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stringlengths 6
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A0A6A6W0R3 | MALQNTHVEEDINTSPPSMHNHSGHLDEAEPNEADLTTESHEEGYRPSDAKIFAGEPDAGKPDAAQPDAGEPDAAESDAGEVDEHTNDPSPEATSNNINIIEEEPRLWLTLNSHGLERIYDYNDGGHCPSELGSTLCQGRYRIIHKLGHGGFGIVWLCRDLHHESPHYVAIKVLVAALSREYCGELEAVQLLKILPEVERGKKHLCVSMDSFQQESPNGTHHCFVYPFIGPRAVDALACLGNSSAAMRKASLDTIEAVACLHKHGICHGDLTAKNILVDLRDLGDLPEADLLEKLGQPEINPVKTSSTETPASAPQYLVYPVDFSKVDPRFISDRIRLIDFGEAFEIKSPPDSIGLPVVYQPPELVLDGHVGVGCDLWALGNCLYELRTGQKLIDVFDANDTDDYLFYMVMLLGKLPEPWWSSTWKARKEHYTDEVDADANNRPFQAGDPAHHRIGDTSIKSQLENALFWNPESRSLDFSKRETPPEELEAFIDLLEKLLRYKPEDRLSAEEALQHPWFRM | Function: Component of the EKC/KEOPS complex that is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. The complex is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. BUD32 has ATPase activity in the context of the EKC/KEOPS complex and likely plays a supporting role to the catalytic subunit KAE1. The EKC/KEOPS complex also promotes both telomere uncapping and telomere elongation. The complex is required for efficient recruitment of transcriptional coactivators.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
EC: 2.7.11.1
Subcellular Location: Chromosome
Sequence Length: 521
Sequence Mass (Da): 58104
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A0A7X6C8F8 | MFLVGEISCVLYNYQLSTVNCQLIVDKLSYHFQDPQRGDIVVFSAPAQALAVCGLPPSFSDPFVKGALGLPGDRVEVKSGQIYINGQLLQESYPAKSPNYRKLTPKIN | 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: 108
Sequence Mass (Da): 11878
Location Topology: Single-pass type II membrane protein
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A0A955W691 | MRVLGVDPGSVRTGYGIIERDGTRLRLITAGTLTAGEKAPLEERLLTIHTGLVALIEEYAPGAAAVEDIFMAKFPNAALKLGHARGVALLAIAQAGLAVHPYPPAVVKRSIVGKGAADKTQVARIVGAMLGLTELPGIDATDALAIALTHAQAARMHAALAPAAKLASAAKSGRPGAPRRAAKGRPPPKTGR | Cofactor: Binds 2 Mg(2+) ion per subunit.
Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair. Endonuclease that resolves HJ intermediates. Cleaves cruciform DNA by making single-stranded nicks across the HJ at symmetrical positions within the homologous arms, yielding a 5'-phosphate and a 3'-hydroxyl group; requires a central core of homology in the junction. The consensus cleavage sequence is 5'-(A/T)TT(C/G)-3'. Cleavage occurs on the 3'-side of the TT dinucleotide at the point of strand exchange. HJ branch migration catalyzed by RuvA-RuvB allows RuvC to scan DNA until it finds its consensus sequence, where it cleaves and resolves the cruciform DNA.
EC: 3.1.21.10
Catalytic Activity: Endonucleolytic cleavage at a junction such as a reciprocal single-stranded crossover between two homologous DNA duplexes (Holliday junction).
Subcellular Location: Cytoplasm
Sequence Length: 192
Sequence Mass (Da): 19632
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A0A1X9T2Q4 | MKVKLLNVTPLKIAIKAIRRCYDSCGDDLGNKDLKLLKSIIKNGHTSTIEHIVFTFDIKGISRAALQELARHRIASLSVESTRYTLKKLKNIDTREFKYEDYLVETGNPIVDVFNRVGLDRTISCLNENIKNDLTKYTLPESYKTSLIWTINARSLRNFLELRSSSKALWELRELSNEIINSLPEEYLILFKDIIKEESNGI | Cofactor: Binds 4 FAD per tetramer. Each FAD binding site is formed by three monomers.
Pathway: Pyrimidine metabolism; dTTP biosynthesis.
Function: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor, and NADPH and FADH(2) as the reductant.
EC: 2.1.1.148
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP + H(+) + NADPH = (6S)-5,6,7,8-tetrahydrofolate + dTMP + NADP(+)
Sequence Length: 202
Sequence Mass (Da): 23280
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A0A7Y5GSQ0 | MTKAVIVEATATGAGTFYHGLYGGAVSQRRAHGKNRGAVGEQLLDPFGNEDAVHTFRSWIDFGGKLEVDLGFGRGGFLVEQASRTRESRWVGFEVRTRLCMEVMDRLNRQGISNVRIIQADARPIVDQFFPVGSISHFYVGFPDPWWKKKHHKRRIFSPEFVHTLHSKLTATGSVILRTDVTDYAQNVREVFNAHGGFDTQVVTPDELVPTDRERRCADFGLPVSRLRFTKKGCL | Pathway: tRNA modification; N(7)-methylguanine-tRNA biosynthesis.
Function: Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA.
EC: 2.1.1.33
Catalytic Activity: guanosine(46) in tRNA + S-adenosyl-L-methionine = N(7)-methylguanosine(46) in tRNA + S-adenosyl-L-homocysteine
Sequence Length: 235
Sequence Mass (Da): 26480
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A0A4Q5XC03 | MQGDLARLGRGLPSGDHPPWWQPSALDDDGGRRAAPLRGGEAARCRHGPANTLWRATVVLRQGAGEPAVAGGDAKVEALGATSEWYRDRGAERRALQHLHRALSAACGRGRAGAEVQLATARAHRGTPLHGAKVTSHGYPLNLLLHNRKCVVVGGGTEAALRTGNLLEAGARVLLVSEEPVPGLELLASPRLHIERRALAEADLDDAWLVVQASTDDVLARRVGGWCEARRIFFCAIDQPEHSTYAHLALARAGSLTLAIGTEGRAPSLGRRLREEFSRVLTEAGAAEEVEQLAALRAATPPSERREVLTRAVADVRLTGALRFRKE | 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: 327
Sequence Mass (Da): 35032
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A0A4Q5X7A3 | MVSAPSEPGSRSSPSSASRVRKRAEYLEIQSGGQRVSGDCLVFILLRRPAGSPLRLGITASRKIGNAVQRNRARRLVREAFRAVFEQLPPAVDIVVIVRRPLGERKLQAVLDEWLRALPRIRRFAGP | 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: 127
Sequence Mass (Da): 14137
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A0A7X7UF57 | MRVLRFAAAVLVAFVLAHILYFVVLLIAPFDPARAKVNRIGRIWTGAWKRILGIKIHVYGEENIRNGGPYLFVSNHVSYLDVLALYNDFPVQLRFLAKKTLVWVPVFGIAFYTLDHVYIDRRKKNAQRGRLELMAEKFRQGKNICIFPGGRRAADGRLGEWKKGAFVLATQHHIPVVPVGIVGSAALHGIGDFFPRPGTITIRIGRPIITERLTYDDRDTLLRQTQEAVRELIENDSHE | EC: 2.3.1.51
Catalytic Activity: a 1-acyl-sn-glycero-3-phosphate + an acyl-CoA = a 1,2-diacyl-sn-glycero-3-phosphate + CoA
Sequence Length: 239
Domain: The HXXXXD motif is essential for acyltransferase activity and may constitute the binding site for the phosphate moiety of the glycerol-3-phosphate.
Sequence Mass (Da): 27167
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A0A1S3TYZ6 | MAFQDFELITERRRNENRQRLRKKIIISVVSAVLLACVVGAATFVVVQRTGSSTKNATPIQEASARPHVDQSSRLVEMICGSAEYKDKCKKTLGEALEKDPKLTEPKDLLKVSFILAENEMNKAFNETTKMEFASPEEKGAYSDCKEMFDDAKDELRRSIDEVGENDAKVLSTKAAEINNWLSAVMNYEQTCIDGIPEGKMREDFTKLFAESRELVSNALAVMSQFASFFSIFQGAGNIHVPWETTDNDAPAPASASGSSASSASSASAPGVAPAGSAPAPSSAPGAAPVPMPSSDDPLPTLPIPTWAGPSEFKGSDEKPTPNVTVAQDGSGDFKTISEALAAIQTPYEGRYVVYVKAGIYDETVTVTRKLVNLTMYGDGGDKSIITGNKNFVDGVRTFQTASFVVLGDGFLGREMQFRNTAGAEKHQAVAARVQADQAMFFNCVFDGYQDTLYAQTHRQFYRDCTITGTIDFIFGDASAVFQNCTILVKKPLENQQNIVTAQGRLDRQENTGFVLQKCVIKAADDLVPLKGTVKNYLGRPWKEYSRTIIMETQIEDLIHPDGWLPWEGDFALKTLYYGEFNNNGVGASTSARVNWPNRKDIDRDEANRYTVEAFLQGSWINGTGVPAQMGLYS | Pathway: Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-gluconate from pectin: step 1/5.
Catalytic Activity: [(1->4)-alpha-D-galacturonosyl methyl ester](n) + n H2O = [(1->4)-alpha-D-galacturonosyl](n) + n H(+) + n methanol
EC: 3.1.1.11
Subcellular Location: Secreted
Sequence Length: 634
Sequence Mass (Da): 69420
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A0A1N7JMX3 | MTRDDQRGNTGPEAEPVKVAKEKEDPAAQAAKRLTQAKARAADVKKHPAKEKKPPEPPEPSPLQPLLDRFVKVLTEGVGSEAVEEAYINRPGGDRPTLVISPEKWLEVARLLLEEESLAFDYLENLSGVDEEDHMEILYHLTSLTHGHDICVKVKTGREEAEVPSVTGVWRAADWHEREIYDLLGVRFTGHPNLERILMPKGWVGHPLRKDYEPYDGGV | 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 hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.
Catalytic Activity: a quinone + 5 H(+)(in) + NADH = a quinol + 4 H(+)(out) + NAD(+)
EC: 7.1.1.-
Subcellular Location: Cell membrane
Sequence Length: 219
Sequence Mass (Da): 24579
Location Topology: Peripheral membrane protein
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A0A518BTS8 | MLVLAALTTSILMVLFLVVGVTMTLVVLVQRPKGGGLAGAFGGASTDAAAVFGASIGDVLTWITVGFFVVWILLAMGMQWSIAAEVHSIPQPPAVQTPAEPATPAPATTAPAPEPGTTQGTPTE | Function: Involved in protein export. Participates in an early event of protein translocation.
Subcellular Location: Cell membrane
Sequence Length: 124
Sequence Mass (Da): 12511
Location Topology: Multi-pass membrane protein
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A0A524L8M1 | MLRPRVSPTGPPVPERRRARLRSGTGGPVGDTLGLNTLGSIAGSLLAGFVLIPRLGLQDWMLFAGALDAAWGTLVLGVVLAGRAVRSRPFALAAAGAAAAGVLCIPLLVPPWSFDVLGAFASSQIRRYVQAGGKVDVAAALRNYRVLYFAEGSTSTISVAEWRGHRTILVNGRTEASDFLPDLQVEYLLGHVPMLLHPDPRAALVIGLGAGITLGAVTAHEQTESITLVEIEPVVLDGTRKFSDLNGAALDDPRLEIVFQDGRNFLKTTPRRFDVITSDPIYPWNAGSGYLYTTEYYRLAAERLNEGGVMCQWWPASDLSNDDFRALVRTFATAFAHTTQWQTTYDVILIGSNRPIQVDLGNFARRLAEPRVARQLARVGLDSPLPFLAEFALDDAGVRSYAEGAPLNTDDNLYLEFRSPLAIGSRAAPFNVLSIDEHRVNPAVILAGLDPFFSSDEEAALELARYQEAKQATTHIYYGARTERFARESLGDSSRRLRRILRKLPDYSPARAQLANGLVQIAVRKVDQKRFADAAKAAGEALELVDDPRAHHMLGIALVHLGRDPEAIPHLEAALQMRPWYWLGYSDLANAYQRAGRGADAIRTLREGLAVEPDDPALAGQLDSLLQSAPAGA | Pathway: Amine and polyamine biosynthesis; spermidine biosynthesis; spermidine from putrescine: step 1/1.
Function: Catalyzes the irreversible transfer of a propylamine group from the amino donor S-adenosylmethioninamine (decarboxy-AdoMet) to putrescine (1,4-diaminobutane) to yield spermidine.
Catalytic Activity: putrescine + S-adenosyl 3-(methylsulfanyl)propylamine = H(+) + S-methyl-5'-thioadenosine + spermidine
Subcellular Location: Cell membrane
Sequence Length: 633
Sequence Mass (Da): 68792
Location Topology: Multi-pass membrane protein
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A0A956CJW0 | MKKLMVVLAIGAVTLFVSRFFVPAEAEHGGAHEPDPAVQGEVFNEDAPAPESAHGHHARVWETDAFWAQIAAFAALLYLIGGGVLGGANSFLQKRKQSIEVNLVEAKALREKAEATYKQYAARLAELDNEIKSLRAEMVKAGEAERDRIIAEAEGKAARMRRDTQFIIEQQLKQLRVDLKHDAAAAAIRTAEEILSSQLNDGDQERLAREFIDRLSSNESPAAQASAAQPVRGAVS | Function: Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0).
