyltransferase that catalyzes four methylations of the modified target histidine residue in translation elongation factor 2 (EF-2), to form an intermediate called diphthine methyl ester. The four successive ... |
A0A938WLP8 | MRQRLLSAIGMAAMVWIGASAQSDVTLTRNGDSYKMSNGTVSVSIGSNGRISEMTFRGGPNVLASNGVYFDYTADKNDNLNPTTSKIVRQTADYAEVVFSNTTADLRFEQGFIMRKGVNGVYVYVVANGTPTSSGVNLREARVCTRLNSSFVNGYVDEVMNGKIPTNAEMAVAEREENVVQDATYRMADGSIYTKYDWAQYVVRDSLHGLMNVNSGVWNIPCSHEWLNGGPMRQELTVHATSKSPITIQMLQGEHFGASSQRYEDGERKIYGPFLIYLNRGSQQQMIADAKRQASQQQAEWPFAWFDHELYPLDRSTVRG... | Catalytic Activity: Endotype eliminative cleavage of L-alpha-rhamnopyranosyl-(1->4)-alpha-D-galactopyranosyluronic acid bonds of rhamnogalacturonan I domains in ramified hairy regions of pectin leaving L-rhamnopyranose at the reducing end and 4-deoxy-4,5-unsaturated D-galactopyranosyluronic acid at the non-reducing end... |
A0A9E3K221 | ILDQWSMLQTVTGVGHSQYNGDVPINTTLTDGKYRMIDDSRGTGGTFGAMAITNANHGTSAGSVYVNDTNTWGDGKQYVAGGPTTNANGQTAAVNAMWGLMNTYDTLKNVFNWLSLDGHNTATYIAAHVNTAYDNAYYSDACRCMFIGDGASFNSLGSIDVIGHEMGHGVTAATSNLTYSGESGGLNESSSDINGEAVEAYARGGGKGDSIPLAGNDWVMGKEISKSGTPLRWMYRPSKDGSSPDAWSNSIKRLDVHYSSGPNNRMFYFLAQGSNADKASDYYSKYLVKTPAAMTGIGLDKAFRIWFKANTTKFTSSTNY... | Function: Extracellular zinc metalloprotease.
EC: 3.4.24.-
Subcellular Location: Secreted
Sequence Length: 370
Sequence Mass (Da): 39355
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A0A7X8SPM1 | MKIGILGIGGIGGFIASKMLQSKDKDEIILITKERQKRAIISEGLTLLDGDKSEKVHVIDVVSTNDKIEKLDILFIAIKSYDLKESLKNIRSSISDKTLIIPLLNGISIKNIICDTLNLSERQVIDGCIYIISNKINDSTIRHVGGPGRIIIGGENQTALNTLQTVLEKYDLDIGYHKDIKEILWKKFLFVSPISAISTANGVTFGALQDDAYLMIQCQSLMEEVILIAKKLGINLSHEDIKNTIEMLKKFPYEAKSSFQLDIEKNQKNEKNILIDDVISLGEKLDLDVINYISINQQIMDRYLCVQ | Pathway: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantoate from 3-methyl-2-oxobutanoate: step 2/2.
Function: Catalyzes the NADPH-dependent reduction of ketopantoate into pantoic acid.
EC: 1.1.1.169
Catalytic Activity: (R)-pantoate + NADP(+) = 2-dehydropantoate + H(+) + NADPH
Sequence Length: 307
Sequen... |
A0A7X7PBR7 | YESRPNVTIDAAALCLKSGNATILRGGSEAFHSNQALGAIIQEGLAQAGLPAHAVQVVDTTDRAAVGEMVTMTEYIDVIVPRGGKGLIERLSREARVPLIKHLDGNCHLYIDKAADPEKAHAIAVNAKTYRYGICGAMETLLVHADVAATILPRIAATLAEKGVELRGCERARAILPTALPATEEDWRTEYLEPILAIRIVDDLDQAVEHIERYSSQHTESIVTEDLGAATRFQREVDSSSVYVNLPTCFADGFEYGLGAEIGISTNRLHARGPVGLEGLTTMKWVLTGEGQLRG | Pathway: Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate 5-semialdehyde from L-glutamate: step 2/2.
