ids stringlengths 6 10 | seqs stringlengths 16 1.02k | texts stringlengths 117 4.4k |
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A0A7V4JF15 | MMLSLSPSIEAAEGRYGLLKDQAVALGVGLILLVIAWRLDYRRLRKLSLVAFGVILLSLLLVHIPGVAMSKGGSRSWIGVGSLSYQPSEFAKIAVILFGAHILSSPRVADRRFWSYMWPFGVLGLLACASVLLEGDLGTAVIIAGLLLGLLWMGGMRFLHWLLVAGGGLAVVAVATLVSEERTSRVLSFLNPFADPYDSGFQLVQSLVALGRGGLFGVGAGQSVQKFQYLPQAHTDMVYAIIGEEFGLLGAGLVIVFFALFCVGCWHLACRAADPMGRLLISGCGLLVAFQAVINIGGVIGALPLTGVPLPFVSYGGNSL... | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Catalytic Activity: [GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)](n)-di-trans,octa-cis-undecaprenyl diphosphate + beta-D-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-di-trans,octa-cis-undecaprenyl diphosphate = [GlcNAc-(1->4)-... |
A0A7G7CRY7 | MKAWHLLLHNVFSLGNSASWIISIILLVITVRTLIAPITWMSIRSGRVSALMRPEKEAIEARYAEATTKEEVAARDDAIRELNKRYNFKPAAGCIPPLIMFPVFIGLYRVILYMASPDNHGADANVGALNPQEIASFREAVYQGIPLTAFPAMPDDWAASMGVTGEQVYNTILPLLVPAIIFTVINMMASLYRSYWTMDFTNTIMRRMYYVMIILGVVFFPWMLWNLATAGPVPLAIVIYWFTSNLYTLIQTLFFNVLLHFKLPLADEHHEHRKGSLERFKQARRDRKDLSRRKRRALLSSSKRAEIKAEEEQRQQELAA... | Function: Required for the insertion and/or proper folding and/or complex formation of integral membrane proteins into the membrane. Involved in integration of membrane proteins that insert both dependently and independently of the Sec translocase complex, as well as at least some lipoproteins. Aids folding of multispa... |
A0A524MAK8 | MGKCWARLNPNSTIGHVALGHGDYGDVLALQRTLHAKRCAGELGDLLLSVEHNPVFTLGRSGMHDHILVAEDTLKQQGIQIHEIERGGDITYHGPGQLVVYPIFDLRGFGKDIHRFIWSLEEAIIQTLSELGIGSARNDGFPGVWVGARKIASIGVYVKNWVTYHGLALNVDVNQAHFRMIRPCGLSIETVSLNDIRDLHMSVAEVGAIVVRQLGALLEKDIVTMDRKEVI | 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... |
A0A6I2W671 | MSEILIVSGTGTDVGKTIVTAAIAANVIRAGKSVSVVKPGQTGVTGDEPGDLAVVAELTSSIEGAADRLLLHEYGRYEPPLAPATAARISGQPPLILADVVASIKGLTSDFIVVEGAGGLLVKYSDEPVWTIADLARELNAEVLLVVASGLGTLHHTAATLEALATRGLTTPGLVIGQWPVEPSLAEKTNVADLQDLGAPLVGAIPAQAGLSGEFAHIAATSLHPRLGGTFDEADFTHTHTQELNR | Pathway: Cofactor biosynthesis; biotin biosynthesis; biotin from 7,8-diaminononanoate: step 1/2.
Function: Catalyzes a mechanistically unusual reaction, the ATP-dependent insertion of CO2 between the N7 and N8 nitrogen atoms of 7,8-diaminopelargonic acid (DAPA, also called 7,8-diammoniononanoate) to form a ureido ring.... |
A0A538DWU4 | MTTSARIERPRGTHDVVPSEQPTWRRVASEAERLCELYGYRPIITPVFEDTALFERTSGTGSDVVQKEMYTFEDRAGRSLTLRPEATAPICRAYVEHGMHREPQPAKLYTIGPMYRYAAPQRGRFREHWQLSVEAIGSEDPALDAELIELYHTLLGNVGVGDFRLELNSIGCRECRPAYVRELRAWLEANLDRLDEATREKAETSPLRVFDNLQAKPRATQEALAEAPKIGESLCDACRDHFSAVRAQLDAYGVSYELXRARRGRPERALRRWSLRRSDRRDRRSGQSRSGVRRGPRAPRSRGRARRCGGAAAPGRRLLR... | Function: Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Catalytic Activity: ATP + L... |
A0A6I2Y5S2 | MSVSVTMPALGESVTEGTVTRWLKQVGDTVAADEPLVEVSTDKVDTEIPSPAAGVLLAIRVGEDETIAVGAELAVIGEASESAGSPAASTMAAEETVIAAPEPAAPAAPAAPAPSPAASSATIPAASGATIAITLPALGESVTEGTVTRWLKQVGDTVAADEPILEISTDKVDTEIPAPASGTLVAINVAEDTTVAVGTELGLIATGAAAPAATPAPAPAPAAPPVSASAPAVTAAVASEPADNTDAYVTPLVRRLAAQEGIDLSTVTGTGVGGRVRKQDVLAAAAARSEQAGTASAPSVPSAPAQAPAPGAPVVSPLRG... | Pathway: Amino-acid degradation; L-lysine degradation via saccharopine pathway; glutaryl-CoA from L-lysine: step 6/6.
Function: E2 component of the 2-oxoglutarate dehydrogenase (OGDH) complex which catalyzes the second step in the conversion of 2-oxoglutarate to succinyl-CoA and CO(2).
EC: 2.3.1.61
Catalytic Activity: ... |
A0A7J9WVF0 | MTDASDSDPARLLVGEIGKPHGTDGEAYMVAISDDPHRFDPGSRLVHGNGTPLVVEGSRIHRGTRLLVKFEGVDSRNAAELLRGPVYVNEDQRRDLEEGHYWQHELVGCRVLTVAGNDVGEVSGVVEGPAQDLISVAHEDKTFLVPLVKEIVVDVDIDARRVTIAPPAGLLD | Function: An accessory protein needed during the final step in the assembly of 30S ribosomal subunit, possibly for assembly of the head region. Essential for efficient processing of 16S rRNA. May be needed both before and after RbfA during the maturation of 16S rRNA. It has affinity for free ribosomal 30S subunits but ... |
A0A524L0D2 | MQDLNKLQKAFNEKFTDTGLAKGTFSAPGRVNLIGGHTDYNEGFVLPIAIEKKIVMLGQLRRDRLVQIFDLGYKAEAKFSLDNLSPYKKDTWVNYLMGAIDEMQKAGYPLQGANLIFISDIPKGAGLSSSAALEVVTALTMEKLNSLEIEPAKMARLCQQAENNFVGVNCGIMDQYVSRLGRKNYALFIDCRSNDYELIPFKNHNYQIVICNSRIQRGLVNSEYNRRREECKSAAEFFAHRLGSKIRTLRDVTIEECKQYQEYLPEPIGRRARHIISENYRVQNGAQALREGNFSAFGQLMIESHRSLKDDYEVSCAELD... | Pathway: Carbohydrate metabolism; galactose metabolism.
Function: Catalyzes the transfer of the gamma-phosphate of ATP to D-galactose to form alpha-D-galactose-1-phosphate (Gal-1-P).
Catalytic Activity: alpha-D-galactose + ATP = ADP + alpha-D-galactose 1-phosphate + H(+)
EC: 2.7.1.6
Subcellular Location: Cytoplasm
Sequ... |
G2QAE3 | MIGTRLAGLGLLVAGVCSASASTSAIELRSAERPLSECPGYQAVNVKTSATGLTADLRLAGSPCNTYGTDLEKLRLEVTYETENRLHVKIRDADELVYQVPESVFPRPKADGISAKKSALTFKYKANPFSFSVSRTKTGEVLFDTSAAPLVFQSEYLRLRTKLPENPNLYGLGEHSDPFRLNTTNYIRTLWSQDSYSTPEGANLYGNHPVYFEHRKSGTHGVFFLNSNGMDIKIDKNPQHLEYNTLGGVFDFYFVAGPSPVDVARQYAEISGLPAPVPYWSFGFHNCRYGYRDVYDVAEMIYNYSAARIPLETSWIDIDY... | Function: Glucosidase involved in the degradation of cellulosic biomass. Has both alpha- and beta-glucosidase activity.
EC: 3.2.1.20
Catalytic Activity: Hydrolysis of terminal, non-reducing (1->4)-linked alpha-D-glucose residues with release of alpha-D-glucose.
Sequence Length: 921
Sequence Mass (Da): 102665
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A0A3A8ZGW9 | MKSVINSFIIAIAMYSRIPMPKITWSQKNMKYSLCFFPVVGAVIGALIYLWGRVCMACGFGQVCFALVGTVIPMIITGEIHLDGLMDTADALHSYEGKEKKLEILKDPHVGAFAVMALVGYCILYAAGLTQIWKTDHLLLLAFGFVISRCLSGLSLVWFRSARKDGLLYTFSSTAHKQTVRVVLVLILGGCFISLILISPVIGAVMALAAMWVWTYYYYMSRKLFGGITGDLAGYFLSLCELSSVLIIGFMGRVL | 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... |
A0A3D3Q9Q6 | MQKQKTTPQDRQEAAKQRRAVAVEGRKRTPPSVFLKEVRLELKKVAWPTRTELWSYTAVVLVAVLFLASLVFGLDFVFSKAIFNLLHAGG | 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: 90
Sequence Mass (Da): 10185
Location Topology: Single-pass membrane protein
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A0A7C3X872 | MAGDRRGVLFLVGTPIGNLEDITLRALRVLREADLIAAEDTRRARKLLSRYDIHTPLISYHGHNERERAEALAREVEAGKLVALVSDAGMPGVSDPGFRAVEECSRRGLDVEVIPGPSSLTAALAVSGLPLSRFRYEGFLPASRAKRRSRLLNLLKEGEALVIYEAPHRILETLGDLAELAPQRRVVLAREMTKLHEEVLRGTAAELLQALGGGKPRGEFVLVVAPGGGMETPPLEELAEEVAALVRSGEPTREAVRAVAKRHGIPQRDVYRAWLEHRETDQGAG | Function: Catalyzes the 2'-O-methylation of the ribose of cytidine 1402 (C1402) in 16S rRNA.