Subcellular Location: Cell membrane
Sequence Length: 236
Sequence Mass (Da): 25725
Location Topology: Single-pass membrane protein
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A0A970M6T7 | MSEVLTFIPQWQILIFSGLFGAAWGSFANVVIARWPLEMSVVRPGSHCFSCQAKVRPWDNIPVLSYFILRGKCRHCGASFSLRYVFVELLLALFSVAVMQRALALYPDAPGWLLGTWLIWFAFIWALVVVAMIDLACWLIPDSIVLPGIAVGVAANALGLLPLGWLEPVVAAGIAYAGLRLLFIDGYQLLTGKPGMGLGDAKLLALFGAFLGYEGTLFALFAGAFQGLVVGLGMVLFRRRKGLDNEPVFEEDLGEDGAPTEPTDDRLRKAKVPFGPFLAAGAIEYLFVGEALIAHYTKWVFYLTLRWFS | Function: Plays an essential role in type IV pili and type II pseudopili formation by proteolytically removing the leader sequence from substrate proteins and subsequently monomethylating the alpha-amino group of the newly exposed N-terminal phenylalanine.
Catalytic Activity: Typically cleaves a -Gly-|-Phe- bond to release an N-terminal, basic peptide of 5-8 residues from type IV prepilin, and then N-methylates the new N-terminal amino group, the methyl donor being S-adenosyl-L-methionine.
EC: 2.1.1.-
Subcellular Location: Cell inner membrane
Sequence Length: 309
Sequence Mass (Da): 33929
Location Topology: Multi-pass membrane protein
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A0A956P6S0 | MNLTLKEFAEQVGGSFEGDPDLRITGVGPIEDARPGQVAFLANEKYARHLATTRASAVLVRAGAEAASPAALVRVADPYFAFASLLPLVAYRPTHPAPGLSPGAFADATARVAPDAIVYPGAYVGPEAEVGARTILYPGVFIGEQARVGEDCILYANVAIAHGCVVGDRVILHPGVSIGADGFGHAKTADGFMKIPQVGNAVVEDDVEIGANSCVDRATMGATVIARGARLDDLVMVGHNCRIGEGTAIVAQAGVSGSTKIGRDCVIGPQAGVLGHLQVGDNTVIVGQSAVRKSIQEGGVYGGTPTQPYPEWRQNVIAGLRAADVRKRVLKLERELERLRKLLESTGGVD | Pathway: Bacterial outer membrane biogenesis; LPS lipid A biosynthesis.
Function: Catalyzes the N-acylation of UDP-3-O-acylglucosamine using 3-hydroxyacyl-ACP as the acyl donor. Is involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.
EC: 2.3.1.191
Catalytic Activity: a (3R)-hydroxyacyl-[ACP] + a UDP-3-O-[(3R)-3-hydroxyacyl]-alpha-D-glucosamine = a UDP-2-N,3-O-bis[(3R)-3-hydroxyacyl]-alpha-D-glucosamine + H(+) + holo-[ACP]
Sequence Length: 350
Sequence Mass (Da): 36404
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A0A6A6W4Y0 | MKPQSLLDYLRERSQVSSDTLDAQIVESLGPFVDNTSNQAIAYGELAKAKHADLLRDAAATAQKFKDSSELQLTDVSIAELAIEIATIRLCLLIVPHVTNCVHVQVNPIHSYSTAQIIINAERIISLFSLIAPDFSPSRVCIKVPSTWEGLRACEVLEQQGINTLATTLFCMEQAVLAGKSGCTYIAPYVNELKVHFEVGYIDPSPNFQLCVEAQKFYAKEKMKTKVLAASLTSVKECAQLSGIDCITIAPALLDGLNGTDVEVLEKEGGEEYASYFNESGTKVDGNVDSFGMDYWSNITEEKQWRQSFKQRNDGRELIKLEEAISIFRNEQAKLEDLVAQYI | Pathway: Carbohydrate degradation; pentose phosphate pathway; D-glyceraldehyde 3-phosphate and beta-D-fructose 6-phosphate from D-ribose 5-phosphate and D-xylulose 5-phosphate (non-oxidative stage): step 2/3.
Function: Catalyzes the rate-limiting step of the non-oxidative phase in the pentose phosphate pathway. Catalyzes the reversible conversion of sedheptulose-7-phosphate and D-glyceraldehyde 3-phosphate into erythrose-4-phosphate and beta-D-fructose 6-phosphate.
EC: 2.2.1.2
Catalytic Activity: D-glyceraldehyde 3-phosphate + D-sedoheptulose 7-phosphate = beta-D-fructose 6-phosphate + D-erythrose 4-phosphate
Sequence Length: 343
Sequence Mass (Da): 38001
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A0A6A6VVE6 | MLSSLLLAAAGLLVKPTYSISLEVSTSGGNSSGALPVGMMFEDVNHGGDGGIHGQLLGDNAFQGTNASLFRYASIGNATLSIDDTNPLTSAIVRSLKVDVPEDASGEVGFSNDGFWGIKLPQGTYSTFFWMSGDYEGDVTVKLVPKTGSGTEFGSTTLAIKKSSKWTKYEAKFDVKAAPNGNNVWALTFDGSKTAGSTLYFTLMSLYLPTYLDKENGLKPELAQPLADIKGRFLRFPGGNNLEGDTIDGRLRWNQTIGPLEDRPGRQDVWSYANTDAIGTLEYLEWAEYMNLEPMMDIFAGLALKGETVTGDALEPYIEDALAQIEYAVGDSSTHWGAIRASHGRTEPFALKYVEIGNEDNLSNGCASYVERFQRFYDAIHAAHPSITLIASTADLNCLPKDLPGDAWLDYHRYDRPDAFVEAFSFFDNIPRTNKYIINEFAAIYHNNGTRATYPTMRSAVAEAIYMMGAQRNSDLVQGLAYAPLIAHLAAVDLYNAWTPSLLSFRNDPPVTILSTSYFVQQMFAQASDPTDRYVDVVADGPLGPTVFWVASVSSGGQGVVKGANYAGVGTALRVRFAGGVEGTKRARVVVLSGDAEARNDEVDPGAVRPVEGVVEEGAEGWFEVEMPAWSVVVLVAE | Pathway: Glycan metabolism; L-arabinan degradation.
EC: 3.2.1.55
Catalytic Activity: Hydrolysis of terminal non-reducing alpha-L-arabinofuranoside residues in alpha-L-arabinosides.
Sequence Length: 638
Sequence Mass (Da): 69027
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A0A9E4JAI3 | MRGQTLAVEIPRRRRRKANRRVMLERRPLFVALAEGLATGARGGAGVLRRLARPVAVVGFLVGVVFGGRWALEHVLESPRFAVAQILVGPVERVSSSEIIALAAVRPGERLLALDPDAIAARVARHPWVQSVHVERKLPSTLQIDVIERRVAAAAMLGGLYLVDPEGLPFKRATTSEAAGLVVLTGLDRQRYTEEPAAVRAAYKQALKLLETYRAVTSRPPLSEVRIDARYGFSLYFLDTGAEVRLGREAHGEKLARLDQILDALENAGLDGPGSLRVVHLDGSPKSRVSLRLTLGDS | Function: Essential cell division protein.
Subcellular Location: Cell membrane
Sequence Length: 298
Sequence Mass (Da): 32458
Location Topology: Single-pass type II membrane protein
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A0A7Y3GC72 | MPAEPSAPVGMAPGNLPADSPARAVLVTLIVCAACSAAIASAVTWLRPYQQAHREADRSSRVRELVTAVPGLEHALGPLGTARLEARIIELATGRYVPGNDPDDFDPRVAILDAEESVALPPERDIAGIGRRAHHGVAYEVRDAEGLRLIVLPVYGAGYLSTLYGYLALDADTQTVRGLGFYEHAETPGLGSEIENPQWLARWPGKLARDATGRVRLGVARGAVDPRSSEATHLVDGISGATKTGDGVSGLLRFWLGPDGFGPYLGRLARERGGTP | Function: NQR complex catalyzes the reduction of ubiquinone-1 to ubiquinol by two successive reactions, coupled with the transport of Na(+) ions from the cytoplasm to the periplasm. NqrA to NqrE are probably involved in the second step, the conversion of ubisemiquinone to ubiquinol.
Catalytic Activity: a ubiquinone + H(+) + n Na(+)(in) + NADH = a ubiquinol + n Na(+)(out) + NAD(+)
EC: 7.2.1.1
Subcellular Location: Cell membrane
Sequence Length: 276
Sequence Mass (Da): 29196
Location Topology: Single-pass membrane protein
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C3X9Z9 | MSDIEAGMTIRSLFSTVPLDPLELRILLEYAIGFSRVKLITHSDHPLTTEQAKALSDVVSRRVCGEPVAYITGKREFFGLSFAVCPDVLIPRPETELLVELALERLPHGGKIVDMGTGSGAIAIAIASERPDAHVFATDVSEKALNMATHNALALLKGKQTVHFSAGNWFYALKNVNETFDLIVSNPPYIDSKDDHLQKGDLRFEPVGALTDHADGLSALKILVSGAQAYLKRGGWLLMEHGYDQAVAVRALLARAGFEEVQSWKDLAGIGRVSGGKRK | 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: 279
Sequence Mass (Da): 30317
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A0A7X7UHV7 | MKSVQPATVDGAVAAPPSKSMMLRAVALGALAPGRSRLDNPTYCDDARAVLGAAQALGAEVETRADAVFIAGGGRPRAARIDCGESGLCLRLFAAVAALFAEPLTLTGRGSLLRRPLPGVEETLAALGATATATNGLPPLIVCGPLAGGKATLDGSETSQFLTGLLIALPLLPRDSRLTVNRLVSQPYVELTLRMTRQAGAEIAVSPDGRQYDIRGGAVYRPQQWRIEGDWSGAAFLMAAGALAGRVAVRGLDPESAQADRALLDILPRFGADVENRVGEIVVRRRERRAFAADLTDCPDLAPPLVALAVHAAGRSVLRGARRLLSKESNRAAALTEEFGKLGARIEWRDDELLIDGCGLNGGDAQCHDDHRIAMALAVAALAGGGEVRLAGDECVAKSYPAFFADLERLTRRNP | Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 6/7.
Function: Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate.
Catalytic Activity: 3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-carboxyvinyl)-3-phosphoshikimate + phosphate
EC: 2.5.1.19
Subcellular Location: Cytoplasm
Sequence Length: 415
Sequence Mass (Da): 43562
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A0A7X9HKP4 | MTTRALRIFPDPVLRERCREIDCFDENLSRLVDDLAESMYAHRGVGLAAPQIGESLRVMVVDVDQREGAPRLLEFVNPRISAADEELEEREEGCLSFPGEAEMVRRPRRVTVQALDRRGQPFEITAEGLLATAMQHEIDHLDGKLFIDYLSRLRRSLVTRRMKKRSREGE | Cofactor: Binds 1 Fe(2+) ion.
Function: Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions.
EC: 3.5.1.88
Catalytic Activity: H2O + N-terminal N-formyl-L-methionyl-[peptide] = formate + N-terminal L-methionyl-[peptide]
Sequence Length: 170
Sequence Mass (Da): 19563
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A0A955XBU3 | MAAKKEEKKPEEPGAPTPSKLPLITLILVGLNLPATGFVAFMALNPVVPPPPEPPPPGPADDPLAVWGPTVDLDTFVVNLNEPTSSRYLRARIQVELADEKASERFERLRPVLRNELLGYLSNLTVEQTLGAEAKETIRSDLMKGITDKVGEDQVKRLFFSEFVVQ | Function: Controls the rotational direction of flagella during chemotaxis.
Subcellular Location: Cell membrane
Sequence Length: 166
Sequence Mass (Da): 18255
Location Topology: Single-pass membrane protein
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A0A8T2MD46 | MRKMLSLISSALRLSAGRTSSGRGAILQFLAAQGEYADFAVDPEPPPHPETHPSPLSDTHSVISSRPSKTLAPLLTVDPAISANEATVETQQPETNRTEAISSENSVAKDSNKANNGHLPDLLSLSPLGDAVDAVISRNSTKQLEMKEPLVSTATLEVSSPVEGATDDLFSKKSWDMIAQTPPPTSAELTPALTPSQAGHAAIPEPQPAGSRVVVSARTYADFTPQATFDIKKCDLHKLEDGPPLQAVLTREEGLKYYRTMQVMRRMELKADQLYKQKIIRGFCHLYDGQEACAVGIEAGINLTDHLITAYRAHGYTLTRGGTVREIMAELTGRRGGIAKGKGGSMHMYTKNFYGGNGIVGAQVPLGAGVALACKYQGKNELCVCLYGDGAANQGQIFETYNMASLWKLPCIFICENNKYGMGTSVERAAASTDYYKRGDFIPGLRVDGMDVLCVREATKFAAEHCRSGKGPILMELQTYRYHGHSMSDPGVSYRTREEIQEVRSKSDPISMLKDRMLNNNMASVEELKEIDVEVRKEIEDAAQFATTDPEPPLEDLCNHIFCNEPPMEVRGTNPWTKLKSVS | Function: The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2), and thereby links the glycolytic pathway to the tricarboxylic cycle.
