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stringlengths 6
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stringlengths 16
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stringlengths 117
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A0A961FXR1 | MDPEERARKLKMAEEVVMEAPDYDALAKPFYDQVAEHGKLAAQVRAAVVTAYEALPKPDDPAIRTPPGREKLRAAAADYAHLMETLTRVEKTLPKWRHDKPVSRTRGVLMFFAGRDWVTNSSWHDFYGLLPLLTGSFLISVLALVVAVPFSVASAIYVNQLAGRREQNLIKPAIEFIQAIPSIVLGFFGILVLGSFLREWSQGQLHVSPHGFVGSLPVIREIFTGICGFLNWVAQYVPGFPMSERLTMLNAGLLLAFMTVPTIFTLAEDALNNVPHSFTEASFALGASKLQTILRVVVPSSLSGIVAAVLLGFGRIIGETMVVLLVAGNKIQIPDFRAGLGVFAQPAHSMTGIIAQELGEVDQGSIHWRALFLVGMVLFTISLVTNFIAQRILAKYHVKA | Function: Part of the binding-protein-dependent transport system for phosphate; probably responsible for the translocation of the substrate across the membrane.
Subcellular Location: Cell membrane
Sequence Length: 400
Sequence Mass (Da): 43801
Location Topology: Multi-pass membrane protein
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A0A1H3DD93 | MESFSAIKKRMKSVDDISQMTNAMKLVSSAKMRRSQLLHDNMYPFFLFCVESMQEMIRKNEHLDNPFFVLDQKQEGDTWKIGYYVLSGDQGLAGAYNNNMVKITEDHVRTKILDNTQKGMSTSYELNVFGRLAREKLMKNGYNVNSEFSFPISEPTYFDARQVSAVMRHRFLNDDFDLVYLLYTRMESSVKMEPVALRLLPVDTKSISRVLPDKLEDAGIATLTGADLEYFPNSDAVFDYLIDSYTNAMVYGAMVDAFATEQTARLTAMENATDNAEEMMKKLELLSNRARQAKITTELTEIVNGAQQADKM | Function: Produces ATP from ADP in the presence of a proton gradient across the membrane. The gamma chain is believed to be important in regulating ATPase activity and the flow of protons through the CF(0) complex.
Subcellular Location: Cell membrane
Sequence Length: 312
Sequence Mass (Da): 35633
Location Topology: Peripheral membrane protein
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A0A1H3EG41 | MAKRVFLVVADSFGIGGAPDAGKFGDEGSNTLAAVLSYSNDPYPNLAKLGLLAIDGEDDPRIISYKKAQESIPSPIGSYARVREVSAGKDSTIGHWEIAGIISDKAQPTYPDGFPDEVIKALEKATGKEYLCNKPYSGTDVIRDYGEEHMKTGKPILYTSADSVLQIAAHEEIIPLEELYDICAKARAVMCGEHAVGRVIARPFVGEPGNFTRTPNRHDFSLAAPSSTMLDLLKSEGFDVISVGKIYDLFAGRGLTESNPTKGNTDGINKTIEFMDRDFNGLCFVNLVDFDMKYGHRNDIEGYATAMHEFDNALGVILGKLKEDDLLIITADHGCDPSTSSTDHSRECIPLLIYGDGYRTPCNMGELTGFNNISGIVLSALMSRNYERDFLPATDSNKPDAENIMSYVDLTNLKTVATDKDIEELIERAASLGTASVCVQPCFVKDAVKYSRGRVSVCTVIGFPNGYSTTATKIFEAKDACDNGASEIDMVININFVKSGRYDEVYDEIKLIADAVHAKGALLKVIIETCDLTEDEKVRLCKIVSDAKADFIKTSTGFGSAGAKVEDIVLMKENVSPDVRIKAAGGIRTVAAAKEMLDAGAIRIGASKLGE | Cofactor: Binds 1 or 2 manganese ions.
Pathway: Carbohydrate degradation; 2-deoxy-D-ribose 1-phosphate degradation; D-glyceraldehyde 3-phosphate and acetaldehyde from 2-deoxy-alpha-D-ribose 1-phosphate: step 2/2.
Function: Catalyzes a reversible aldol reaction between acetaldehyde and D-glyceraldehyde 3-phosphate to generate 2-deoxy-D-ribose 5-phosphate.
Catalytic Activity: 2-deoxy-D-ribose 5-phosphate = acetaldehyde + D-glyceraldehyde 3-phosphate
Subcellular Location: Cytoplasm
Sequence Length: 611
Sequence Mass (Da): 66032
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A0A6P6KSZ6 | MPDAMIRRSMLFFTLLVHFARGQVSYSIPEEISKGSMVGNIAQDLGLDLQRLKSGKARIYTRDSTEYIELNRNTGLLLIREKMDRESLCAKTTPCALHLQMILENPMEFYTITIEIMDINDNAPSFQKKDFSFEISESAVAGAGFMLGGAFDADVGTNDLQSYSLKPADKFQLELHSQADGSKNVEMILEKPLDRETQSSFTLLLEAFDGGDPVLSGTVQIHITVLDINDNAPVFTQKVYKTTITENAPKGTVLTVVSASDADEGSNSVVTYYISDTVNKNVADMFLINEKSGELILNGHIDYERVNHYELNIQGKDQGGLSNACKVIIDVLDINDNSPNINIVSSSHSVSEGSKSGTVISVLNVDDLDSGSNGQVQCVLNDDMSFSITSPSSNFFSLQTEQELDREREAEYNITVICTDEGVPALSSNVSLRVQITDVNDNAPVFEKSHYEAYVLENNTPGLSIFTVKASDADWNQNARVSYILEDSTVNGVYVSSYVSVQPDSGLITAVRSFDYEQLKDFHFRVKAQDGGSPPLSSNVTVKITIKDQNDNAPQVLYPVQTGASVVAEIVPRAAEVGYLVTKVVAVDVDSGQNAWLSYKLQKATDRALFEVGLQNGEIRTVRQVTDKDAFKQKLTVVVEDNGQPSRSAVVSINVAVADSFPEVLSEFTDFTHKKQYDENLTFYLVLALAAVSFLFITSVVVIISVKIYRWRQSRFLYQSNLPVIPYYPPHYADTGVTGTLPHGYNYEVCMTTDSRKSDCKFSTLGGQNVLMVDPSFAETMQHTIKKNSGLQNEHSTSQKPPNADWRFPPNQRPGPSGQHRFHTLQQRWTPYEKSRAGAHPDEAGASAGVIAGTRPWPNPPTEAEQFQAMMVAANVSEATATLGPRYNPQYGPDYRQNVFIPGSTATLMANPQQQVPQQALPPPQALPPVEAPKAAQTPASKKKPTKKDKK | Function: Potential calcium-dependent cell-adhesion protein. May be involved in the establishment and maintenance of specific neuronal connections in the brain.
Subcellular Location: Cell membrane
Sequence Length: 951
Sequence Mass (Da): 104689
Location Topology: Single-pass type I membrane protein
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A0A0G1CMN2 | MGTLYIVSTPIGNLEDITIRALHTLFSVDAIACEDTRVTGNLWELLKNKYNDLISVTHKPILIPYHNNNEQTITPELIQLLKQGKNIALVSDAGTPLVSDPGYRIVTEVQKQNIPIIVVPGVSAFLTALTGSGLQTNTWTFLGYLPEKQSRRITKLRNMKKSSVMLSSTYICYVAPHKFIQTMKDIHQSLGDIPCVIGRELTKIHEEYWKGTPQEAFGHFSHPKGEFVLLFTL | 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: 233
Sequence Mass (Da): 26133
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B4L4H7 | MQSSVFILTVIFAIIASNAPQIDALLRRCYQCRSRGELGSCKDPFTFNATDVDNEPGLSAIPCASGWCGKVIEGGGPYALDDYDTAIQRMCVQRGPDDNIDRCADTIYNYKKVYMCFCQGDLCNGTDGRWRQHHLLLLLTPTSIVFNMIVNKIFV | 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 excitability.
Subcellular Location: Cell membrane
Sequence Length: 155
Sequence Mass (Da): 17272
Location Topology: Lipid-anchor
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A0A960ND91 | MKSPRFERIALCAALLLCAGSAAFAQRKLPTISAFELGYSVRGWTVDDGLKGPYVGAFVQSPDGALLFSDSEGVIRYNGIAFEDLIETAPPGVPRRNILAIHEGPDGRLWTAGLNGQAMREADGRWAAVGEDRGGHSGVGKFARGPDGRLWCAVSTGSGLVLSAWEDGRFQPVPEKPLRTGYVQELMFDSAGQLWLSVADQGGGPPVYRLEGDSLVPESAADDRVGVLFHKEGDTRLWLATEQGIRVREGDAWREMVAFSDELPEKNGFSACSVDREGNYWIATRSLAVWVCRPDGEVSRLISEVVKLPNLVRDLFARRDGTIWFNGENGLVQLRRQPFTLWPQFQRDQRAPIRAMAEDGEGTIWFGGIGIYSLRPGEFVRPHWQDDTAVPSVYGIVGNPEGGAWFTAGRNSLNAVSSAAQRFVAQPPQGAGGVVDLAHHEGGVWYGLAKNLLRLQEGRLVPDLPEGVPPGFLECLAAAPAGFRSKGLFCHQDGKWRFAGLEGDVGALGMAPDNTVWARRGDGELCWLRDGQWYHANAGEMGIPTEFHMVCSREGSIWFQGLRGPVIRIDRKAAEAWLQGDHNVDLRLRTYGRAEGLAAEQAPYGSRKRTLMEDSRGRIWVATVLGTSAWLPSNDARHAAEASRVEPMPVLIEKVLVDDEPVANLNDTLTMMPNQHRLEIHYAGLDLAAPESVRYRYRIEGYQDEWADVEHRHAAYFQRIPPGNYRFQVIAADRYGVWNEDGAALAITVLPHWWEHWSFRIGAPAALVIFLLGVAWLRIRSFRHRALERARLHDEFSRGLIEAQESERARIAGELHDDLGQDLLVMKSRIDLARRRSGSATEQDTLRQMSESAADVLYKMRSLSHQLRPLHLDHLGLSASVKSLVKEVAEAAKLDYEVEADDTAEGLSPEAKVTVYRMLQEALNNIVKHAEAGSVKVELQRHDGRVTLTVEDDGRGFQQQTPAPGGGHSGHGLLAMKERCSLVGGRMIVNSKPGVGTLVLIEVPVPKAQES | Function: Member of the two-component regulatory system NreB/NreC involved in the control of dissimilatory nitrate/nitrite reduction in response to oxygen. NreB functions as a direct oxygen sensor histidine kinase which is autophosphorylated, in the absence of oxygen, probably at the conserved histidine residue, and transfers its phosphate group probably to a conserved aspartate residue of NreC. NreB/NreC activates the expression of the nitrate (narGHJI) and nitrite (nir) reductase operons, as well as the putative nitrate transporter gene narT.
Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Cytoplasm
Sequence Length: 1011
Sequence Mass (Da): 111482
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D6STN3 | MQYFLDLALKTAQGNMLADSEQKTLLELPYEETHRLFPGAELLRRNFCANKIRVCAITNAKSGKCSEDCAFCAQSAHHNTSINSYPLKNPGQMSLEGRNMSAQGVNRFSLVTSGKGLEAEEVQQVCRVTRELASQGISPCASLGVLKQQELQELKDAGLTRYHHNLETAPGFFPSICTTHDYSQRTETVRLARQTGLSVCSGAVFGLGESDAHVLELALTLRELDVDAVPVNFLVPIPGTPLENNDQLTPLRCLKIICMLRYMLPRHEIIVCGGRLENLGELHPLIFMAGASGLMTGNYLTRQGRGVAEDMQMITDMGLEPA | Cofactor: Binds 1 [2Fe-2S] cluster. The cluster is coordinated with 3 cysteines and 1 arginine.
Pathway: Cofactor biosynthesis; biotin biosynthesis; biotin from 7,8-diaminononanoate: step 2/2.
Function: Catalyzes the conversion of dethiobiotin (DTB) to biotin by the insertion of a sulfur atom into dethiobiotin via a radical-based mechanism.
EC: 2.8.1.6
Catalytic Activity: (4R,5S)-dethiobiotin + [sulfur carrier]-SH + 2 reduced [2Fe-2S]-[ferredoxin] + 2 S-adenosyl-L-methionine = 2 5'-deoxyadenosine + [sulfur carrier]-H + biotin + 2 L-methionine + 2 oxidized [2Fe-2S]-[ferredoxin]
Sequence Length: 322
Sequence Mass (Da): 35354
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A0A0P9DNX9 | ERGGEKRNAVLLVDFNFKTIDDLCRRVSLGKKGYVYIIDESAGNIVYHPQQQLIYIGLKYENVEQALKYTYGNYLDSSSGDMRLITIATVNNIGWKIIGVSYMDEIVTAKKEIGGFIAWLLLFVVVFVLLISAFMSAKISQPIRRLERSMSKVEQGVFDIHIQVQGDDEVGRLSRRFNYMVARIRELMGQIIREQEAKRRGELEVLQAQIHPHFLYNTLNSVVRLAGGGKSEEVITMITALSKFFRISLSKGRTVISIQDELEHVRNYLIIQKMRYKNKFEFAIEAEPEVLGCRTLKLILQPIVENAIYHGIEMMADEGFIRITAELVGEKVRLQVIDNGLGIPADKLERLLTGEAASGEGSSVGLRNVHERIRLGYGEAYGLEIESQLEEGTTVTLWIPAVRTEGAEER | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Membrane
Sequence Length: 410
Sequence Mass (Da): 46406
Location Topology: Multi-pass membrane protein
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A0A961B7C0 | TLYVTLEPCSTRGRTGACTDAILEGRFRRVVIGTADPNPKHSGAAISILRNRGVEVECGCLESKATDLIRFFAKHVTTGRPYLIAKSAITLDGRTTLRNGDGPWISSKESRRDVQRWRRRIDAILIGGETLRRDNPRLTLRGAFAKGRPQPWRIVLSQSGDLPEEAYPFTDSHRDRTRVFVGESLEAVLDRLGAEGVTSAMLESGGRLFGAALSAGLIDEIILYVAPFLGGGSTGLGSPGGFLADLESPTFKRFGNDIRVTGRPRLRPLS | Pathway: Cofactor biosynthesis; riboflavin biosynthesis; 5-amino-6-(D-ribitylamino)uracil from GTP: step 2/4.
