ids stringlengths 6 10 | seqs stringlengths 16 1.02k | texts stringlengths 117 4.4k |
|---|---|---|
A0A7Y2E1N1 | MDSKVAGRYAKSLLELAVQKSLQDTVFNDMQLVTDTADASRDLSLLMKNPIVNHDKKVAVIKALFENKVNELSMSFMLQVINKGREFYLVDTSKRYISLYKTQKGIEIAHLTTAIAIDDNLRAKIHGLIQQMAPGKSIEVVETVKPDIIGGFVLKVGDRQFDTRVTKKINELKMQFEDNLYLKDY | 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 c... |
A0A943WC09 | MSYFPFFVDIKGWLCVIVGGGKVAYRKVCGLLAFGADLHVIATAFIPEFEHLGNQSGRLRRSCREFQEEDLRGADLVIAASDDEGLNQRISVFCRQAHIPVNSASGKEDSSFLFPALITEGPVTIGISTGGNSPALAHFLKERIQGVLPEEIGETAQELGKLREIFQKQYPDSPALRRSLSGTLAEESLKTGKIPDECALIEAQNLMNKKTDKRTNTT | 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: 218
Sequence Mass (Da): 23869
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A0A970EVZ3 | MILKELIGPDDDGKKITTILRHKMGLSGRMVSRLKTVEGICVNGIPVFTNYICREGDLVTANVALAEAPQEVPAEYGDLTVLYEDDFLLAVYKPEGMITHPSRTQFTDTLMGYVLGYLSQSGSTTCHALNRLDRYTSGIVLFAKSSYAKALFSQSLKKARKTYMAIVYGKVVAGCGTINLPIVRLQKENIQRGISADGAKAITNFQVLDTVRYEDCNLSILKLEPETGRTHQLRVHCMSLGHPIIGDQIYHNDKSKEISERLNIHGQLLHAGRLMFHHPVYNKDIDIHCPVMRDNMKPMLDLCDC | Function: Responsible for synthesis of pseudouridine from uracil.
EC: 5.4.99.-
Catalytic Activity: a uridine in RNA = a pseudouridine in RNA
Sequence Length: 305
Sequence Mass (Da): 34086
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A0A927RNQ5 | MRLQPIHIGHITTENNVFLAPLAGYTNYPFRRLAKGYGAGLCYTEMVSAKGLKYGNENTENLLYTDENEGLAAAQIFGSDPSVMRAACENAALAQFPIVDINMGCPVPKIYKNGEGSALLENPLLAEKIVRECVKSGKIITVKYRIGVDKEHIITAEFAKRMEGAGASLITVHGRTKDKVYAGEVNYQEIAAAKRAVKIPVIANGGVFSKEDAEKLLEETGTDGVMVARAALFHPQIFCEITGGKTESKRAMFERQLAWTAERFDERFTTVFMRKMAAFYVKGERGASAYKERLFAAKNAEEIATIVKEMWD | Function: Catalyzes the synthesis of 5,6-dihydrouridine (D), a modified base found in the D-loop of most tRNAs, via the reduction of the C5-C6 double bond in target uridines.
EC: 1.3.1.-
Catalytic Activity: a 5,6-dihydrouridine in tRNA + NAD(+) = a uridine in tRNA + H(+) + NADH
Sequence Length: 312
Sequence Mass (Da): ... |
A0A356M2J8 | MIYETIIIGGGPAGMAAAIYAARSGLNAVLLERSSSLGGQLIVADWIDNYPGYPEGINGADLMNNFALQVERFQVPVHYEGVEKLELNGLIKKVQTSQGTYESRTVVLATGAEHRTLNIPGEARLTGAGVSYCAVCDGMFFRKKKVVVIGGGDTALKGAEYLTRFAREVVLVHRRDLFRGAKVLDDKVRKNERVRLLLNTIPLAIEGEQTVEGILLRNKISGEEHREPCDGVFLFVGTAPNSELITQEILDENGYVVTDENMATVIPGVFACGDLRRKALRQVSTAAGEGAAAADSAFSYLASLIQ | Cofactor: Binds 1 FAD per subunit.