Catalytic Activity: cytidine(1402) in 16S rRNA + S-adenosyl-L-methionine = 2'-O-methylcytidine(1402) in 16S rRNA + H(+) + S-adenosyl-L-homocysteine
EC: 2.1.1.198
Subcellular Location: Cytoplasm
Sequence Length: 285
Sequence Mas... |
A0A538MAS7 | MVLPARGLRTVAGGAPPPPGPLGSGGGGARAGARAAAGLRPLPEPPYAVDRPGHLRHDRAGSLIADVCGRGWPRGAGRRRGAAAVIQTPALEFRPILPEILLCTFAIVGMLYEAFARRPDPVPHLAIATVGILAAVVSASALWHWTGSPYVMGDTVAVDKFSVVARFVLLGAALVGCLYYAHYGSRDPGSFRGEFYPLTLFATAGMTLITAANDLIVIFLALELLSLSLYVLTGITGRRRASEAAMKYLLLGAFSSAFFLYGIAMAYGAATSTKIVGVAAPGIVQALAGQTGSRALALLAMALLVVGFGFKVSAAPFHMW... | 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 a menaquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrog... |
A0A4P7RCC1 | MELTDIAVDASQQSQEKDYFITRNGKRYAGVHLLIDLHGASHLSDIAYIEKTMRRCVEASRATLLHIHLHRFEPDGVSGVAVLAESHISVHTWPESRYAAFDVFMCGDTSPEVCIEIMREAFEAERVDVQEILRGEVHE | PTM: Is synthesized initially as an inactive proenzyme. Formation of the active enzyme involves a self-maturation process in which the active site pyruvoyl group is generated from an internal serine residue via an autocatalytic post-translational modification. Two non-identical subunits are generated from the proenzyme... |
A0A4P5S4N1 | MLPIMLDLRDRKVLVVGGGRIATRKAHALVHEGALVTVIALSITEELREMHNVNVVERAYSTGDALKFQLVITATGDHVVDQQIYDEANAAGIWVNSADDPQRCSFYLAATHRDGNVVIAVSTEGKSPALATHLRNQIAATLPQNLGQAALELSRQRAELHEAGVSTESLDWSQRVIDALD | Pathway: Porphyrin-containing compound metabolism; siroheme biosynthesis; sirohydrochlorin from precorrin-2: step 1/1.
EC: 1.3.1.76
Catalytic Activity: NAD(+) + precorrin-2 = 2 H(+) + NADH + sirohydrochlorin
Sequence Length: 181
Sequence Mass (Da): 19655
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A0A2E7T281 | MTQVLSTYLDDLTEPDQDARTELTTRLDDILRPAGALQRLDELAVFMAGWQTSSVPRVDKPTILIFASDHGVAAAGVSAYPSSVTEAMMSAFESGLSTVNAFARISGATVNAVDVGIGRPTGDIRFEPAMTETRFLEALNCGREAVSASDSDLLVLGEMGIGNTTSSAAISAALLGGNVSEWVGRGTGVNDEGLRRKRDAVQQAVERIDSAEPGEILRQLGGAEIVAIAGAIIEARHRRIPVVLDGFVVAAAAAPLYAYNRLALQHCLAAHQSAEIGHRRLLEYMGLEPLLDLNFRLGEASGGAAVIPLIAMACAAANDV... | Pathway: Nucleoside biosynthesis; alpha-ribazole biosynthesis; alpha-ribazole from 5,6-dimethylbenzimidazole: step 1/2.
Function: Catalyzes the synthesis of alpha-ribazole-5'-phosphate from nicotinate mononucleotide (NAMN) and 5,6-dimethylbenzimidazole (DMB).
EC: 2.4.2.21
Catalytic Activity: 5,6-dimethylbenzimidazole +... |
A0A803YNC7 | PHPLLTALLLLSEVVDLQTGLSEFSVLQRRLKHGWNEFSVDATEPIWKKYLDQFKNPLILLLLASALVSVITKEYEDAASITMAVLIVVTVAFIQEYRSEKSLEELNKLVPPECNCLREGKLQHLLARELVPGDIIYLSVGDRVPADLRLIEVTDLLVDESSFTGEAEPCNKTDGVLLEAGDITTLSNVVFMGTLVRYGKGKGVVIGTGENSQFGEVFKMMQAEETPKTPLQKSMDRLGKQLTLFSFGIIGLIMLIGWLQGKHLLSMFTIGVSLAVAAIPEGLPIVVTVTLVLGVLRMAKKRVIVKKLPIVETLGCCNVI... | Function: Catalyzes the hydrolysis of ATP coupled with the transport of calcium.
Catalytic Activity: ATP + Ca(2+)(in) + H2O = ADP + Ca(2+)(out) + H(+) + phosphate
EC: 7.2.2.10
Subcellular Location: Membrane
Sequence Length: 899
Sequence Mass (Da): 98395
Location Topology: Multi-pass membrane protein
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A0A7X7ZX88 | MKKDGRRMSGKPPKRDQVAAEDRWAVEAIFKTDEEWESAFRATEDYGRAFQAWAGRLGESPESLAGAIAEMLAQQRALEKLGLYAGMRQDEDLSNALHSSMDDRCTARRNEVAAAQSFFMPELLSIDPAVMAEWLRSPVLEGYATWLEEMLRYRPHTLSEPEEKLLAMSGDALQGFHAGFGKLNNVDMPARLPEITDQNGRRTKLTNSNLVPLMEESDPGVRRAAFDGYYRELSGNLNTAAALLNGQVKSHIFMAKARRHASALEASLFHDLVSTEVYRALIDAVHNRLPVMHGYYAAKKSALGLDTLSPCDLYLPAVRY... | Cofactor: Binds 1 zinc ion.
Function: Has oligopeptidase activity and degrades a variety of small bioactive peptides.
EC: 3.4.24.-
Sequence Length: 610
Sequence Mass (Da): 68530
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A0A7K1ES27 | MLAQQNRLRKASEFALATKGKRVAGENFLLYVATPQHGERSGAPVKVGLIVGKNVGNSVVRHRVSRQIRHAIAPHLEKFSDGTFLLFRAHPGAAKSAEGNLSGEISALVEKYFSVAR | 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... |
A0A521XP69 | MAPVNRGPGLLAPHSTACRGARSGRRWQAADVPSIPWPEARRLARAAAAPLEVVRAPLDTALGAVLAEPLAARTDLPPFDAAAMDGWAVSGIGPWEALPARDRGSRYDEPQPLLDGTAIPVHTGEQLPPGCSGVLRREQAVVEQTSYGPRLLVGDADTATPSGRPGYVEPGTDVRPRGQECREGDVLLEPGGVVTPAVVGLAAAAGHDELVVVRPPVVGLLVLGDELLSSGPARHGKVRDALGPLVPAWVAALGSRCNPPIRVPDTVAELQAALDDANVDVVVTTGSTARSTADHLHTALAALGADLLVDTVAVRPGHPM... | Pathway: Cofactor biosynthesis; molybdopterin biosynthesis.
Function: Catalyzes the insertion of molybdate into adenylated molybdopterin with the concomitant release of AMP.
EC: 2.10.1.1
Catalytic Activity: adenylyl-molybdopterin + H(+) + molybdate = AMP + H2O + Mo-molybdopterin
Sequence Length: 439
Sequence Mass (Da):... |
A0A075R502 | MLEPTFQEVQHYASTHNFIPIRLTLLADQETPISLYQKCTEQAAFLLESVEGGGRWSRYSFIGLRPFLRVEAIDQQVTLLKESGEREQYNRNPMEVLRELCQQYRAPSIAEFPPLTGGAIGYLGYNTLRYVETQLPKHQNQPLDIPDMHVVFVDEMLVYDHAKQEIQCMVHIRVSEEDTEESLQIKYAKASARLVALRDHILHTPIPKDTRLQQYQLSQLDEAVKKPETSSLQSNMSLSEYKTMILKAKEYIASGDIFQVVLSQRMTMKTDVDPFAVYRMLRTTNPSPYLYYLPFGSATLVGASPEVLVKVQNKKVEVRP... | Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 1/5.
Function: Part of a heterotetrameric complex that catalyzes the two-step biosynthesis of anthranilate, an intermediate in the biosynthesis of L-tryptophan. In the first step, the glutamine-binding beta subunit (TrpG) of... |
A0A2G8JZH7 | MEFDPKEHQHIRYNPLKDDWILVSPHRMKRPWKGQTEKQVEENIPRHDPKNPLCPGATRAKGEVNPNYTSTFMFENDFPALLQEGAPAPREDDHPLLQARSAVGTCQVMCFHPWSDVTLPLMSNAEVEEVIRKWADIISDLGAKYEWVQIFENKGAVMGCSNPHPHCQERIVVENSSWLVVVPYWATWPYETMLLPKRHILRLSDLTEAEVKDLAEITKKLLTKYDNLFETTFPYSMGWHGAPTGSKLREDQSHWQLHAMYYPPLLRSATVKKFMVGYEMLAQSQRDLTAEQLILFLPWQVFWIPPLIM | Pathway: Carbohydrate metabolism; galactose metabolism.
EC: 2.7.7.12
Catalytic Activity: alpha-D-galactose 1-phosphate + UDP-alpha-D-glucose = alpha-D-glucose 1-phosphate + UDP-alpha-D-galactose
Sequence Length: 309
Sequence Mass (Da): 35937
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A0A4Y7ST13 | MATFISFSYKAFANCATLQREPLTHAGLLVAQTGMARLLNCLVSVLIFVSYFVVTVIPATTPYIERTGEDRHAYSMHSREARERQAFSLHSRTPSDGSDPQSIRSRSTGKEITTFSVRNAFASTVNVPREGTCPAPIALVGKAPKKNIWAGLTNQEAKAILAYVYGSNSGLNLTTYEKKGLWDNYVYLIEQIMPNKTDALAYIDSDGPLPDRYARVAVSFGVVEDPYYEDYIVGPLPISNKTKVEPLTYFHNKGSSKQYNYRHDDDLRSLWTSQLCEQFQDITLALLGTYINTTNATSILQGIDPLWWEEDGRVIEWVQF... | PTM: Topaquinone (TPQ) is generated by copper-dependent autoxidation of a specific tyrosyl residue.
Cofactor: Contains 1 topaquinone per subunit.
EC: 1.4.3.-
Sequence Length: 868
Sequence Mass (Da): 97775
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A0A411M5Y4 | MLYFIFGVWAGVMGLSLSVLIRLELGASGSFMGSDQIYNMIVTSHAFVMIFMFVMLVMMGGFGNYLVLLMLSILDMAFLRMNNMSFWLLVLSMVLLSLSMFMGQGSGTGWTVYLLLSMNISHSGLSVDLTIFGLHLAGASSIMASINFITTVLNMKMYGLEKVSLFSWSIMLTAILLLLSLLVLAGAITMLLFDRNFNTSFFDLVGGGDLILYQHLF | 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... |
A0A7K1BD51 | MSDLEIQLTEELRQRAAKVVPRFDLAGVVADAHTGSGPLHVRDDRQPRRWLAVAASLFLVIAAGAAIAVQVSRSETISEPTSSDQGEGTGPTDTVPTRQIIVSGESMAPTLRDGATITVEMSVDAAHVPNRFDIIALSRLDGVALPMTLLKRVIALPGEYVAFENCHVLVNGVRLDEPYVDLTQQQSDGCGADQPEMLVPDGTVFVLGDSRGRSSDSRAFGPVPLSTVDGTVLSASSS | 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: 238
Sequence Mass (Da): 25173
Location Topology: Single-pass type II membrane protein
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A0A4Q1SYK7 | MPNKMKIAIAQAGGPTAVINSSLYGFLKGFSHCDNVQVYGIYGGIAGLIDGRFIHLNHRAVGEYEWLQNVPGAALGAGRKPLSEQDIGRIILQLKEKGVSALAIVGGNGTMWSCNQIAETAREMGYNLQVIGIPKTVDNDLVETDHTPGYGSAARFVAHAVRDLAFDLESMKNFENVRVVETMGRNVGWLAASSTYFRNSPDDAPHIVCLPEIPFNMDQFLESVNKVHRRLGYAIVVVSEGLKDKHGNSVSEIELSKSRDHKVLGGVGGLVSERITTELGLSSRYENLGILQRCTHFMVSNQDRLEARMVGEKAAEALLE... | Pathway: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 3/4.