EC: 1.2.4.1
Catalytic Activity: (R)-N(6)-lipoyl-L-lysyl-[dihydrolipoyllysine-residue acetyltransferase] + H(+) + pyruvate = (R)-N(6)-(S(8)-acetyldihydrolipoyl)-L-lysyl-[dihydrolipoyllysine-residue acetyltransferase] + CO2
Sequence Length: 583
Sequence Mass (Da): 63604
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A0A956RIE3 | MPAPTAVDKPGALLINLGTPEAPEPGPVRRYLREFLSDPRVIDINPISRWLLLNLVILPFRPARSAAAYRKVWTPEGSPLLVHGRALTAEVQRRLPDWEVRLAMRYGQPSLRDGLAALREAGCDRVVALPLYPQYAASSTGSTIEALYRIAGEMWNTPFITLVPPFYEHPGFIEALAERGRAVLEELRPDHVLFSFHGLPLRHLTKGDPAGHCKADAGCCARISAVNQNCYRAQSHATARALAAALGVAEDGYTVSFQSRLGRTEWIKPYTDE | Pathway: Porphyrin-containing compound metabolism; protoheme biosynthesis; protoheme from protoporphyrin-IX: step 1/1.
Function: Catalyzes the ferrous insertion into protoporphyrin IX.
Catalytic Activity: 2 H(+) + heme b = Fe(2+) + protoporphyrin IX
EC: 4.98.1.1
Subcellular Location: Cytoplasm
Sequence Length: 273
Sequence Mass (Da): 30142
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A0A971FC85 | MPKMKYVYYAIVAVVAVGCLAAINLLKPESAVSADQQQKEEAREMLAQADKISEEAKAGADQEIAKPEQPETKENAPVDMPEKAPEKFSVEFECTNGTFVVECVTEWAPLGAERFYTLVKEGFFNDAGFFRVVPGFVVQFGLAADPSATAKWKERKLRDDPVTQSNKKGYITFAMAGPNTRTSQVFINYRDNTNLDGMGFAPFGKVVSGMEVVEAINAEAGERPNQGMITFEGNAYLKKNFPKMDFIKKATIKQ | Function: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
EC: 5.2.1.8
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Length: 254
Sequence Mass (Da): 28065
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A0A955ZKA3 | MRGRIFAVIAAVSLLVGCDHTTKHLAETSLRYSGPKVLVPGVLDLSYVQNHDVAFNLLSWMPTTWRAPLLLAIGVLAVVGLVVWLAKRRSAPPLQAVAVALILAGALGNTADRLLRGYVVDFIHVHRWPVFNVADIAVVVGVILLLIGPKITEWRSRAAPTPS | 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-, in which Xaa is hydrophobic (preferably Leu), and Yaa (Ala or Ser) and Zaa (Gly or Ala) have small, neutral side chains.
EC: 3.4.23.36
Subcellular Location: Cell membrane
Sequence Length: 163
Sequence Mass (Da): 17610
Location Topology: Multi-pass membrane protein
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A0A077ZKU1 | MERRFVSYVWRQMNASQREWFNYFLSTHFWGPVVNFGLPLASFNDMRHSPEIISGSMTLALACYSLAFMRFAWKVQPRNLLLLFCHTSNEIAQAIQGYRFLNYHYGWTLPGIKKYTFTFTLQYVSRPTFSAKNESTFN | Function: Mediates the uptake of pyruvate into mitochondria.
Subcellular Location: Membrane
Sequence Length: 138
Sequence Mass (Da): 16352
Location Topology: Multi-pass membrane protein
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A0A0E2D504 | SNSGEILSSKDARRYEAGGGGTIPTTPPTPPDTNYGICFPDQTPCIKQGSASTRFSGVKTITTYTAGEENHYELKDYSRGKGIITYSWEFIEDPFMGIYLLNVPIVDINNGWTKFEYHDDYNHDALLDAHWGIEMTYDYFKSVHNRLSYDGNDSKVVNNVHYFNIFVGNNAYWDPMTEEIYYIYCPHNSSTCKSLNLPIILDPTYEDFTSLDIVSHEFGHGINGDLAGFTYDPEPGALDEGFSDIWNVGVNNYVNKVLGMQKNIWLVGDETVPGGGMRSVSNPKSTTVMSPGPNTYYGGLWDSENNEAHTNSLVLSHWFYTLSKGKQGINDHWCEYNVSGINIEKAEKIAYAALYYLFPTSGYTSARTAAIYSAKALYGKFSSEVKSTIDAWDAVGVPADTTSRGGQGMYKPHYYITFVKLSNLERSSGNDCGYKDNSYLHPTVIKGFTYNMVLSSEGEVSIPSKVHKWRVWIDFNRNGSFESSEMVVQDSINDTFGGTLQKSIQIPTSALTGDTRMRVSMKAVQSGESYQLANESFTEGEVEDYSITINNFSI | Function: Extracellular zinc metalloprotease.
EC: 3.4.24.-
Subcellular Location: Secreted
Sequence Length: 554
Sequence Mass (Da): 61836
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A0A3M2F5C4 | MVLRGKRKKKGLLITFEGPDGSGKTTHARRLVRKLRRQGWEVVLTREPGGTPFGDRVRKILLDRKFEEEIGARTELLLYEAIRAHHVKNVIAPAIANGEIVVCDRFTDASVAYQGWGRRLGEKEVKAINAFATGGITPDLTILLDLKPEVGLGVIETRRNGGKDGLDRVEAAGITFHRRVRRGYRSLARKERNRIVMIRRAEDPEETFKKIEDAVETFLKRKGAGVSGVGKEPRRRRRVAGMKMPRKR | 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: 248
Sequence Mass (Da): 28038
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A0A831XK65 | MGHKLYRFRATTLNEALRCMRAKLGPDAVVVNTSEVREGGFLGFLSEKKFELTATAGPSATSNEPGQRRPSIPERIYAAQSPPRAAEGIAETRAYYQKVVEEAQQRLAPATKTNPGEGRTAGGRVVPFRNTEPAPAAEGSRRGHPMDDMRHSVNEMREMLQVLVAETADSGPVKEYAEHYRALVNQGLSRRLAASLIERTVKSGSSDLLKDRRIFRERLKLQIRSDVQATNGLMLTPGIRRTIALVGPTGVGKTTNVAKLAAEFAVRERLRVAMVTCDTFRIAAPEQLRVYAEIIDVPMQIVNDANEMAAAMRTFSDYDLILVDTAGGSQFNIEQLEELKQTLTPARPDEVLLLLGANTQLHELYNTLDSFSRLRPTSLFFTKLDETRHYGSLYSLYAESKLPLSYFSTGQSVPDDIEIVNPGKVAHLVVEAGETCDRSST | Function: Necessary for flagellar biosynthesis. May be involved in translocation of the flagellum.
Subcellular Location: Cell membrane
Sequence Length: 441
Sequence Mass (Da): 48699
Location Topology: Peripheral membrane protein
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A0A7X7UGB5 | MRWLKEKYGVLILGLTVSLVLDQLTKMLVIFQLPKHAGRAIIPGIFDLYHVHNTGSAFSLFRDNPVTFFLIVNLAAIGFILYFFAKLERGELRLAAAFSLIMGGALGNLLDRLRHGFVIDFFRLHFNDLSWPVFNVADIAIFSGVCLFALNLIRSELQLRKSQGA | 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-, in which Xaa is hydrophobic (preferably Leu), and Yaa (Ala or Ser) and Zaa (Gly or Ala) have small, neutral side chains.
EC: 3.4.23.36
Subcellular Location: Cell membrane
Sequence Length: 165
Sequence Mass (Da): 18598
Location Topology: Multi-pass membrane protein
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A0A3M2F1Z8 | MKKVRTYFEEVWNEVKWEGGKVTWPSNEEVKGSTIVVIVTVALMAVYFAVVDTGIGWAVAKMLGVR | 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: 66
Sequence Mass (Da): 7405
Location Topology: Single-pass membrane protein
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A0A947HKR4 | MEAIVERANLDWKNLGFALVPTDVNVVYRWRDGVWSAPEFRENFDLNLPMAATALHYGQAIFEGLKAFELADGRVAIFRPDENAARMQFGAKKLLMEAPPEDLFIEACVEIVRRNRRFVPPYESGAALYLRPFLLGVSAQVGVRPAVDYLFAVFATPVGPYFKGAKRTIRLRVDEEVHRAAPLGVGDVKAAGNYAAGMRAVSAAQRDGFDNVIYLDARESRYLDETGATNFYGVTHGSSGPSYVTPKSRSILASITNKSLMILAKDLGYKVEHRPVDVAELGSFSEAGAVGTGAGIAPVGSIEWRGKTYDYGDVPGPVTQALLTELTGIQRGTLGDRYGWLLPV | Pathway: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 4/4.
EC: 2.6.1.42
Catalytic Activity: 2-oxoglutarate + L-isoleucine = (S)-3-methyl-2-oxopentanoate + L-glutamate
Sequence Length: 344
Sequence Mass (Da): 37553
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A0A956C4Q3 | MAFGIPTKSAPTSEPSARGAAVGDLVPEARERGRDPDGHASAARAMFDRIAPTYDVLNKVMTAGIDRRWRSRAVAALHGAPSGAALDLCAGTLDLAALLERAYPTERVVACDFSAKMLELGRGKVTRTESLVADALALPFDDGAFTRVICGFGMRNLSDLRRGLSEVRRVLAPGGVFVTLELFAPALARSKAFHSLFAKRVLPAMGKAIARDEEAYGYLSKSMLGFVTRGEYEDMLRDEGFSAVRGSDLTLGVASVVRAEVAGGPA | Pathway: Quinol/quinone metabolism; menaquinone biosynthesis; menaquinol from 1,4-dihydroxy-2-naphthoate: step 2/2.
Function: Methyltransferase required for the conversion of demethylmenaquinol (DMKH2) to menaquinol (MKH2).
EC: 2.1.1.163
Catalytic Activity: a 2-demethylmenaquinol + S-adenosyl-L-methionine = a menaquinol + H(+) + S-adenosyl-L-homocysteine
Sequence Length: 266
Sequence Mass (Da): 28232
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A0A1Z8L1N0 | MYPWIDLYYFKIPSFGLMVATAFLICHHLLKKEFKKNNLKENIIDDIIFYAVISAILGSKIYYIIETQSYYMFYTNLQNIFIKLFSFNIPGFITELQNLGSGLVFNGGFICALVLIAIYVYRHSLDFLFLADIVTPYILLGHGIGRIGCLLVGDDYGIPSKLPWALSFPEGIPTTTINTFMTNFSFLNYTREELSIFLVPGQDSVITVHPTQIYEMILYFLGFILIKKFYHKLSFTKGSIFSIYLIVGGFSRFVVEFLRTNERYLFNFSSAQFISLFMVITGLIYLSYLYKNNNSYGKN | 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: 299
Sequence Mass (Da): 34536
Location Topology: Multi-pass membrane protein
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A0A1K1P046 | MPEIPAVYQNRELSWIKFNKRVLEEASDGALPLMERLTFAAIYMSNLDEFLRVRGGALLARSLKNDEQLDNKSLMRPSEQLSAVYREVRILQPLKDKLVTDLDRALAEKGIRRLEYERLSPAMQQRADDLFYHSIKPFLNTYILDSGDSFPFIESGRIYAVLRLENERGSFTAVVSDTAEHERMLTFTEDGFAYILAEDILIAKADTLFSGYTVTEKLLIRASRSAAVTLDDEPNITSDRLEAMSLVLAKRRVMQPVRLQILGSCTDLTADMLAETLDVGQDAVFIEHSPLEMKYVFALRDILAERSELFYPPYQPVIPKNIAADRPIHQQAAEKDILLSYPYESMEPFLRLLEEAAEDDSVLSVKMTLYRVADGSRVIAALCRAAQNGKQVTVCTELRARFDEQHNIDCSKQLIAAGCKVIHGMPFIKVHSKLCLITRMVNGEPLYVTQIGTGNYNERTALQYADFTLMTADPVIARDADRVFAELENGMVVTETSALLVSPQRLRMPLAAMIDDEIRLARSGADAYIGLKMNGLTDKLLIDKLIEASQAGVKTDLIVRGVCCLTAGVTGYTENIRIISIVGRYLEHSRIYIFGKGERQAVYISSADLMTRNTTRRVEAAVRINDPDLKAQLIGYFGTQLDDDCSARVMLPDGSYERLHGGHTDCQKVFAQQAQESAAKPEPAPPTLPEQPPEIVPEPETPQEEKPPEKKRGLLRRILDLFRRKKK | PTM: An intermediate of this reaction is the autophosphorylated ppk in which a phosphate is covalently linked to a histidine residue through a N-P bond.
Function: Catalyzes the reversible transfer of the terminal phosphate of ATP to form a long-chain polyphosphate (polyP).
EC: 2.7.4.1
Catalytic Activity: [phosphate](n) + ATP = [phosphate](n+1) + ADP
Sequence Length: 727
Sequence Mass (Da): 81733
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A0A7X7C985 | MIKIALCGYKGRMGGRIEFFLSQDPDMKILSRIDAEDAVAGAFDDIDVVIDFSSPSGAIEHIGEAAAKRKPFVLGTTGFSSDQEAEITRAASKIALLKSSNMSIGVNLLLKIIEETTAALGNSYSISIEETHHVHKKDSPSGTALMMKKSAAKNFNGEIGIVSHRKGEVAGDHKIAFEGEEETLTFFHHAKSRDLFARGAVAAAKWIVGRKAGLYTMQDVLFKYPLKSWLQQ | Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 4/4.
Function: Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate.
Catalytic Activity: (S)-2,3,4,5-tetrahydrodipicolinate + H2O + NAD(+) = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADH
EC: 1.17.1.8
Subcellular Location: Cytoplasm
Sequence Length: 232
Sequence Mass (Da): 25246
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A0A7V2TTB3 | MNLRVIKSFYFEAARRIPGSDNEITGCSYRVDVIAAGSPHPVYGWIVDFGDMKAALDPLVRHLDHSLLDDVPGLENTAPERIRAWLLDRIQPRPAWLEDIRVLALTVDCFRLIDLPASADEHLPDRVAFHFAAAQALDVLPAGHPCRNLHGHTYRVEAGVEQLRQPETRAKLESLLADVFGQLNNAHLNRVPGLQPPTCERMADWLWRRLENAGLRPNLVAIQETHKNRCECRGD | Pathway: Purine metabolism; 7-cyano-7-deazaguanine biosynthesis.