Function: Catalyzes the NADPH-dependent reduction of L-glutamate 5-phosphate into L-glutamate 5-semialdehyde and phosphate. The product spontaneously undergoes cyclization to form 1-pyrroline-5-carboxylate.
... |
A0A0E9NDL6 | MSFRIPSLIPRVSAFARPSHIARPLRSAVRHASTTPPPPPRFPNFPNGRPRMSAEQAKNNESFIYYTLSVFIGAFGVTYAVVPLYRLICQTTGFAGTPNTDASRFTPDKLIPVKDAKRIKVTFVGTVSDALQWTFTPQQREVHVLPGETALAFFTATNRSSEDIIGIATYNVNPQQAAQYFSKIQCFCFEEQRLLAGETIDMPIFFFIDPDFADDPLMKDIRTVTLSYTFFKARYDNGMLVPATN | Function: Exerts its effect at some terminal stage of cytochrome c oxidase synthesis, probably by being involved in the insertion of the copper B into subunit I.
Subcellular Location: Mitochondrion inner membrane
Sequence Length: 245
Sequence Mass (Da): 27493
Location Topology: Single-pass membrane protein
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A0A931PRT3 | MTTRGKFARVLLKLSGEALGGEQGFGRDAETFQKLAEQISRARKQSKTQIAIVVGGGNIIRGSDIKGMDRVVADQIGMLATVQNAMALAEALEERDIPTIIQSAVQVAYARPINPKKARAYLDRGYIVIFAGGTGNPFVTTDTAAAVRAREIHADVLLKATNVEGVFTADPKKDKSAKLLKRVSYDEAYARGLEVMDLASLALCKEHSLPVIVFDLYKPKNLEKAIAGEPVGTWVSA | Pathway: Pyrimidine metabolism; CTP biosynthesis via de novo pathway; UDP from UMP (UMPK route): step 1/1.
Function: Catalyzes the reversible phosphorylation of UMP to UDP.
Catalytic Activity: ATP + UMP = ADP + UDP
EC: 2.7.4.22
Subcellular Location: Cytoplasm
Sequence Length: 237
Sequence Mass (Da): 25544
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A0A931LPT8 | MPEPKLTSPTVIRHLLGQYQIHLKKSLGQNFLADENILELIVTHAQLSRDDIVIEIGAGMGTLTHKLSNEAKHIVAVEIDSRLMPLLTENLRHCSNVTLVNQDFLDVNLADLVRAQRATSVKIVGNLPYKITSPILERLIAHRSFIESACVMVQREVADKLIAEPGNREASAVTIFAQAYANVEFLIKVSHHVFFPKPEVDSALLRLNFLKEPRFRAPEEIFFRVVRAAFNLRRKTLKKALAQSPLSGLPSEIILKALVEAQIDPERRGETLSIDEFDRVAMALSKDYLARSVFF | Function: Specifically dimethylates two adjacent adenosines (A1518 and A1519) in the loop of a conserved hairpin near the 3'-end of 16S rRNA in the 30S particle. May play a critical role in biogenesis of 30S subunits.
Catalytic Activity: adenosine(1518)/adenosine(1519) in 16S rRNA + 4 S-adenosyl-L-methionine = 4 H(+) +... |
A0A834NA71 | MVSNTFWMLLTVFLTIFANSGSALRCWECSSHMNAMCGDPMNSTDHQAMFHVKECGRGPYASSKPICRKMVKRDGGDRVVIRSCAIPNHDETDITDGPCSPLMTNGRDMVESCHICSTDLCNSASGLLTTQSLYIAGLILIGYRFFESNYNRVM | Function: Required for homeostatic regulation of sleep under normal conditions and after sleep deprivation. Important regulator of the Sh K(+) channel, acting as a signaling molecule that connects sleep drive to lowered membrane excitability, possibly by enhancing K(+) channel activity and thus reducing neuronal excita... |
A0A1G0LR29 | MLTIAAPEELRALVRDRAKAGARVGFVPTMGYLHEGHLALVAEAQRQADVVVMSIFVNPLQFGPTEDFASYPRDPGRDTQRAQQAGVDLLWMPAREQMYPASPAVTVAPGPVGAILEGAVRPGHFAGVLTVVSKLFAIVDPDVAVFGRKDAQQAALVRMMIRDLSLRVRLIVAPTVRAHDGLALSSRNIYLTTEQRAQALALPRALA | Pathway: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantothenate from (R)-pantoate and beta-alanine: step 1/1.