Function: Converts 2,5-diamino-6-(ribosylamino)-4(3h)-pyrimidinone 5'-phosphate into 5-amino-6-(ribosylamino)-2,4(1h,3h)-pyrimidinedione 5'-phosphate.
EC: 1.1.1.193
Sequence Length: 270
Sequence Mass (Da): 29405
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A0A951US31 | MAAPGWVEEGNPTFGRVVGLRLCETQPTILLNTKRIEFKETLNYSNLFLPILVGIISTFIFSYLSIAWLLRYLQRQSTWVFVWYRLAFGIVILGAIFSRN | Catalytic Activity: di-trans,octa-cis-undecaprenyl diphosphate + H2O = di-trans,octa-cis-undecaprenyl phosphate + H(+) + phosphate
EC: 3.6.1.27
Subcellular Location: Membrane
Sequence Length: 100
Sequence Mass (Da): 11561
Location Topology: Multi-pass membrane protein
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A0A950GYA7 | MAGLAVAEALDRARSYSHAVVSFVGPDGYPVNVAAPFAVHDGGSLEIGPLGRDVQPAPGSTVEVTFSHIRPQPGIGYDERRYVNVWGTGRLDGPLLHVAPTRAAGWDEAETPFFEYAERSVPAGRAYIAELGVEPRLSPWWTFFLATRLPFLTATFIPVGLGGAVAAYDGRFEGLWFALALVAAVAVHLGLNMANDLFDDASGADAANVTPTPFSGGSRVLQYGLVSRRVMLVGCAACYAVALGLGLLLAVERGWPLLAIGAVGIVLSLVYSGPPFRLVHRGLGEPVTALGFGPVMAEGTYFATTGHWSGAAALASIPVAILIALVL | Pathway: Quinol/quinone metabolism; menaquinone biosynthesis.
Subcellular Location: Membrane
Sequence Length: 327
Sequence Mass (Da): 34180
Location Topology: Multi-pass membrane protein
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A0A849Y758 | MRARTGYFITFEGSEGAGKSTQIRRLASRLRRAGHRVIVTREPGVTSLGRRIRHLLQFSRAGQGMTEEAELLLFGANRAQHTREVILPALRRGEIVISDRYADSSVVYQGVGRALGRGFVERMNRFATGGLAPDLTFVLDLDPVEGLRRARGKTRRADRMEAQKAAFYRLVREGFRGLARAEPRRVKLVDARAGIAEVAARIEALLPARFRGGREKGARAAPRQTVFPKE | Function: Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis.
EC: 2.7.4.9
Catalytic Activity: ATP + dTMP = ADP + dTDP
Sequence Length: 230
Sequence Mass (Da): 25650
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A0A2E6X9T7 | MTSRGSSPIVLAAGGTGGHVFPAEALAAELTGRNYRLILFTDQRGCAFSGVLRDVETYRIHSSSSLRNKIPYFVRSGFKLALGLFQAIHLLRKLNPCAVIGFGGYASVPTMLAASLGVYPTLIHEQNAVLGRANKFLAHRVNNIATCFTVVEGLPETISSKVLVSGMPVRSGIIDYQNCDYHTVTPESPFHILVIGGSQGARVLSDVVPASIASMPEPIRQRFKIVQQCRPEDIERVHATYASAGLNAELASFFDDLPVRLAAAHLVIARAGASTIAELTTIGRPSILVPYPYAINNHQARNANAIDEAGAGWVLTESSFSVEKLRECLESLIRMPSVLERAAANAKALGEPEAVKKLADMVVRLIRDANISDGCVA | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Cell wall formation. Catalyzes the transfer of a GlcNAc subunit on undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide (lipid intermediate I) to form undecaprenyl-pyrophosphoryl-MurNAc-(pentapeptide)GlcNAc (lipid intermediate II).
Catalytic Activity: di-trans-octa-cis-undecaprenyl diphospho-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine + UDP-N-acetyl-alpha-D-glucosamine = di-trans-octa-cis-undecaprenyl diphospho-[N-acetyl-alpha-D-glucosaminyl-(1->4)]-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine + H(+) + UDP
EC: 2.4.1.227
Subcellular Location: Cell membrane
Sequence Length: 377
Sequence Mass (Da): 40461
Location Topology: Peripheral membrane protein
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A0A0L7RGR2 | MANPGDYISCGGFAFYNNFDSANLSRVELVKEPEILEKDGCESENKSCKSSNSEDTADYEFNLWTKHDCHGTQFQNNNRTWFYFGVKASTPGACVKFNIVNLNKQVKMFSQGMCPVFKIVPGHLHWERIRDRPTYTLDQKGSDFTLSFTYAIPENPKAMTYFAFTYPFSYNDLQNYLRRVEARVSKRAITSADDVYYHRECAIKSLEGRRMDLITISSFHNISTEREDRLNNMFPDKNEERPFKFWDKKVIFISARVHPGETPSSFVFNGFLNFLVNREDQIAAHLRRLYVFKLIPMLNPDGVARGHYRMDTRGVNLNRVYLNPSLKDHPTIYAARTLIRYYHYSYQLPKEDETSNMCLGNGENTLTIIDSSCAIANIVRDTTTRLLQQVTLMTLDEKHKDQPEIFQECALPKTNLDDMPQGGGEGLCNKAEESNNSVELKSDKKTYTAVGIGQLPKEDSGLYLYIDFHGHASKKGVFMYGNYFDNVEDTIMCMLLPKLMSINNPNFHFSSCNFTERNMYIIDKKDGMSREGSGRVAVYKLTGLIRSYTLECNYNSGRIVNTIPARVRDGVNKPVTSMFVPPKYTPAVFEAVGAALGPSILDLTNNNPNSRLPNSQYRSLRGVRSCLKLAYVNSLSSPNGKTLHKDDNNIIPSDSYNLKDIESQISNSSGSKNSLKSDTSLVKKPCIIRRTTSLYTAVKRIKNNKKPRQTLTRRPLKSQCVSNIENGSKLPIIGPKNVVKSFLKSSENRLKNSCFGCINDSSEVQIRDIQYVNKKLVTTNKLSKMALSSEETAIVKHGAKRLKIVSTRMNKGRPEVGESSNNSPEATKSLSKTILLSNKPNARGTSKAIKKHCHKIEQNKSKSSKSKKSVEIV | Catalytic Activity: C-terminal L-alpha-aminoacyl-L-glutamyl-L-glutamyl-[tubulin] + H2O = C-terminal L-alpha-aminoacyl-L-glutamyl-[tubulin] + L-glutamate
EC: 3.4.17.24
Subcellular Location: Cytoplasm
Sequence Length: 873
Sequence Mass (Da): 98779
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A0A2E6W4B9 | MSPVYNSIGVLLAGGLARRMGGGDKSLREVGERMILEWVVERSRPQVERLLLNANGDVTRFKHFGLPVVPDVLDGFVGPLAGVLSGLEWAIGSGCDVRWIVSFATDAPFIPINMVERFEAEAVSTDSDIVCASSGGRRHPVFALWPVTIAEDLRKALVYEKVRKIDRFTANYNVQVVEFDTDPIDPFFNVNDPGNLEEANTLYRQLKYERAI | Function: Transfers a GMP moiety from GTP to Mo-molybdopterin (Mo-MPT) cofactor (Moco or molybdenum cofactor) to form Mo-molybdopterin guanine dinucleotide (Mo-MGD) cofactor.
Catalytic Activity: GTP + H(+) + Mo-molybdopterin = diphosphate + Mo-molybdopterin guanine dinucleotide
EC: 2.7.7.77
Subcellular Location: Cytoplasm
Sequence Length: 212
Domain: The N-terminal domain determines nucleotide recognition and specific binding, while the C-terminal domain determines the specific binding to the target protein.
Sequence Mass (Da): 23569
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A0A2D8YX43 | MTDISTFLDMGGYAGFVWPSYGAVIGVLAVLLWLSLRGLKAAERELAQLEGEAPRARRASPTNDGAAQP | Function: Required for the export of heme to the periplasm for the biogenesis of c-type cytochromes.
Subcellular Location: Cell inner membrane
Sequence Length: 69
Sequence Mass (Da): 7334
Location Topology: Single-pass membrane protein
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A0A2E5MVP3 | MEKTTIPSDIAKLSFEDALEQLEKIVRELEEGSGELEKSIEAYERGAQLKFHCESKLQEAQTRVEKVVLADDGEVALVSAELD | Function: Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.
Catalytic Activity: Exonucleolytic cleavage in either 5'- to 3'- or 3'- to 5'-direction to yield nucleoside 5'-phosphates.
EC: 3.1.11.6
Subcellular Location: Cytoplasm
Sequence Length: 83
Sequence Mass (Da): 9265
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A0A1H6HGU4 | MRLFAAGLAVFLSIAPVSAGAGDLPEDFVRLRDIDSTISQDIRYAGPHNFIGVPVDGYLRAECWLTRPAALALKGVQDDLRAQGGGHSLIVFDCYRPQRAVDHFVRWAADPADTLTRAEFYPDLDKRDLFRLGYIAERSGHSRGSTVDVGLTGPGARPAQPYRAGQALTACTAPYRERFADGGLDLGTGYDCFDSRSHPASTEVGAEARENRRILAEAMEARRFVGIAEEYWHFTLRDEPYPDRRFDVPVE | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes hydrolysis of the D-alanyl-D-alanine dipeptide.
EC: 3.4.13.22
Catalytic Activity: D-alanyl-D-alanine + H2O = 2 D-alanine
Sequence Length: 251
Sequence Mass (Da): 27793
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A0A847CKS2 | MKKIKIFVLVLLILSLTACKQKNEEEISMYNNATVNAGFDTYISISVATTSQEKFDEYFNNLISDFKYLNQLFDIYNNYDGVNNIKTINDNAGIQPVEVDPIIIEMLELSKEYYDISDGQFDITLGPVLKIWHTYREEGLLLLEQGKLGSTPNIEDLIEANKCKGWDKVEINKENSTVYLNESCASLDVGAIAKGYATEYVAEKLEKENIKVGIVDAGGNNRTINTKLDGTPWNVGIQDPTGGSGSIIVVKSEGSKSFVTSGDYQRYYVSEDGKQYHHIIDPRTLFPSNYFHSVTVITEDSGVADVLSTTLYTVDFDTGNKIIEKFKKENPTQELEVIWIMDKDIDVNTEYKKQHSGYLIAYTKDLQDSIVWN | Cofactor: Magnesium. Can also use manganese.
Function: Flavin transferase that catalyzes the transfer of the FMN moiety of FAD and its covalent binding to the hydroxyl group of a threonine residue in a target flavoprotein.
EC: 2.7.1.180
Catalytic Activity: FAD + L-threonyl-[protein] = AMP + FMN-L-threonyl-[protein] + H(+)
Subcellular Location: Cell inner membrane
Sequence Length: 373
Sequence Mass (Da): 42092
Location Topology: Lipid-anchor
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A0A0D6JBV4 | MTNSAAPDSRNNTKPVQSDAEPAVGGAQLGKMLLEVGPLGVFFFANSQGGIFWGTGCFMAATLVALSLSFIIYKKIPIMPLISGVFILVFGALTLWLHDDLFIKIKPTLVNTLFGSILAAGLFFNQYLLKYVFGEVFRLRDEGWKLLTIRWAMFFFLLAALNEIVWRNFSDEFWISFKLFGIMPLTLVFAMAQVGLLKKYDASPKTP | Function: Plays a role in cell envelope biogenesis, maintenance of cell envelope integrity and membrane homeostasis.
Subcellular Location: Cell inner membrane
Sequence Length: 207
Sequence Mass (Da): 23094
Location Topology: Multi-pass membrane protein
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A0A9E4D280 | MQSESPRLSILGWDESHREQLEAPGPGRVLARVATEHRGYYDLFGLEPDPLVVADNAVVSPAFRRGATGPLDFPSVGDWVTVSPAAGAEGADVIETVLSRRSLFVRRAPGREPRPQAVGANIDHVLIVTGLDGDLSERRLERYLAVAYGGHAQPSIVLSKADRAGHSDDIADALVAIDRVAPGVRVIVTSSVSRRGVDELADLAADNSTVALVGSSGVGKSSLVNALVGEQLQLVQETRQDGRGRHTTVRRDLIPMASGGLLLDTPGMREVQLWDDSGLDQAFPEIAEAAADCRFGDCAHSGEPGCAVAAAVDTGLISAARLASYRQLEAEVEALHDELEERRRNRGEGRRER | Cofactor: Binds 1 zinc ion per subunit.
Function: One of several proteins that assist in the late maturation steps of the functional core of the 30S ribosomal subunit. Helps release RbfA from mature subunits. May play a role in the assembly of ribosomal proteins into the subunit. Circularly permuted GTPase that catalyzes slow GTP hydrolysis, GTPase activity is stimulated by the 30S ribosomal subunit.
EC: 3.6.1.-
Subcellular Location: Cytoplasm
Sequence Length: 353
Sequence Mass (Da): 37695
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B8CWJ4 | MIDVSSKKVAVIGLSKRTGVSVARTLVNCGAEVIVSDIKEKKDLKDEIEMLNEYEVEFDLGGHSNKLLDVDLIIVSPGVPLNLPFFKSISEKGIPVISEIEFAYHLTEANIIAITGTNGKTTTTALTGEILDKADIGEVRVGGNIGKPLIDVVQGLKKNDWVVAEVSSFQLETIRDFKPHISAFLNFSPDHLDRHLSVENYWKAKKRIFENQMSGDYALVNYDDYKVLKAVEDCSARVFGVSLKDNIEQGIYLEEDKLIINSADRSEVVLPVESIPLKGKHNIYNIAFASLIAYLAGASTEAIKEGVYQFIPEPHRLEEVTVLKDRVMVIDDSKATNPHAAINALKSFDQPIVLIAGGQDRDADFSEFAREIVSRVRALILLGETKDKLAETVLRMGFNNIYKVRDMNEAVRKAIAHTEPGDVLLLSPGCPSWDMYDSYKKRGQEFKEAVNKIRGS | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA).