EC: 1.8.1.9
Catalytic Activity: [thioredoxin]-dithiol + NADP(+) = [thioredoxin]-disulfide + H(+) + NADPH
Sequence Length: 306
Sequence Mass (Da): 33033
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A0A943II99 | MEYTEKLTQLDSRLTAVGITFYREEPMSRHTTLRIGGPAERLVCPDSERQLLTAAKLCRELELPVLLIGRGSNLLVSDQGLRGVVLCPRAETGEITCTGEGRFRLPAGLTLARAANFAAEQGYAGLEFAHGIPGTVGGAIYMNAGAYGGEMKDIITRVEVLDSDGTVRWLPADECGFSYRQSRFSQSGEWVLSAEVQLTPGCSREIYAVMERLGTARREKQPLEYPSAGSAFKRPPEGTPPAAALIDRCGLKGLQVGGAQVSEKHAGFIINRGGATASDVAELMRQVQKTVQEREGVLLEPEIRLLGSFEEGM | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Cell wall formation.
Catalytic Activity: NADP(+) + UDP-N-acetyl-alpha-D-muramate = H(+) + NADPH + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine
EC: 1.3.1.98
Subcellular Location: Cytoplasm
Sequence Length: 313
Sequence Mass (Da): 33876
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A0A943C9Q9 | MYYELYIDLFFLENIIMDYLLLFTVKRLLRKKIKKRKLLLSSFIGSALLCVILLTPFPKTKIWMIFGNMAGGALMLKISSAEGEKVEWGRELILFYLVTFCAGGIFQMIETIFSASFLKIFLPGALLLQGIFYSFREIRQQTAQEYEVTLYWHGKEMRCRGLLDTGNRLKNPWNHRPVMVVYYEAVRTLFSCQEQRQLEQMFQLLAPEKATERFFYIPYHSIGKEGGLLPCVILDEMIIKGYKRNFRIQKPSAALCRMPVSKCGSYEVILQPLFTESENEIKK | Function: Probable aspartic protease that is responsible for the proteolytic cleavage of the RNA polymerase sigma E factor (SigE/spoIIGB) to yield the active peptide in the mother cell during sporulation. Responds to a signal from the forespore that is triggered by the extracellular signal protein SpoIIR.
EC: 3.4.23.-
... |
A0A927NRJ5 | MRRKNRKKFVETIDEKVRLWYNEFMIGKRIIAFDIGDKRIGVAISDPFNEYAMPCETYFRTKSFFADVENIAKIAKDKGAGTIVCGMPVNFDGSESVQTVKTRDFIEVLKQKTDLPIELEDERFTTMQAREVQIQGGVKRGDRKKSIDSIAASYILDGYLSRMKKRAVAKEWAETHSDSAEDILD | Function: Could be a nuclease involved in processing of the 5'-end of pre-16S rRNA.
EC: 3.1.-.-
Subcellular Location: Cytoplasm
Sequence Length: 185
Sequence Mass (Da): 21218
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A0A1W2CTX9 | MAYLVLANGTIFEGKRIGAPVDRIGELVFTTGMEGYLETLTDPSYYGQIVTQTFPMIGNYGVIEEDFEGNSTLFGYIVRELCDTPSNFRSAYPLNDYLVAKGIPGLCGVDTREIVRITREEGVMNAMICDEVPADLSAIRSFTVKDAVASVSSNIKEFFPAEGVEKCRVALIDYGAKHNIIRSLEKRGCSVTVWPSSTTAETILESDPDGIMLSNGPGDPKENKECIAQLKKLIGKLPVFGICLGHQLTALALGGDTIKLKYGHRGGNQPVKDLAAGRTYITSQNHGYAVVADSLKGIGTESFRNANDGSCEGMDYPDLK... | Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl phosphate from bicarbonate: step 1/1.
EC: 6.3.5.5
Catalytic Activity: 2 ATP + H2O + hydrogencarbonate + L-glutamine = 2 ADP + carbamoyl phosphate + 2 H(+) + L-glutamate + phosphate
Sequence Length: 353
Sequence Mass (Da): 38252
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A0A0H4NYK8 | MRINKKKQKWIYFWVVVVPSILTIMLFYRILLDNERDNYRQHIEWIASIHQNQIDQFIGETITGLNILAYSLDPMLNDLDSVKMILKKTQNQDPRYGGMYILDLKGNVVTGTNDLLKHYNFRYMDYFREVLLTKHTVVSDHQEKIDNQHVIAAASPILSNNKVIAVLVAHIQVDYIRNIMKQLTPDQAISFENSKGKTIFTVNKPPKNNDTENKIRYPLEQLPWNIVLTADNRYYRDVIRSTILFAIIPFIFFHILFLVFKYFMLKRQTKLERVQIEAQKLELIGTLAAGIAHEIRNPLTGIKGLVQLLSEKYQDQTDRF... | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Membrane
Sequence Length: 504
Sequence Mass (Da): 58139
Location Topology: Multi-pass membrane protein
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A0A9E1AVE0 | METARQTALNLLIKAEKGQAYSNLALNAALSQSQLSAQDRSLVTALFYGVLERKITLDYVIQQYSNLKLNKISFDILSVLRMGVYQLAFMDAIPDSAAVNESVMLAEYCRKKSAKGFVNAVLRSFVRDHNQIAYPDSSNLSFCYSVRYSCPEWLVEKWISEYGAEQTEQILAHSLGRPPVTVRVNTLKVTSEVLLQRLRDEKVTARLHPTVQNCITIEKSGDIEGLPSYQQGLFYVQDIASQLCCLALAPQKGERILDLCAAPGGKSFTTALLMENSGTIESFDLYPKRTHLIETGAKRLGISNMKVRTANANQFLPELV... | Function: Specifically methylates the cytosine at position 967 (m5C967) of 16S rRNA.