Function: Catalyzes the phosphorylation of D-fructose 6-phosphate, the first committing step of glycolysis. Uses inorganic phosphate (PPi) as phosphoryl donor instead of ATP like common ATP-depe... |
A0A161SG15 | MKILVINSGSSSIKFRLFESSTGETLAGGLLERIGLAEGRMEYRRGTDGKITTERPIPNHQAGISMVLASLTDPVSGALGSLSEIQAVGHRIVHGGERFTQPVEITNEVISEIEQNSFMAPLHNPANLLGIRAAMEMLEGVRNVAVFDTSFHQTMPPVAYVYPLTWDLYKEKGFRRYGFHGTSHQYVAERTAAMLGRPLSELNTIVCHLGNGSSITAVKQGRSIDTSLGYGTVCGVMMGTRSGDVDPAILIELMENHGMSASEVKDLVYKKSGLLGISGVSSDMRDVERAAESGNERAVLALDLFADKVRKYIGAYAVTL... | Cofactor: Mg(2+). Can also accept Mn(2+).
Pathway: Metabolic intermediate biosynthesis; acetyl-CoA biosynthesis; acetyl-CoA from acetate: step 1/2.
Function: Catalyzes the formation of acetyl phosphate from acetate and ATP. Can also catalyze the reverse reaction.
EC: 2.7.2.1
Subcellular Location: Cytoplasm
Catalytic Ac... |
A0A803XZR0 | KAEGESLWDKLDHYYRIVKSTLLLHQSPTTGLFPTKTHGDNHKAKVHDNLYCAACSWALALAYRRIDDDKGRTHELEHSAIKCMRGILYCYMRQADKVKYCSVDRIIYLCYNTVTIYICIYSACNALVNI | Pathway: Glycan biosynthesis; glycogen metabolism.
Function: Phosphorylase b kinase catalyzes the phosphorylation of serine in certain substrates, including troponin I.
Subcellular Location: Cell membrane
Sequence Length: 130
Sequence Mass (Da): 15011
Location Topology: Lipid-anchor
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A0A0F2J619 | MGIKINQNDVVVLFGPTCVGKTSLSLELAQYLNGEIINADSMQIYKHLNVCTAKPSNEQLNSVKHYLIDFLEPDEMYSCGKFATDAEAIIKELIKNQKKPLIVGGSGLYIRALTTGIFSNSEANWKLRQELLLKEKQCPGFLYDYLSRVDKDYAEKILSSDLKRTVRALEVYIETGNTMSQMQTTMTRKTLPYNFIKICLNRNRQELYEMINRRVDKMINSGLIDEIKGLLNYNMSITSKQVIGYKEVLSYLNGNVSLSEVIEQIKKATRRYAKRQLIWFRKETNTKWVDISGIFDTNKALEKLMLELN | 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... |
A0A7J9WWE0 | MDTISIRNLRVATHIGVTEEERSEPQWVLVSVDLQTDLRPAAKSDDLEDTVNYHWATNEIAAIVRSSKCQLLEYLAGKIASQMSRIERVDGVTVEVAKESPPVEEDVGGIVVRIERT | 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... |
A0A7K0W042 | MITKKAARRVAKPVVLIAEELSPATLDALGPDFEVVNCDGADRGELLAALAKGVDAVLIRSATKMDAEAIAAAKGLKVIARAGVGLDNVDIPAATAAGVMVVNAPTSNIVSAAELAISLLLASARFISPAHAALRNGKWARSKFTGAELFEKTLGIVGFGRIGQLVAQRMQAFGMDVIAYDPYLQPARAAQLGVRLVDLDELLRTADFITIHLPKTKETANLIGVEALKKVKPSVRIVNAARGGVLDEAALYDAIVEGRVGGAGLDVFATEPCTDSPLFTLDKVVATPHLGASTDEAQERAGIAVAVSVRKALAGELVPD... | Pathway: Amino-acid biosynthesis; L-serine biosynthesis; L-serine from 3-phospho-D-glycerate: step 1/3.
EC: 1.1.1.95
Catalytic Activity: (2R)-3-phosphoglycerate + NAD(+) = 3-phosphooxypyruvate + H(+) + NADH
Sequence Length: 404
Sequence Mass (Da): 41943
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A0A803Y2Y1 | MAGLINNLLILILVLQSICLGFRSSLSVFKRYKDATRSLSSECFGSTRPVISFGLSDFALDIRMPGVTPKQSDTYLCMSVPLPVDDEAYVVDFKPHASMDTVHHMLLFGCNEPSSNENYWDCDEGICKDKSNILYAWARNAPPTRLPKGVGFRVGGETGSKFFVLQVHYGDISAFRGIIWVLNYRQPLIAGMYLMMSVNTVIPPGEKVVDADIACHYKRFPMHLFAYRVHTHRLGKVVSGYRVRNGQWTLIGRQSPQVPQAFYPVEHPVDVSYDDILAARCVFSGEGRTTETHIGGTANDEMCNFYIMYYMEAKHAVSYT... | Cofactor: Binds 2 Cu(2+) ions per subunit.
Catalytic Activity: a [peptide]-C-terminal (2S)-2-hydroxyglycine = a [peptide]-C-terminal amide + glyoxylate
Subcellular Location: Cytoplasmic vesicle
Sequence Length: 814
Sequence Mass (Da): 90513
Location Topology: Single-pass membrane protein
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A0A6I2XZZ1 | MSSPQTMTARRAQIRSLLLDTIVTSQDQLRTLLRELGVDVTQATLSRDLEAIGAAKGIAPDGCVRYVVPEMSLATRLVPAAGLDLIARVIGDVLVSAVAAENLVVLRTPPGAAMYLAGTLDRSGVPQIVGTVAGDDTVIVVTPGASEAAELCVRLLDLASGTGAEALTPYRSPGGRTASSASRRRTS | Pathway: Amino-acid biosynthesis; L-arginine biosynthesis [regulation].
Function: Regulates arginine biosynthesis genes.
Subcellular Location: Cytoplasm
Sequence Length: 187
Sequence Mass (Da): 19322
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A0A926DDV7 | MTRILTGAQMRAVDARAIDSGIPGELLMEHAGRAVFEETLRHRPISGARRYYILCGGGNNGGDGYVVARLLHEAGAAALAVTTGGRQPSGDAALMAQRLAESGCSTLSWREFGAELPTPGAQDVIVDAMLGTGSAGAPRGAAADAIRWANASPACRIAVDLPSGAVCDTGAVSEPTFRAELTVTFACEKPLHRLYPARSACGRVVVRDIGIPAALLEGEHSMLLPYDRAAFLRALPRLGPLEHKGSRGKLLIVAGSERMAGAALMAAGSALRSGCGYVTLAAPEPVLAAARVRLPEAVALPLPCDAQGFLDERAVPLLRE... | Cofactor: Binds 1 potassium ion per subunit.
Function: Bifunctional enzyme that catalyzes the epimerization of the S- and R-forms of NAD(P)HX and the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. This allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that... |
F3LFS0 | MSLNEFSLIKQFFTRQAQQSSVIKSVGDDCAILSVPHNQQLVVSMDTLVAGRHFPESATPYQIATRAFCTSVSDLAAMGATPLWFTLGLTLPSSDEQWLSQFSEGLFAAAKPFNMDLVGGDTTKGPLTITVQAHGVVEKNCALQRDAAQIGDRVFVSGYLGDGAAALALLQHKITASDELSDYLVSRFYSPVPQIALGQVIAPFTHAAIDISDGLLADAQHIADASQVSLVIDVDRLPIHPSLHDAMQKGMLGYERDAILSRALTGGDDYQLLFTVSESQLPAVNALIEDKLIHATEIGSVAANTDEQYTVQCAINGVPY... | Pathway: Cofactor biosynthesis; thiamine diphosphate biosynthesis; thiamine diphosphate from thiamine phosphate: step 1/1.
Function: Catalyzes the ATP-dependent phosphorylation of thiamine-monophosphate (TMP) to form thiamine-pyrophosphate (TPP), the active form of vitamin B1.
EC: 2.7.4.16
Catalytic Activity: ATP + thi... |
A0A851Y7Z2 | MTLTHSCNTPWADNWLVDTGDEPALHHGLSSFGKIVLEEMNCLGMIMDLAHVSVETMKVALNLSKAPMIFRHSSAYSLCPHRHNMLNDEPRMVVSARAQPQAGRGTQGSKQDSGLPLPQGSTSSLVMVNFYKAYVTCGETATLKDVAGEAGARVGGVSVPPLPAHPVPLAPTDHMDHVKKVAGAQSVGFGGDYDGVS | Catalytic Activity: an L-aminoacyl-L-amino acid + H2O = 2 an L-alpha-amino acid
EC: 3.4.13.19
Subcellular Location: Membrane
Sequence Length: 197
Sequence Mass (Da): 20890
Location Topology: Lipid-anchor
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A0A6B3W2V8 | MAQSERLRVVVDAASGDGGADTALAAASLALRDDPSLELTLVGRRNLPERLARYGLGGHDRVELLAAEQVLEMDVGAAQALRRGQGSSMQLGLEQLAAGRAAAVVSAGSTGALMALSRQVLGMLPGVERPALMAALPTADQVVWMLDLGANVGVNAQRLHEFAQMGSTVVRVVTGRPPRIGLLNIGSEPGKGPDVVREAARMIEADPQLDYAGFIEADRVIAGDVDLVVCDGFAGNVLLKTAEGMARLMFHEMRQQTGPWRGLVLKRPLQRLYDKLDPARHNGAPLLGVRGIVIKSHGGACKRGFASAIRLAALEARRNL... | 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-... |
A0A7V3FRX5 | MTLWSRRSSSRKRTTEGTTACASAGSYHARRQGRLSMNERQKNILLLALTGILLVGSWVLFWPPAEKITQGLDIQGGLSVILTAEETTGAVTAADMERAETVVRNRVDGLGVKEASIQRQGNDSILIQIPGIDNPQEALAVLGSTGQLEFVDVESITDSATKAAIIAGQDRVKLVEGTYVPFLTGDKVTNATVSQNPQTAQIEVNVTMNAEGTKIWGDYTTRSVNKQVAIVLDRTVQSAPVVNEPILDGRTAISGTFTADEAKNLKTVLETGALPVSLVPLESRIVGPTLGQDSLRQGVYAALIGLGLVCLYVLVFYRGL... | 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: 486
Sequence Mass (Da): 51083
Location... |
A0A7V9EKR5 | MAIVARTARAQTKAPLAALSSDRRSRLRWEVPKVAEGSESFDLVILGGGNAGYAAAFRANELGLSVAMVERDKVGGTCLHRGCIPTKALLHAAELTDEFRAAGDFGIIVNDEPTVDWGKVLDFKNSVVGSMYKGLQGLVKRHKVTLVEGGGRLSDPKTVVVETDDGERSLTADKAVLLATGSYPRNLPFIEADGDRVLNSSYGLIADDIPSSIVIVGGNYIGLEFASVYQSFGAKVEVVEMLERIAPAEDEEVSAALLKALKARGMSFHLGASVTGAEANDSGVEVEIETEGNKETLTADRMLVAVGRGPRTDGMGFDEA... | Cofactor: Binds 1 FAD per subunit.