Catalytic Activity: ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate
EC: 6.3.2.9
Subcellular Location: Cytoplasm
Sequence Length: 456
Sequence Mass (Da): 50613
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A0A1I0NN14 | MTAYTATVTVRLKRGVLDPEAETTKGALERLGFELEDLRSADRFEIDLEADSADGARERASEMAERLLANPTIHDYDVEVAER | 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 conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate. The FGAM synthase complex is composed of three subunits. PurQ produces an ammonia molecule by converting glutamine to glutamate. PurL transfers the ammonia molecule to FGAR to form FGAM in an ATP-dependent manner. PurS interacts with PurQ and PurL and is thought to assist in the transfer of the ammonia molecule from PurQ to PurL.
Catalytic Activity: ATP + H2O + L-glutamine + N(2)-formyl-N(1)-(5-phospho-beta-D-ribosyl)glycinamide = 2-formamido-N(1)-(5-O-phospho-beta-D-ribosyl)acetamidine + ADP + H(+) + L-glutamate + phosphate
EC: 6.3.5.3
Subcellular Location: Cytoplasm
Sequence Length: 83
Sequence Mass (Da): 9269
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A0A7W2CBB9 | MSFSLWIDPSFGASGDMLLGAFSEMLDDPDQALFPLRNLPIEDWKIDFEETLRNGLTATKAEVSYRETSTERKWSEIDALLKESSLPHPVIEGSRRTFLILAQVEAEQHGVTLDEVHFHEVGAVDAILDVVGTWLLRFALEDEVGAIEEIAIGPVGIGSGSVKASHGTLPLPAPATIGILKDCPVTNVSTNSETCTPTGAALLVSMVNRWGNIPNGYIRKSSRGAGTRNPTEYPNIISMVLTENSKTHKSSKTKYLIETNVDDVTPEILATTIEKLLELGAEDAWITPIIMKKGRPGQEIKVLCSADYLQSLQDLLLASTGSLGCRIIQVDKIELARTFETITLYNETVNIKVGPYGAKPEQKDLLRIAEKTNISLRQLSDEANFAFNKKQKQN | Function: Involved in the biosynthesis of a nickel-pincer cofactor ((SCS)Ni(II) pincer complex). Binds Ni(2+), and functions in nickel delivery to pyridinium-3,5-bisthiocarboxylic acid mononucleotide (P2TMN), to form the mature cofactor. Is thus probably required for the activation of nickel-pincer cofactor-dependent enzymes.
EC: 4.99.1.12
Catalytic Activity: Ni(II)-pyridinium-3,5-bisthiocarboxylate mononucleotide = Ni(2+) + pyridinium-3,5-bisthiocarboxylate mononucleotide
Sequence Length: 394
Sequence Mass (Da): 43250
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A0A284VLB0 | MGNRANFKGIKGKDMNWFYLQKYLPEYLTSEDMAAIDENAATLGIPGLMLMENAGAGTARITKENHKVDEKRIVIIAGTGNNGGDGCVAARHLLNLGASVCVILLGQPDDIRTHEAKTNWEVLSNLDVGIKVVKARNPSDLELLRNEIKSSDIIIDAILGTGIKGSIREPIATAIQLMNESGKPVVAIDTPTGLDPSTGDVKGDAIKAELTVTFHRMKKGLIDMEEYTGKVYVCDIGIPIEAELFTGPGDVRRVVKPRSLYSHKGDYGYVLVIGGSDVYSGAPALAAMASLRTGAGLAISGVPESASSAVKSYAPDIIVHPLEGDILSKRNIPYIKGLLEKVDSLIIGPGLGLAPETVDTIGEILHLSKVKKLPTLIDADAIKALKDDLEFLRDGDFLLTPHAGEFETISGVRVPNSWKERVETCVEFAKENRCTLLLKGHETVITDGKRLKINRTGNPAMATGGTGDVLSGIVGAYLAQGTDTFNAASAGAFIHGKVGDLAYEEKGFHIVASDLLDKIPVVLKHFDVEVKK | 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 is a result of enzymatic or heat-dependent hydration.
Catalytic Activity: (6R)-NADHX = (6S)-NADHX
Sequence Length: 532
Sequence Mass (Da): 56868
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A0A061IGF8 | KLSSIHSALHTCLVVQRKKPTAWATGHHTLQGTMVSQYKPGQLIHASWNFTIDEKYSFCFIRYNKNNKIWEVINYNATGILEKWEKNAELAQDLAVLSMGDSRHCLEEYLKHQKEMPSEDEPPLSKAGKDVVLHLPTDGVILDGRESTDDHAIVHYEWTLKQGDPSVDMKVPQPGTLKLSHLKEGVYIFQLTVTDTVGQRSSDNVSVSVLPRTYSMGGCSSVCSRYHFFCDNGCCIDITLACDGVRQCPDGSDEDFCQNLGLDRKMVTHTVATSAQPGTTGPSEGEGDPWFEKPQKVTPHNQPAIVPHSEKRVHSTQWAPESQIFPIMPDGNSSRKNQEGSYIFQSKNDQARGEHPAPEAGAVLPLALGLAITALLLLMVTCRLRLVKQKLKKARPITSEESDYLINGMYL | Function: Acts as a ligand for KLRK1.
Subcellular Location: Cell membrane
Sequence Length: 411
Sequence Mass (Da): 45744
Location Topology: Lipid-anchor
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A0A960E2Q6 | MSDQTTPTPVEEPTQHGVLSRLYHGETDWNIVGRWKLWFAISGVMLLIGGTAVVTRGLNLGIDFTGGTVWEVPAGDATVAEVESAVSDLGYNDVQVQEFTQVSGEGDARSLRVEAESQTEPTAATTDALDTALADLRSAADSVRGGSADRLNGVGNQLDGIEGPFDDEIPAELTDLQDQLDGFADGLDAAEDQTAYVTEVADLMAADVDALAEAEQAHREEVGRSVSEALAELTGSDIDQVTVDTVGASWGQQISQKAETALVVFLIVVLLYITLRFEFRMAVATVAALLHDLLIVIGVYALFQFPVTPATVIAILTILGYSIYDTIVVFDRVDENTRLVGRKTKLTYTDVANRSMNQVLMRSLNTSITTLLPITAVLVIGSFLLGATTLQEFGLALFVGVVSGTYSSIFIATPLLALLKEREPRYREVRERIAEHRPATGDDDEGELAGAAAGPGGDGPLITPRPRKQGKKR | 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: 473
Sequence Mass (Da): 50653
Location Topology: Multi-pass membrane protein
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D6SP88 | MIFDQYQGQRVHLGITGSVAAYRTLDLVRLLQKSSLSVSATITSSGCAFIGPLTLSALGADPVYTPDYSPVEQPFAHLSSQFSPHVFMVAPATANILAKASSGIADDLLSTQILSYPGRVLFAPAMNPNMWNNAATRHNIRQLRDFGHEIIEPDSGKVACGEQGQGRFPDIASLYYICLRELTSKDMVSTKVLITAGPTHEYFDLVRYWSNPSSGRMGLAIALALWLRGAEIHFVHGPMQPLLPLPGFHIYPVTTARDMYDKCSALWPDCTLGVFSAAVADFAPEKATDLKFKKQGRSALQVKMNPTLDILAEMSASRARDQKIVGFAAEAENLEANASAKLSTKSLDMIVANQVTSDCTPFGSDENQVLIMDKTGRMEYLPKLSKQKIAWRMADWILEL | Cofactor: Binds 1 FMN per subunit.
Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 2/5.
Function: Catalyzes two sequential steps in the biosynthesis of coenzyme A. In the first step cysteine is conjugated to 4'-phosphopantothenate to form 4-phosphopantothenoylcysteine. In the second step the latter compound is decarboxylated to form 4'-phosphopantotheine.
Catalytic Activity: (R)-4'-phosphopantothenate + CTP + L-cysteine = CMP + diphosphate + H(+) + N-[(R)-4-phosphopantothenoyl]-L-cysteine
Sequence Length: 400
Sequence Mass (Da): 43823
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A9A4N9 | MSESKEPNVVGINVLKQNGVDVDELVNELIKNAAVEFTAYYYFTNLRAHCTGMEGEGLKGIIEDARLEDLSHFESCIERIYQLGGSLPNDATEFIKISGCEFLQLPPNPTDHKAILEKCLKAEQGAIVNWNKICKMTLGKDPATYDIAKDILAEEIEHESWFLELIYGRPSGHMRRKYAGERPHTRKHSRALDMA | Function: Protects DNA from oxidative damage by sequestering intracellular Fe2+ ion and storing it in the form of Fe3+ oxyhydroxide mineral. One hydrogen peroxide oxidizes two Fe2+ ions, which prevents hydroxyl radical production by the Fenton reaction.
Catalytic Activity: 2 Fe(2+) + 2 H(+) + H2O2 = 2 Fe(3+) + 2 H2O
EC: 1.16.-.-
Subcellular Location: Cytoplasm
Sequence Length: 195
Sequence Mass (Da): 22025
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A0A940IAY3 | MVKLSRDNRGVTLVELLVVVVILSIIATVSVIAIGNIIQTQRDKAFVGNAYMLVEAARLYLTEQQIQGQSVGRIPYQLLVERDWMEELIDPYTSTKLNHQENHSYVSVKDGTVEGVCLKGHTKNLCFFDGSVQPIPLKALSVELIREN | Function: Required for transformation and DNA binding.
Subcellular Location: Cell membrane
Sequence Length: 148
Sequence Mass (Da): 16554
Location Topology: Single-pass membrane protein
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A0A3E2HLS2 | MPTIPCPRKGEADPVHAIFSLYVRFRQAYHAVKDRILAILYYHHRTPELIQKDVKVLSRLPQHLSVILKLEDARRGGAGLETLVDEVAEIASWCACAGIPMLSVYEKTGILKGYIPATHKAISRKLSSYFGPEHPILSLRAPNVSSLESVTSTPRGEPTEHPVPHVSVLLLSAEDSQDSLVDLTKTLAEMAQRSKLSPNDISQDLIDAEISESIMGEPDLLLLFGPVVELSGYXPMANPTYRNISCSR | Pathway: Protein modification; protein glycosylation.
EC: 2.5.1.87
Catalytic Activity: (2E,6E)-farnesyl diphosphate + n isopentenyl diphosphate = di-trans,poly-cis-polyprenyl diphosphate + n diphosphate
Sequence Length: 248
Sequence Mass (Da): 27344
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A0A6F8PRK1 | MKLVVTWTLALLITTALATLMLYDNGIVSMAWGGWIVETSLSFFVGGFLVLFIAAYFAVNFIIKIWRFPRYWRNRSQMRRYSKAQGAMTEGMIALEYGEWYKAEKALIRGAKQSEAGLINYLSAAKMAQNQNAFDRRDKYLQQARDAYPQEYMLIGLVEARLLLEQAPWEGLALLQALHEQEPKHETVLAEFCKVLVQLQQWDELERLMPLIRASKALVRDELWSLQRELWAGKLSQTKDVDALDHLWHQLSSKEQQEPVILAEYVEQRIGFGEEVGVAELIEKALKRQWDNRLCHQFGRLTLGPAFELLKKAEKWSKSQSENPILLLTLGRLACRSQMWAMGKSYLKQSLRIEPQLETFHALARCFEAEGQESEAALVYKQAIEQLQQKN | Pathway: Porphyrin-containing compound metabolism; protoheme biosynthesis.
Function: Involved in a late step of protoheme IX synthesis.
Subcellular Location: Cell inner membrane
Sequence Length: 391
Sequence Mass (Da): 45148
Location Topology: Multi-pass membrane protein
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A0A0B8NXY2 | MLPAGVSTSTALQFLMLSVGAIILLTTNVDPKKIVNTNVFIAGMSAVIIIFGIAWMSDTIIAHNKPYIISLVEDVVKAHPWTFAIAMYASSVFLKSQAAVLTIMLPLGFALGIPAEVLIGVLPACYAYYFFPFYPSDLAAITFDRSGTTKIGKYILNHSFLIPGFIGVLVATFIGYSLSVGLLPIWLWAVAIVALVFGVNSYMNRLSSETLKLA | Catalytic Activity: (S)-malate(in) + succinate(out) = (S)-malate(out) + succinate(in)
Subcellular Location: Cell inner membrane
Sequence Length: 214
Sequence Mass (Da): 23089
Location Topology: Multi-pass membrane protein
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A0A1Q3MPB6 | MNLMQPTHLLILLVIVVLLFGGSKIPELMKGVGKGIGEFQKGINESKMDNDGKKSDEKEDAKS | 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. TatA could form the protein-conducting channel of the Tat system.
Subcellular Location: Cell membrane
Sequence Length: 63
Sequence Mass (Da): 6871
Location Topology: Single-pass membrane protein
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A0A9D5NDP9 | MNGFFYIDKQSDWTSRDVCNKVQKIFNLPKVGHIGTLDPFATGLLIVCVGKATKASAYYDDNEKEYVATLKMGKKTSTGDLTGEVVEEKEIVSFTKKDILDVFKSLTGEIEQQIPMTSAVHVNGVKLYQYLHKGVEVDRPTRKVVVKDISLIEVGEDYIVFKATVSKGTYIRVLGEDIASKLNNLGYISSLRRTRIGDVKVEEAKTLGEVKDSDLVSIASLLKDIPSVVLSGERLIKAKNGMTISFDDITKSDRILLIDENNNVIAIYGYDHLNYYKCLRGLY | 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: 283
Sequence Mass (Da): 31608
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A0A960XLW2 | SFARYRRIFHHLLDMVCRRQPELVVLVDFTGFNRRFAHALRERIARQSPVFGNWQPRIVQYVSPQVWASRPGRGRKLAADIDLLLCLFSFEQDWYARRVPDLQVEWVGHPICDRHPAQWQALTGDDASDSGGDRPPLLLLLPGSRRSELQRHLPVMLEAARQLGGRKPLRARIVLPGEHLKALALRIAGAVGARAPAHSRDETAPSRLSLPLGGRGNNLTVELRVGELAQSLGEARVAIASTGTVTLECALFGVPTVALYKTSRLTYQIAKRLVTVDCMAMPNILAGSRVFPEFIQDAATPENLANAALELLTDDTRRRTVRRALRQLAQGLGGPGASRRAAAHLGQLVDS | Function: Condensation of UDP-2,3-diacylglucosamine and 2,3-diacylglucosamine-1-phosphate to form lipid A disaccharide, a precursor of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.