EC: 4.1.2.50
Catalytic Activity: 7,8-dihydroneopterin 3'-triphosphate + H2O = 6-carboxy-5,6,7,8-tetrahydropterin + acetaldehyde + 2 H(+) + triphosphate
Sequence Length: 235
Sequence Mass (Da): 26524
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A0A7Z9KWT9 | MSQTLAELGEDALIQFIAETFDSNSSIQVGIGDDCAVIQSPSNLHVVTTDAMIEKVHFSRETMSAAQIGRKLVAVNVSDIAAMGARPAYGMLSMCLPEDLSVRWIKELISGVASEAGQYGFSIAGGDLCASPGPVFLNLTLSGTLVASKPILRSTARPGDGLFVTGTLGTSAYGLRLLSSGQHVNDASQSVAKHRVPGAQLENADVLARWEGCHAMMDISDGLAIDANRLAKASSVRLTVNIDALPLHEELEGLPDEEAQELAIYGGEDYELLFSAAGPPPIKATRIGSVEAGAGSVNWVRDGRPYELLNNASYRHFKTNSATQESK | 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 + thiamine phosphate = ADP + thiamine diphosphate
Sequence Length: 327
Sequence Mass (Da): 34588
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V8NVH0 | MFYALAIICDDFFVPSLEKICERLHLSEDVAGATFMAAGSSAPELFTSVIGVFITKGDVGVGTIVGSAVFNILCIIGVCGLFAGQQEQNGNWAEVASIFKDIKDSWERVLNKMQSIEEKLERSEQDAQEEEELIRGSEENSEKNQQTMMMRMKRQ | Catalytic Activity: Ca(2+)(out) + K(+)(out) + 4 Na(+)(in) = Ca(2+)(in) + K(+)(in) + 4 Na(+)(out)
Subcellular Location: Membrane
Sequence Length: 155
Sequence Mass (Da): 17252
Location Topology: Multi-pass membrane protein
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A0A956G9C0 | MARTIRRAAVLGAGVMGSGIAAHLAGVGIDTVLLDIVPPDLEGKQRDNKRERDRFARTAIEKAKKAKPPVFYSKEDAQLITTGNLDDDLALLERCDWIVEAVTERMAIKRSLFEKVDRVRKQGCIVTSNTSGLEIAGMVEGRSEDFRKNFFVTHFFNPVRFMKLLELVPGSDTDPEAFDFMARFGGDVLGKGIVFGKDTPNFVANRIGTYGMLYILHAMRGGENEPFSVEEIDSVFGAPTGRPKSAVFRTADIVGLDTLLHVADNCYDSLVNDECRETFKAPKWLREMVEQKKWLGSKSGQGFYKKIGKDIHALDLGSWQYKPKESVRIGSVGAVRKIEDPRARLKAMLAQDDRHAQLAWDVTAHTLTYSARRMGEIADDIVNIDNALKWGFQWDLGPFETWDAIGVRESVERMDKDGIEVPANVRAMLDSGRSSFYGGSEAKPTYYDFSSSSEKAVPLDERAVRIAALKQGEKVLYKNAGATLYDMDDGVILAEFHTKLNAVDSDIIGALNKAIDMAEGEGWNGIVIGNEDARSFSAGANLFGIVMAINQKQWDQLEQEITRFQQTTLRLRYSGVPVVAAPAGLALGGGAEITMGADAVRAHAETYMGLVEVGVGLIPGGGGNAQMLERVLAGVPDDPNFNTLPLIQRAFMNIGMAKVAVGAEDARELGMLRPHDGVTLNRDLLLHDAKATVLGMARAGYRKPRPVRFRLPGISASTTIRWFVDNMRQGGQVSDHDALIAGKLAHVLCGGDTSPRVKVTQQQLLDLEREAFLSLCGEEKTKARIEHMLMKNKPLRN | Pathway: Lipid metabolism; fatty acid beta-oxidation.
EC: 1.1.1.35
Catalytic Activity: a (3S)-3-hydroxyacyl-CoA + NAD(+) = a 3-oxoacyl-CoA + H(+) + NADH
Sequence Length: 797
Sequence Mass (Da): 87604
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A0A955VV59 | MTSSTLRVLTSPIGPIRIEVLDGRVRHVGIADGTEPATPTPAEHSGDAAVASVAVEQVQEYLDRRRTRFDLPLDLPGTPFQRSVWEVLQGIPYGETISYGELARRVGNPAAQRAVGGANRSNPIAIVVPCHRVIGADGGLGGYAFGVERKRWLLDLEQG | Function: Involved in the cellular defense against the biological effects of O6-methylguanine (O6-MeG) and O4-methylthymine (O4-MeT) in DNA. Repairs the methylated nucleobase in DNA by stoichiometrically transferring the methyl group to a cysteine residue in the enzyme. This is a suicide reaction: the enzyme is irreversibly inactivated.
Catalytic Activity: a 4-O-methyl-thymidine in DNA + L-cysteinyl-[protein] = a thymidine in DNA + S-methyl-L-cysteinyl-[protein]
EC: 2.1.1.63
Subcellular Location: Cytoplasm
Sequence Length: 159
Sequence Mass (Da): 17078
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A0A955X2V0 | MKFVDEVKIWVRSGRGGDGCGSLLREANRPRGGPDGGDGGDGGSVLFVAERNLSTLLDFRYTRHYRAEHGQNGMSRQKYGRKGKDCTIRVPVGTVISDNETGEVLADLTENEAVVVAVPGGKGGKGNMHFATSTNQAPRQFERGEEAVERELILTLKLLADVGLVGFPNAGKSTFISRISAAKPKVADYPFTTLSPNLGMVRLGYEEGFVVADIPGLIEGASEGAGLGHRFLKHVERVSVLAFVLSVSYEEGRTPEADYEVLVRELEHYDADLARKPRMILLAKADLPDTAEHEAAVRALAERDGAPFFVISSVTGQGLDAVVRALNEVVVADRAARAAGLDDDGPDDDEDAFDDEDDAYDDEDGDEDGDEDGDDELE | Function: An essential GTPase which binds GTP, GDP and possibly (p)ppGpp with moderate affinity, with high nucleotide exchange rates and a fairly low GTP hydrolysis rate. Plays a role in control of the cell cycle, stress response, ribosome biogenesis and in those bacteria that undergo differentiation, in morphogenesis control.
EC: 3.6.5.-
Subcellular Location: Cytoplasm
Sequence Length: 378
Sequence Mass (Da): 40685
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A0A3A4JXM6 | MRVVVAMSGGVDSSVAAALLVEAGHEVIGLTMNVWDYGRDACDTAAGRACCSPSDIEDARQVCRSLGIRFYPMNFRDAFRSRVVGPFIDAYLRGETPNPCVLCNSVLKFDQLLRQAEAIEADAMATGHYAQLLRGEDEKIHLLRAVDRPKDQSYFLFGITPRVAARLLFPLGGLTKPEVRGLAERFGLRVAAKRESQDACFAADGSYAELIAADPRAAETGEGDIVDLDGRVVGRHDGFWRFTIGQRRGLAVAAGERIYVVRLEPEHNRVVIGPETALFRSELTLRDLSLVAEESLSDGMTLHCQIRSRHHAAPATLHGLDGGPLAPGASARVVFERPQSAITPGQAAVLYRGDEVLGGGWITEAGR | 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 Location: Cytoplasm
Sequence Length: 367
Sequence Mass (Da): 39752
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A0A818ZYL7 | MTAYNLPKDKQIELVRIAQAIATSGKGILAADEPADVMASRWAPVNIENTEENRRYYRQLLFRTKESSHYISGIILCHETFHHKTDDDYTPFPRLLQENGILPGITVDQSTVVLGGTDNEPTTQGLDNLEERCREYKKLGAQFAKWRAVITIGPNSPSQLAIDENAKTLARYASICQQCGLVPIVEPEVSQDGDHDLDECQRVTEKVLATVYKALNDYHVYLEGTLLKPNMVTPGNKSTKQYSIEQIAEATVITFRRTVPIAVPGIMFLSGGHNEENSTVYLNAINRVALYKPWLLSFSYGRALQTSVLHAWKGDKANDEQARNEFLRLAKQNSLASLGKYEIMFRHNSASSIMKYILVTGGVISGIGKGIISSSIGTILRSHGFRVTSIKIDPYINIDAGTFSPYEHGEVFVLDDGGEVDLDLGNYERFLDVTLHRDNNITTGKIYQYVIDKERRGDYLGKTVQVVPHITDAIQEWVERVARISVDEDKSEPDLCIIELGGTIGDIESMSFVEAFRQFQFRVKKENFCLVHVSLVPQPNSTKEHKTKPTQHSVKELRGYGLTPDLIICRSATPMPLSAKEKVSMFCQVDKEHVICIPDVKTLFRVPLLMEENGVFNFLSTRLHLMPKSNYDRSLMIKWRDLAERYVIFNRKNKRKQIYS | Pathway: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 4/4.
EC: 4.1.2.13
Catalytic Activity: beta-D-fructose 1,6-bisphosphate = D-glyceraldehyde 3-phosphate + dihydroxyacetone phosphate
Sequence Length: 660
Sequence Mass (Da): 74619
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A0A956BBD4 | MTDLLPTRWYNIRADVPFELPETRFEGGSPPAKDGPMTSPRLVAQNMSPMPNLRIPEEVRAAYRLWRPTPLRRARTLEAALKTPAKIYYKYEGTSPTGTFKVNTALAQAFLLKQDGVKRLTTHSNDGYWGSSLAFACHRFGLDLSIYLLRGTLDAQPTRKVLMESFGADVQDGARTVGEAVSQALVTAVRSKGDIRFATGFLTDYVLLHNTVIGLEAEAQMQLEGATPDVIFACASSGANFGGLCFPFLRHVLAEEAETRVVAVESAACPSMTRGRYIYEHPDREALSPQFKMYTVGRNYQHPEGHLGSLIFHGLSPLVSALVAEDYVEPMAVKQTEAFAAGLRFLKAEGILPAPECAHAVHAAIEEAERCREAGEEKTILVGISGHALLDTRGYRALRDGTLEDLIPTDDEIKAWLPEGAWDDPENFDADSTYA | Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5.
EC: 4.2.1.20
Catalytic Activity: (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan
Sequence Length: 435
Sequence Mass (Da): 47806
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A0A956FEZ9 | MIGWLRGLVRVRDALRGEVVLDVGGVGYLVTVSWQTLGDVPEVEQPCQLWVHTHVREEALQLFGFSSTAERDVFRLLTGVPQVGPKLAVAVLGGFPLPELLAAIAGGERATLERIPGVGKRTAERILLDLKDKVGVLLEALPAAQGPAPAAEATSGDDQLRDEARLVLVSLGWKAKAVDAALETALAASEGSESLDALVRRALAQLMAR | Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair, while the RuvA-RuvB complex plays an important role in the rescue of blocked DNA replication forks via replication fork reversal (RFR). RuvA specifically binds to HJ cruciform DNA, conferring on it an open structure. The RuvB hexamer acts as an ATP-dependent pump, pulling dsDNA into and through the RuvAB complex. HJ branch migration allows RuvC to scan DNA until it finds its consensus sequence, where it cleaves and resolves the cruciform DNA.
Subcellular Location: Cytoplasm
Sequence Length: 209
Domain: Has three domains with a flexible linker between the domains II and III and assumes an 'L' shape. Domain III is highly mobile and contacts RuvB.
Sequence Mass (Da): 22183
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A0A2D9HD92 | MYIVTDEKSYETLMAELQECVGRLEAGSLGVEEALSLFEKGVGLSKEARQRLEGLEGRLERLLADGQVESLKVEETQ | 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: 77
Sequence Mass (Da): 8560
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A0A7X7C9R5 | MRLPLGWVRQYVNVKAKPEKLALALTISGLEVESIERVGGECIFEIGVTPNRGDCLSIIGIAREISAAFGLPLKPPSFASVKGKGKMAGRIKVSVRSSQRCPRYCAKIIEGIRIGSSPDWMVKRLAECGVRSINNVVDATNYVMLLTGQPLHAFDLSRVRGNKIVVKQADEGMKFKALDGVERILSREDLMICDGEGPVALAGIMGGENSEVREDTHSLLLESAFFEPKGVRRSSRRLGLASESSRRFERGVDPLGLLDALNLLTKLVVESAGGTPSADHIDLFPKKILPRKISISSAEVKRILGIDLKPAAISKLIKSIGMKVSPASPGKLNVSVPTFRPDIEREVDLIEEVARLHGYDNISSRMPEVAMKSITRPKYFEQEAAVRSALAGSGLTETVLYAFTSAESLTPFAEAGGTHVALANPISADQSVMRTMLLPGLLDVYKLNASRHRHDSRIYAFQNVFSKTDSAGGFRETRCFAGLLSGARNLGAWERAKENVDFYDAKGVVENVMAALGIHSDTIFQRGEGYSFLHPGRFAHILCRGKRVGFVGELHPEVAAKWDLQRGVYLFEINFRLVAEMSLGEPARFAELSKFPFVERDISMLLPDRIPAVEVEKSIQDSGETLITKVSIFDLYKGKGIPEGQKSLAVSMRFATHDRTLTDEEVGMAMEKIVETLKTKLGATLRT | 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: 687
Sequence Mass (Da): 75272
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A0A7X9P6U6 | MIRHSHHRLHFVGIGGIGMSGIAEILVNLGYRVSGSDLKANDNTARLEKLGVRIVTGAHAAEHVPPGTDVVVVSSAIRSGNPEVLEARRRGIPVIPRAEMLAELMRLREGVAVGGTHGKTTTTSLIATIAAHAGLDPTVVIGGRLNALGSNAKLGQGDWIVVESDESDGSFLRLSPRIVVVTNIDPEHLEHYGDFEKLRAAFLQFANGVPFYGLTVLCLDHPVVQGLIPELTKRFVTYGLAAQADYRALDVRPALDGWGSTFTLLVRGTERGEITVRMPGTHNVLNALAALAVADEMGVLPVQAAEALASFRGVQRRFTVAGTAGGVTVIDDYGHHPAEIVATLEAARGCRPRRIAAVFQPHRYTRVARLFDEFARAFNRADHLLVTEIYSAGEDPLPGVSAAKLAQAIRQHGHRDVTFVPELAAAVEHLRGWVREGDMVLTLGAGDVAWVGRELLRLRGGSEGIDRRAPFSSETTRGPGGAERRRRSSRRKG | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Cell wall formation.