EC: 1.8.1.4
Catalytic Activity: (R)-N(6)-dihydrolipoyl-L-lysyl-[protein] + NAD(+) = (R)-N(6)-lipoyl-L-lysyl-[protein] + H(+) + NADH
Sequence Length: 509
Sequence Mass (Da): 53950
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A0A1H3ST50 | MAPINTVDKSATRRYVTIAVVSLVLLLAGSVLLALRYDLYPVQTTVMDPAVGRGQQVLVASQTNGAQLRTGDVVVVASDGWADEPAGMDYILRVGAVAGDTILCCTDAGKVTVDGAVKEPPTITGDAPGAPAFNVKVPDGRVFLLGDRRDIARDSRAHLGLDGGTVPLSAVKGRVVAKLAPPGSVSGLDSGTGVSVNPLDPDGTYLYAAVLVLLGLIGLVYALVRALKARPRRPGESAVPVATG | 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: 244
Sequence Mass (Da): 25018
Location Topology: Single-pass type II membrane protein
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A0A538FDC1 | MTVGEALAHGTNVLAEAGIDTARLEAELLLAKACDDCARALLYMELRRELTAEAEAAYEELLTRRAQREPLAYILGHWGFRRLTLKTDKRALIPRPETEIVVERALRHLHGLEEPAVLDVGTGTGAIALAIADEHPQARVTAIDASEDALALARENFDLLDLDGRVRLVEHDLTEGLGRDEFDLVVSNPPYIEPEDLETLQPEVRDWEPRIALVAHG | Function: Methylates the class 1 translation termination release factors RF1/PrfA and RF2/PrfB on the glutamine residue of the universally conserved GGQ motif.
EC: 2.1.1.297
Catalytic Activity: L-glutaminyl-[peptide chain release factor] + S-adenosyl-L-methionine = H(+) + N(5)-methyl-L-glutaminyl-[peptide chain release... |
A0A538JNJ2 | MAHPPAHVPTHESRESARARLQGRGDDDDAVRHGDAERPRPVPPRDRRDRPRAGPGRAGGTPTPGDAGRAVAGPRVHAGARRGRAGDPRLDVAGLRILVVNAGSTSLKLSVVADDGSTKEVESLAQEVDAVAHRVVHGGARFRDPVVVDDEVAEALAELAELAPLHNGPALAALVDARRVLPDVPHVAVFDTAFHATLPEEAAVYAVPRRWREDWGIRRYGFHGLSVQWAAERVTARRLVVCHLGGGCSVTAVLDGRSVETTMGFSPLEGIPMATRSGSIDAEIVVHLLRTGKLGLDDVERTLERESGLLGLSGLSARLE... | Cofactor: Mg(2+). Can also accept Mn(2+).
Pathway: Metabolic intermediate biosynthesis; acetyl-CoA biosynthesis; acetyl-CoA from acetate: step 1/2.
Function: Catalyzes the formation of acetyl phosphate from acetate and ATP. Can also catalyze the reverse reaction.
EC: 2.7.2.1
Subcellular Location: Cytoplasm
Catalytic Ac... |
A0A538LUU7 | MLIGAHVSPAGGLARAIERGVERGCRAIQIFNQSPRMWRPSTYREADVEAFRRAMADSPVDAVLIHTVYLLNCASEDAEIRAKSLASLVHSLRAGQALGARGVVLHAGSAKRGDAAHAIRRAGETIRRALAESERCQLHLENTAGAGGTLGRTLEELAELLAAAGGSRRLRVCLDSCHLLASGYDIRTPAGMDALVREIAARVGLERIGSLHLNDSQAPLGSNRDRHANIGQGQLGQRGCAAFLGTPALQQLPCVLETPGEKRGGAKREEVQLAVRLHERGVAARRRASARAAAASASAGRGGYKRR | Cofactor: Binds 3 Zn(2+) ions.
Function: Endonuclease IV plays a role in DNA repair. It cleaves phosphodiester bonds at apurinic or apyrimidinic (AP) sites, generating a 3'-hydroxyl group and a 5'-terminal sugar phosphate.
EC: 3.1.21.2
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphooligonucleotide end-produc... |
F3BAM8 | MENKKLVVYFLIKLAIVFAVVVAMFTLVFGVLFCKGETMYPRLRDGDVAIYYRLTTDYQVGDVVVFESGGQSIAARIVAREGDTIELDKEGRLLVNGNIQQEEVFFPTEPIAGGITYPYRIEKDSFFLLCDNRPAASDSRFFGAVSQKKIKGKVINLFRRRGI | Catalytic Activity: Cleavage of hydrophobic, N-terminal signal or leader sequences from secreted and periplasmic proteins.
EC: 3.4.21.89
Subcellular Location: Cell membrane
Sequence Length: 163
Sequence Mass (Da): 18390
Location Topology: Single-pass type II membrane protein
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A0A920H6P1 | MQNKKNSYHSKIKKEINSCLVKSKILDRNHLKKPIKGESINLDLSKHNINKKILNNLYQILENTNYKSNLKSLLNGEEINHSEKRPVLHCALRGTYKNLDKSVIKLLEKERKEMFSLADQISSGKLKGSSGKKITNIVSVGIGGSYLPIKFAYDALKKFRVNKIKIDFVYNLDVRNIFDVLENIDVERTLFVFISKSFNTMETLEALNFIKKLLIKDKKISNYREHLFAVTTNQEAAIKMKINSKNILSMPEGVGGRFSLWSNVSFPLVVSIGSKNFKKLLEGAKSADSHFIKRKPENNIPINLALISYYYSTFSTSSHA... | Pathway: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 2/4.
EC: 5.3.1.9
Catalytic Activity: alpha-D-glucose 6-phosphate = beta-D-fructose 6-phosphate
Sequence Length: 359
Sequence Mass (Da): 41087
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A0A538D4F2 | MADSSFDVLVIGSGASGLAAAVSAARSGVRVAVATKGALQSCNSAKAQGGIQAAFGDDDSPEQHAQDVWESSHETADRELVEILTSEAPSAIHWLEELGVEFTRENGGYRLARCGGASRKRLLQVGDRTGHAITTALRDVVEGSDVHTFPKSPLADLARTENGWRARCGDTTVVLAAGGRCYREAEERGELSTNHPGATGEVTQIAVDLGAELRDFDALQYHPNGGAWPPNMQGYSIPETTRAYGAVLLNADGEEFTDSLGPRDAVSQAIFDEVEKGKGVETPDGRPAVYLDTTRIPE | Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; iminoaspartate from L-aspartate (oxidase route): step 1/1.
Function: Catalyzes the oxidation of L-aspartate to iminoaspartate, the first step in the de novo biosynthesis of NAD(+).
EC: 1.4.3.16
Catalytic Activity: L-aspartate + O2 = H2O2 + iminosuccinate
Sequence Len... |
Q0RX58 | MTITDDNPLAQRIALAPTLAEIRAEERVMAAISQLSRGEAIILTDGIGSPTSGEVVFPAARISTADAAFAIRYSSGFLQVALPPDRCDALWLPAQQGAAPGTAQCVTVDAATGITTGISAADRARTIRLLASPDASPASFSRPGHVVPLRADAALPISDFGHPEAAVHLVAAAGFPPAAVLTTVVGTTHPTDVASGNDLQEFARTHQLPIVGLRDLDSEKTPLPILHVSVDLPSGRTSLESFTDLGHNYLVVAVGEVSGREDVPVHLLPADRVLIDAGSPGAEPRILIGLPQTPEDEYGRAIDGLHRQHSMIRAVLRRLG... | Pathway: Cofactor biosynthesis; riboflavin biosynthesis; 2-hydroxy-3-oxobutyl phosphate from D-ribulose 5-phosphate: step 1/1.
Function: Catalyzes the conversion of D-ribulose 5-phosphate to formate and 3,4-dihydroxy-2-butanone 4-phosphate.
EC: 4.1.99.12
Sequence Length: 334
Sequence Mass (Da): 35065
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A0A2E3JQR6 | MPNVNLDKVIASLKLAIDEVTNVSSISQLKKEYLGPDSIIAKERHNLSQYSDDQKKKIGPMINDATKEMESLLESATQKFELEASKLKEQKEKTDISINWYEAEFGSHHVLTSTMQEVVEIFSNIGFKVESGPEAETSWHNFDALNTPIWHPARYESDTLYLDYGDKNSTLLRTQTSTVQARHMQKNEPPIFIVVPGRVFRSDQLDATHSPVFHQIEGLAVDEGVTFTDLKGTLEYFAKEFFGKNTKTKFIPHFFPFTEPSAEMLVQWKDDEWLEILGCGMVDPNVFKNVGYKKHHQGYAFGMGVERLSMIRYGIDHIKN... | Cofactor: Binds 2 magnesium ions per tetramer.