EC: 2.4.1.182
Catalytic Activity: a lipid X + a UDP-2-N,3-O-bis[(3R)-3-hydroxyacyl]-alpha-D-glucosamine = a lipid A disaccharide + H(+) + UDP
Sequence Length: 351
Sequence Mass (Da): 38787
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A0A7X0SNG3 | MLRSFFFARQSIRAKIFLAFSCVTALSLMAVSAVLYIHMSGEATRNATRFASDNLRHSNEVMQMILEDVDRINTVVVADSGSVDVIAALRSDAFDPSYEWFREKQGVTALLTNLIAYKTPITSIAVVGLNGKMYTSGTPEWVEKQRLTDDAIRQVSEGAGKHVYILRRGADGEPEALMVGRPIHYNNRPIGAVITELDYRQIERIYQAGLTPGVANDVVAQDGRIIVSGNPQLPADAALHTLAAEPPAVPKASSRIVINGERYITVSSAMPYAGWTAQSAIPVRTLLPRYQQLRLQMAETAAAVFLAVLIVSMGVAAGITRNLRRLYQDIQHVKQGRMTVRASIRTKDEVGHLYRAFSGMVEQLKVLMNDIKRGERQKREAELQALQAQVGPHFLYNTLNSIKYLARLRHASNIEETVASLIDLLRAVLGNTKEFVTLREELDYVQAYLNIQKLRFNNRIEARIRIDPELYGCVLPKMIVQPIVENAMIHGLAPLRQGGTLAIEGFRDGGFLVVSVTDDGVGMSGDQIERLLRKGGTEGSGRSSFSGIGIANVRERIRMTCGPESQLQISSVQGEFTTVKLRLPLAEGEGACDAARAVGG | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Membrane
Sequence Length: 600
Sequence Mass (Da): 65977
Location Topology: Multi-pass membrane protein
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A0A1W9P4G7 | MCMLKIGKAVLGKQPKIVLTIGEIKPHLLKPSLLKKVDILEVRIDCFKDIEEGNVVSFIWAVKKACLRATRKEKPIIATIRSKKEGGARYISPLIRLRLFKAVMPLVDGVDIEINSPILRKVFQEVRAKRKKVILSYHNFKQTPPDNKLKEIIKQAREKRGDIIKIACFAKSKKDTLRLLNLLFKHRGKNIVAISLGEEGIISRFLFPFFGSLWTYACLDKPFAPGQMNAAKMREALDRISNCSNV | Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7.
Function: Involved in the third step of the chorismate pathway, which leads to the biosynthesis of aromatic amino acids. Catalyzes the cis-dehydration of 3-dehydroquinate (DHQ) and introduces the first double bond of the aromatic ring to yield 3-dehydroshikimate.
EC: 4.2.1.10
Catalytic Activity: 3-dehydroquinate = 3-dehydroshikimate + H2O
Sequence Length: 246
Sequence Mass (Da): 27966
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A0A927WX26 | MKLVIVESPTKAKTIERYLGKDYKVLASFGHVRDLAMSGYNDLGVDIDNDFTPKYEIVPKSERVIKQLSAKAKDAEEVLLATDPDREGEAISWHLAELLDLDIDDTKRLEFHEITKKAILEAIENPRTIDMNLVHSQEARRITDRIIGFKLSALVQKKLNARSAGRVQSVALKLIVDREREIESFQKEVSYKIEAVFKIGKKEYTSILVNEKGKEVEFENKEEAMKVLSILSNQMKVLSCDAEEKQNYSLYPLTTSSLQQEAFSHYKYRASKTMKIAQSLYEGVDLDSGRVGLITYMRTDSIRLSPKFIYAAKEYIKDTYGEEYVGYAKTQKENDNVQDAHEAIRPTDVNITPSSIKDKISKDEYNLYKLIWIRAVVSIMTAEKYSLKTIIFDNKGYTFKATGKSSIFEGYKKLYKELSNSKYEDIEDLEVNSIIPVKENKLKEEETKPPYRYSEASLIKKMEEEGIGRPSTYASTIDSLHKSLYIKEENKYLKPTDIALLVNDRLQDYFKDFINVKYTAKMEKELDHIADGSLNKLVYLHHTYDDFKEPFESATIIMPKQAVMLDETCPECGGQLRVSRSKFGEFISCSNYPTCSFKKAKEDELTGKEKECPICHEGKLVVRKGKYSNFLGCNRYPKCTYMEPLKKHFFKKKK | Function: Releases the supercoiling and torsional tension of DNA, which is introduced during the DNA replication and transcription, by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(5'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3'-OH DNA strand. The free DNA strand then undergoes passage around the unbroken strand, thus removing DNA supercoils. Finally, in the religation step, the DNA 3'-OH attacks the covalent intermediate to expel the active-site tyrosine and restore the DNA phosphodiester backbone.
EC: 5.6.2.1
Catalytic Activity: ATP-independent breakage of single-stranded DNA, followed by passage and rejoining.
Sequence Length: 654
Sequence Mass (Da): 75295
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A0A924RSK0 | MRLFYALPLPLEVQNALEVAQKKLRGNWRAVRPDHLHITFAFLPKAPEGALQTLVKLGHKVGRNFAPFKVRLRGTGYFPGAGSPRVWFVKAEALLSGGEEGDEMGLISSELRSGLTLPFEDKPFKAHITLARKKGPAPRLEPMIFPLEWEAEEFVLIESQLHKSGPEYRTVKKFSLTGPKRPPKPLKPERLPEAEASRVSPLEPEELEVPSLLEPSQTNPRPNDL | 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: 225
Sequence Mass (Da): 25220
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A0A963N9C2 | MSAAMFIVMLLCFAFSIPIAVSIGFASIAGIQLFGSVPLLVVPKEIFGAIDKFALAAIPFFILAGNLMEVGGISRRLVEFAKAIVGGLQGGLAMTCVLTCLIFAAVSGSSVATTFAIGAILIPAMIKHGYPTGFATSLQATSAELGVIIPPSIPMILYGVSAEVSIGELFVAGFGPGLLIVAGLIVFVWIWSKIKGFGKDDHLGRLPFGTAFRQAALALMMPVIILGGIYGGIFTPTEAAVVAVFYALAVGMLVYREIRFEHLFPIFKKSV | Function: Part of the tripartite ATP-independent periplasmic (TRAP) transport system.
Subcellular Location: Cell inner membrane
Sequence Length: 271
Sequence Mass (Da): 28397
Location Topology: Multi-pass membrane protein
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F0SEG5 | MSEEIEKNKIYPTFNFTQGEVLLINKPYKWTSFDIVGKLRNSLKPLKLKVGHAGTLDPLATGLLIICTGKLTKQIDSFQAEEKEYTGTITLGSTTPSYDLETEPDQFFDISGISENQIKENTKHFIGDIEQFPPIHSALKKDGERLYLKARRGEEVKVSARKVSITEFEITRIELPEVDFRVVCSKGTYIRSLAHDFGKQLGIGAHLSKLRRTKSGNFRIDNAFEIMELVNHIKEIKQDPEFK | 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: 243
Sequence Mass (Da): 27651
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A0A6P6P6U1 | MNTVVIISIGTQFMHIALFHQAGYLNQAQWDGLTGRIVLNKTDGLRKEFNLDLISLKEDGTAKRAADAASRPTKLWTKIGVWNSYTGLNLTEMIDSKNITDSLANRTLIVTTILENPYVMYKKSDKVLYGNDRFEGYCLDLLKELSNILGFTYEVKLVSDGKYGAQNDKGEWNGMVRELIDHIADLAVAPLTITYVREKVIDFSKPFMTLGISILYRKPNGTNPGVFSFLNPLTPDIWMYVLLACLGVSCVLFVIARFTPYEWYNPHPCNSSSEVIENNFTLLNSLWFGVAALMRQVSSGVMDLMLVKRGL | Function: Receptor for glutamate that functions as a ligand-gated ion channel in the central nervous system and plays an important role in excitatory synaptic transmission. L-glutamate acts as an excitatory neurotransmitter at many synapses in the central nervous system.
Subcellular Location: Cell membrane
Sequence Length: 311
Sequence Mass (Da): 34990
Location Topology: Multi-pass membrane protein
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A0A832NGN6 | MGSSKRIAALDFGEARIGVAVSDPLRLFAQGVAVVCASEGWEEELASLLKRYEVELVLVGVPIREDGQPSHQAAKVLSQAEALIALLPEVRFAFVDERYTTKLAHSYLREVGRGMRRAKELSDMVAAEILLQEYLDAQRKEGSDGER | Function: Could be a nuclease involved in processing of the 5'-end of pre-16S rRNA.
EC: 3.1.-.-
Subcellular Location: Cytoplasm
Sequence Length: 147
Sequence Mass (Da): 16216
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A0A357QZ06 | MQQYFINQALTLNQPFSLSNEQKHHILTVMRYGVGKHVRVIDVDAKTFICEIVSTNPFQLMPFEQRVELTEPSVDITLIVGWIKKERFEWMLQKVSEAGATRVIPLISAYTVVKEKEDTLDKKLIRYNKITEEAAEQSRRTRSTEVLAPISLAAVGDYLSD | Function: Specifically methylates the N3 position of the uracil ring of uridine 1498 (m3U1498) in 16S rRNA. Acts on the fully assembled 30S ribosomal subunit.
Catalytic Activity: S-adenosyl-L-methionine + uridine(1498) in 16S rRNA = H(+) + N(3)-methyluridine(1498) in 16S rRNA + S-adenosyl-L-homocysteine
EC: 2.1.1.193
Subcellular Location: Cytoplasm
Sequence Length: 161
Sequence Mass (Da): 18486
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A0A520XS58 | MYSFLASHIDWIKALHVIAVIFWMAGMMYLPRLYVYHSQAVPDGEMEKALIGQEHRLLRIIINPAMIVAFLLGLVLVVLRHDQLAMISWLWIKLFAVFILFYIHGILAADRKKFARGERPRTEKFYRILNEVPAILIIIIVIMAIVEPF | Cofactor: Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; protoporphyrin-IX from protoporphyrinogen-IX: step 1/1.
Function: Catalyzes the oxidation of protoporphyrinogen IX to protoporphyrin IX.
EC: 1.3.99.-
Subcellular Location: Cell membrane
Catalytic Activity: 3 A + protoporphyrinogen IX = 3 AH2 + protoporphyrin IX
Sequence Length: 149
Sequence Mass (Da): 17360
Location Topology: Multi-pass membrane protein
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A0A357QYK5 | MYFNSMDIRRVSLCPIRKSAIYLMKKENVYMNKQLVIATNNGHKVEEFKKIFEPIGFEVTSTKDLGIDLEVEETASTYQENALIKAMAYRDLVSGWILADDSGIEIEALDFQPGVFSARYLGEQTPYEIKNRMILEKLEEETNRRAQFVCSIALVNEEGSYWVTINTCKGSIAHQILGSHGFGYDPIFIPDGYEQSFAQLPPEVKNEVSHRGKASKAAATYLHYLSEESYHE | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Pyrophosphatase that catalyzes the hydrolysis of nucleoside triphosphates to their monophosphate derivatives, with a high preference for the non-canonical purine nucleotides XTP (xanthosine triphosphate), dITP (deoxyinosine triphosphate) and ITP. Seems to function as a house-cleaning enzyme that removes non-canonical purine nucleotides from the nucleotide pool, thus preventing their incorporation into DNA/RNA and avoiding chromosomal lesions.
EC: 3.6.1.66
Catalytic Activity: H2O + ITP = diphosphate + H(+) + IMP
Sequence Length: 232
Sequence Mass (Da): 26413
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B8D0R7 | MEHKRLGRREVKTIFAGEFYVTTSSDVIISTLLGSCVAVCLSDDFNSVYGMNHFMLPTRVRESNNVYSGKYGEDAMELLITEMEKRGARINYMTAKVFGGGQVAGTTHSNVARANIRLAIQFLKKKGIPIIARDVGGKHGRQIYFWPRKNVFSRKIKMTEIKDVSVNE | Function: Probably deamidates glutamine residues to glutamate on methyl-accepting chemotaxis receptors (MCPs), playing an important role in chemotaxis.
EC: 3.5.1.44
Catalytic Activity: H2O + L-glutaminyl-[protein] = L-glutamyl-[protein] + NH4(+)
Sequence Length: 168
Sequence Mass (Da): 18927
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A0A9D5RWF1 | MKRYRRILKSEEFQEIIHHKRFFTSPSLCLYSAPRKKENSRIGLSVGKKIGCAVVRNKCKRQLRMMAIDIIPFEDNRDYIILARANYFNYSYEENKKQLENLYKKFKIRKEKKEKQNEIQ | Function: RNaseP catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5'-leader sequence and broadening the substrate specificity of the ribozyme.
EC: 3.1.26.5
Catalytic Activity: Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor.
Sequence Length: 120
Sequence Mass (Da): 14610
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A0A2P7EER4 | MNDAVIIRGLRLWAHVGVLEWERKYGQWFELDINLYLPLAXAGENDDLTKTLNYADVIESIRQLARQINCQTIECFSEQXIKTIDSIYGVMPXEXELRKCNAPIAGFNGCVAVRRRRD | Pathway: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate from 7,8-dihydroneopterin triphosphate: step 3/4.
Function: Catalyzes the conversion of 7,8-dihydroneopterin to 6-hydroxymethyl-7,8-dihydropterin.