Catalytic Activity: ATP + L-alanine + UDP-N-acetyl-alpha-D-muramate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine
EC: 6.3.2.8
Subcellular Location: Cytoplasm
Sequence Length: 493
Sequence Mass (Da): 53054
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A0A7S3M0B3 | MMCYLTTLSIVSSFLVPKIRSNVFKVSCPCITTAISSMSSTSQPSITAVSDSSVNRLLKQTNAWCGVNGLMYTDGKVNWTPAPLSLIPNAFSSDSLLYAFKMQPIINKLVDGISRDREFLLDKLSTVSESDEFTKRILQLYMQVPESVVKNDLQCGILRSDYMINNDHRALQVEINTIASSFGYLSKKVSDYHRYILERNEKNEDLHTIVASTLEASFASAEDAKTKVKAQNVLNNPSSVELAKVLALAHQQCKEENAAVLFIVQPNERNIADQRAFELQLWEAHRVPVEFLTLAEVHARARLEGPSEDWGKQSLVIGPAPGTVGSEFTVSVAYFRAGYTPNDYPTEDEWAARKVIEQSSAVKCPNTGYQLAGTKAIQASLCLPGVLERFLTVEESVELRRCFAAQYSLVALTDLSAEGAELRTATEQAVAQATADGAPWVLKPQREGGGNNLYGVELSNFLKEHAGQSVLSGYVLMQRIFPLPQKTAFLRAGALQILPSISELGVYGTYLSYGACPQETTNEEKVLCNAYGGYLLRTKPEGVDEGGVASGYSVLSSVILE | Cofactor: Binds 1 Mg(2+) ion per subunit.
Pathway: Sulfur metabolism; glutathione biosynthesis; glutathione from L-cysteine and L-glutamate: step 2/2.
EC: 6.3.2.3
Catalytic Activity: ATP + gamma-L-glutamyl-L-cysteine + glycine = ADP + glutathione + H(+) + phosphate
Sequence Length: 561
Sequence Mass (Da): 61479
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A0A3B1KE89 | MEFNRKRDSDSMKFKRRDVKMQKREYSEGPLTRQKQASSTTPAGCMCKPLKIFTSNVRGIKLIKNRVDKLNKLAALNPDILFIQELRLNHIEQIKEAQQLWKIGKSVISIGSDLADGVGILFNTYNLEIIKRRDIIPGRLLVLDCNLKGQKLRLINVYTSSDRSKKIQLFRKLPELLCSGHDIILAGDFNTVTEENDREASTHFKLSKEGKILKEICDEFEMKDSFRVMYPDSFGFTRYDNKTKTRIDRIYVSKQANLNDYKTVTPGSEE | Cofactor: Probably binds two magnesium or manganese ions per subunit.
Catalytic Activity: Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleoside 5'-phosphates.
EC: 3.1.11.2
Subcellular Location: Mitochondrion
Sequence Length: 270
Sequence Mass (Da): 31204
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A0A7S3M597 | TPSAASDDTACQVDIFPNVDFICLVAGAIPWYKELAGGLPIAPHGRVGPAVVRAAGCALLAGNLWLRMTSLDCFVEKKTPVAHHQAARVMITDGPFEYSRNPTYVSMVGALGAFGLIMNSWWGVASAAPLFAYLHFHVIPAEEAYMRNRFPEFAEYMQAAPRWLGPL | Pathway: Phospholipid metabolism; phosphatidylcholine biosynthesis.
Subcellular Location: Membrane
Sequence Length: 167
Sequence Mass (Da): 18152
Location Topology: Multi-pass membrane protein
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A0A3M2CUG7 | MTPKPTQPKLSTPASKPQVWGSRMSEPPDPRNVLYCAGRDVAPRPMADSALVPFDLWQNRAHVLMLAKQGIVSRKIASRILAALDDLESLWERREFVLDPAREDVHINIEHFVATVIGPEASGSMHTARSRNDQTTTVVRLYVRDRLLSFAESLVRLIDVLLDASRKYAHLPIAGLTHYQPASVTTFGHWLASYAQALLRDLERAEQTLHRLNVSPLGAAASFGTTWKIDRAYTAQLLGFDSVQGNTLDCISTRWEFEAEAAVLVAFVLTHLSTIAQDLIVLSLPQVGIVRVADRFTTGSSIMPQKRNPDFAEVTRAKAALVQQLVPTLLGIARGLPSGYNRDTQWTKYAIMDVFDEATAAPEIFADVIATLQVNEARARESAETNFINAVDVADTLARESGAPFRVCYQIISQAVRECESRGRLLPDVVVQLAREAGVQVQSVNFLSAEQILNEKNHIGGPAPSALAREIRNVREQLQQRKKQLAAFRKRLTRAKMKIEQERKKLRQSPK | Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 3/3.
Catalytic Activity: 2-(N(omega)-L-arginino)succinate = fumarate + L-arginine
EC: 4.3.2.1
Subcellular Location: Cytoplasm
Sequence Length: 511
Sequence Mass (Da): 56877
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A0A3M2F8Q2 | MTAPNRFWSGGGGKEGKEEEEEGAKMTGHCSTPAEIEARAEEERILLVGPANVGKSCLFTGLTKKFVNVSNYPGTTVEITAARKDELLWLDTPGMTGLIPTSEEEEVTLRILLEKEDDIVVAVIDARDLPRGLSMLAALSDFQHRFVVALNMYDEALDAGIEIEVAKLESEIGVPVVPTVAVRRQGISRLRHRLVEAARLKIAPREPRDVENLLGEVAEGFSDRTHPRIRARLALGGRRDLAGIRDAAEAERIGEYRRRFSVSYGVSYTGLYARSRSVAVAPILEKVFHSPRSSGTGWSSLLGDFAVHPLWGWPILLAVLWCVYEFVGVFGAGTIVDFIENTVFGKWFLPWLSSVLGRIPPGFVRDFLISDLAGGWNGLLVGPYGLVSMGVTYSIAIILPVVSTFFLAFSFMEDSGYLPRLAVMLDRPFRAMGLNGRAVLPLVLGLGCDTMATMTARILPSRKERLLVTFLLALAIPCSAQLGVIGALMVSLSLKAILVWVVVILGVLLVAGWIGSRVLPGTPDPFLMPLPPMRLPRLGNILVKTVARTEWYLREAVPLFIIGTFILWLLAAVHVLGKIETLFAPVVVGMLGLPREAARAFLMGFLRRDYGAAGLYAIFKQGLTGGTLPPAMEVDLVVALVTITLFVPCVANFLMIGKERGWKTAAWIGLITMIAALGVGTGTRVLLEALGWAG | Function: Probable transporter of a GTP-driven Fe(2+) uptake system.
Subcellular Location: Cell inner membrane
Sequence Length: 694
Sequence Mass (Da): 75439
Location Topology: Multi-pass membrane protein
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A0A956BNY1 | DGLRALAAMGDPLHRLLRRTQLGDGLVLEQRTVPMGTLLVIFESRPDALVQVAALAVRSGNGLLLKGGKEAAYSNRALHAVLAGALAPLPSAALGLVEGRADVDALLKLDGLVDLVIPRGSNALVRHVQENTRIPVLGHADGVCHVFVDADADPERALAVVLDSKLDYPAACNAMETLLVHEGYPHADALIAGLRDAGVRLRGGPSAAARWGLPPVEDFHTEYSDTEASVALVPDVDAAIAHIHRFGSGHTEAIVTRDTSVAERFLARVDSASVFHDCSTRFADGFRYGLGAEVGISTSRIHARGPVGVEGLLTTRWTLRGGGHTVGAVKRGEWSFDHSDLL | Pathway: Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate 5-semialdehyde from L-glutamate: step 2/2.
Function: Catalyzes the NADPH-dependent reduction of L-glutamate 5-phosphate into L-glutamate 5-semialdehyde and phosphate. The product spontaneously undergoes cyclization to form 1-pyrroline-5-carboxylate.
Catalytic Activity: L-glutamate 5-semialdehyde + NADP(+) + phosphate = H(+) + L-glutamyl 5-phosphate + NADPH
EC: 1.2.1.41
Subcellular Location: Cytoplasm
Sequence Length: 342
Sequence Mass (Da): 36150
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A0A348MU88 | MTSVSLATLAQHINATIQASADDVVAAESIMIHKVAPLDKAQSGDVAFLNDKKYLKSLATAKASAVILTQKLAADYDGVALVVNDAYIGFALAAQLLDPTPKPHYAIHPSAYVDETAQLGNNVSVGPNAVIEAGVELGDDVSIGAGAVIRVNAKIGAQSMIHPNVTIYHSCELGVHVVIHSNTVIGSDGYGYAPNGGKWITIPQTGKVVIGDYTEIGASTTIDRGALEDTIIGQHVIIDNQVHIAHNVVIGDGACLCGGTMMAGSVNIGKNVIIAGTVAINGHISICDNVQITGNTMVTSDITEPGVYSSGMPHSPYSEWRRNSVRIRQLDSVFKRVKTLENQVQRIQSSDSDE | Pathway: Bacterial outer membrane biogenesis; LPS lipid A biosynthesis.
Function: Catalyzes the N-acylation of UDP-3-O-acylglucosamine using 3-hydroxyacyl-ACP as the acyl donor. Is involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.
EC: 2.3.1.191
Catalytic Activity: a (3R)-hydroxyacyl-[ACP] + a UDP-3-O-[(3R)-3-hydroxyacyl]-alpha-D-glucosamine = a UDP-2-N,3-O-bis[(3R)-3-hydroxyacyl]-alpha-D-glucosamine + H(+) + holo-[ACP]
Sequence Length: 354
Sequence Mass (Da): 37200
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A0A956KDD9 | MQTVLEESGSPGAALVDPAADLSSFDLLVGTYAGGLGPVALERAIEARVDLLDLADIETHVYDERRAAVERRGIAVYPAAGFCPGLVNVLLQRELARGGVARIEVLAGTLAPVPNYFPFLWCFEDMVLEFDGPSVQVQGGVERTFPPFAGQREETLFGVAAESYLAQSGFEQLTRRAGLTDFTYRNLRPAGFRTFFEFLRAHGAFEPDVIAVTKALLERRLHENISLAQITVEGAQRRRWLVSARARSDAPLNSMQRITAACAAAFVTRLRSIDRRPGVHWPEEFGTDEPSLHSLLSTVQQLGVSIELNPPALWIGSVSSRERDFDLTLERCAPGGSFVERGGPALALLREPVLRREGDAVIVTSRDGTFRVREPGGRCEVSVSCPGGATRALRFFERLALEYLPESVALVTRRDNYTAPYRHEGLIFTRSVAVHQSAYQRIEIAEHPVYGRLLMLDGEVSVSEYDEALYSRTLRDVGRRSTPRRVCILGGGDCGVLRAVLEHRSVEAVVMVELDPEVVRMCSEHLPAIVSGADRDARATIVYDDAFAFLERTDARFDEVIYDLSDTPIGSVSDEQLVASMRRALAPGGRIAIQCGGAADWNRGHRERVLAALRAGFATVEVERVVIPSFNEGEWVFAGAC | Pathway: Amine and polyamine biosynthesis; spermidine biosynthesis; spermidine from putrescine: step 1/1.
Function: Catalyzes the irreversible transfer of a propylamine group from the amino donor S-adenosylmethioninamine (decarboxy-AdoMet) to putrescine (1,4-diaminobutane) to yield spermidine.
Catalytic Activity: putrescine + S-adenosyl 3-(methylsulfanyl)propylamine = H(+) + S-methyl-5'-thioadenosine + spermidine
Sequence Length: 641
Sequence Mass (Da): 70403
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A0A1G1WPA4 | MPKINFDILTLFPNYFETPLQTSLLGKAIEKKLIGVNLHDSRQFGLGKNKSVDDTPFGGGVGMIMRADVLGEATASILAKRSLKPTVILFDPTGAKLTQKMVKQFSKKKAFLLVCGRYEGIDQRYKDIFVDKEISIGDYIVSGGEVAALVFIEAVSRLVKGVLGEESSVETESFSPKGEGEKQLLLEYPQYTRPRIYRKKPVPDVLLSGDHEKIAEWREKQSLSRTKNLRPDLLKN | Function: Specifically methylates guanosine-37 in various tRNAs.