EC: 6.3.2.1
Catalytic Activity: (R)-pantoate + ATP + beta-alanine = (R)-pantothenate + AMP + diphosphate + H(+)
Sequence Length: 207
Sequence Mass (Da): 22325
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E3NTF6 | MQWTTAYTESVHTYANTINTHEGGTHEEGFRGALTTLVNRYAREKNILREKDDNLSGDDVREGLTAVISVKLGEPQFEGQTKTKLGNTEAKAFVQKVVGDQLGDWFERNPGPAKDIIRKAIQAATARLAARKARETARRKGLLESGGMPGKLSDCTSKDPTISEIFIVEGDSAGGSAKTGRNPHTQAILPLRGKILNVEKARLDRALNNTEVQAMITAFGAGIGEEFDPEKARYHKIVLMADADVDGQHITTLLLTLLFRYMRPLIDLGYVYLAQPPLYRIKWANAEHEYVFSDAERDERLTAGSQAGRRLVKESGVQRY... | Function: Control of topological states of DNA by transient breakage and subsequent rejoining of DNA strands. Topoisomerase II makes double-strand breaks.
EC: 5.6.2.2
Catalytic Activity: ATP-dependent breakage, passage and rejoining of double-stranded DNA.
Sequence Length: 875
Sequence Mass (Da): 96813
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A0A368A5L1 | MSNKILIDASHKEETRVVVTRGNRIEEIDFESEHKKQLKGNIYLARITRVEPSLQAAFVEYGGNRHGFLAFSEIHPDYYQIPVTDRLALLEAEEQATKLDNENSDFIISEIEQKKLGKEKSRTRTVVSDVVSEYPNSDRNDTLAVDNTNSEDTVEFIGAEDALEEVPTQRVQRRNYRIQEVIKRRQILLVQIMKEERGNKGAALTTYLSLAGRYSVLMPNTARGGGISRKITSIADRKRLREILKDLSVPKGMGIILRTAGANRTKAEVKRDYEYLMRLWENVRNLTLNSIAPSLVYEESSLIKRSIRDLYNKDIDEILV... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Endoribonuclease that plays a central role in RNA processing and decay. Required for the maturation of 5S and 16S rRNAs and the majority of tRNAs. Also involved in the degradation of most mRNAs.
EC: 3.1.26.12
Catalytic Activity: Endonucleolytic cleavage of single-stra... |
A0A5C5V7N4 | MSSMPPGPDHPAMSVAELTAQIKGLVEESFPSVWVTGEVSNFARPASGHCYFTLKDQHAQIRAVVWKGSAARLKFDLTDGLEIVCHGRLDLYAPRGSYQLVIDQAQPQGVGSLELALRQLKEKLTAEGLFDADRKRPLPSFPRRVGFVTSPTGAAIRDFLEVARRRWSGTQVLVIPTRVQGDGAAEEIAAAVQLANRVRPALDVLVVGRGGGSIEDLWCFNEAPVVRAVAASEIPTVSAVGHEIDVTLCDLAADVRAFTPSEAAERVIPSGDEFAGRVQTLHNRLHGTARRATQLRRQRLEALASRRPLARPYSLIQDHS... | 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... |
A0A1Q3RDA8 | MNKIIIIAGPTAVGKTDLSIELAKTLSTEIISADSVQIYEKLDIGSAKPTLEEMAGIKHHLIDVVSPFDSFSVSDYAKAAKAAIKGLHDQGKIPVIVGGTGLYINALLYEMDFSESAADPEFREAMEKLARESGGEVLYQRLCDIDPDAAKRVHPNNLKRVIRALEINHITGRPMADFASDPKPTEDYDVLLFGLTRDREQLYDRINRRVHIIFEQGLLKEVDGLKNLGLDDSFQSMQGIGYKEVLTYYKGGMTYDELVDAIQQGSRHYAKRQFTWFKRYDNIKWLDLDELSTGDAISEILKYL | 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... |
A0A5B8ELR4 | MRVCIVGAGAIGGWIGTRLAASGAAEVSALARGATLGALRTHGWRLDQDGVRTTAPARVSESTADLGEQDVVVLTVKATALAAVVDRLEPLLGADTVVLPFLNGVPWWFTHGSDLGSLESVDPGGRVAAAVPFERVLGGVVHASCAAVEPGLVRHHLGNGLIVGEPGGGASARVDAVAGVLGAAGFDVTSSTDVRRDAWYKLWGNMTMNPVTALTGATGDRVLDDPLVRGLCSSAMLEAQRIGDLVGCPVRETPEDRHVVTSRLGALRTSMLLDVEAGRPLELDALIGAVHELGRRLDVPTPAVDAIFGLTRLFGRVHGL... | Pathway: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantoate from 3-methyl-2-oxobutanoate: step 2/2.