EC: 4.1.2.25
Catalytic Activity: 7,8-dihydroneopterin = 6-hydroxymethyl-7,8-dihydropterin + glycolaldehyde
Sequence Length: 118
Sequence Mass (Da): 13589
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A0A5C8P6L4 | MLARFNLMLAFLLVICALGLVTSQHRARKLFIDLERAQTHAVEHEVRWDQLQVEQTELAKASLIDERARRELGMQAVPADRTLHLSVDPVTRSVSLSQPWIERPSGARLSGVRAAATGPRKPDNASGTRRASPAGAPRAAPTGAPPAKGVRQ | Function: Essential cell division protein. May link together the upstream cell division proteins, which are predominantly cytoplasmic, with the downstream cell division proteins, which are predominantly periplasmic.
Subcellular Location: Cell inner membrane
Sequence Length: 152
Sequence Mass (Da): 16541
Location Topology: Single-pass type II membrane protein
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A0A1Q9NIP9 | MLQTCTITELIINCCYFVGLYEDINSMTFPTSPNNKRIKGNILDNTKINLKDYFSLTKPRIIVLLTVTGIGGFFVPQPNMIGVSFLDLLIFVFVGYAAAGGAMTINNYIDRDIDILMDRTKDRPSVREEGLEPIKVLQFGIVLTTLGIVTAGLYFNLLTALFLSWGALFYLFGYSLFLKRKSILNTILGGLASPAPVWVGYAARTNSIPIEGWLLGAIVFIWTPSHTWALSTKHMADYKRANIPMLPVRLGMEKTAKITMFAGIITMIYGTWFAYYLESSSLVIIALIIPNMILFYGLWVFYDKPSTHTADICFKAHNAWMAIIFGIIVLFLWI | Pathway: Porphyrin-containing compound metabolism; heme O biosynthesis; heme O from protoheme: step 1/1.
Function: Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group.
Catalytic Activity: (2E,6E)-farnesyl diphosphate + H2O + heme b = diphosphate + Fe(II)-heme o
EC: 2.5.1.141
Subcellular Location: Cell membrane
Sequence Length: 334
Sequence Mass (Da): 37514
Location Topology: Multi-pass membrane protein
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A0A5C8P3F5 | MSEWLAMGGHGFYIWSSYAMMALCVAAEMWSLRQRRKAAWQRVDEAREEHESARPARRTETE | Function: Required for the export of heme to the periplasm for the biogenesis of c-type cytochromes.
Subcellular Location: Cell inner membrane
Sequence Length: 62
Sequence Mass (Da): 7319
Location Topology: Single-pass membrane protein
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A0A0L7QU56 | IFFVLVTLISTYAFVLAYKNTKFMLKQKIEVKTEDVVTMDMSRKLTEDKKISMQEKDERLWKKTEVANYKTTTFSIFCNNALFLALV | Function: TRAP proteins are part of a complex whose function is to bind calcium to the ER membrane and thereby regulate the retention of ER resident proteins.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 87
Sequence Mass (Da): 10242
Location Topology: Multi-pass membrane protein
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A0A663EHH9 | MNWGVFEGLLSGVNKYSTAFGRIWLSVVFIFRLLVYVVAAERVWSDDHKDFDCNTRQPGCTNVCYDHFFPVSHIRLWALQLILVTCPSLLVIMHVAYREAKEQRHRAAGGDDGRCIYPNPGKKRGGLWWTYLLSLIFKAGVDVVFLYIFYHLYRNYTLPRLVKCELPPCPNTVDCFISRPTEKNIFTLFMVVTACVCVMLSLVEAAYLIGKRCRECLLAGSGDSHQHGQDCALSPHRARGHGGAGFPRGGLQTSHGLHPRHGLQPRHAVRGGGSSLELPGGKQEPLTCPAPSSSSSSSSSIPPVQEPWGWQHLGVGLCSKALCLSRPGEGTLHHSAEFGVNPGAVGHVRSPRADRDKQLRGGCELPVVPGGRACPSQSGLAGPEGILAMNKNFCPSEMMAKLVVLLLLGHNTAKRGARAASPLERHRSHGQLRAGFGPAAVTNSWLPARVCWRKATENWRSPWSWA | Function: One gap junction consists of a cluster of closely packed pairs of transmembrane channels, the connexons, through which materials of low MW diffuse from one cell to a neighboring cell.
Subcellular Location: Cell junction
Sequence Length: 466
Sequence Mass (Da): 51108
Location Topology: Multi-pass membrane protein
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A0A6F8PYB0 | MNRIFIDVGNSRIKYAVSEDGHYEYLGAELVQDFLANIEQSLFAEVNDIDEVYFSTVGSLQNLDELTSAIQQHWNIIPTQLNAQRSCCGLTSGYADFHKLGSDRWLAMQGALAITTQPFIVVDAGTALTIDAVIDGQHKGGFIVPGLSTMHNSLATGTALLEMPTNNDLPEDMSQNLLANNTASAVLAGTLYMSAAFVNQVVVDLNQQLQTQFKLFLTGGDAAQLASLLDYQYSYIPDLVLHGMCSVVESVKKS | Cofactor: A monovalent cation. Ammonium or potassium.
Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 1/5.
Function: Catalyzes the phosphorylation of pantothenate (Pan), the first step in CoA biosynthesis.
EC: 2.7.1.33
Subcellular Location: Cytoplasm
Catalytic Activity: (R)-pantothenate + ATP = (R)-4'-phosphopantothenate + ADP + H(+)
Sequence Length: 254
Sequence Mass (Da): 27604
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A9KV33 | MTDQELAPSIAQCGIALLLAAFLHIALTAAVFWSPAVITPTGQAKAVGNGGIEISLGPAGSAASALQQTTAPVAEQKSEPITEQLDKPEPLPPVAKKVTPTPRPKPKPITPTPQDELTTQSEVNEQHSSPTETPSPTALAASANEVGQSGEGHSAEQNKAASGDNMTGGGLLGDTQDYTATLLAWLEQHKEYPRTARNRRQQGTVMLYFVLDRQGRVSASRIEQSSGYQTLDAEALKMLERAQPLPAIPDAMPNETLELVVPVQFFLR | Function: Interacts with outer membrane receptor proteins that carry out high-affinity binding and energy dependent uptake into the periplasmic space of specific substrates. It could act to transduce energy from the cytoplasmic membrane to specific energy-requiring processes in the outer membrane, resulting in the release into the periplasm of ligands bound by these outer membrane proteins.
Subcellular Location: Cell inner membrane
Sequence Length: 268
Sequence Mass (Da): 28462
Location Topology: Single-pass membrane protein
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A0A3C2CY67 | ESFKLYIFLSGIIFLVIVLSLVTYVLISLLLKKMYNLKDSMKRVAKGDFNFDVDIKGQDEIAELAFHFKSMLGKINSLIADAVNKQATAKETELKALKTQIDSHFLYNTLENIKMMAEIEGKYDISDAITSLGEMMRYNLRWKNDFVVLEEELNYIKNYVDIMNLRMDGLLTLKIEVPKDLLEQEVLKMSLQPIIENAVKHGIVPNNLSREGVITVKASYVDGSAIIDIKDNGVGMSPAHCELLNSRIQSDLDPQYEASKTGNGIGVKNVYERIKLYYGEGYGVSVTSVEGEYTVVTVAIPGKIMKGGSRSV | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Membrane
Sequence Length: 312
Sequence Mass (Da): 34943
Location Topology: Multi-pass membrane protein
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A0A396TWK6 | MTNDKFDRELNSLYQQRQSQITPPNVCVSEKSSAPKRTPLQFIAVFVAGGFASFAIMAFISHLSSAPEPDMAIPLTHVEIDINDVVDDDEDQTVIVIKQPLPKPPTSTQPLAQESMIPSPVAPITPLLAEDIVISPATDTRLPTINLSAFKIEPVLKVMPKYPRNVTLKKVSSIQLRYTITTDGAVKDIVVVKSDVANTLEKATKKALLQWRYKPHATYPIQNEIIFEFEPNEP | Function: Interacts with outer membrane receptor proteins that carry out high-affinity binding and energy dependent uptake into the periplasmic space of specific substrates. It could act to transduce energy from the cytoplasmic membrane to specific energy-requiring processes in the outer membrane, resulting in the release into the periplasm of ligands bound by these outer membrane proteins.
Subcellular Location: Cell inner membrane
Sequence Length: 234
Sequence Mass (Da): 25975
Location Topology: Single-pass membrane protein
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A0A9E6FAN0 | MPDFEYVANALDLRERLDKVLVKAMPGFSRNRIQQLIDFGYVLVNDEEVKRNTKVRENDIITAEYPEAESLEVVAEKMDLDVLYEDSDLLVINKPKGLVVHPGAGNPSHTLVNGLLYHCQDLSGINGITRPGIVHRIDKDTSGCLVVAKNDKSHHELSHQLQERTLKRTYWALIHGVLEHNSGRIEAPIGRDKSDRQKMTVTAINSKPAVTHFKVLERFKNMTLVECQLETGRTHQIRVHFQYIGFPLVGDLKYGLHQTLDTDGQCLHALAIDFIHPTSEQAMHFEAPLPTYFTTLIQKLRSGDAV | Function: Responsible for synthesis of pseudouridine from uracil.
EC: 5.4.99.-
Catalytic Activity: a uridine in RNA = a pseudouridine in RNA
Sequence Length: 306
Sequence Mass (Da): 34620
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A0A2E3L3L1 | MTSSDASACFLLAGMFFSIVFLLAPSVSVTVQIIALGIAVSVLGLPHGAIDTYIARQNGLWLSSSGLATFTGVYLLITFFVIGAWVVLPVLSLSVFLIISAWHFGTDANAQNFAERWLFGSLVFCLPALFHPIDVANLYEILSGPLARNIVSITCVWAPISAIIVIFMICTQLSDRPQRRKDIATILGLITFAWVLPPLVYFAIYFCALHSPTHFCRVIKLIPASDRRRAIMHTIVFTVITLTLAGLSLNMLFGELPVEQSVVQIVFVGLAALTVPHMVLIDGICRSKLG | Function: Catalyzes the cleavage of beta-carotene at its central double bond (15,15') to yield two molecules of all-trans-retinal.
Catalytic Activity: all-trans-beta-carotene + O2 = 2 all-trans-retinal
EC: 1.13.11.63
Subcellular Location: Cell membrane
Sequence Length: 290
Sequence Mass (Da): 31583
Location Topology: Multi-pass membrane protein
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F4XGH3 | MSKKPQYDPEEIRFPDQVIKTAPLVKEMEDSYIEYAMSVIVGRALPDVRDGLKPVHRRILYAMYEDGLTSDKPFKKSATCVGDVLGRYHPHGDQSVYDALVRLGQDFSMRYVLVDGHGNFGSIDGDPPAAYRYTEARMSKLSNEMLRDIEKETVDWDPNFDESRKEPRVLPSRFPNLLVNGSSGIAVGMATNIPPHNLTEVINAVICVLDNENATLDDLMEHIQGPDFPTKGMIMGRSGIRAAYATGKGHIRVRARTEFEEFGKDRTRIIVTEIPYQVNKRMLIKNMADQVEDKRLEGISDIRDESDRNGMRIVIELKRDANPQVVLNRLIAQTQLQVTFAINMLALVHDQKQPKILTLREILDEYIAFQEQIITRRTIYDRRKAQERAHLLEGLLIAQDNIDEVIKIIRTSYDNAKERLMTRFGLDDVQAQAILDMRLKALQGLDREKLEAEYKELEERIAYYDKLLSDEGLLRQVLKDELTEIRDKYGDQRKTEIAFVEDDLDIEDLIEEEQCVFTLTQAGYIKRTPVSEYAAQSKGGQGRKGITTRDEDCVVDVFTASTHDYLFFFTDTGKVYRKKGYQIPESGKTAKGTNIVNILQVEQGEKVQTMIHTRELDNPDLYLVMVTRNGTVKRLPVTALKNIRNSGIRALRLEEGDQLISVRETDGTKKILIATHDGMAVCFDENDVRPMGRDAVGVRGIRLREGDYVVSAARATAGRTVLTITEKGYGKRTPVEDYRITNRGGIGIKNYAVTEKTGKIVGIKVVDGSEDLLLVTQAGILIRTHVDAIREAGRATQGVIVMRFKEEGDKVISLALAEREETAEVAQPETAEAETMEAETTETPEETQADQE | Function: A type II topoisomerase that negatively supercoils closed circular double-stranded (ds) DNA in an ATP-dependent manner to modulate DNA topology and maintain chromosomes in an underwound state. Negative supercoiling favors strand separation, and DNA replication, transcription, recombination and repair, all of which involve strand separation. Also able to catalyze the interconversion of other topological isomers of dsDNA rings, including catenanes and knotted rings. Type II topoisomerases break and join 2 DNA strands simultaneously in an ATP-dependent manner.
Catalytic Activity: ATP-dependent breakage, passage and rejoining of double-stranded DNA.
EC: 5.6.2.2
Subcellular Location: Cytoplasm
Sequence Length: 852
Sequence Mass (Da): 96257
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A0A960EU19 | MPDDRCEVVLYHPDHNARLSRLPLTHVRKVVDLWAERSTGLGARDDVNYVLVFENHGAEVGATIAHPHGQIYAYPDVPAAPAHQFARLTAGHQLLEESEELTIVERDGWRAWVPSAPIHPYGLRIAPLAVRPDLPSLDDQERDGMASVMSEALARLEGVFDPPMPYMFWIHQRPFDGDSWPGAHMHVEVVGPHRSPGVMRYVAAAELGSGQYLNPVVPEDAAERLRAVKLGDAG | 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: 234
Sequence Mass (Da): 25904
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A0A2E6W1M2 | MWRKHYMNINKSIIRTADICDEYPEASVIQINFKDYGKKHEFQGVAVIYSTFEDIRGIKELLASDGEGKVLLVNGQGSLRRALCGGKIAAKACSSGWEGLIFNGAIRDQHEIVEIDIGIKAIGSSPKRPSQDGIGGLKKSTVLGDVVVNSGDYIYADRDGVVVLTANAK | Function: Catalyzes the aldol cleavage of 4-hydroxy-4-methyl-2-oxoglutarate (HMG) into 2 molecules of pyruvate. Also contains a secondary oxaloacetate (OAA) decarboxylase activity due to the common pyruvate enolate transition state formed following C-C bond cleavage in the retro-aldol and decarboxylation reactions.