Catalytic Activity: guanosine(37) in tRNA + S-adenosyl-L-methionine = H(+) + N(1)-methylguanosine(37) in tRNA + S-adenosyl-L-homocysteine
EC: 2.1.1.228
Subcellular Location: Cytoplasm
Sequence Length: 236
Sequence Mass (Da): 26379
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A0A5B8LPH6 | MIAIIVFVAMAVYLLLNIPVPVAVSLSAMTAMTLNGGMDLQVVVQRMFYGLNNYIYLAIPLFVLLGQIMMTAKITERLVDFALVLVGHMRGGLAQVAVVACAVMSSISGSSSADAAATGAVLGPSMVKQGYSPGFASAVIGAASAGAALIPPSITMIVYASLSNVSIARLFVAGIIPGILVGAALMFAIWRSAIKYNLPVGTERPTVKVVGKASARAFLVLLAPIIIIGGVVGGVFTPTESAAVAVLYTLFLAFVVYRSLRLRDMIGVLERSLVITAQLMLTLAAASIFSWIIARAGLPNQVAQLPIFQGDSGWIVLMLVINIVVFLLGIFLEGSPLLVIVTPIFLAPALAAGIDPTHLGIVLAINLAIGGISPPFGMLMFVACAVTPATMVQFSKAIVPFIVLICAVVLVISYVPQITLWLPDILNL | Function: Part of the tripartite ATP-independent periplasmic (TRAP) transport system.
Subcellular Location: Cell inner membrane
Sequence Length: 428
Sequence Mass (Da): 44705
Location Topology: Multi-pass membrane protein
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A0A2Z5TGR7 | MKKKKIIFNWKLNGNKYTIKCFINKVTYFIKENLEKINKNNIEILISPPIIYLDYVNNLLNNNVNIKLCSQNTDINYLGPFTGEISLKMLKDINVKYVIIGHSERKKFHNENKDIISKKFYISKISNIEPILCIGYEKNILNQIEDIINKYGINILYNTNIAYEPISSIGTGIIPSIDHINNINNMILNFLYKFDKNIKNNINILYGGSVSYKNVYNLIFKTNINGLLIGKSSTKIFDIIKIIKNIILI | Pathway: Carbohydrate biosynthesis; gluconeogenesis.
Catalytic Activity: D-glyceraldehyde 3-phosphate = dihydroxyacetone phosphate
EC: 5.3.1.1
Subcellular Location: Cytoplasm
Sequence Length: 249
Sequence Mass (Da): 28849
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A0A964NJN0 | MKIQALAELLGGELRGDGDRVVRRVAALDEASESDVGVCFSSRFRPALRATNATAVLVTRDFVSDVPEGTPCVVVSDGRAALHQTLRCLHPQVLRRVHPETVRGPSHPTIHATAIVHKDARLGANVEVGPLVVIEAFATIGPSVRIGAQCFIGEGVHIGAGTTLAPRVVVLEGSVLGDEVEVGSGTVIGSPGFGFDAQGRLPHPGRVVIERGVYIGANVCIDRATLGETRVGAGARIDNLVQLGHGVRVGAGAVLCGQVGLAGGAVVLAGAVIGGQAGVAGTCTVGEGARVAAQSGVTRSLAAGGTYSGHPAEENRLRLRRLAFVKRLVDRSRDDRRRDDP | Pathway: Bacterial outer membrane biogenesis; LPS lipid A biosynthesis.
Function: Catalyzes the N-acylation of UDP-3-O-acylglucosamine using 3-hydroxyacyl-ACP as the acyl donor. Is involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.
EC: 2.3.1.191
Catalytic Activity: a (3R)-hydroxyacyl-[ACP] + a UDP-3-O-[(3R)-3-hydroxyacyl]-alpha-D-glucosamine = a UDP-2-N,3-O-bis[(3R)-3-hydroxyacyl]-alpha-D-glucosamine + H(+) + holo-[ACP]
Sequence Length: 341
Sequence Mass (Da): 35205
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A0A955V8W4 | MTTRTLHRAHRTLIASILAATFALAPVAAFAAEDGHEAPQAEIGPGDHEAEHGHDPLVGHSPKVRPAAEDHHWWLGQELIPASARQSVADLLGKQWLFGDPPQKVDVGHIFLALIVFFMGLGLALSARRQVQGDVLPPAKWSPAAFFDIVVEALMGVMMTMMSRKKALKHLPLMTAVAVFILFSNCLALIPGLYPPTQNLNTNLALGLIAFLYYNYQGIKTHGIAKYLAHFAGPILAIAPLMFVIELVSHFVRPLSLSIRLLGNMFGDHQVLFVFLGFSVPLLPLPIMFLGLLVCIVQTLVFTMLFIVYVALATEEHEHEHDHGHGHGHEQGAAPAHAH | 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: 339
Sequence Mass (Da): 37037
Location Topology: Multi-pass membrane protein
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A0A970M7V5 | MAGAAKETATPLEAAAVIVGVAQGGTQAKGIPMSRIATLILAAGQGTRMKSQLPKVLHPLCGAPLIAYPLQLAAQMKSETTVLVVGHGRDAVQRAVAQCPGGDRVRFAVQTEQRGTGHAVMCALPALKEHDGWMLILSGDVPLLTHRTLQRLQRQMQGSTAPLGFVTFVPGNSAGYGRVVRENDEVRAIVEHRDCTPKQRAIKEANAGTYLIEAAFLRSALKKLRQDNAQNEFFLTDLVAMAAQRGAVPTVQADEAEVHGINDRVDLAQVERVLLSQKAQTLMRNGVTLHDPDTICIHPAVSVGPDTDIGRGVHITGQSRIGAGCHIEPGVLLHDTVVADGARVRAYSVIEGSHIGAGAQVGPMARLRPGSRLGDNAHVGNWVELKNTVMGDNSKASHLAYLGDGDIGDNANIGAGVIFCNYDGYLKHRTTIEEDVFVGSDCQLIAPVTLHRGAYIASGATVTHDVPEDAMAIARARQVNRADMGRLFRERQAAEKALRAAANESPKARRKSTARPKPPAKGKPR | 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 coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N-acetylglucosamine-1-phosphate (GlcNAc-1-P), which is converted into UDP-GlcNAc by the transfer of uridine 5-monophosphate (from uridine 5-triphosphate), a reaction catalyzed by the N-terminal domain.
Catalytic Activity: H(+) + N-acetyl-alpha-D-glucosamine 1-phosphate + UTP = diphosphate + UDP-N-acetyl-alpha-D-glucosamine
Subcellular Location: Cytoplasm
Sequence Length: 525
Sequence Mass (Da): 55903
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A0A956LNS6 | MKLRNHTGPLRWRLYAVGVSALYFLVVSPPVFASPAAGGHGEAGHGEAAGHGAAAAGHGEAAGEHAAGGHGAVHDGISWLGDEHTVGFVFTLINFAALVAMAYLLVFKNLIRKNAARHDEIKAKLDEATEAKATAEEVIGRVSSLLDQFEREKAEILQTARKNAETSSRQIVEEARAEAEKIRAAAVAAAEREAASRRLEIEREIVDSAIEKAEAILVSQFSESDQRRIVDDYVTRVASAPLAGGAS | Function: Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0).
Subcellular Location: Cell membrane
Sequence Length: 247
Sequence Mass (Da): 26224
Location Topology: Single-pass membrane protein
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A0A956PAX5 | MDNPYIAILILLAFAIVFCAAFLTLSWLLGPKHPNARKLAVYECGVPPVGDARDRFHVKYSLVAILFVIFDVEAVFLYPWAVRAQALGWYGFAAITLFLVILTVGLAYEWKRGAMEWR | Function: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.
Catalytic Activity: a quinone + 5 H(+)(in) + NADH = a quinol + 4 H(+)(out) + NAD(+)
EC: 7.1.1.-
Subcellular Location: Cell membrane
Sequence Length: 118
Sequence Mass (Da): 13352
Location Topology: Multi-pass membrane protein
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A0A955UZ77 | MSDATIEFPRAMGEQDAMLWRMERDRRFRSTLLSVTVLDAPPDRARFTAKIARMAAEIPRLRQRIVPMPELVSTPIWAWAEDFDLAYHLRFLRLGGAGTMRELLDFTAAIGRQAFDPERPPWEFYAIDGLREGPGGENGAAILWKMHHAVTDGVAGVRIMRHSFDLAPDGDLRAAPPPRALEPGEDADVARLSSEAVRERLAQVPGRLWEGARKAVDVARDPVGAAQSAARDLASLRRLLADMPGPLSPVMTARSTNFHVDAFQVPIAALKAAAHAAGGTVSDAFLAGVTGGLHRYHARHGKPVAALNASIPISLRNAAADSDVAGTHIAVARLALRIDEPDPARRIRAHHAVVAEARDEPAQAYSDVVAGVLYRLPLPLALRTYAASATKNDLVASSVPGIPAPVFVAGARARAFLTFGPLSGAAVNATLFTIDDMANVSLNADAAAVPDLDALVACVREGFDEVLALA | 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: 470
Sequence Mass (Da): 50256
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A0A1Z8L1C4 | MFGTLYIVATPIGNLGDISFRAKEVLSEVDFIAVEDTRVSKKILTKFDINIKMIVYNNFNESKQVDKIVNLLKDGKNVALISDAGTPCISDPGYLLVNNCKINDIKVTSVPGPSSLISALSTSGLPSDSFYFEGFLPKKKGRKTKFEFLNLLPCTVILFESPKRVNKTLLNIREYMGEDRIISIHREMTKIYEEVFFGSIKESIDFFSDKNNKGEFVLIIAKQNYSL | 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: 227
Sequence Mass (Da): 25559
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A0A4Y8USC1 | MADVARSSPPSNARSAVPSPVSSAALVAAGGTLGVTVRALLEGAFPAAPGGWPWTTTAINVTGSLLLGLLLTALARRGPDAGRRRAVRLGVGTGVIGGYTTYSTFVLEVERLVTGGAVVTGVAYALVSVVLGVAAAVLGVVLAGGRAGARGQAAHDPDALVEERARPGDGPRAGEVRP | Function: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Subcellular Location: Cell membrane
Sequence Length: 178
Sequence Mass (Da): 17597
Location Topology: Multi-pass membrane protein
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A0A9E4MIJ2 | MSKATPFPILLLGAGGREHALAWKLLQSPLCARLIVVPGNPGIADLGDRVACVAASPTDAGQLIALAKREDIGLVVCGPEAPLVSGVGDAFRSAGVPFFGPSQAAAEIEGSKAFAKSVMVTAGVPTAAYGTFSDVGEAEAFIAKQARPVVVKADGLCAGKGVEVTSHADEARAAVRRMLEDKVFGESGAKVVIEERLEGREASILGICDGERFVLLASSEDHKAVLDGDKGPNTGGMGAYSPSPLVDEAMMEEIGSRIFAPTLRTMAALGRPFQGLLYAGLMLTPDRGPLVIEFNCRFGDPETQAVLPRLVDDIVPWMLGAAEGRLPEGQLAWRPGTSVCVVMAAAGYPVAVRTGDAISGLPAVADQDPDNSVLVFHAGTRHDGKSLLTAGGRVLGVTAVGTSLDAARKRAYGAVEGIRFEGAHFRWDIGLRGQG | Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-diphosphate: step 2/2.
EC: 6.3.4.13
Catalytic Activity: 5-phospho-beta-D-ribosylamine + ATP + glycine = ADP + H(+) + N(1)-(5-phospho-beta-D-ribosyl)glycinamide + phosphate
Sequence Length: 435
Sequence Mass (Da): 45118
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A0A955VCR5 | MTLERVVIAGGGTGGHVYPGVAIAEEVLRRNAAATVVFVGTARGMEAKIVPPLGYPLELITVSRLKGGGLLERLKGLFRLPVGIWQSWRLLRRHKPQVVVGVGGYASGPTLLAAWMTRRPTAIQEQNAAPGLTNRWLGKLARKVFVGFPAARASFADKKVMETGNPVRAALAARLSRAAESAAVSQGGGALRVLIVGGSQGARFLNENVPSLLAAVRAASPDLALTVVHQTGPADEEATRSRYASGPLAAAATVKPYIDDMPAAYAAADLVICRAGASTVAEITAIGLPSVLVPFPFAADDHQAKNAEALVAAGAARMVRQEAWREDELAAWLCAVAKDRSQLEAMSAHSKQLSRLDAAQQIVTTLEGIAR | 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: 371
Sequence Mass (Da): 38924
Location Topology: Peripheral membrane protein
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A0A2E5HR40 | MRTLGLDIGTRRIGVALSDEMGWTGMPLETIQVKRNNAHIERIAAICREREVSAIVAGIPLNMDGSEGRAVRKVRALLARVQEVTGLPIHEWDERLTTVAAERVLKQSGMHHARRKQVVDQLSASLILQGYLEAQANAQTS | Function: Could be a nuclease involved in processing of the 5'-end of pre-16S rRNA.
EC: 3.1.-.-
Subcellular Location: Cytoplasm
Sequence Length: 141
Sequence Mass (Da): 15574
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A0A2M6XA98 | MPELPEVETIVRQLNRAIRGRTITNFTCSSPKMLATRKLADFQKKIKNKKILKLERRGKIILISLSRDLALAIHLRLTGQLFVREVKAPADRFNRAVFTLGKKLELRFNDLRLFGQIWLYPKAEIENNFDKIQKLGPEPFDKTFTLENFKNILRNRRTKIKALLLDQSKISGLGNIYSDEVLFYAGIAPLAPANKISSPRAKKFYLGIKIILADAIASHGTSVDTYYDATGKKGKYAAKLKVYRRTGQPCFKCDTKIQRIKIGGRSSHFCPKCQKL | Cofactor: Binds 1 zinc ion per subunit.