Catalytic Activity: cytidine(967) in 16S rRNA + S-adenosyl-L-methionine = 5-methylcytidine(967) in 16S rRNA + H(+) + S-adenosyl-L-homocysteine
EC: 2.1.1.176
Subcellular Location: Cytoplasm
Sequence Length: 442
Sequence Mass (Da): 49496... |
A0A970EZG0 | MLSTPTNNSKARKASGKKLRSTGPFLTIVKWFFKVFGTLLLIGMTTGAMLGCIFAIYINRYISTSIDIDPGDFQLDLTSFVYYLDKKTGEYKVLEELYARENRVWVSYEDIPDHLVDALIAIEDKRFWQHHGVDWYRTVSAFFNMFLGMKDNFGGSTITQQLIKNLTEEDEVTVRRKISEIFRALELEKEYSKEDILEWYLNLVYFSQGCNGVQSAAQTYFGKDVSELTLAESAAIVGITNLPTKYDPYINRENNKARQEVILREMYKQGLISEDEMNKAIKEKLVFRRDARQVSSEETRSKYQSYFVDQVIEDVLTDLM... | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Cell wall formation. Synthesis of cross-linked peptidoglycan from the lipid intermediates. The enzyme has a penicillin-insensitive transglycosylase N-terminal domain (formation of linear glycan strands) and a penicillin-sensitive transpeptidase C-term... |
A0A927NLL6 | MNEKITAISTPIGRGAISIVRMSGDGVIDVARQMFAKMPDQPGLLQLGKLDAGEFCDQAMCVYFKAPRSYTGEDMVEFQLHGGYAIANGVLKACIQKGCRLAENGEFTKRAYLNGKINLSNVEGIMDMIDAENIAAVENGYKMLSGKLDGKINLLQDKLTDLLAQIEVALDYPEEDLEFITKDQVQDVLRFAIDETQKLLDSAAKGRIIKNGVDIAIVGKTNVGKSSLLNALVGFDRAIVTNIEGTTRDTLSESYIYKDVKFNFIDTAGLRQTDDVVESIGIERSLQAVEKADIVLLVFDGGEIPQEYIEIKTNPKTICV... | Cofactor: Binds 1 potassium ion per subunit.
Function: Exhibits a very high intrinsic GTPase hydrolysis rate. Involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34.
EC: 3.6.-.-
Subcellular Location: Cytoplasm
Sequence Length: 433
S... |
A0A1Q7WXV1 | MARRRHLLTAAALGLFVLAADQATKVWAQQTLRPGQQLTAIAGWLWFRLASNSGATFGVLQGHNVLFLAVSALLLLAVVVVLMRGVASSMLAAAALGAVAGGTTGNLLDRIRLGSVIDFIEVHSWPTTFNLADAAIRIGVVVYVVALLVGLRRRL | 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-, ... |
A0A970K4C3 | MTQGEILTICREAVLTALTIAAPFLIASLIIGIVISVFQAATQIHEQTITFVPKILSAALILLFIGAWIINVIVGFTENVFTMINNLS | Function: Role in flagellar biosynthesis.
Subcellular Location: Cell membrane
Sequence Length: 88
Sequence Mass (Da): 9500
Location Topology: Multi-pass membrane protein
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A0A9D7ZAR3 | MGKINLCIDIGNTSTKAGVFIDGQMTEYIKPFTHQHFSDIYDENVQVLVSKTGLNLELERLLSNEHYLSHDSPIPLELVYDTPETLGPDRIAAAVGAYYMDANSSWLIIDIGTCITLDLLNKNRFLGGMISAGSAIRLRAIREY | Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 1/5.