Function: Catalyzes the NADPH-dependent reduction of ketopantoate into pantoic acid.
EC: 1.1.1.169
Catalytic Activity: (R)-pantoate + NADP(+) = 2-dehydropantoate + H(+) + NADPH
Sequence Length: 326
Sequen... |
J0TPJ1 | MQEIGILENLQKSLALKEGMLSYEMLGKSLSYNPYLPRVIPQTKNCVFVTPDEVLEKLLKENTHTDCVIVNFKGLYEIGAPSVFDLEVLGLLRRHASSLIVHEDFFISHYQLLESLVQGSDGVILDEELLKEDLKGMVEFAWRLGLGVFVETHKPDYTHLKDLGVLGVLEISPHSYNQKKVVFLD | Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 4/5.
EC: 4.1.1.48
Catalytic Activity: 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate + H(+) = (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + CO2 + H2O
Sequence Length: 185
Sequence Mass (Da): 20973
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A0A662EYK6 | MSDAIHRPVMRTEAVRFLAPDRGGIYVDGTVGLGGHAAAILAAGPEVRLIGIDRDPQALRYAAARLAQFGDRVRLVHGNYRDLAEILAGLGIEAIDGFLLDLGLSSLQLDAPERGFSFRADGPLDMRMDPTQGRSAADLVNAASVEELARILRDYGEERFAGRIARAIVAARPIETTRALAEIVRRAIPRRFHERRIDPATRTFQALRIAVNDELRNLQDGLAAGFAALRPGGVIVVISFHSLEDRIVKRFFRKLATPRYESLAPGPPLPPQAEVLTKKPLRPSEEEIGENPRARSAKLRACRKL | Function: Specifically methylates the N4 position of cytidine in position 1402 (C1402) of 16S rRNA.
Catalytic Activity: cytidine(1402) in 16S rRNA + S-adenosyl-L-methionine = H(+) + N(4)-methylcytidine(1402) in 16S rRNA + S-adenosyl-L-homocysteine
EC: 2.1.1.199
Subcellular Location: Cytoplasm
Sequence Length: 305
Seque... |
A0A662ES82 | MLLAVDIGNLQVGLGVYDGREWRGRFRIRAVPEKTADEYTVLLEGLFSRVGISPRKISGAIIASVVPPLTETFRKLCKGSFGITALVVGPGVRTGLELRVDHPSEVGPDLVADAVAAYERCRSACIAVDFATATTFTCVNEKGALVGVSIAPGLKVAAEALAQRAAKLPKIPLTPPRRAIGKNTQEALQSGVILGGVGMVEGLIRALSAELGGNARVIATGPYAEPIMGLTELIHEHDPWLTLEGLRIIAERNRYPPAPR | 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... |
A0A519PFS9 | MNLNATLFAQFAVFFILALFTMKFVWPPLMKALDERAERIANGLAAADRGKADLAAAEKRVQAEMAGARDEVQKRIADAEKRAAQIIEAAKATAAEEAARIVAAANADAEQQ | Function: Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0). The b'-subunit is a diverged and duplicated form of b found in plants and photosynthetic bacteria.