Catalytic Activity: ATP + L-phenylalanine + tRNA(Phe) = AMP + diphosphate + H(+) + L-phenylalanyl-tRNA(Phe)
EC: 6.1.1.20
Subcellular Location: Cytoplasm
Sequence Length: 333
Sequence Mass (Da): 38275
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A0A7C3X0L7 | MIPPGRREGGPEEGASGEDGMGISGRISITGLRAFAYHGCTPQEKERGQNFLVDLELEYDISAAAREDRLEKAVDYDRLAASVRELVIRERYDLIETLAERIARHVLDATPASWVRVKVRKPEAPLSCEVAEVAVELTLRRHG | 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... |
A0A1F4V4P5 | MLDYIIIALASFFITFLISFPFINLLYKFNIRRVSKIDLEKALPGRKVKFGTPIMGGTVIIISTLILLFLFLRGWKYYPMISAVLIIGGIFGAVDEYINTLGRTITAIRISRKNGEGRSLITVNKWFAPIKKVLMIPWKMFEEALRVMGSEQRGLKSHYKFILHLLIAGIAIAFFIDKQHSAAIYIPFAGNFFLGYFYYPILAFLLLFFANAFGITDGMDGLSAGTHSIVFLAYAILATFLGYTEVAYLCFILFGAELAFLYFNIFPARMEMSDVGTLPLGMLLVLSAAIIHREISLIFIGAIFIIEILSSVSQQWFVKL... | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Catalyzes the initial step of the lipid cycle reactions in the biosynthesis of the cell wall peptidoglycan: transfers peptidoglycan precursor phospho-MurNAc-pentapeptide from UDP-MurNAc-pentapeptide onto the lipid carrier undecaprenyl phosphate, yield... |
A0A831SJW7 | DIGVLAGIGKAKVKVFKKPRVAIISTGNEVVPPQDVPQVGEIRDINSYTLGACVKKANGIPIYGGIVKDEANFLEQEIRKFIEKDRVEAVVISGGSSMGSRDITLEVLSKLGKPGVLIHGVSVKPGKPTIIAIADNRPLFGLPGHPVSALIIFDLFVRPLISWLQGEDYHNDFFPKLEAELISNVVSDPGREDYIRVVLYEENGKFYAKPILGKSGLISTMVRASGLVKIGLNVEGLKKGSKVMVRLF | Pathway: Cofactor biosynthesis; molybdopterin biosynthesis.
Function: Catalyzes the insertion of molybdate into adenylated molybdopterin with the concomitant release of AMP.
EC: 2.10.1.1
Catalytic Activity: adenylyl-molybdopterin + H(+) + molybdate = AMP + H2O + Mo-molybdopterin
Sequence Length: 248
Sequence Mass (Da):... |
J7XAM2 | MYIFLGTESIEEMVNGLTRQFIIAGVITFLLTAITIFLLSRLLTKPLLHMKQATEKMSKGDLSVSLTTTRNDEIGELAESIQTLANDLHYMKTERSEFLASVAHELRTPLTYVRGYADIALKEDIPPEQRLQYLSIIKDESDYITNLVQDLFSLAQMEKHNFFIQVKEVHLHTFLTRITEKINVMYGEKQIKVVFTCPLSLLVKLDEQRFEQVMANILNNAYRHSKEHSHINISVTEEHKHISIKIEDKGEGIPPEDLPHIFDRFYRVDKARTRATGGTGLGLSIVKEIVELHGGNITATSEVDHGSCFTISLPSI | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Membrane
Sequence Length: 316
Sequence Mass (Da): 35912
Location Topology: Multi-pass membrane protein
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A0A6V8EX78 | MTEGILVSNHMCGSKTPEKCYPSCLGGPCMNPAILVATGGALGALGRWAIGSLSTGMAFPWATLGVNLIGSLLLGVLAAAFSSGTISKDAVLLLGVGFMGAFTTMSTYSFEAVEMGESGAFGALAGYVVVTALGCPLLALLGWRGMSLLMS | Function: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Subcellular Location: Cell membrane
Sequence Length: 151
Sequence Mass (Da): 15204
Location Topology: Multi-pass membrane protein
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A0A538JKK6 | MRRLLVLATTALLTFPAAASARGTFDPSTEFEQHEWVPIHLGPVNMSITKAVVYLFIGAALTILLGLVLMRGRTLNRRQTVGEAIYEIAQVQVAEQGLPSRAIHRWFPYVASLMLFIWVVNMLGFIPLPLTGETWHGIPVWGIYAATSSLSVTLALALLTFFFTHFEGIRENGPIRYFKSWIPEVPKAILPLIVPLEVLGQFMRLISLSVRLFANMLAGHMLILTFIGLIFVLENVYLAVVRRSSSPPCQPSTSARPSSRNTRRNQCSTPSSSRPAVT | Function: Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane.
Subcellular Location: Cell membrane
Sequence Length: 278
Sequence Mass (Da): 30887
Location Topology: Multi-pass membrane protein
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A0A7V9UZJ3 | MRLALAQLNAVVGDLEGNREKIVTYLRQARDEGADLVLFPELAVTGYPPEDLLLRPGFLRAARESLDKIAAEATGVVAFVGTPWLDRDLANACAVCADGEIRGVYRKHFLPNYGVFDEHRYFAEGRDLLLVRFEDAIVGPTICEDVWQPGPPATDLALGGAQLLVNLSASPFYVGKAEEREEMLVTRARDTSAFVAFCNLVGGQDELVFDGHSVVLDDAGEVIARARGFEEQLLVVDVEPTFALGRRLRDVRRRGLERSRESVPSFEVLDLGALPAREPAAAPEIVGYAPELEQMRLGLALGLRDYVVKNGFADVVVGTS... | Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from deamido-NAD(+) (L-Gln route): step 1/1.
Function: Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses L-glutamine as a nitrogen source.
EC: 6.3.5.1
Catalytic Activity: ATP + deamido-NAD(+) + H2O + L-glutamine = AMP + diphosphate + H(+) ... |
A0A358SNA0 | MDIRLLGTGGDQGWPCPGCRCASCMRGRAAGRRRAPGQVLVDGALRIDAGQPPAGQPATGYQVTRLEGGWDVTGPDGGRLLLAAGPAAVPRPAEGTRPFDVALLDLLHSPAQLGELRARGLLRPAAVAAALYMDHRIESEPELARRAALWGACVPADGDSLASPGPLAATGGQPDGRAADARPGGVPLPHRTLILGGARSGKSREAELRLAGQPAVTYLAAGPWPGGSWTGADGSPDAEWAQRVAAHQAARPRHWRTVESLDVAGVLASQDGAILLDGIGTWLAAVMDEAGAWTAEQAEQAEATERAGGAERAGWAERAG... | Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis; adenosylcobalamin from cob(II)yrinate a,c-diamide: step 5/7.
Function: Catalyzes ATP-dependent phosphorylation of adenosylcobinamide and addition of GMP to adenosylcobinamide phosphate.
EC: 2.7.1.156
Catalytic Activity: adenosylcob(III)inamide + ATP = aden... |
A0A1V5K6K3 | MQHTLLEILKKGTAYLVQQRVPNARLDAEVLFANVLGLERIQLYVLFDRPMNQDELDRYKRDLMLRARGVPVAYIIGRREFMSLPISVGPGVLIPRPDTEILVEQAVEWMKAFRDAGSEAPRVIDMCTGSGAIACAIAHHAPWCRVLAADVSPDALKYAAMNIADLHLEDRVHTVAGDLFAAVPAEWRGADLVVSNPPYIPTQVLAGLEREIREHEPRIALDGGADGLIFYRRLAGEASAVLRPGGRMLVEVGDGQADDVGRILAQHGWTDILTVADYSGTPRVVSASPSGPGDSGGSSGSERREHS | Function: Methylates the class 1 translation termination release factors RF1/PrfA and RF2/PrfB on the glutamine residue of the universally conserved GGQ motif.
EC: 2.1.1.297
Catalytic Activity: L-glutaminyl-[peptide chain release factor] + S-adenosyl-L-methionine = H(+) + N(5)-methyl-L-glutaminyl-[peptide chain release... |
A0A521XM15 | MSEGYAGGRGPLLRLWGVPVHVPASGVVGVALIAVLWAPNFVLSGAPASQQYALAVIFAVLLYLSILLHEAAHAFAARAFGYPVTKIVLWVLGGFTQYERARPAPGKEAAIAAAGPLTTLAVAGLAYLALAATGDSLDVRAVVVLEALAWGNAFMGLYNLLPGLPLDGGAVLRSAVWALTGSENRGAVVAGWAGRGLAVLMIVTPFALAFARDVRPSLGLVVVAAIFAAFLWTGASDALRRARVNRHIPGLSARRLARRAVNVDADLPLAEAIRRMTAAGARSIVVVDRDGRPIGVGEDAAIAAVPPARQPWLAVSAVAR... | Cofactor: Binds 1 zinc ion per subunit.
Subcellular Location: Cell membrane
Sequence Length: 387
Sequence Mass (Da): 40127
Location Topology: Multi-pass membrane protein
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A0A803YB57 | IALQILQHSPQGGQQSEERKSYKWKQLLFFITFITFSIAVCVYFHHNWYCRPGVYTIFAFLEYVVVFSNMAFHMTAFWDFSNKELVVGPHSRGTVAAWDTRADSRCLFAVGWQSSCCLW | Function: Involved in the lipid remodeling steps of GPI-anchor maturation. Required for stable expression of GPI-anchored proteins at the cell surface.
Subcellular Location: Membrane
Sequence Length: 119
Sequence Mass (Da): 13902
Location Topology: Multi-pass membrane protein
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A0A7K0MYS2 | GMAGAPRLSAASALRAGSGVVVVYSPDPSGADSLADSPADSPADSPADSLRQGTAESAESPADSLRQGRGSSAESAESAKSRAESIEPTVSWGSEVITRVIPLGQEGRLNSDSSEYLIEAARRFDAVLIGPGLGADHGVAEMVRALIGGVAAPIVLDADGLNALGGDLSALQERAELGLGPVILTPHEGEFERLSGEVGSDRVAAARGLAREAAATVLLKGPTTVIAEPGGAAYIVNSGGPWLATAGSGDVLAGIIAALLASGISPGRAAAAGAWLHCRASDFAGHTCLVASDLLSAIPAAWPRFSGTMTDQHQ | Function: Catalyzes the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. Together with NAD(P)HX epimerase, which catalyzes the epimerization of the S- and R-forms, the enzyme allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or ... |
A0A926DCI2 | MHTEESFDGSYKADDMLRAAVTAGMRAVALTDHCDLGSPAFYDPFDIDVKRQRRKYDAVAPLFADRLDVRFGLELGQPNQQPEKAEQILRETEFDFVIGSLHNLRGERDFYFLDYHSLDVPALLSRYFDELIEMVEQDFDVLGHLSYPWRYLSEAGMKQPWENYEEQIRLIYRRLIETGRGIEINTSGLRMSMGVTMPDLPLVRLYRELGGEIVTIGSDAHEPAHVGSGIRRGAALAREAGFSHIALYRGRKPQFVPITED | 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: 261
Sequence Mass (Da): 29848
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A0A7J4FY62 | MKKYDVLVVGGGPGGYPAAIRASQNGAKVAIIERDRFGGECTNYGCIPTKALLKGAKIASDLAKYPFVVGDTEIDYRELVKWVRKVSNRSSRGIEYLLKGYGVDIYKGEAIFKDIRNVTVNGEELYGDKIILAMGSKPVDIPGFTVDGEYIHNNRSILDISELPNSIAIIGAGYIGVEYATIFSELGVDVYLIELLDRVLPLMDKDFSMLMDRLLKKKDVKIYTGVKAEEWVRNGESLMVKLSNNVKLEVDTVLIAVGRKPNSRDLDKLGVKLDNEGFVIVDEMNKTSIDGVYAVGDLAGKPMLAHKAFLEGVIAGENAS... | Cofactor: Binds 1 FAD per subunit.