EC: 4.1.1.112
Catalytic Activity: 4-hydroxy-4-methyl-2-oxoglutarate = 2 pyruvate
Sequence Length: 169
Sequence Mass (Da): 18344
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A0A7C6H149 | MPVLSTIIYILLFLFFISLLIIFHELGHLAAAKAFNVYCLEFSVGMGPLIFKRKRKGGETQFSLRAIPFGGYVAMYGEGVELPEGVKIDKSRSLNGVKWWKRAIILLAGILMNSLLALVFFAVSNTFPQQILYRNQLNIAASSIASDAGIEDGTIFKIYQEFNYDDPVSESKKTFYLIDKETTINDDDSIKYATCLNYESLDSFSKRDLADYIFIYEQVDNNPDFAKKVDMSLITTAKINFTSMVKDVESGEMVADQIYPIVISKEGDKFASFGASLYLETWTNDFKGVVTQTFTDFGNSSVLLFKAIGDLFTKPSSWNNMGGIIAVGFETTAVLQNFGIGKFLFYWGFISVNLAIFNLLPFPGLDGWHLLVLIIEGITRRKVPEKVKNIVSFVGLAALLVLMGVIVIKDLLKYVFFLVL | EC: 3.4.24.-
Subcellular Location: Membrane
Sequence Length: 420
Sequence Mass (Da): 47032
Location Topology: Multi-pass membrane protein
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A0A960MWX1 | VDNGVLHFRIVRKAPGRLVGEALTEGQMGSRRHINLPGVRVNLPSLTDKDREDIALAAAIDADYVAISFVRDAGHVGDLRKALEAQGSPARIVSKIEDQEAMRHLREIVEASDAVMVARGDLGIEVHIEELPVVQRTILEECARVGRKVIVATHMLESMIENPVPTRAEVTDVANAVYEQADAIMLSGETSVGHYPVKCVEIMDRIARRMERERGARFCEAIELTTEKQHTVRS | Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 5/5.
EC: 2.7.1.40
Catalytic Activity: ATP + pyruvate = ADP + H(+) + phosphoenolpyruvate
Sequence Length: 234
Sequence Mass (Da): 25874
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A0A4D8XQY1 | MHQLVTGPEILELDKSVGIPPIIMMENAGLSVSNYILNRLVLKNQYLSVAVVCGGGNNGADGLVVARKLHSLGHHVEVFFVSPRVCGDVDSVLSSFKSEEGLLNAQLALVTHEIPFHTTLGHLGKFSVIIDAILGAGTRPTSDFAQETRLQCVFDAINDLCKEALVVSVDVPSGICPTSGICLYARPIRPSATITFGRVKSGLAFYQYVGELVLATISYPRHVEFKSDRGIMSFCDIPILSSRDPLGHKGSFGKVFVLAGSGRYYGAPMFSSMSFLKAGGGYARLFCPNAVGAVVAGSAPEVVQLGNEWTEVVEEFLITDSDVVVAGPGIGLDQAACDDLNSCIKVMIRSRVKAVVFDGDALTILAKGKSMLQSVVAQLTNAGIDTILTPHPGELRRLFSVSETSEYGRICATQKVIASSYKDQKLTVVVKGATSATVSSHSIVLKVSGNSGMATCGSGDSLTGVIAAMVCNSLLSNDIQEAITAGVFIHGLAGDLAATSVGEDGMVATDILNHIPAAMQELRTSRDSLIKKYLPRIV | 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 is a result of enzymatic or heat-dependent hydration.
Catalytic Activity: (6R)-NADHX = (6S)-NADHX
Sequence Length: 538
Sequence Mass (Da): 56840
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B8CY37 | MLNTIKKWLIAIRPFGFATTLVSTTLGASLAFYHGSFNPGLYFMTMAPLLLIHTGTNLINDYYDYKFGLDGEQSLSSSGLNRVNGQIKLNQIYTVAIACFLASIPFGAYLTLLRGPIIFILGTLGALAGYFYTASPISYKYYGLGGPSIFIFMGVMMVWGMFYIQTGINSWYPVLVGLPVSFLITGMQHSNELRDYENDMKNGIKTAPVIMGFERARYYYYFLIISAYISLVLLITYNLLPLWTTLAFITIPLAYLPVKKVATATSQNDLKGIDYQMARLNIQFGIFLSGAIIISKYM | Pathway: Quinol/quinone metabolism; menaquinone biosynthesis; menaquinol from 1,4-dihydroxy-2-naphthoate: step 1/2.
Function: Conversion of 1,4-dihydroxy-2-naphthoate (DHNA) to demethylmenaquinone (DMK).
Catalytic Activity: 1,4-dihydroxy-2-naphthoate + an all-trans-polyprenyl diphosphate + H(+) = a 2-demethylmenaquinol + CO2 + diphosphate
EC: 2.5.1.74
Subcellular Location: Cell inner membrane
Sequence Length: 298
Sequence Mass (Da): 33309
Location Topology: Multi-pass membrane protein
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A0A0G0BBB0 | MSKEILHIWGPFSIQSYGLCMAIGILVASWLFLRDKRRESIISYDQFNKVITFAIIIAIVGGRSLFLAEESESITDFLGIFKIWEGGLSSLGAILSVLIFVPIYLNSLGVNFIRFFDLAALYAPIIECIARIGCFTAGCCFGMETSLPWAVLHKEYTSLGQTVYKYVHPTQIYSSIVALFIFILMQIVVQKRLKKQGQLIAAYLMLTSLARFSIDFLRGDRTYFDNTASFSSLSSSQLISILICLLSFISIILIQIYSKKTKNK | Pathway: Protein modification; lipoprotein biosynthesis (diacylglyceryl transfer).
Function: Catalyzes the transfer of the diacylglyceryl group from phosphatidylglycerol to the sulfhydryl group of the N-terminal cysteine of a prolipoprotein, the first step in the formation of mature lipoproteins.
Catalytic Activity: 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol) + L-cysteinyl-[prolipoprotein] = H(+) + S-1,2-diacyl-sn-glyceryl-L-cysteinyl-[prolipoprotein] + sn-glycerol 1-phosphate
EC: 2.5.1.145
Subcellular Location: Cell membrane
Sequence Length: 264
Sequence Mass (Da): 29703
Location Topology: Multi-pass membrane protein
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A0A7V7BN84 | MLTITDLKQFVYCPRVIYYTYVQPVPKKPTFKMVYGREQHAELNKKEKRRGLKQYNLIEGERIFGYPIRSLEMGLTGKLDILIDTKDENGQRYFPVECKDTDRGIYNNIKYQLVAYAMCLEEMTNSIVSEGFIYIIPEGKAHKIEITSEQKEFVRKMISMINKIIKDEYYPEPRARKRCWDCEYIRYCNDHDISSQEEQKEKNLELVKRLFNMEERI | Cofactor: Mg(2+) or Mn(2+) required for ssDNA cleavage activity.
Function: CRISPR (clustered regularly interspaced short palindromic repeat) is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA).
EC: 3.1.12.1
Sequence Length: 217
Sequence Mass (Da): 26016
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A0A832BA78 | MELTGAQSLIKSLENQGVDVVFGLPGGAILPVYDPIIDSSIRHILVRHEQGAGHAAEGYAQVTGRPGVAIVTSGPGATNIVTPLANAYMDSTPLVVVTGQVATNSIGTDAFQEVDITGVTSGVTKHNWLVTDAQDIPSVIAEAFHVATTGRPGPVLVDFPKDVANAVTTWQDPGPVDLPGYRPSPSPDPAAVAAAADLILAAERPVLYVGGGVLKADASQALADLVELTGIPVVTTLMARGAFPDSHRLCLGMPGMHGNYTAVTAMQRADLLVALGSRFDDRVTGKVSGFAPHAKVVHVDIDRAEIGKVRRPEVAVVADCRLAIEALAAVLRARASARPDVLDPGRLAPWIATIADWRARFPLAYDRSVSTGTRHGSQLLKPQFVIEQLRATTPDDTVLVSGVGQHQMWAAQHWRFDQPRSWVNSGGLGTMGFAVPAAIGAKVGRPDRMVWAVDGDGCFQMT | Cofactor: Binds 1 Mg(2+) ion per subunit.
Pathway: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 1/4.
EC: 2.2.1.6
Catalytic Activity: H(+) + 2 pyruvate = (2S)-2-acetolactate + CO2
Sequence Length: 462
Sequence Mass (Da): 48624
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A0A3C2CUL2 | MGDFEIFGIPVSLGTMVYQAVLFTILVFLLKRFFFTKLVNAMEKRQQTIDNQLQIAEKTRMDAERLLYDQQAAAAKARLEAKELMLKTQQQADAILQDARKDANKIRSQAREDLKSRRSVSQK | Function: F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation.
Subcellular Location: Membrane
Sequence Length: 123
Sequence Mass (Da): 14183
Location Topology: Single-pass membrane protein
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A0A350IY65 | MQNFMNWMEAHVMPVAGKLGTNRYLKAISSGFIAIMAATIVGSIFTLIGNLPFTGWTAWLASTGLNKILALPGQCTTDLIAVYAVFFIAYNLAQTFEVDGKGAGLAALVSFFVVTGRATYFASAAEDAAAVSALSTGFLGAKGLFTAMIVALIGARIYVFIVKKGWVIKLPDSVPPNVAGSFNALIPSFFVVVVFLLVAMGMSFTSYGDLHTMIFTVIQSNLMRFMGDNIFSWLFFNFMTNILWFFGLHGGNIVGSITNPVYTPLALENLAAFEAGETVMPYIITGAFGKTFTFGGVGSMFGLAILMTFFAKSKQYKMLGKLSLPTTFFFINEPLLFGIPVVLNPLFFLPLMFTTPLLGTLTYFMMKIGVVPIPHGIQLPWTMPPVFNGFLQAGIGLAIWEVLMVLASMVIYYPFFKMGDKQALAEENGEA | Function: The phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS), a major carbohydrate active -transport system, catalyzes the phosphorylation of incoming sugar substrates concomitant with their translocation across the cell membrane.
Subcellular Location: Membrane
Sequence Length: 431
Sequence Mass (Da): 46812
Location Topology: Multi-pass membrane protein
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A0A7X8AQA5 | MSKEKLSFEQKLARLNAIVSELESGKLSLDASLKLFEEGNALSKELATELNEAKLKIEELQGK | Function: Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.
Catalytic Activity: Exonucleolytic cleavage in either 5'- to 3'- or 3'- to 5'-direction to yield nucleoside 5'-phosphates.
EC: 3.1.11.6
Subcellular Location: Cytoplasm
Sequence Length: 63
Sequence Mass (Da): 6992
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A0A847CJU8 | MLENLVDEFKDKKVLIWGLGLEGNSTYTFIKNILPDQQLFICDRNKPDQSMFKNDIVIDEKDLDTSEYDIVMKAPGIKVKKNTGNISGQAPLFLKYFKDNVIGVTGTKGKSTTASLIYHVLQGKFSNIYLVGNIGVPCFDILKFMTLDSIVVFEISCHQLEFSTSSPYIGVLLNLFEEHLDFYDSYELYKNAKKQIYLNQTNNQMAIINYDIINEVEDPERFMWINKDIYADGKTLVTPYDSVTINETRLIGSHNMSNLAVVYYITHVLYGITNDMFLERVKTFKPLQHRLSFVGTFNTITYVNDSISTIGQSTIQAIKSLDNVSTVLIGGYERNIDYSELISFLKNVEIDNIILMYKTGKRILGSLDETKAKVYYVDDLKEAVKLAKTITKRNKICLLSPAAASFGHFKNFEERGNIFSDLVRLDY | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA).
Catalytic Activity: ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate
EC: 6.3.2.9
Subcellular Location: Cytoplasm
Sequence Length: 427
Sequence Mass (Da): 48724
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A0A960J075 | FAMGSSTENSAFGPTRNPRDTTKVPGGSSGGSTAAVAAGFAAVGLGSDTGGSIRQPAALCGVVGMKPTYGRVSRYGLVAFASSLDQIGPLTHTVADTARVLEVIGGHDPADTTSIPEAMPALESVLGDGVAGLRVGVVRELMGEGIAPDVAARVREAAEVLAAAGAEVGEASVPAVTYGLSAYYLIAPAEASSNLSRYDGVRYGLRVDAPTTPEMNLASRTAGFGAEVKRRIMLGTYALSAGYYDAYYGKAQKVRTLIIRDFAAAYESFDLLLAPTSPTTAFPLGAKVSDPLTMYLNDICTIPSNLAGQPAVSVPFGAGDDGLPVGVQLLAPALAEAPLLRAAAVLEEGAPS | Function: Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in organisms which lack glutaminyl-tRNA synthetase. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu-tRNA(Gln).
EC: 6.3.5.7
Catalytic Activity: ATP + H2O + L-glutamine + L-glutamyl-tRNA(Gln) = ADP + H(+) + L-glutamate + L-glutaminyl-tRNA(Gln) + phosphate
Sequence Length: 352
Sequence Mass (Da): 35771
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A0A520XVB1 | MARNARDHSVLAAFGAHHRGRTRVVLLGLDPPGNHRVIKPLVEGDEALVLGLGLYGVAVARALRSRGISVTVAEDRPTDLTATLAEELDVTLLAEPAVEALVEALARADAFVPSPGVPQQHGAFAAAVATGVPTISEFDMARWWDNRPIVAITGTDGKTTVTMLTVEMLQRSGVAAAAAGNNDLPLIEAIDDPQTAVFVVEASSFRLAHTQRFAPRAAAWLNFAPDHLDVHLDLTSYEDAKASIWADLPVGGLAVATLADPTVMKHVPTDRRVSTIGLTEGTSRVVGDELSIDDVPICRIDELPRHFDHDITNTLTAATLALELGATRTGVRDAIMSSEALPHRIQFVETIEGIDFYNDSKATVPHAVVTATGSFDSVILIAGGRNKGLDLRDMASRSPSVREVVAIGEAAPDIESAFGGLAPTVVAQDMRDAIRIAFRIADPGEVVLLSPGCASYDSYTSYVARGEDFIGLVAELAKDQRDGDNP | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA).