Function: Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized purines, such as 7,8-dihydro-8-oxoguanine (8-oxoG). Has AP (apurinic/apyrimidinic) lyase activity and introduces nicks in the DNA strand. Cleaves the DNA backbone by beta-delta elimination to generate a single-strand break at the site of the removed base with both 3'- and 5'-phosphates.
EC: 3.2.2.23
Catalytic Activity: 2'-deoxyribonucleotide-(2'-deoxyribose 5'-phosphate)-2'-deoxyribonucleotide-DNA = a 3'-end 2'-deoxyribonucleotide-(2,3-dehydro-2,3-deoxyribose 5'-phosphate)-DNA + a 5'-end 5'-monophospho-2'-deoxyribonucleoside-DNA + H(+)
Sequence Length: 276
Sequence Mass (Da): 31487
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A0A2Z4Y537 | MKPYLSVLGLFHLPTYGMFVATGILVGTWLATRLARRAQLPEGFALDAVFYVVLAGLAGGRLTYMAIEWRATLRDPVAALFNSGGMVFLGGFFCGLAALYAYCRFKKVPFALVADVFAPAVALAHCFGRIGCLFAGCCYGAPAHGWLGHLIAIRYPRLTGPDGAITGSWPYLDHLEQGWVTTADAYSLPVYATPILEALFNLGLAAALLWLWRRRRFDGHIALVYVMAYSVARFLLEFLRGDQIRGFFGALSTSQWLSLFALAGAFAIYWRRQASARAATNNDPCNT | 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: 287
Sequence Mass (Da): 31442
Location Topology: Multi-pass membrane protein
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A0A1A9QZD8 | MGGLIGGSLSEGGADVTLIDVNAEHVDALRQNGLKLKTDKGERYIPIPVLFPWEVSKTYDLIIVFTKTMHTTSAIAAIRSAIDANTVLLSLQNGLDNKLSLMEFVDQKNIMVGITTYPADMKGPGCVESHGEGIVRLASASAAPPLLDYMPGLFARGDMKAIIDPQVEVAIWEKVIFNAALNGLCAVTRSTVGQIGAHADTRELAFQIIGELCATAHACGFAVQGERIEKTVSEALEQHSSHKPSMLQDVLAERPTEIEAICGAAVRRAEEHNIPVPVTRTILGLVRHIDWHL | 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: 293
Sequence Mass (Da): 31563
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A0A816VIE6 | MEIFAVCLLLRNPSYPQLLGLLLWMILWEWIIQSCKWLGFMHGGCCLTPYILFSISLVIILALISLYVSNMAVAPTINRVHINLAHVRNTNNGDNVDLIKQQQGSILEQKWFRIVDMLKRIAYLFIFPTETIAILKIKFGGYIKKMPEMPLDELAHTLNDLDFCYATLNKVSRSFGIVIQQLPQPLKDSICIFYLVLRGLDSIEDDMTYPDDKKIFLLCNFHNNLLIENWSVKNVGDTEDYRILLENFGKVINVFKSLDSESQSIILNITSRMGTGMAEYVGKTGSIETVASYNLYCHYVAGLVGHGLAALFSHSGLEDPGLHVHEHLSNSAGLFLQKTNIIRDYLEDLQAGRTWWPKEIWCHYAVDLSEFVNNPHGERSLECLNHMVLDALNHVPDVINNLARVKHPKILESCAIPQVMAIATLAELYNNPLVFTSVVKIRKGLACKLLLNCSTLNEVYAWFDFFITKIGRKIPKRINVNTHNMHKLVNRVKKLSNINLKP | Pathway: Terpene metabolism; lanosterol biosynthesis; lanosterol from farnesyl diphosphate: step 1/3.
Function: Catalyzes the condensation of 2 farnesyl pyrophosphate (FPP) moieties to form squalene.
EC: 2.5.1.21
Catalytic Activity: 2 (2E,6E)-farnesyl diphosphate + H(+) + NADH = 2 diphosphate + NAD(+) + squalene
Sequence Length: 502
Sequence Mass (Da): 57186
|
A6WE55 | MGETPPVTHVSGWRVVVPVKGGDGAKSRLALPGPARRSLALAMALDCLAVCLRTPGVGLVVCVSDDPEVTAAARSAGAVTVSAGRPGLAAAVEAGVTCLERGPTAVLLGDLPALRAEDLGAALADALARPGPALVTDADGRGSVLLADRDGAPPHRFGPGSARAHLDAGARPLSAALPSLRRDVDTVEDLAEALALGVGPRTREALAAAAIPLT | Pathway: Cofactor biosynthesis; coenzyme F420 biosynthesis.
Function: Guanylyltransferase that catalyzes the activation of phosphoenolpyruvate (PEP) as enolpyruvoyl-2-diphospho-5'-guanosine, via the condensation of PEP with GTP. It is involved in the biosynthesis of coenzyme F420, a hydride carrier cofactor.
EC: 2.7.7.105
Catalytic Activity: GTP + H(+) + phosphoenolpyruvate = diphosphate + enolpyruvoyl-2-diphospho-5'-guanosine
Sequence Length: 214
Sequence Mass (Da): 21250
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A0A956F8U7 | MKPEIEITDDPGARAGARLAETIAAVASERGRCRLGVPGGSSPIPVFHWLAQHLEPGLASSLVVTWVDERHLPVEEGAGWRSLPAQSNLRGTWEHWLSRCAVPPPTVPMALPGTLAEATARYADAFVARLGALDVVLLGMGEDGHIASLFPGHAALEATGVCVAVPDGPKPPPERISLTLPVLQDVERAVLVATGAGKANALARVHAGDRSLPLGRYQPRGDWHWVLDPAAASELQRKST | 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(+)
Sequence Length: 240
Sequence Mass (Da): 25379
|
A0A7Z9HWJ0 | MATLKSTLVDAIKKLQDVTDSPRFDAELLLCHSLKIDRAALMLRMNDALEIPASFDSMVDRRLQSEPIAYILGEWEFYSMSLAIRPPMLVPRPETEHLVEAVLDLLPQPDARILEIGTGSGCISIAIAKHAPSCSILATDIKQDNLELAHENMVRHGLENRITSNQGSLFEPVTEPNQLFHIVCSNPPYVASEESGSLSRDIRDYEDPDALFSGEDGLDLIRDLIAQAPDYLHPGGFLIFEIGIDQHQTVSVLLEEHGYDDISFRNDLAGIKRVAMGRKPE | 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: 281
Sequence Mass (Da): 31243
|
A0A3D1RB26 | TAEPCGVCRPCIEIAAGSSVDVAEIDGASNNGVEDVRQIRERVTYLPQRDRHKIYIIDEVHMLTTQAFNALLKTLEEPPPHVKFIFATTEPHKLPDTILSRCQRHNFRRIPAQRMVERLQHIAKEEGSTISDRALSLIVRQSEGGMRDALSLLDMVLSACGREANDEAVAEALGAIDRTAVQEICEALVRRDAKAVLARIEALHNLGADFRRLAEELALHLRHLLVARSVGEAPEELADSERKAALTLANQTDPAHLARLFDLLHGAIWEVSRAAEPRLAMEVTLLKGIHLAPSAPVSELIARVDTLSRKLGDAAPGTSAAEGVRP | 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.
EC: 2.7.7.7
Catalytic Activity: a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)
Sequence Length: 326
Sequence Mass (Da): 35704
|
A0A1E5BZ63 | MRLLSDPKYVALTEATWSIFDDYQHQVASSHWRPSYHISPVAGLLNDPNGFCFFNNEYHLFYQWYPFGIAHGMKHWAHVKSDDLVNWSSPTLAMTPDTDYDARGVYSGAAYCLKQKNGDQECLLYFTGNLKYENDIRDATQCVATLSKDGVVTKSVQNPLIPTVPAGYSGHVRDPKVFAVGNEYRMLLGAQTEQEKGCVLVYRSDDAMAWELMGELDVRFTNDDDTIGGYMWECPDFFELDGCDVLVFSPQGITPKGDHFHNEFNVVYCLGRADWRTLTFDVEVMQELDRGFDFYAPQTMDNHPTGERILSAWAGCGDPDYPSDREGWSNCLTFPRALTIQDNQLCQRPVDAIQALYAEHQQGEGMGSGIKVLAAGIPNRYRFTLTLDGVKCLTTLSLLATENESLDLIIDADEKRITLDRSNMSSRFAKQWGEQRRASYPVGETLEIDVLIDGSIAEIFIDGGRLAFTARVFPHSPHSKIELNSTSEIHYHFDAYEISPSVNTSPITSEALVPQELHTELTKES | Pathway: Glycan biosynthesis; sucrose metabolism.
Function: Enables the bacterium to metabolize sucrose as a sole carbon source.
Catalytic Activity: Hydrolysis of terminal non-reducing beta-D-fructofuranoside residues in beta-D-fructofuranosides.
EC: 3.2.1.26
Subcellular Location: Cytoplasm
Sequence Length: 525
Sequence Mass (Da): 59129
|
A0A1H7IBL4 | MFGSKDDNKPQASEERKGLFGWGRKKDAAAETSAESAPAAPASAAQPAAKVEQPAARPAEEKAGFFNRLKQGLSKTGATLGEGMASMFLGRRVIDDDLLEEIETRLLTSDVGVEATRVIMENLTWQVERKDLTDADGLFQALQKELAALLKPVEQPLQIAGASPYVILVVGVNGVGKTTTIGKLAKKLQQDGKKVMLAAGDTFRAAAVEQLQVWGERNQIPVIAQHTGADSASVIFDAVQAAKSRGCDVLIADTAGRLHNKDNLMEELKKVKRVMGKLDSSAPHEVLLVLDAGTGQNALNQAKQFNQAVNLTGLALTKLDGTAKGGVIFALAQQMKLPIRYIGVGEGIDDLRPFVADDFVRALFAGVANG | 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). Interaction with SRP-RNC leads to the transfer of the RNC complex to the Sec translocase for insertion into the membrane, the hydrolysis of GTP by both Ffh and FtsY, and the dissociation of the SRP-FtsY complex into the individual components.
Subcellular Location: Cell membrane
Sequence Length: 370
Sequence Mass (Da): 39353
Location Topology: Peripheral membrane protein
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A0A553IGQ7 | MKVNKYQDYQIINKYCLFVLGSPLFFNLRFVVKRVYSIKSKNELDLVFKEKKSVGNGYFVIYFIPHETPHFKYAISIGKKFGNAVERNQAKRRLRYIVSNYSNYINPKYRFVIVVRPQSNLLPYDLIKENITKLLIKAKLIEKEAQN | 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: 147
Sequence Mass (Da): 17481
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A0A259MCN8 | MAGMTTRSEQACFGGTIGFYSHASTEIGVEMRFSVFVPSNASARPLPALYFLAGLTCTEETFMMKANALRYAAELGLVLVAPDTSPRGLGLPGEEDDWDFGTGAGFYLDAEAEPWRQNYRMYSYVTRELPALVEATFPVDAARRGVFGHSMGGHGALVVALKNPQAYRSVSAFAPICNPVAVPWGEKAFGNYLGPDRARWAAWDASELLKQGNRFAGPILVDQGLKDQFLAPQLRPDALEAAAASAGQELILRRHEAYDHSYWFIQTFIEDHLRWHAERLGA | Function: Serine hydrolase involved in the detoxification of formaldehyde.
EC: 3.1.2.12
Catalytic Activity: H2O + S-formylglutathione = formate + glutathione + H(+)
Sequence Length: 282
Sequence Mass (Da): 30984
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A0A956JCU3 | MRVPFARLHPEAELPRRMSAQAAGLDLVACLGDGGRIELAPGGRALIPTGLAVALPPGYEGQVRPRSGLALRHGVTVLNAPGTIDADYRGEIGVLLINLGAEPFGVAHGDRIAQLVVAPVSPAEPVLVEALEAATSERGTGGYGSTGGFGPSGSSPR | Pathway: Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP (dUTP route): step 2/2.
Function: This enzyme is involved in nucleotide metabolism: it produces dUMP, the immediate precursor of thymidine nucleotides and it decreases the intracellular concentration of dUTP so that uracil cannot be incorporated into DNA.
EC: 3.6.1.23
Catalytic Activity: dUTP + H2O = diphosphate + dUMP + H(+)
Sequence Length: 157
Sequence Mass (Da): 15919
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A0A955YWN8 | MTRIAIATLAFAGATAFVGAAAADKLPDEAVAQAGPEAGEHKAGDPSGGHGTGTGQGGGGGRGLGHGTGGGTTQHGDAHGTGEAAGGGGGHGTGTGGGGGANRGEPARDQHGPAGEHDPVHADEHGGHHGPEAINWTDVLDKKKPAFAAVVINLGILLTLYYWLGKKPVADALKQRRVNIGKDIDDAERMLKEAEERAKLHQASLTNIEGDAKTAQAALVAAGEGEVQRMLAEAEERSARMKRDAERLVEQERKQMRQDLLMETIALAADTAEATLKANATAKDHERLAEELLAELTKVPAATTRAGGAA | Function: Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0).