EC: 1.8.1.4
Catalytic Activity: (R)-N(6)-dihydrolipoyl-L-lysyl-[protein] + NAD(+) = (R)-N(6)-lipoyl-L-lysyl-[protein] + H(+) + NADH
Sequence Length: 452
Sequence Mass (Da): 49418
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A0A3E0PW21 | MEEALSMSKGLRINRRFTQEGESPYDLIEWSRRDSRITNPDGSTVFEMKGAEIPAGWSQVAADIMVSKYFRKAGVPQFDDEGEQIFDESGQPATGPERSAKQVFDRLAGTWRHWGEKEGYFASTADAEAFEDELKYMLATQMAAPNSPQWFNTGLNYAYGLTGPAQGFWYVDGKDGQLKASPDSYSRPAPHACFILSVGDDLVNPGGIMDLWVREARIFKFGSGAGSNFSAIRAADERLSGGGKSSGVMSFLKIGDRAAGAIKSGGTTRRAAKMVILDVDHPDIETFVDWKKVEEEKARMLIQHGGFPADFNGEAYATVS... | Function: Catalyzes the reduction of ribonucleotides to deoxyribonucleotides. May function to provide a pool of deoxyribonucleotide precursors for DNA repair during oxygen limitation and/or for immediate growth after restoration of oxygen.
EC: 1.17.4.1
Catalytic Activity: [thioredoxin]-disulfide + a 2'-deoxyribonucleos... |
A0A3D9L4W8 | MAQELNKYSKTITQDPSQPASQAQLYATGLTEEEMKKAQVGIVSTGFEGNPCNMHLNILAHQVKKGVKEADLVGLIFHTIGVSDGISNGTTGMKYSLISRDIIADSIETVVQAQFYDAVVPVVGCDKNMPAAIMALGRLNRPGLMVYGGTVKPGKWKGEDLNIVSAFEAYGAKMGGNISDEDYQGIIKNSIPGPGACGGMYTANTMASAIEAMGMSLPFSSSNPAESENKQSETRKVGLAVRNLMEKNILPRDIMTKKAFENAISTIMVLGGSTNAVLHLIAMARAVDVDITLDDFQRISDKTPFIADLKPSGRFLMEDL... | Cofactor: Binds 1 [2Fe-2S] cluster per subunit. This cluster acts as a Lewis acid cofactor.
Pathway: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 3/4.
Function: Functions in the biosynthesis of branched-chain amino acids. Catalyzes the dehydration of (2R,3R)-2,3-dihydroxy-3... |
A0A8J6YPS4 | MKKMAMIVAYDGTRYYGFQRQSTLPTIQERLEEALLRLHQRKTGVTGAGRTDARVHATGQVIHFMTDLGIPPERWPYALQAFLPEDIQIRAAYPVEDSFHARFSAVGKRYRYRIDRGKMRNLFTRNYALHYPYHLENDKIKEAASFLLGRHDFSAFAASGSSVKNHIRTLYDIQVVEVGDELQFTFWGDGFLYNMVRILVGTLLEVGGGRRDVKEIVKLLMSGDRTKAGVTVPPHGLTLEEVLYPEGTFQLKK | Function: Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs.
EC: 5.4.99.12
Catalytic Activity: uridine(38/39/40) in tRNA = pseudouridine(38/39/40) in tRNA
Sequence Length: 253
Sequence Mass (Da): 28914
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A0A7V9ELQ5 | MTVIIAMDGPAGAGKSTIAREVARALGFKHVDTGAMYRAVALGVLDRGLEGESSTAIEELASTLDIEVDGNRVWIDGVEASARIRGAEVNGVVSAVAARPGVRRHLADRQRRLAAGDGVVMEGRDIGSVVFPDAAVKLYLTAAIEERARRRLEELPAGAESSLDETAAAIATRDAADAGRTESPLVRAPDAVVVDSTGKDVREVVDQVLAIITRAVPGLITVQPEG | Catalytic Activity: ATP + CMP = ADP + CDP
EC: 2.7.4.25
Subcellular Location: Cytoplasm
Sequence Length: 226
Sequence Mass (Da): 23584
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A0A523S8S0 | MSGGIDSSMAAKILKDNGWEIIGVTMKLLPYDFGWKDGAKTCCSPKDIEAARKVSLKLNIPHVVINLIQPFEEKIINPFCLEYQQGRTPNPCVECNKYIKFGALLEKIKTLGASFLATGHYCRIEKSLNSGLYEIKKGLDKSKDQSYVLWKLNQDQISQIKTPIGMLSKDDVRKKANSIFPFLEKKNESQDICFIPEDNFHSFLASKLKNIKEGAIINTNGKIIGTHKGYPFYTIGQRKGLGISHSKPLYVKEIIPEKNIIMAGEEKDIMQKSLKVKNTNFISGNPPGNNFKAMVKIRYNFKETSAEIKIESKKTAAIFF... | Function: Catalyzes the 2-thiolation of uridine at the wobble position (U34) of tRNA, leading to the formation of s(2)U34.
Catalytic Activity: AH2 + ATP + S-sulfanyl-L-cysteinyl-[protein] + uridine(34) in tRNA = 2-thiouridine(34) in tRNA + A + AMP + diphosphate + H(+) + L-cysteinyl-[protein]
EC: 2.8.1.13
Subcellular Lo... |
A0A538ISV0 | MTPLAVSILPILIPAIVVVLVLVGFVGVRSRRRVRPAPPAERVAPPEAVAPPREVEAPAREVQAPPRVPEARAPEAPEIEAPPPPEPPPPVVAPRRRVRSIGASLARLFKGTALTEQEWEELEEVLLRADVGVAATQRIVGAMRSRRDVADGMAALKDELVSALGHPDRSLKTKPGGTTVWLITGVNGVGKTTTIGKLAAQLRDEGRSVVLAAADTFRAAADQQLERWAELSGADIVKHAPGADPAAVVYDGVAAAKARARDVLIVDTAGRLQTKKNLMEELGKIRRILDRETGAPEEVLLVLDATTGQNGVAQARAFAE... | Function: Involved in targeting and insertion of nascent membrane proteins into the cytoplasmic membrane. Acts as a receptor for the complex formed by the signal recognition particle (SRP) and the ribosome-nascent chain (RNC).
Subcellular Location: Cell membrane
Sequence Length: 381
Sequence Mass (Da): 39960
Location T... |
A0A7V9UYC0 | MLSKISSAATCAQIPRPPTSKRSSVPRSFVREARRRGIGTRRERIGPIVERLAEEHRDAEIALRFRSDLELLVSVMLSAQTTDTNVNRVTERLFEKYRGPEDYLAVPEEELQRDIYATGFFRQKTKAIRGTMQALLEHFDGQVPRRLEQLVTLPGVARKTANVVAAELGHAQGIVVDTHVRRLSQRLGLTREELPVKIERDLQKIVPRADWARFPHLLIWHGRRVCDARNPLCEICVLANLCPSSRVALVSQRVRA | Cofactor: Binds 1 [4Fe-4S] cluster.
Function: DNA repair enzyme that has both DNA N-glycosylase activity and AP-lyase activity. The DNA N-glycosylase activity releases various damaged pyrimidines from DNA by cleaving the N-glycosidic bond, leaving an AP (apurinic/apyrimidinic) site. The AP-lyase activity cleaves the ph... |
A0A2D5WMC0 | MSSPKLIYSIYENRLQRNLEKENLPKHIGLIHDGHRRYARKEGLLSFEVSYKIGMTRLKECIAWCDEVGIDYITSWLLSRENLSRPIEELGPYFQVLNELFEELLIDDVVDNFKIEFIGSISMLPEFLQETINQLKEVRGGGQKTLTIALGYGGRQEILDAIKGLIDENRNEENDFDSLIKNVTDEQLRQHLYSPDAPDIDLIIRTSGESRLSGFLLWQSAYSEVIFQDVYWPEFRKIDFLRCLREYTQRDRRFGK | Cofactor: Binds 2 magnesium ions per subunit.
Function: Catalyzes the condensation of isopentenyl diphosphate (IPP) with allylic pyrophosphates generating different type of terpenoids.
EC: 2.5.1.-
Sequence Length: 256
Sequence Mass (Da): 30035
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A0A523S6I7 | MKVILINNQSKIKLDLDLIREVAAYISDKFDKDLKSELNIVFSEGKEIRKLNKKYRKIDRETDVLSFSYISDKDKIGPGASSYTVGEVIICPEVAQSNILKQDENWNLNLEIILLIIHGILHIYNYDHEEEKNRIDMESIQDSLVSDTRRTFKL | Cofactor: Binds 1 zinc ion.
Function: Single strand-specific metallo-endoribonuclease involved in late-stage 70S ribosome quality control and in maturation of the 3' terminus of the 16S rRNA.
EC: 3.1.-.-
Subcellular Location: Cytoplasm
Sequence Length: 154
Sequence Mass (Da): 17917
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A0A6G0A696 | MPGATGSAWFRESRFPRSGSRPSRGRPNESSTRPVASAAADVTRRSVGPRQFGYMFGVAGGVVLVDQLTKWWAVNDLTDGPIHVVWTLDFTLAHNTGAAFSSAQAFGPLIGILALALVAGLVWVGRAIDNRPGAVSLGLVLGGAMGNLCDRIFREGDGLLGGPVVDFIDLGWWPIFNVADMSIVIGGILLLLFGLREEVRS | Pathway: Protein modification; lipoprotein biosynthesis (signal peptide cleavage).
Function: This protein specifically catalyzes the removal of signal peptides from prolipoproteins.
Catalytic Activity: Release of signal peptides from bacterial membrane prolipoproteins. Hydrolyzes -Xaa-Yaa-Zaa-|-(S,diacylglyceryl)Cys-, ... |
A0A3P8WTY3 | MVESSPSPLPERAIYGFVLFLGSQFSFMLYCIWAFTPEEWLHSIGFTYWPQKYWALALPIYLVVAIVIAVLLLFGINMNNTAPLDSMDSITDLYARNRNTGGEQTGNVPKLKDVSISEVNKMFYLLPKQH | Pathway: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor biosynthesis.
Function: Part of the complex catalyzing the transfer of N-acetylglucosamine from UDP-N-acetylglucosamine to phosphatidylinositol, the first step of GPI biosynthesis.
Subcellular Location: Membrane
Sequence Length: 130
Sequence Mass (Da... |
A0A538B4G8 | MRPPHHVAREVHREGGTTHQVSRSPRPALLVLEDGSAFRGKSFGAEGEAFGEAVFNTAMSGYQEVLTDPSYIGQIVTMTSPHQGNYGVNAEDVESGRVGVAGFVVRHASSRASSWRAEETLGDYLARAGVPAIEGVDTRRLTLRIRQKGAMRSGISTVDLDPESMSERVRQTPGMEGADLAAKASTGEPYEARDVVGPASPAPGRIFRVAAVDFGLKRNIIRLLSQNGCETTIFPARTEASTVLAGDFDGVFLSNGPGDPAATTYGIETVKGFIGRVPVFGICLGHQLLALALGGRTFKLKFGHRGVNQPVRDLETGRVE... | Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl phosphate from bicarbonate: step 1/1.