Subcellular Location: Membrane
Sequence Length: 112
Sequence Mass (Da): 12060
Location Topology: Single-pass membrane p... |
A0A2X4NAW7 | METEIINISKSNNKEEIYNKLITYYKDNKLIAIPTETVYGLSADAMSDEAVCKIYEAKGRPSDNPLIVHFYEMNQLNDIVDYQDERVDKLIENFWPGPMTLILNAKENNGISKKVSAGLSTLAVRMPSNKTARQILKETKVLLAAPSANTSGKPSPTKFEHVYHDLNGKIDVIIEDEQSDIGLESTVIDCTRTPLVIARPGEITKEDIEGILGLGSVKYNDEVMVDTQTPIAPGMKYRHYSPEAELLYYEDSLEKALEFLKTKNKKTGFITYKSNEHLFENLNISVKYLADNEKSVEQSNKNLYNILREFDEEKVEEIYI... | 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... |
E3NV34 | MFETKNVDSVQSMNSVLMNIKDFRQSMEMLTKYDWVPIPIAYPQVVFLAVRVYFIICLISRQYLLSAPPTEAQSIVRIMTILQFVFFVGWMKVAEALLNPLGEDDDDFECNWLIDRNMSTGIEIVDTLS | Function: Forms chloride channels.
Subcellular Location: Cell membrane
Sequence Length: 129
Sequence Mass (Da): 14924
Location Topology: Multi-pass membrane protein
|
A0A1Q3RGM3 | MNEQMKITPRYLHGILSMPPSKSISHRAIICAALSQGTSRVENLVLSEDIKASIAAMIQFGAKIELDYNPISNRYTANIWGIKEAVDRPLTIDCRESGSTARFLIPFFQLTKSKVTFVGAEGLMKRPFGPYLRLFESQKLQYQSHSGALPITVSGSWQPGEYELVGNVSSQFITGLLFVLPLLEGDSQIRIKPPFESVDYVKLTISCLKKFGIDIIWKDDLTLWINGHQSYHASDYWVEGDYSQAAFWLVANSIGSHIVIEGLNTASEQGDKRIIEIIEQVTKQSESEGYLEIDVSQCPDLVPIIAVLCTVKPGLFKITG... | Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 6/7.
Function: Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-ph... |
A0A3M0G889 | MRVVITRVAEASVTVDGDLVSQLPRPGLLVLVGIARGDGPQDARAVAAKTWSLRILRDERSASDTNAPILVISQFTLHAATRRGRRPSWSAAASGDVSEPLVELFCRELEALGAEVGRGRFGAEMQVASVNDGPITILIDTQDWR | Function: An aminoacyl-tRNA editing enzyme that deacylates mischarged D-aminoacyl-tRNAs. Also deacylates mischarged glycyl-tRNA(Ala), protecting cells against glycine mischarging by AlaRS. Acts via tRNA-based rather than protein-based catalysis; rejects L-amino acids rather than detecting D-amino acids in the active si... |
A0A1F3J3C0 | MRISYDISLKQYNTFGIDVKAVCMAEIENADDLIALSESSLPEPLFCIGQGSNLLFTRDFNGTLIRMNNTGWGVISSQGDEVTIRANAGCIWDELVEQTLIKGYFGFENLSHIPGTVGSTPVQNIGAYGAEASQFIVSVHAFDRESQKFFDIENKDCDFGYRHSIFKSKPAWIVVSVDYRLKSVAATSTHYKAVETFLQENNLDGSDPMVVRKAVIAIRESKLPDYKQIGNAGSFFRNPVVEKKVFDQLHKKFPEMPFYAEADEKFKIPAAWLIEKSGWKGFQGFHAGVHDKQPLILINLGGASGQEIKMLAEEIQTSIK... | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Cell wall formation.
Catalytic Activity: NADP(+) + UDP-N-acetyl-alpha-D-muramate = H(+) + NADPH + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine
EC: 1.3.1.98
Subcellular Location: Cytoplasm
Sequence Length: 334
Sequence Mass (Da): 37349
|
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