Subcellular Location: Cell membrane
Sequence Length: 310
Sequence Mass (Da): 31636
Location Topology: Single-pass membrane protein
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A0A955U5R0 | MLDWCDGSPLATATWVDWLDIVLLAIVIYRVLVVMRGTRAAQSLIGLAFVGMLYLLSDLIGLVAVHWVLDKLVVYLVLFLLILFQDDIRKALARAGGFLFGGSTRIAARPSDANVMEEVIKAAFSLAHRKIGALMVIERSASLDAYVEGAYAMDAVVSTELLQSIFHPSSPLHDGAVVLAGGRIRAAGVFLPISLSPDVGRWGTRHRAAIGLSEETDGLCVVVSEERGTVALVSRGQVTPIADTNDLRQRLVEKMGEDEPPAANEEVTGARA | Function: Catalyzes the condensation of 2 ATP molecules into cyclic di-AMP (c-di-AMP), a second messenger used to regulate differing processes in different bacteria.
EC: 2.7.7.85
Catalytic Activity: 2 ATP = 3',3'-c-di-AMP + 2 diphosphate
Sequence Length: 272
Sequence Mass (Da): 29261
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A0A956AC32 | MSAGDLADRVHDTLRDSCGVAAGDPLVVGFSGGADSTALALLLSELGHPLRLVLVDHGNRPLGGERRQIETLAGMLGCAFEIRSVVVAEEASWEAAARRSRYAALLEAAEGDRPCAVATGHTADDQAETVLLRILRGSGLRGLRAIHYRREDAVVRPLLDVRRTDLRAYLDRRGVTWCDDPTNEEPRFLRNRLRREVMPALEGFSATAISQLAHLAQAAADELELLERLLAPTLDVDPTAGIDLTTLPSPIGAALVRRLLERHAPHSAVTRRQIEALVRLCSSFDGERELHLPEGITTRRVYDRLYFFDNPDRRNSSSAPQHGASREKTQTLSNSLRDTSSSQEITAISGKWPANHRTTTRHTETQMAIDGPCLVHLPSGALEISIGPPELPLSDRRCVAFSIQNVNFPLFIETAPLDGHFRPFGCPYTRKIKDLLTEAKIPRSDRALATLLSCRGRPLWLIGIRRSSEAPIGDDGPFLVARFTPSDAPIFTDPK | Function: Ligates lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine.
Catalytic Activity: ATP + cytidine(34) in tRNA(Ile2) + L-lysine = AMP + diphosphate + H(+) + lysidine(34) in tRNA(Ile2)
EC: 6.3.4.19
Subcellular Location: Cytoplasm
Sequence Length: 495
Domain: The N-terminal region contains the highly conserved SGGXDS motif, predicted to be a P-loop motif involved in ATP binding.
Sequence Mass (Da): 54338
|
A0A955ZSF3 | MDCTTAFAASLALAPGVLGFALSRITHASARRARALTRAGAGLCLLLTLGLIGATAFAPGGTAGGPLPGASAGAGALFGAPPLVRVDGLTLLMAATVGLIGFVVARFSERYLDGDPRQARFCQWLSFTVSAVLTMVVTGHLLVLVAAWIAAGHGLDALLRHRNERPGALRTARARRYVARIGELCLVAVLVLSQRAFGSLDLAVVLEAAAAGTAPASVEAIAWLLVLAAMTMSVQLPFEGWLPDSMETPTPVSALMHAGLVNAGGFLLLRTSPLLVEAPLALGLLAVVGASTAIYGALVMLVQTDIKRKYAYSTVSQMGFMMLQCGLGAFGAAAMHLVGHSFYKGHAFLSAASQVDPSVPRARAGRASRPGPAAVTGALLAGLAAVAIPVWLLELDPSAKPGLLVLGAILALAVAQVALIGAAPGRPGIEALVESLLLGAGFSLAYFVGLGLFEGALAGVIPTRTIDLPYGLEAGLVALFALVFVAQLALSRWPDHPLVRRAWVHASNGFYLDPLRRRLRERMLALAPSLPPIITRRIAPEGGR | Function: Part of an energy-coupled inorganic carbon pump.
Subcellular Location: Cell membrane
Sequence Length: 544
Sequence Mass (Da): 56204
Location Topology: Multi-pass membrane protein
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A0A956CKY4 | LILVDTKYEFGKTADGTIVVIDEIHTPDSSRYWKLESYESRLAAGQEPDSFDKEYVRRWLADAGYRGDGTPPTIPDDVRIEAARRYIEACDTVRGGAFVPDTTPPDTRIEQNLRRKGFG | Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate: step 1/2.
EC: 6.3.2.6
Catalytic Activity: 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + ATP + L-aspartate = (2S)-2-[5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamido]succinate + ADP + 2 H(+) + phosphate
Sequence Length: 119
Sequence Mass (Da): 13454
|
A0A2D5QM56 | MTSSVLSKQAQASSDLSIQSLNLLTLFPEAVTPYFQFGVTGRAIKRGVIDLHCVNFRDYAEGNYKAVDDLPFGGGAGMVIQAEPVAKALDDLIEKGRNLGTVIMLAPTGRVFTQADAERLSQASTLTFVCGRYEGIDARLNIEYVNEVFSIGDYILSGGELAAMVMIDAIARLKPGVLNNAESATYESHSAQSGSLLEHPHYTRPATWRGHSVPAVLMSGHHARIQAWRREESLKTTARVRPELLENIDLTPEECSMLEQIRRGE | Function: Specifically methylates guanosine-37 in various tRNAs.
Catalytic Activity: guanosine(37) in tRNA + S-adenosyl-L-methionine = H(+) + N(1)-methylguanosine(37) in tRNA + S-adenosyl-L-homocysteine
EC: 2.1.1.228
Subcellular Location: Cytoplasm
Sequence Length: 265
Sequence Mass (Da): 29022
|
A0A935D5P1 | MRVLGLDPGTRHFGWGLAERVGVRLRHVAHGVISPGEALPLGERLVRIEEGLIEVLSAHAPNECAIESLFFARDPSAAAKLGHARGVALLVCARAGLPTGEYPPARVKSTVAGGGRAEKDQVAQMVRLILSLPALPPADAADALAVALTHLQRAPLAARLGPPARPAPRPRRQASLRAK | Cofactor: Binds 2 Mg(2+) ion per subunit.
Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair. Endonuclease that resolves HJ intermediates. Cleaves cruciform DNA by making single-stranded nicks across the HJ at symmetrical positions within the homologous arms, yielding a 5'-phosphate and a 3'-hydroxyl group; requires a central core of homology in the junction. The consensus cleavage sequence is 5'-(A/T)TT(C/G)-3'. Cleavage occurs on the 3'-side of the TT dinucleotide at the point of strand exchange. HJ branch migration catalyzed by RuvA-RuvB allows RuvC to scan DNA until it finds its consensus sequence, where it cleaves and resolves the cruciform DNA.
EC: 3.1.21.10
Catalytic Activity: Endonucleolytic cleavage at a junction such as a reciprocal single-stranded crossover between two homologous DNA duplexes (Holliday junction).
Subcellular Location: Cytoplasm
Sequence Length: 179
Sequence Mass (Da): 18809
|
A0A4Q5XEP5 | MRVSVLASGEGTTLQAILDACAAGEIPARVVLVISNNGGSGALRRAREAGAAAVHLSSKTHPEPGALDQALAATLASYEVDVVMLAGYMKKLEPVVLERYRGRILNTHPALLPKFGGHGMYGMRVHEAVVAAQESESGPSLHLVDAEYDTGRVLAQAKVPVLASDTAETLAARVQERERRLVVDVIGQIARGELRLGD | Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide from N(1)-(5-phospho-D-ribosyl)glycinamide (10-formyl THF route): step 1/1.
Function: Catalyzes the transfer of a formyl group from 10-formyltetrahydrofolate to 5-phospho-ribosyl-glycinamide (GAR), producing 5-phospho-ribosyl-N-formylglycinamide (FGAR) and tetrahydrofolate.
EC: 2.1.2.2
Catalytic Activity: (6S)-10-formyltetrahydrofolate + N(1)-(5-phospho-beta-D-ribosyl)glycinamide = (6S)-5,6,7,8-tetrahydrofolate + H(+) + N(2)-formyl-N(1)-(5-phospho-beta-D-ribosyl)glycinamide
Sequence Length: 198
Sequence Mass (Da): 20894
|
A0A4R6BAS7 | MKKVTKAIIPAAGLGSRFLPATKAMPKEMLPILDTPTIQYIVEEAVAAGIEDIIIVTGKHKRAIEDHFDTQLELELNLKEKNKTALLEKVEHSTNLANIFYVRQKAPRGLGHAVWTAKQFIGDEPFAVLLGDDIVDAEVPGIKQLINVYEQTGKSVIGAKTVTKEETERYGIIESTEQNGRMYKVDKLIEKPKLGTTDSQLAIMGRYVLTPDIFEYLDEQEIGTGGEIQLTDAIQKVNENSEVYAYDFEGNRYDVGDKIGFVKTTMEYAMRSELKDDLVPFLEKLMVKYLK | Pathway: Glycolipid metabolism; diglucosyl-diacylglycerol biosynthesis.
EC: 2.7.7.9
Catalytic Activity: alpha-D-glucose 1-phosphate + H(+) + UTP = diphosphate + UDP-alpha-D-glucose
Sequence Length: 291
Sequence Mass (Da): 32677
|
A0A1Q5T9W2 | MEYKAGKRKTKEADMVQLAAQALCLEEMFDRPVAKGALYYYQSRRRLEVDVTKPLRRLVEETIQNVREMLQNDRLPPPVNDARCRDCSLQDVCMPQVPANVAAWISEENDHD | 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: 112
Sequence Mass (Da): 12981
|
A0A1F2Z0C9 | MKKMLTTLQGIKSDTPPIWLMRQAGRYLPEYLATRTKAGSFLDLCYNPELATEVTLQPIRRFGFDASILFSDILVVPHALGQELSFAENHGPVLGALPENLVFDPSDFHKKLEPVYQAIEGIRAGLQTEGFSETALIGFSGAPWTLACYMIDRKGSKDFAATRIMALKDEEKFNALIELLVSAISSYLIKQIERGAEIVQIFDSWAGVLPPSQFSKWVTQPTQKIVANIRAVYPDTPIIGFPKGAGVLYQNYASLTGLTAIGIDTQMPVNWVRDNLQPSIIVQGNLDPFTLASGSPALLKEADAILSALGDKPFIFNLGHGIDKSTPPEQVKRLVDHIRGYSHDQ | Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 4/4.
Function: Catalyzes the decarboxylation of four acetate groups of uroporphyrinogen-III to yield coproporphyrinogen-III.
Catalytic Activity: 4 H(+) + uroporphyrinogen III = 4 CO2 + coproporphyrinogen III
EC: 4.1.1.37
Subcellular Location: Cytoplasm
Sequence Length: 345
Sequence Mass (Da): 37974
|
A0A935ZF17 | MAHRSFRSVLGVLPVLALAACASHGDGDDPSALEASHAQSLAEATGGTFRVEMSRELANVRHVEGRMAHAALEGATAHEKALSLFKAQPKLLGLASPAHELRVEREEASESGTHVRFQETVAGIPVRGAEVTVHFGRDGELFSMDARIVPGLTIDPTPKLTADEARARATSELLARVPGIASGDVREGAQPELVVFAEPGREARLAWHHVARAMSQETAAVLDVTLDALTGEVLEAFDDLETIKVKGAGVLGDEKEFEATQNGTTFTMVDGTRPAQIRTFTAGTQQTLPGTAVTSQMQNSWDNVQRGKGAAVDAHFYAAFVYDYYKSRFGRNGIDGNNAPMVSTVHFGNAYDNAFWDGTQMAYGDGGTAFRALSAGIDVVAHEFTHGVTTSTSKLVYQGQPGALNEAISDILSTYIEHAYKPDDAKNWVTGENVGLGGPIRDLTNPKAKRQPSNMKEFVNTQQDNGGVHINSGIPNNAAYLMTMGGTNPYSQIKVGGKLGWEKAEKLWYEVETKYFQARTDFAGAATMTVNAATALGYTPADIAVVKCAWIAVGVMQGTCDPAASGSPSPAPSGSSTSPTPSPSPSGSSSTGTPAPGTPQGVAPTPRDGLLSSRNDGCNQSGSGTKDVSAIVGVGLVLGALARRRKTTR | Function: Extracellular zinc metalloprotease.
EC: 3.4.24.-
Subcellular Location: Secreted
Sequence Length: 649
Sequence Mass (Da): 68297
|
A0A2H0DF65 | MKRLGLGAIFSVVVTFFLFVFMAFLIRTTDKGIDRVKTKVLDFTIVQPDDAERTKARKKPKKPEPPKEPPPPQAAAAPSKNKPMQNMVNLDIPKLQLGVGGSGAFLGNVGSNDGMGDGDAIPTLLFNPQYPRQALMDGTEGFVRLKFIVQSDGSPRDVVIVNSNPKRLFDKSALRAIYKWKFRPRKVDGVNVEQSMFYTMVFKMGEE | 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: 207
Sequence Mass (Da): 23022
Location Topology: Single-pass membrane protein
|
A0A956LHN6 | MSPRVFACGPHATPPALVPGGRLVLDRDESHYLRRVRRVRVGATVEVIDGAGALWSATLADDDARACALELGERLPTITPPRVVDLVLCMPESAATLTALTGASEAGAHSITLARSARSSTSPPSAARQLRVLRAAQRQCGRPLPPEVHGPMSLTDAVRAHAVNGQGFFAWAAPAVRAQSERPNVVGPRVWLVVGPEGGLVEEEVNVLREVGATAIGLGPWVLRSETAAIAGIALLLNV | 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: 239
Sequence Mass (Da): 25035
|
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