EC: 2.7.1.33
Catalytic Activity: (R)-pantothenate + ATP = (R)-4'-phosphopantothenate + ADP + H(+)
Sequence Length: 144
Sequence Mass (Da): 16023
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A0A7L5BW37 | MRDTERAAAAPRGMYALRAARAASLTIGFALAVQSLYTAYFGVWEPWFHRSLVTLFSVAAVTLSVPLAARVRTQSRLTPALCWLVDALMIVIFTLAVEQLFAAYEHVDDIMLSYSPYQIAISVLAVGCLLELSRRLFGLPLLLFCLAVFLYCIFGNSLPWVFHHSGFTLSQTMETLWFGLQGVFGSPLGVVVQIIFVFIVFGVVLERTGAGEALIRLAFHFTARSRGGPAQAAIVASALFGTMSGSVAANVVGTGSFTIPIIKRRGFAPHVAGGVEAAASTGGQFVPPVMGAAAFVMADITGIPYLQICLAALIPAILYY... | Function: Part of the tripartite ATP-independent periplasmic (TRAP) transport system.
Subcellular Location: Cell inner membrane
Sequence Length: 656
Sequence Mass (Da): 68962
Location Topology: Multi-pass membrane protein
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A0A7T7AMP9 | MKDNFKKRKNLLNFIRRNREKPQLENKEDDNFNDHLFYKCPNCEKSILKDNLPETNWICSSCGFYLPLNSKERLDLVMDMGYEEIQGQVNYSNPLDFPNYVEKLENNRKKSGQDEAIRVALGKIKGSSCVVAVLDSSFLMGSMGTYVGEEVTKAFEKAMDLNLPVIIFSASGGARMQEGILSLMQMAKTSNAVRQHSEKGLLYISCLTNPTTGGVTASFASLGDIIIAEPNALIGFAGPRVIKQTIKQDLPEGFQSSEFLMEHGFIDTIVERENLKEVLSIILKIHGVED | Cofactor: Binds 1 zinc ion per subunit.
Pathway: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1.
Function: Component of the acetyl coenzyme A carboxylase (ACC) complex. Biotin carboxylase (BC) catalyzes the carboxylation of biotin on its carrier protein (BCCP) and then the CO(2) group... |
A0A927NNZ1 | MTANVRAWQETDISKIAQVERVCFSDPWSEKDLLSCLSLPIYKTYLIEENSKIVAYACQSVIFEDSEVLNIAVAPNHRGRGYGRKLMQEMLNTAVALKACNVFLEVRVSNETAKSLYRSFGFEEYGLRKNYYPDGENALLMKKTF | Function: Acetylates the N-terminal alanine of ribosomal protein bS18.
Catalytic Activity: acetyl-CoA + N-terminal L-alanyl-[ribosomal protein bS18] = CoA + H(+) + N-terminal N(alpha)-acetyl-L-alanyl-[ribosomal protein bS18]
EC: 2.3.1.266
Subcellular Location: Cytoplasm
Sequence Length: 145
Sequence Mass (Da): 16593
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A0A316RMZ6 | MYEELIKSARSASGNSYSPYSSFPVGAALLCADGSVFCGCNVENSSYSATVCAERTALVSAVAAGKRDFSAIAIYTPRVCSGFVPCAVCLQALSEFCAGSLEIVCVDGSGGVARHTLAELLPFAFRLGCGEDK | Function: This enzyme scavenges exogenous and endogenous cytidine and 2'-deoxycytidine for UMP synthesis.
EC: 3.5.4.5
Catalytic Activity: 2'-deoxycytidine + H(+) + H2O = 2'-deoxyuridine + NH4(+)
Sequence Length: 133
Sequence Mass (Da): 13742
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A0A2H0SL08 | MAWELLLNILPILLMVVFFLFLFRQARSGAGDMMGFGRSKAKMFIKGKQDVKFADVGGMDEAKQELEEIVDFLKNPKKYTKVGARTPKGVLLVGPSGTGKTLLARAVAGEANVQFLSIAGSEFMEMLVGVGASRARDLFQTAKKLAPSIIFIDEVDAIGRMRGQGSMGGHDEREQTLNQILVEMDGFTQNDNVVVMAATNRGDMLDPALVRPGRFDRRVMVNLPDLEERKFILKIHAKGKPFTDEVNWDRVAKRTVGFSGADLENMLNEAAIGVARENRSQVTMEDIEEASLKVKLGPSKKRLRDDYERKMTAYHEAGHA... | Cofactor: Binds 1 zinc ion per subunit.
Function: Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins.