Catalytic Activity: ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate
EC: 6.3.2.9
Subcellular Location: Cytoplasm
Sequence Length: 486
Sequence Mass (Da): 51571
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Q65Q75 | MRKYLTLILAAFAGFAVAEEPSSSLTMEQIPENIAPAYTNPQKDAGNIPTTFPFQPPLVPHSVRGLQVTKNANQCLSCHSPEVSPTTGAPRVPESHFLDRDGKPTEGTSPRRYFCLQCHVQQTDVNPIIQNKFESIRAKQGK | PTM: Binds 2 heme C groups per subunit.
Function: Electron transfer subunit of the periplasmic nitrate reductase complex NapAB.
Subcellular Location: Periplasm
Sequence Length: 142
Sequence Mass (Da): 15647
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A0A8N1S5Y0 | MCRSMKRVKIVPDRPNRLFESWLEEWRDEATLRNSELRSHFTKALDSLKRYPLPLETAGIKEDCTTTLRQKPVVEKCDVEIQTETVVAKQDKIIKKNAPRRLINASEAKSKEVARQICLKPSTFDIILLVDTQETCGSKTKPQHDATLKELTQLSVLFEVRRLTIGDFVWIARCRETNDELIIPYIIERKRMDDLSASIVDGRFHEQKVIQECFL | Function: Interacts with EME1 to form a DNA structure-specific endonuclease with substrate preference for branched DNA structures with a 5'-end at the branch nick. Typical substrates include 3'-flap structures, D-loops, replication forks and nicked Holliday junctions. May be required in mitosis for the processing of stalled or collapsed replication fork intermediates. May be required in meiosis for the repair of meiosis-specific double strand breaks subsequent to single-end invasion (SEI).
EC: 3.1.22.-
Subcellular Location: Nucleus
Sequence Length: 215
Sequence Mass (Da): 25015
|
A0A8N1S7G1 | MLARAFEIYGQFCSGHPLEVIVTISTLTVCLLNLDTGNGQMREENLSDAYCHHDRCDTMDLKATNVIVMTIIRCLAVLFTYHQFRNLQRIGSKYILGIVGLFTVFSSVVFTSSVVSFSRSDIADLKGRLIFYLLRINLSKAATLAKYALSARNQEEVKANIARGMSLLGPTITVDTLVEALLIGIGSLSGIRRLEILCTFACLGVIVNYIVFMTFYPACLSLTIEISRGNNNMRQLSADRIFIMQPLNEEDQKPNPVVERVKMIMIFGLLVVHVHRYASPLSFLGASALTNEEVIQLVKHKDIAAYQLEKAVGDMERGVDIRRLVVGNAGKFTEEMIDLPYRHYDYSKVFGACCENVIGYVPVPVGIVGPLLIDGQLYHVPMATTEGCLVASTNRGSRALMKCGVTTRVTADGMTRAPVVQFPDIVRACEAMSWIEQSQNFQELKNSFDQTSRFARLIRIQPRIAGRDLHMRFVATTGDAMGMNMLSKGTERALLTMQTYFPDMEIISLSGNLCTDKKPAAVNWIEGRGKSVVCEAIVPAEDVTFVLKTTVNKLIKLNNKKNFTGSALAGSIGGFNAHAANIVTAIFIATGQDPAQNVSSSNCLTLMEAWGEDGKDLRVTCTMPSIEVGTVGGGTGLPAQGACLAMLGVKGAHPTEPGENAKRLARIVCATVLAAELSLMAALASGDLVKSHLRHNRSSVQISNSMHPTHSSSSSNDGNRLTVPSTSPVS | Pathway: Metabolic intermediate biosynthesis; (R)-mevalonate biosynthesis; (R)-mevalonate from acetyl-CoA: step 3/3.
Catalytic Activity: (R)-mevalonate + CoA + 2 NADP(+) = (3S)-hydroxy-3-methylglutaryl-CoA + 2 H(+) + 2 NADPH
EC: 1.1.1.34
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 730
Sequence Mass (Da): 79394
Location Topology: Multi-pass membrane protein
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A0A960E020 | MEQPADDRHQERMSDLESLMWGLEADPMLSSTFANLSWLDGPPDPERLRARMWRATREIPRLRRRVVGGFGPLAPHWEDDPDFDLDRHLRWTRLPPGATDADVRALAVELAAAPFDRERPLWEFVVVDGLPDGRAAMVQKLHHTITDGEGGIRMSLAFIDLERDGPELPPLDDGPPPPADRRPWDGALDAALDLARRNAQGARRLVESATDLARDPLHVASILAELPAETAATTRSMVRQLAVVDSHRSPLWSDRSLDRALATFDVPLDAVKAAATSLGGSVNDLFVAAACGGAGAYHRRRGVGVDELRMSMPVSTRTDRAPGGNAFSPTRVLVPVDSDPRRRFEAVHERLAVTKTERALGVASSLAGLGNLLPRPVLVRLARQQVLTVDFATSNVRAAPFDLYIAGALMTHNHPLGPVAGTAWNLTTMSYRGELNIGLHVDRAAVDDPGALADDIAAGFDELLEAGGVRRRPRG | 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: 475
Sequence Mass (Da): 51701
|
A0A2N4X764 | MKILLTRRRTNAGNYVSDVKEADEYTIANEHIASIDLMERAARAFVNFFESKYSVSYKKIVVLCGLGDNGGDGLAIARMLYHSGFEVEVIVLDYSERKSDNFKTNLGRLVNKIDVRLCKADVDLPLINPDYLYIDALLGAGLSRPLEGILKTLVINLNASAAELVSVDIPSGLFADSPNGSDDVIVKANQTITFQTPKLAFFLPQNAAYVGDWWVVNIGLHDGFISQLNSGYEYTDAPMARQLIKPRNKFSNKGNFGHALMIAGSFGMIGAAVLSSRACLRSGVGKVTVYTPACGYTILQSSVPEAMCLPTDNQKELEDMPPLNNYQAIGIGCGIGTNPGTASMIEAILKNVKVPVVIDADALNIIAADNHQLSLIPAGAVLTPHPKEFQRLIGKTWANDYEKLDLLAAFAVRHQCIVCLKGAFTAIASPDGKIYFNSTGNAGMAKGGSGDVLTGMILALLAQGYTPINASLLGVYEHGLAGDRAAQLKGTTAMIASDIIENIRF | 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 is a result of enzymatic or heat-dependent hydration.
Catalytic Activity: (6R)-NADHX = (6S)-NADHX
Sequence Length: 505
Sequence Mass (Da): 54260
|
A0A920VGH6 | MLLVSAFLGLGSLLRPSRNTPQKVMNYESGFDPQGDMWSQSNIRYYVFALMFVLFDVEAVFIFPWATRLEVYGVFGLVEMAIFIFILALGLFYAWRKRLLPMDLSRRR | Function: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain.
Catalytic Activity: a quinone + 5 H(+)(in) + NADH = a quinol + 4 H(+)(out) + NAD(+)
EC: 7.1.1.-
Subcellular Location: Cell membrane
Sequence Length: 108
Sequence Mass (Da): 12627
Location Topology: Multi-pass membrane protein
|
A0A927WXX3 | MRILVSNDDGFDAPGIHSLAKALCPLGEVTVVAPATQQTAKGHSLTIGSEIRVQKRFFEEGIPGYAVWGTPKDCVDLAVDALLERRPDLIVTGINEGPNLCNDCVSSGTIGGAIAGFINGIPSIATSLDTGDHFDYDKCAPAIRKIAGWFMKMPYNREFALSVNFPNTDEDFKGIVVAESGGIHTFDAHYTVVREDSDSQYYVIPGGFVVLNDVIEDLDHDIYAMLQGYIAMTPVHFDMVHHTALDTLRKDWNEYDR | Cofactor: Binds 1 divalent metal cation per subunit.
Function: Nucleotidase that shows phosphatase activity on nucleoside 5'-monophosphates.
EC: 3.1.3.5
Catalytic Activity: a ribonucleoside 5'-phosphate + H2O = a ribonucleoside + phosphate
Subcellular Location: Cytoplasm
Sequence Length: 257
Sequence Mass (Da): 28170
|
A0A7I8V4A2 | MLELYKNLMNLCESSEVAKFFYKDFTGPMDGKFRVFSYHYASYSEWLKPDALECRGIMFEMDGDTPIRIASRPMEKFFNLNENPLTMGIDISDVEYIMDKADGSLVSSYVDDGYLYLKSKTSLYSDQARQASALLNSEEYSSLHQVILELALDGYTVNMEFVSPNNRVVLAYQEPQLFVLNVRDNTTGEYIKYDDLYANAKIRPYLINAYGISDPTTWVEGVRELEGVEGYIAVLNTGQRFKVKTEWYSALHHTKDSITSNERLFASVVSANSDDLRSLFAGDEYAIKKISAFEQAYLDYLGKSLELCQSFYDEYRGRARKDYAIAAQKATVNQRHLFGVIMNMYEGTVDVDKLLKDLERVFLKYWAGYVPKEYEKEIEISEE | Cofactor: Binds 2 magnesium ions that perform the catalytic activity via a two-metal mechanism. One of the catalytic Mg(2+), which is coordinated by 5 water molecules, engages the lysine nucleophile and the ATP alpha phosphate while the Mg(2+) orients the PPi leaving group.
Function: Involved in countering a host defense mechanism which, following viral infection, activates the host anticodon nuclease and shuts off viral translation. Repairs 5'-PO4 and 3'-OH groups in the cleaved host tRNA.
EC: 6.5.1.3
Catalytic Activity: ATP + (ribonucleotide)n-3'-hydroxyl + 5'-phospho-(ribonucleotide)m = (ribonucleotide)n+m + AMP + diphosphate.
Sequence Length: 383
Sequence Mass (Da): 44122
|
A0A9D9GWK3 | MINIINDIEAKNIDEITIKKGIASKELMKRAGVGIYKEIKKYLAKDSKVLIVTGRGGNAGDGYVLANELLKHNYEVNIYQIEKNKEIKNLEAKFYQEEYIANKGKFIDNLVDQYDIYVDAIFGSGLNKEISGEYKEVINILNSFNGLKISIDIPSGVNGSTGEIMGIAFKCDYLYTIEFYKIGFIINRGRNYFNKVRIVHIGLDGSDINNNCFCLNKLDFARFFPKRERISNKGTYGRVALIGGCKEYLGSILLSYNAISALRCGVGYTTLCIPQSLVPLYSLHYPEIMYKGMSDNDGHIKFNKDDLDSLLKMNAIAIGMGIGISEEVYKVIVYLLNNYEGKLIIDADGINSLSKYGIDALVTHKCDVILTPHIKEFSRLINKEIKCLNLETLSYLKEFTNKYKVIINLKSETSVASDGKTFYFNITGNPSLAKGGSGDVLSGITLGMVVKNIDLLKEVSLASYILGKASDFAIETINENSVIASDIINKISDVLNYISQVK | 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 is a result of enzymatic or heat-dependent hydration.
Catalytic Activity: (6R)-NADHX = (6S)-NADHX
Sequence Length: 502
Sequence Mass (Da): 55912
|
A0A1W9P3S5 | MHLTTGIDLVEVKRMKAAVERWGERLLNRVFTPQEIEYSTRGASFYPLRNPRRRRGIPETCGVSSNMVYQHLAGRFAAKEATIKCLGEEIKQRPMAWKDIEIVNNSEGKPEIRFNQKKRRNKKRISLTISHTKDYAVAQAIAYS | 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: 144
Sequence Mass (Da): 16649
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A0A6A5ZFE7 | MASCIPIIRAAFFALTHAHGGVYTYNIDSKNYTGLKSPYSEPRYGLPEPNRPYTLSLFTDYVPIKSGGSVTAWWSNTYVWDKNAWSCDDEYLSDPAHECGLSNWIHAHGPMMVYMAAYPGSCSDVRPSTLSWFKITQEGLRPGHKAGDAAGWLQGDIMGKPLTVRGWIVKIPKSLKSGNYLIRHEILGLESDCPHLYPQCAQLNVTGTGIETKAPGMEYLVKFPGAYRPSDLGLNVYT | Function: Has endoglucanase activity on substrates containing beta-1,4 glycosidic bonds. Involved in the degradation of complex natural cellulosic substrates.
Catalytic Activity: Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.
EC: 3.2.1.4
Subcellular Location: Secreted
Sequence Length: 238
Domain: Has a modular structure: an endo-beta-1,4-glucanase catalytic module at the N-terminus, a linker rich in serines and threonines, and a C-terminal carbohydrate-binding module (CBM). The genes for catalytic modules and CBMs seem to have evolved separately and have been linked by gene fusion.
Sequence Mass (Da): 26373
|
A0A1Y1SDR2 | MNNRHHLQAVAPPSRALGENLRQAELRAPRYTSYPTALEFTGQVGPAALLEQMDKTNQEPIPAALSLYVHLPFCAAACFYCGCNRVISRSAQRRSDYLDLIEREISVLAPHLDRDRPVVQIHFGGGTPNSYRPLELARLIRTLSSQFSIHADCEISMEVDPRQYQPGDALAWAALGINRISLGVQDVSREVQQAINRLQPREQIAELVDEARKADMHGINFDLIYGLPRQTLAGVDDNVDLVALLQPDRIAVFHYAHLPQRFPAQRVIDESELPGLATRLAMQARYSELLTQLGYRHIGMDHFSHPDDSLARALAQGTLQRNFQGYSTAAGSDIIGLGVSAISSVGRLYAQNHSDLTAYRRALENKQLATQRGWHRSDDDLQRHAIIQQVMCQQRIDFNAFGGARAFHTRYAKALGQLRQLDPSGQLVRIETEALYILPAGRNVLRLIARCFDRYAARRNTQQLARAV | Cofactor: Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; protoporphyrinogen-IX from coproporphyrinogen-III (AdoMet route): step 1/1.