EC: 6.3.5.5
Catalytic Activity: 2 ATP + H2O + hydrogencarbonate + L-glutamine = 2 ADP + carbamoyl phosphate + 2 H(+) + L-glutamate + phosphate
Sequence Length: 412
Sequence Mass (Da): 44022
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A0A7K1DCG4 | MTTTTATGITRPVNWNKLEDSMDLEVWNRLTSNFWLPEKVPMSNDIQSWGTLTAQEQNLTRHVFTGLTMLDTIQGTVGAISLIPDALTSHEEAVYTNIAFMESVHAKSYSSIFSTLCSTDEIEEAFRWAEENPYLQKKAEIILGYYRGDDPLKRKVASTLLESFLFYSGFYLPMYWSSRAKLTNTGDLIRLIIRDEAIHGYYIGYKFQKGMELETEARREEIKSYTYDLLMELYENEIKYTADLYDPLGLTEDVKHFLHYNANKALMNLGFDPLFPKEVSEVSPAILSALSPNADENHDFFSGSGSSYVIGKHEATEDDD... | Cofactor: Binds 2 iron ions per subunit.
Pathway: Genetic information processing; DNA replication.
Function: Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides.
EC: 1.17.4.1
Catalytic Activity: [thioredoxin]-disulfide + a 2'-deo... |
A0A7V9TQ31 | MTPDDAAGGPSADSPRASARERRRNAALIVAIGAVWLLLDQASKEWAEAELTGRPPVPVLGDLLQFRLLYNPGAAFSMGTGSTWIFTVLASVVVVVLVWQSRDVETPAWRWAFGLLLGGAGGNLTDRLLRDPGPGRGHVVDFIELPNFPVFNVADIGITSAAVLIALLALRGTPLAGAQATAQTEEAA | Pathway: Protein modification; lipoprotein biosynthesis (signal peptide cleavage).
Function: This protein specifically catalyzes the removal of signal peptides from prolipoproteins.
Catalytic Activity: Release of signal peptides from bacterial membrane prolipoproteins. Hydrolyzes -Xaa-Yaa-Zaa-|-(S,diacylglyceryl)Cys-, ... |
A0A832XZS7 | MVRLFFALECPGLETEGLPRTYISEKARNYHVTIAFLGERPNSEFEVQRVADVCIGRLPLELEYQKLGAFQKPSNARVLWMGVKSSGIQDLASRVRLVSKSEDRPFLAHVTIARFRKQTNLEDLISKHVDTQFGKGSVSNLILFKSELMRLGAIHTPLYSVDGKGKVEHLI | Function: Hydrolyzes RNA 2',3'-cyclic phosphodiester to an RNA 2'-phosphomonoester.
EC: 3.1.4.58
Catalytic Activity: a 3'-end 2',3'-cyclophospho-ribonucleotide-RNA + H2O = a 3'-end 2'-phospho-ribonucleotide-RNA + H(+)
Sequence Length: 171
Sequence Mass (Da): 19313
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A0A7K0RE25 | MPLRGTQEARSRCGLRRSHHPGADASQKSNRVNPAELVVLPDRDALIQRVSADVVHHLEHLLASQDVVHLSLTGGTVGIAVLNQIGNEHTAVDWTRVHLWWSDERWLARHDPERNAQQARPGFIDRLPFSLTHVHEMPAPDDGLSLDEAALAYADELRAVGLGVAGLGFDISLLGVGADGHVASLFPDQGRDLEGHQAVLAVRHSPKPPPERLSLSLDAINSSQHVWVAAVGEDKSGAIAATRILTNDRRLPVALVHGRAETRIYCDVSASPQQ | Pathway: Carbohydrate degradation; pentose phosphate pathway; D-ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step 2/3.
Function: Hydrolysis of 6-phosphogluconolactone to 6-phosphogluconate.
EC: 3.1.1.31
Catalytic Activity: 6-phospho-D-glucono-1,5-lactone + H2O = 6-phospho-D-gluconate + H(+)
Sequen... |
A0A1F4V3B7 | MSQEKNDKPFVKTESEFKGSKISLETGKLAIQAGSSVLAKLGDTTVLVTVVSTPTIEETDGFPLRVEYEERFYAGGLIGGSRFTRREGKPSDEAIVSGRLIDHAIRPLFSKDFGNDTQIVVTVLSIDQKHSPVLLGFIATSAAFSLSGLPFDGSIVPLRIHKVNGAIETTLDKENEDSEMDLLVSYLEGGSKVQAIEARGNVVNEEEVLNAVKMGAEESKPLFAFLKDFAEKSGAVPKEYPKAWLTKDLISKFAKESLPVLQKVRADMKEFDRSKWNEAVEKLISDLVEKYNDEYSEFELKLIVGEVEKDMVRDMVLNKK... | Function: Involved in mRNA degradation. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'-direction.
Catalytic Activity: phosphate + RNA(n+1) = a ribonucleoside 5'-diphosphate + RNA(n)
EC: 2.7.7.8
Subcellular Location: Cytoplasm
Sequence Length: 753
Sequence Mass (Da): 82... |
A0A653HBU8 | LTIYKPQLTSTFSIFHRISGAFLATMVLFSILFFGIGDLSLTFYYFYTFVFFLTFYFHWFIILLVNFTLLALCYHLSNGVRHLWWDWGLFLELSRVYTSGIIMLFCAAFLFVSNMIRF | Cofactor: The heme is bound between the two transmembrane subunits.
Subcellular Location: Membrane
Sequence Length: 118
Sequence Mass (Da): 14058
Location Topology: Multi-pass membrane protein
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A0A7K1E3C1 | MEGIPASHALHEVQGQRRASLKAIVQLAERLARSRRAILLLSLSLLSLDQASKWWVVTYLDGRPPIAVIGDLLRFNHTTNSGAAFNIGSNFTIFLTVFALIVTTGLIIFARKVADLRWAIGFGVLLGGVLGNLTDRIFREPQFLHGHVVDFIQLPNWPIFNVADIAITCSGFWIAYLLLRDIKPFATFGDDDE | Pathway: Protein modification; lipoprotein biosynthesis (signal peptide cleavage).
Function: This protein specifically catalyzes the removal of signal peptides from prolipoproteins.
Catalytic Activity: Release of signal peptides from bacterial membrane prolipoproteins. Hydrolyzes -Xaa-Yaa-Zaa-|-(S,diacylglyceryl)Cys-, ... |
A0A7V9V102 | MTRFRLLTSEALRSIGANKSTTLAAVVTVLVGMFLLGVFIGLGTWLVSWSDSKKKELAVHTFIKDESTPRQINDLRTFLESHALVKSGGVKFITKDEALKIMEKRSPELTRNLASNPLPASFDIVPTKGEDTETIALDIQQAKLAAVDEVTWGQEVSKRILALARGIQIVFLIAIVVLLVASTIDIANTIRLSIFARRREVEVMKLVGATNWFVRGPFMLEGLMTGLVGSLAAILLLFLGREIAVPSILPNDRTSAEVQAMPFMWTSLILLMVGLGIGALGSGLTLRKFLRV | Function: Part of the ABC transporter FtsEX involved in cellular division.
Subcellular Location: Membrane
Sequence Length: 292
Sequence Mass (Da): 31915
Location Topology: Multi-pass membrane protein
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A0A7X7E7T0 | MTTFVGVIVAIVGLGVLILAHEFGHFIVAKATGMRVEEFSLGFGPFLVSRRIGETVYGISAFPLGGYVRVTGMHKEDFELRVAEAREAEAEQRAQIAGDRRPQDPEERLAGKSVLSAEEIAATPVEKRYYSHPLWQKLLFIVAGVVMNMILAFVLIWIVGAGQGEYVTTKVIDEVGEGTPAATAGVRPGDEILSVAGAKTGSWEDIRAEILTHPGETVTIVVQRDGAPVELTAQILEQEDGTGYLGVSPTGEERDLGFASGFGYAARTTWEMVTLIFKGIGMMFSGDVSVTGDQGLAGPVGIIQLSTEAYQGGYYLMLLA... | EC: 3.4.24.-
Subcellular Location: Membrane
Sequence Length: 388
Sequence Mass (Da): 41676
Location Topology: Multi-pass membrane protein
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A0A3A4PNA6 | MCRDEREGNMKIAVVGIGSLGTVVGALLTRGGLDVVMVDANEEIVRALNNEGARLEGNLGLVQPVRAVTPDGMEGEYDLVVYLVKSTYDEQALPRVAPHLGEKSALITLQNGVPEEKVASFIGRERTLGGAVLWSAERLSPGVSRMTSDPDQMGYEIGELDGKMTGRIEMVKDVLDNAGSATITGNLAGVRWTKLLFNVGASGISTALGASGGRIMDDDKATDAVIFIMIETVLTARALGISMEPMRGVDPGVILDLARQDMGNFRNLLRGLIGDFRDAKASMLQDLEKGLPCEVDSINGYLSAMAAKVGVAAPVNDQVT... | 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: 350
Sequen... |
A0A836RCL7 | MKKTFISQVKETLFTILIALVLALIIRAFILQTFYIPTGSMIPTIMPGDRIIALKFWYYIAPLKRGDIVVFKSPEESKILVKRLVGLPGDTILIKDGKVYVNG | 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: 103
Sequence Mass (Da): 11613
Location Topology: Single-pass type II membrane protein
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A0A353FVU7 | MARVAVDLLGGDEGAPVVADAIAAVLVGDTDGRAADSTPPSIQICVVGPHDLARELLAERGIDVDAHGDITIAHAQESVPMSSSSHDTLDMLRERQDLSSLVGVEEVRSGRADAFVSIGHTGATVGASAFGLGRVRGMGRPGLAVELPAAHGPVILLDCGAAPHATAEDLVRFAAVGASYARIVGIESPRIGLLSIGGERGKGDHLRKQTDIRLAEEFAAEYVGAVEGHDLMAQARADVIVVDGFTGNVALKSMEGALRWSVGAMGTAYGSIDPAREVLRSTHLLSGASLLGVDGNIVVGHGASRADEIHGCIRRAAMLH... | 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-... |
A0A523VAB9 | MMERQMTQDRKMPAKKPKQKFNLWTFLKDLPKKVVKFLRNVVHELRRVTWPTRKALLTYTVVVLVTIAIFGVLLGLYDFIFLQLVELLVKI | 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: 91
Sequence Mass (Da): 10845
Location Topology: Single-pass membrane protein
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A0A2E0RA34 | MDDKWTXISQLINRKFRREATSCDYEVGLLTTYRTIGRCSLFLKAENKKELNHALDICRQKDIEVAVIGNGSNLLISDDGFEGLIIKLGSEFEEVNIIEGHAYVGGAAKLPVVARSTSSKGLTGFEWAVGVPGTXGGAVKMNAGGHGSDMEASIESVDVLDTKTSLTKTLYPNELLFGYRQSSISRNQLVTNAVLKLSEGNPEESSEVIKEIVRWRLANQPGGQNAGSVFTNPKDKSAGXLIEDSGCKGMRVGSAEVSTKHANFIQVDVGGKAQDIRDLMELVSESVYSKFGILLTTETEMIGFG | 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: 305
Sequence Mass (Da): 32980
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A0A538KQQ0 | MRKRPVLQMVLIGVIGLAILIPIALVIPWFPSNGSKQAGNVRTLYTVLLLTTIPIFVLVETVVVFSVWKFRMRPGDEEKDGPPIHGNTRLEVLWTVLPAILILSLCTYAYTVLHSNEASKTSEMTVNVSERQFAFEFSYPQAGGKTVVSPVLYLPKGRPVVFKIRSLDVVHSFFVPEFSEKIDAVPGITTTLRVTPTRLGTYPAECTELCGAGHSLMRATVYVVPSATFRSWLSSQPANSAPPIGTPPSSANQAGVPGAATTPTAGASSAKSAAPAGASAAGVAGGKTVFTGSAACSSCHTLGAAGATGTIGPDLDTRLR... | 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(... |
A0A2A4WIV7 | MENKKRPVFLDLTRIDMPVMAVLSVAHRITGILMFLSIPIVIYLLGLSLSSPQGYETVTSLFDSGLFRLIILLALWGFAHHFFAGIRYFMLDLDIGVDVVNGRRSAWCVLGAGIITTVIGMVMIL | Cofactor: The heme is bound between the two transmembrane subunits.
Function: Membrane-anchoring subunit of succinate dehydrogenase (SDH).
Subcellular Location: Membrane
Sequence Length: 125
Sequence Mass (Da): 13886
Location Topology: Multi-pass membrane protein
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A0A076HU07 | MAEIIKMPKMSDTMTEGVIASWLKKVGDKVKSGDILAEVETDKATMELENYEDGTLLHIGPQAGEAVPVDGLLAIVGKEGEDISALLGGAAPAAAPAPEAAPAPEAAPAPAAAPAAPAPEAPKAEAPALAAPAPAAAPASNGKKATVIRMPKMSDTMTEGTIASWLKKIGDKVKSGDVLAEVETDKATMELENYEDGTLLYIGPKDGESVAVDGILAIIGEEGADVEALLGGQSGGSAAPATPAPASEAASAPEPAPAATPAPAPAAPAVAAPAAAVTAVAPAPAGTRILASPLAKSIAREKGIDLNGVKGSGENGRIVS... | Cofactor: Binds 2 lipoyl cofactors covalently.
Function: The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E... |
A0A6I2X5S3 | MTHDSGTQDSGIKVGSVAEAPFAVHDISALLADYISRLGNTWIEGQISEVRETRTLTFMKLRDTQDESTVPIYMTTQALHDLNWKVEQGARVIIQAKADWWTKKGTLQFKILQIRSVGLGELMARLEALRNILAAEGLFAPERKKELPFLPRRIGLICGQNSDAMHDVIENSKRRWPDVEFVVREVPVQGPTAVRQVCDAITELDAIDDVDVIVVARGGGSFEDLLPFSDETLIRTVAACVTPVVAAIGHEEDRPLIDYVADYRASTPTDAARRIVPDVVTEIAQLRNLRSQMFRAVEIRLSAHAKDIATIRSKPALAHP... | 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... |
A0A920L954 | MISLIQKCILLDKPPGFTSNKVLNIVKKKLDIKKAGFSGTLDPFASGLLIIFLNKSTKACSFFLDSDKSYSGEIKLGKTSSTGDPTGEISVTSKKVFIEEDKIKAIQNKFFGESFQKPPKFSAIKINGQRAYELARKGVNVDIPERKIFVNNLDIIKTSESTLKINISCSKGTYIRSIAQDISKEFGYDGYLLSLRRESIGKISLKNALSFNDLETLSIEKIYSRLVSVDTLFVDTNKIALDKDECTKVCNGQEVFSSQFSPGQALIYSHNRDFIGIGEVSQEKVLFPKKIFV | Function: Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs.
EC: 5.4.99.25
Catalytic Activity: uridine(55) in tRNA = pseudouridine(55) in tRNA
Sequence Length: 293
Sequence Mass (Da): 32604
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A0A387BGB6 | MKIRRLTHEERCADKSLSVLTEIILGILLENYDETPWSAHYIATDLANVHSHYFLAELNERVIGFLAISSFMDEIEITNIAVLPEFQGHGVASQLLTELSVFTGTIFLEVRESNLVAQKLYEKFEFKTYHIRKNYYDNPRENALLMRKEQF | Function: Acetylates the N-terminal alanine of ribosomal protein bS18.
Catalytic Activity: acetyl-CoA + N-terminal L-alanyl-[ribosomal protein bS18] = CoA + H(+) + N-terminal N(alpha)-acetyl-L-alanyl-[ribosomal protein bS18]
EC: 2.3.1.266
Subcellular Location: Cytoplasm
Sequence Length: 151
Sequence Mass (Da): 17615
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A0A3A4VG27 | MKQPTVPSGLKDILPKEERELSKIKEITKKAFKSWGYLSIKTPAFEYYDLLTAQTGDFITGEVFKFFDSDGALLALRPEMTTPIARLVAQRYSQGPTPIRLSYVADVFRQEKPRQGQQRQFLQAGIELIGSSSGFSDAETIIILIETLKKVGLRDFRVGIGQIDFVNGLIEQLTKDVEVAKEIRKLIARKNLVGLSVFLKRMKASKKSKDALLKAITLNGKYVLTQAKELAGNIKSQAALNNLIKIKSLIQSYGYLENVVFDLSIVRDFDYYTGVVFEAYSPQVGLPIAGGGRYDGLLKTFGVDMPSAGFAIGLERLHIA... | Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/9.
Function: Required for the first step of histidine biosynthesis. May allow the feedback regulation of ATP phosphoribosyltransferase activity by histidine.
Subcellular Location: Cytoplasm
Sequen... |
A0A1V5G131 | MTGWRCFVTGTDTGVGKTHASLALLHALRRRHGSAFGMKPVASGADQRKQGLRNADAMDLQSASQPRPEYDWVNPYCLREPTAPEIAARFEQVQIELRGIVAAYAHLSTLSPYGVVEGVGGWMAPLSAELMQADVARALGLPVVLVVGMRLGCISHGLLTARAIRADGLPLLGWIANDIDPELAHAEAYFDTLQQRLGLPCLGRLPHGHPAHLCELNLPT | Pathway: Cofactor biosynthesis; biotin biosynthesis; biotin from 7,8-diaminononanoate: step 1/2.
Function: Catalyzes a mechanistically unusual reaction, the ATP-dependent insertion of CO2 between the N7 and N8 nitrogen atoms of 7,8-diaminopelargonic acid (DAPA, also called 7,8-diammoniononanoate) to form a ureido ring.... |
M1W4U7 | MIKRYTRDHEWIDLSADRKRATIGVSEYAAKELGDVVYVELPIVGEVIEQGDAMGAVESVKSASDINAPIRCKITDGNAALEAKPSTINDVPEDDSNGGGWIAKVEVDEAGAKQFDELMDAEAYKAFIAEE | Cofactor: Binds 1 lipoyl cofactor covalently.
Function: The H protein shuttles the methylamine group of glycine from the P protein to the T protein.
Subcellular Location: Mitochondrion
Sequence Length: 131
Sequence Mass (Da): 14205
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A0A538IHT1 | MPKPPARALAAIVMAAGESKRFKTKTPKVLHDLAGRPLIAHVLSALKPLRLTKAVVVTGRGANQVEATIKDVTFARQEKQLGTADAARTGDEALGDFQGDVLVLPGDTPLVTTKTLRVLIAYHRNQKAAATILTAKLDYPTGYGRIVRTNNDVDKIVEQTDATEQQRQIKEVNGGIYVFDRAALRSALTKVERANKQKEFYLTDVIAILKEKGEKVLAKAAPDPIEILGINDRAQLALVAKLLRQRTNATLMRNGVTIVDPDFTYIDPTVKVGPDTVIHPPTFLHGATRIGEGCEIGPGARITDSRIDDGATVIFSVLDN... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Pathway: Bacterial outer membrane biogenesis; LPS lipid A biosynthesis.
Function: Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C-terminal domain catalyzes the transfer of acetyl group from acetyl c... |
A0A1V5K9N5 | MARRDIRAAVDIGSGTVRAVIAESRPGGVSLVGAGHCASAGLRKGVVIDIEAAGAAVANAVAMAESESGTAVSSVLVGVSGSHLCSAPSLGRTTVATSDREIAQEDVDRALESCRQAGAAPDREIVQIVPREFAIDGQAGIQRPVGMSGVILEVDAQVISGSSTALQNVRRAVSRANLEIDGMVLQSVACAEAVLSQEEAESGAIVLDIGLATTDIAVYRDGGLLHASLVPIGGGHITNDIALVLKVPVAYAEDLKLRYGAATADDVSPDDKCGGEAGVSRQILCQIIEARLDQLFDRVKRDLAEAGVDGQYAGGVVIVG... | Function: Cell division protein that is involved in the assembly of the Z ring. May serve as a membrane anchor for the Z ring.
Subcellular Location: Cell membrane
Sequence Length: 407
Sequence Mass (Da): 41513
Location Topology: Peripheral membrane protein
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A0A523VL10 | MKKVSVIGTGYVGLVSGACFEHLGHQVLCIDKDEKKIAALKDGKCPIHEEGLEELLKKADNLSFDTDISRISESEIIFICVGTPEKENGDADLSYVYSVCEEIAGNLGEGQTVVAKSTIPVDSISKIKEILRKSNVDFNFASNPEFLAQGTAVKDFLEPDRVVIGSETEEGGKELEQLYQNMKAPIVKTDVESAIMIKYAANTFLATKVSFINSIARLCEKVGANVNDVAKGMGMDKRIGTRFLKAGIGYGGSCFTKDTKALIKTASKNGLSLDILKEVNKTNEEQRKLVIEKLRRHLGDLTDKQISMFGLAFKPGTDDL... | Pathway: Nucleotide-sugar biosynthesis; UDP-alpha-D-glucuronate biosynthesis; UDP-alpha-D-glucuronate from UDP-alpha-D-glucose: step 1/1.
EC: 1.1.1.22
Catalytic Activity: H2O + 2 NAD(+) + UDP-alpha-D-glucose = 3 H(+) + 2 NADH + UDP-alpha-D-glucuronate
Sequence Length: 422
Sequence Mass (Da): 46207
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