Catalytic Activity: coproporphyrinogen III + 2 S-adenosyl-L-methionine = 2 5'-deoxyadenosine + 2 CO2 + 2 L-methionine + protoporphyrinogen IX
EC: 1.3.98.3
Subcellular Location: Cytoplasm
Sequence Length: 468
Sequence Mass (Da): 52467
|
A0A7H4PCN8 | MKDACLLPLLRLDEASELARLAAPVLHARTLQPVSGSDIDLQLRCSYTPDQGSTRIERVLASGTGARIVTSHDDVCLIEFQVPGGQDFKLAHKELDAILKRAQLRPLAVGVHADRKLLQFCYTSEVADSALKLLDEAGLPGELRLRQKLALVAMVGAGVTRNPLHCHRFWQQLKGQPVEFTWQSEEGISLVAVLRAGPTESLIQGLHQSLFRAEKRIGLVLFGKGNIGSRWLELFAREQTTLSARTGFEFILAGVVDSRRSLLNYEGLDASRALAFFNDEAIEQDEESLFLWMRAHPYDDLVVLDVTASAQLADQYLDFASHGFHVISANKLAGASSSSKYRQIHDAFEKTGRHWLYNATVGAGLPVNHTVRDLIDSGDTILALSGIFSGTLSWLFLQFDGTVPFTDLVDQAWQQGLTEPDPRVDLSGKDVMRKLVILAREAGYDIEPDQVRVESLVPAHCEEGSVDHFFENGEALNDQMLQRLEAAREMGLVLRYVARFDANGKARVGVEAVREEHPLAALLPCDNVFAIESRWYRDNPLVIRGPGAVAM | Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 1/4.
EC: 1.1.1.3
Catalytic Activity: L-homoserine + NAD(+) = H(+) + L-aspartate 4-semialdehyde + NADH
Sequence Length: 551
Sequence Mass (Da): 60954
|
G8JT40 | MRIWAENIKRSNYYRYAVPFVKFVLMCYGSWAYCHLFCFVELRDHLHHNAVAVFLTCMNIFLTLILWYIWIQIVVIGPGKQPTVLPFRIIPDAPCDEGTASKDETVVVSVIPPDIYQCDPQGYPMWCSTCQSLKIERSHHSELLKYCVPRFDHYCVWLGTVIGRKNYKLFMQYVMYFTIYLVTASLTIALFMKRIVDYNKEHDLTLNLNIIVLFILVLAFAFFVTPLFAVFSFYMSCNRTSLDIIQKKAIKRHRKAYFCVYNPEDRYRYVVDCLPAEQYNIWNKRNAWLNIKEFIGSNIWLWFIPIGTNISDFQVSRNEEYYNAIVGPYREDLSDNYKSILLNRINQGDYVTRLRVYGDEVKERCDSLHGEV | Catalytic Activity: hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein]
EC: 2.3.1.225
Subcellular Location: Membrane
Sequence Length: 372
Domain: The DHHC domain is required for palmitoyltransferase activity.
Sequence Mass (Da): 44019
Location Topology: Multi-pass membrane protein
|
A0A927X0I0 | MIHLNVHSCYSFLSSTIRIDSYLERLVKKHEDSAVLTDINNMCGVMEFIKKCEKSNLKPIIGMEVSVFKYDAEYKVILIALNTNGYYNLLKITPLLNRDLTMEKLFEYQDDIAFIIPSTRSYFGNAIHKDELEVAIKEIEFLKENIKLLYIGLEAYNKIDLEDVKTIRNLKTGVTLLALNEVNSLEKDNETLSVLKAIKDNKLISEVKTDFSQRYLKSEAEMAKLFLQEEIDNTHKVASLVTKYEFSSSIKMIKYCENSKEFLNSLALKGLSKRLNGKINKEYKDRLEYELSIIDKMGYNDYFLVVYDYVKFAKSNDIIVGPGRGSAGGSLVAYVLGITDIDPIKYDLYFERFLNPGRTSMPDIDIDFEDRRRDEVIEYLKNRWGVNHVASIATFQTMGIKQAIRDVCRVLGTSSSTMNVFSKKIPTLRDISTENIFEYSPEFKEFVSSNKQYQQIFELARKLEGLPRQMSLHAAGVIISDKSLENYVPVVVNEIGYICEFEHEYLEELGLFKMDLLGLKNITIINDCLHVIHKTNPNFKLHDIDLGDERLYIGMNENLLSGIFQLESSGMRKALLTIKPTCFDDVCATIALFRPGPRDFIPTYAERKNSNEPIKYPDSCLEEILRSTQGIIIYQEQVLEICRKMALFSYGEADIFRRIISKKDSSKLEEVKKDFIEGGIKNGKNVDLLNKVFNMLAKFAGYGFNKAHTVAYSYIACWMMYFKLYYPSVFFSCLMNNFAGISMNDKFFEYLVETKKLGVKVISPSVNSKKVGFYNEGEYIRFALNQIKGVNSNIVNEIIKENVNPFKDYIDFVVRMKPRGLTDKHLEALIYAGALDEFGLNRASMIASIEVVMSYASRVVIINKDQYLIDYDLASRPLLKVVNEENDLEKEKEVTGSYLSGFPLEKDRENLTKNEYSLVANLQDGKTAKIAVMIRSIKTMKDRKGNVMALIKASDESGDIDLTLFASSYENLIKELDVGDYAYIVGKVEVRERVTMIIDNAKRIRRK | Function: DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. This DNA polymerase also exhibits 3' to 5' exonuclease activity. The alpha chain is the DNA polymerase.
Catalytic Activity: a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)
EC: 2.7.7.7
Subcellular Location: Cytoplasm
Sequence Length: 1007
Sequence Mass (Da): 115445
|
D7B6X0 | MSADDRAPRSRHVAAMAGIAACGGAAGAVARHLVAQAWPTPDGGPPLATLAVNLAGSVLIGVLVAAAAGPRPAPPWVRQLLGTGFLGGFTTYSAHVLDTGALAASGRVAEAAAYMALTLVGAVAGTALGAWATGRAVRALVRRRRP | Function: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Subcellular Location: Cell membrane
Sequence Length: 146
Sequence Mass (Da): 14438
Location Topology: Multi-pass membrane protein
|
A0A518XJM8 | MSAMKNSCLLIGLLALYYLLPLEFRGLWQPDETRYAEISREMIEHGSWISPHFFDLRYFEKPVGGYWINNIGQLLFGHSNFAVRFGSVFSTMLSALMLYWLSARIGMTRNAAIAAVIIYLTSLLVYGIGTYAVLDPMLTLWMTAAMSSYWFATEAQGRRQSICRYALFGFFCGLGFMTKGFLALAVPALVIFPWMVKQKRFTQVLIYGPVAVISAGLTCAPWAIAIHHEQPDFWNYFFWVEHIQRFAEDNAQHKAPFWYYLPVLLAGSLPWLALLPGAIKKGCQSSANTYLLSWAVIPLIFFSIAKGKLPTYILPCFAPLAMLMAQYGVELARTKSRTLQINAWINIGFGSVAVLAVFFFLAPWGIAHKPVYAPQEINKVVMAAVIFMGWALAGLFSLNGNWLRAALCPLVLALGLGYAIPDGISNTKQPGRFIDHIASNLGESRYIATNSTGVGSAIAWRMERSDIYFYHQEGELKYGLSYPDDSRRFISEVLMADWVKQHRKKGNISVVLMLGRDESIPTSLPPAETTYHEGRMLYLFYGALP | Pathway: Lipopolysaccharide metabolism; 4-amino-4-deoxy-beta-L-arabinose-lipid A biosynthesis.
Function: Catalyzes the transfer of the L-Ara4N moiety of the glycolipid undecaprenyl phosphate-alpha-L-Ara4N to lipid A. The modified arabinose is attached to lipid A and is required for resistance to polymyxin and cationic antimicrobial peptides.
Catalytic Activity: 4-amino-4-deoxy-alpha-L-arabinopyranosyl di-trans,octa-cis-undecaprenyl phosphate + lipid IVA = lipid IIA + di-trans,octa-cis-undecaprenyl phosphate.
EC: 2.4.2.43
Subcellular Location: Cell inner membrane
Sequence Length: 545
Sequence Mass (Da): 61261
Location Topology: Multi-pass membrane protein
|
A0A950ZAG5 | MKILELIQKTTAFFQKKNVPEPRLNVEWLVAHALRIKRLDLYLQFERELSEGELEPLRELVRRRAEREPLQYILGETEFFGRKYHVDRRALIPRRETEHLIEAALLKLPADFACRGVDLGTGSGVLAITLALERPASKWLLIDASDDALALASENARQHGLGKDRVEFRRSSWWSAVSADERFDLIVSNPPYVRADELERLQPEILRHEPAAALDGGADGLAAYREIIAGAAAHAAESANAILEIGFDQAEAVASIFRQAGWKPAKPIRDLQGHARVIMASR | 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 factor] + S-adenosyl-L-homocysteine
Sequence Length: 282
Sequence Mass (Da): 31681
|
A0A1G3FWS8 | MSRLIPLLVPCLIGLAGFSSAQTAEPPALPLQQAAPPQEAITAPPAAPLPPAGAAIPGAPAAADMPAAAPQASPAPQAPAEGITAPPATVEATPAAPATVAPAAPVPQPPAPLQPAAPAPAEPAPAAPMAPANVAATPVLPGPTPETLPSVHDLSPMGMYAQAHWVVKGVMLLLVAACFLTWTVWLFKTVELIVAKSRARHSRRVLHDAESLAAATAALSRRRDPAAFMARAVQEELVRSDALLMAAGPEGMKERGGSLVDRIETQALARIRRGTGLLATVGSVAPFVGLFGTVWGIMNSFISIAETKTTNLAVVAPGIAEALFATAIGLVAAIPAVVIYNHFSRSIAAYRLALGDAGAATLRLLSRDIDQRRAREG | Function: Involved in the TonB-dependent energy-dependent transport of various receptor-bound substrates. Protects ExbD from proteolytic degradation and functionally stabilizes TonB.
Subcellular Location: Cell inner membrane
Sequence Length: 377
Sequence Mass (Da): 38451
Location Topology: Multi-pass membrane protein
|
A0A7Y1U2U4 | LFLIVVGILSALGIYAGTSGLLGAGINDFFGWGVGVFRYFAPPTLIAAGLAVIRRSDESHQLLPRWIVGGAITLFATVGLVHLAGDSPGWGSTVEEFSAAGGVLGLAIGGPLMAIASFWGALLILIALLIGGLTISTGVPLKTIIDGTAAKAKPLAGAAASGTKSLFVMRGDADTIDLRDEPPPLPSMLVDGKPTDFVDPAGNELDATIEIPVPSAEPPEPSPEPAKDTTAEPVFDQDGDEVEPTVVVPQPPIPPQQLEAAELAVTTQGDRTWILPPMSLLQRSGSQSVDEQAVLGRGRVLERALADHGVETRLVNMVVGPTVTRFELELGLGVKVSRIKSLNDDIAYAMASPDVRIIAPIPGKQAIGVEVPNEQRQIVAVGDILGSAEASEATGPLSVAIGRDINGHSMLADLTKMPHTLVAGATGAGKSSGINSIITSLLMRNTPDDVRMILIDPKRVEMTQYERIPHLLTQPVTDPKKAANALAWAVREMERRYELLEECRFRDIGGYNAAFDRGEVKAKKGQMGPDGEPRQMKRLPYILVVVDELSDLMMVAARDVEESIVRIGQKARAVGIHMVIATQRPSVDVITGLIKANVPARIAYAVSSMQDSRVILGSPGAERLVGKGDMLFQDPTSSTPTRLQGAWVEESEVRRVVGHWRDQMAEGESDKSVLDESPEHAPAAAATPSGFGPAPAAAPSSPSDMITADRPGDDDTDDLLWQAMDLVVSSGLGSTSMLQRKLRVGFARAGRIMDELELKGVVGPSEGSKAREVLLTPEQLAQLRGQS | Function: Essential cell division protein that coordinates cell division and chromosome segregation. The N-terminus is involved in assembly of the cell-division machinery. The C-terminus functions as a DNA motor that moves dsDNA in an ATP-dependent manner towards the dif recombination site, which is located within the replication terminus region. Required for activation of the Xer recombinase, allowing activation of chromosome unlinking by recombination.
Subcellular Location: Membrane
Sequence Length: 787
Sequence Mass (Da): 83295
Location Topology: Multi-pass membrane protein
|
A0A1M6KNE9 | MKDVALVLAAGSGTRMQSETKKQFIVLDQKPILYYSLKAFEESGVEKIVIVTSKEDIDYCRKGIVERYHFSKVTEIVEGGAQRFHSVYRGLKAVGDCDNVLIHDAARPMITTELIEDIRSALREHKAVITAVPVKDTIKSSDPDGFVTGTPDRKALWQVQTPQAFRFDLIKAAYGYVIREGMEDVTDDGMALERYTHGSERIKLLEGSYENIKVTTPEDLLIATVFLGKRDKNQVDTKYK | 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 Activity: 2-C-methyl-D-erythritol 4-phosphate + CTP + H(+) = 4-CDP-2-C-methyl-D-erythritol + diphosphate
Sequence Length: 240
Sequence Mass (Da): 27024
|
A0A0T2Z023 | MTINYLSLAVREVSLLSPYVPGKSIDELERETGMASHRIIKLASNETPMRPNPHVIQAIQDELRNITRYPDASGFRLKAKLSEKFGLKSEAITLGNGSNDLLFMIAQAFLGAGRNAVFSQHSFSVYEAAAKATGASTQEVLALNWGSDLDQILTAINRETRVIFLANPNNPTGTWFDRRAFEAFIDRVPRETIVVLDEAYIEYADDPSLPNGLDYLHSYPNLIVSRSMCKAYGLAGLRIGFAASSPEVAGILNRVRQPFNVNSLALAGACAALDDDTYLQRGRQVNRQGQQQLQEGLSRLGISWIPSRTNFLAVNFERPARSVYDALLMEGIIVRRLDGYGMPNHLRISVGLKTENIRLLDALGSIMRKGSW | Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 7/9.
EC: 2.6.1.9
Catalytic Activity: 2-oxoglutarate + L-histidinol phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate
Sequence Length: 372
Sequence Mass (Da): 41189
|
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