EC: 3.4.24.-
Subcellular Location: Cell membrane
Sequence Length: 502
Sequence Mass (Da): 55323
Locat... |
A0A970PSS2 | MSIAITPFGKNNEGRQVAKITLTNAKGSSASFINYGAHIVSIIVPDKEGIFADVCLGYDSVEDYGRPRNGHIGSTVGRYANRIGGAKFELNGIEYHLPANDGKNCLHGGMDGFRRKLWSYDVKEASECDSVTMTYVSPDGEEGFPGTLTTTVTFTFDDNNRLGIRYEAVSDADTVINFTNHAYFNLAGEGDTLAHLLKIEADEITEVDEELIPTGWFAQIKETPYDLRSFKSHRDCLKERRNHPAFDRADGFDVNYVINGEGFRLAATVREPNSRREMTVETDQPGIQLYSGQGLKATGKGGAAYGPYAGIALETQHHPD... | Pathway: Carbohydrate metabolism; hexose metabolism.
EC: 5.1.3.3
Catalytic Activity: alpha-D-glucose = beta-D-glucose
Sequence Length: 322
Sequence Mass (Da): 35347
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A0A943WJ45 | MSSINSLKKNRDFQRVYSKRQSFANRSLVMYKMSNDRADTRIGISVSKKVGNSVVRHRVTRVIRECCRLHEKELIQGLDIVIVARPLAKEQGLMEIEEAFFHVGRKLNIFLESK | 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... |
A0A0K0DY23 | MAEIGPSSIITRARISPYPAISIEDALNIINNEINEIMDCKEVHFESVDVGRILAENIVAQYDHPSERLSTKDGYAVLANDGIGERKVVSYITAGLDGGGGYLKRGECYRVSTGSMLPEGADAVVQVENTTILQHDNVEEKIISINVEPLVNQDIRPIGCDFRKGEVLVQSNTRIGPAEKGMIVQSGMTSVRIYRKPKVCVMSTGNELIDPLFDGQIPKGKIRDSNRPQLLSLFNSYGFHAIDVGIAPDDREALTKKIGEAFEFSNVIVTSGGVSMGEKDLLKSVLKEDFNFDIGFGRVFMKPGLPTTFATGKYRSQDKR... | Pathway: Cofactor biosynthesis; molybdopterin biosynthesis.
Function: Catalyzes two steps in the biosynthesis of the molybdenum cofactor. In the first step, molybdopterin is adenylated. Subsequently, molybdate is inserted into adenylated molybdopterin and AMP is released.
Catalytic Activity: ATP + H(+) + molybdopterin ... |
A0A971WDU3 | MQKNKGVVIDASVRGATINASDNKKPSRPRRTGPSKAKAVGSTQKETVKIAFLGGLNEVGKNMTLYEYGGEMIVVDCGMGFPDQDMLGVDIVLPDFSYAEQNADKIKGIVVTHAHEDHIGGLPYLLRLMNVPIYGTRLTIGMIQRKLKEHGLLRNAKLNVVSPGDKIDLGRFNVECIHVNHSIPDALAFAIRCKAGTIIQTGDFKIDSTPIDGDMMDLTRVSQIGKEKVLCLLSDSTNAERPGYAVSEKKVGEAFETLFQKAEGKRIIVATFASNIHRVQQIMDVAHRLRKKVVVSGRSLENVVGVAQELGYLNIPEGLL... | Function: An RNase that has 5'-3' exonuclease and possibly endonuclease activity. Involved in maturation of rRNA and in some organisms also mRNA maturation and/or decay.
EC: 3.1.-.-
Subcellular Location: Cytoplasm
Sequence Length: 597
Sequence Mass (Da): 65537
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A0A9E2AI48 | MARKRKFSKGIKVDSRKLQSIIFNTMKRNPKQRYHAKQLIKKLKIKNSPDSVNHALIQLANEGRINFLPNGKYKFRKGSTFKEVGLHLKGIVDMTMSGAAFVICEDSVEDIYVPRAHVNGALNNDEVEVSLLYRKTGRRPEGKIINILKRSRDTFIGDLYRKGKKAYVIPTNPTIPMRINISAKDLNDAEDGMIVVTKITHWPNASYPDAQGKILTTLGELGDNDSEMKSILVENGFDWEFPEKVLRQANQIPSEITDGDIAERRDMRDIFTITIDPVDAKDFDDALSIAYLPQGDIEVGIHIADVTHYVKPNTVLDKEA... | Function: 3'-5' exoribonuclease that releases 5'-nucleoside monophosphates and is involved in maturation of structured RNAs.
Catalytic Activity: Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleoside 5'-phosphates.
EC: 3.1.13.1
Subcellular Location: Cytoplasm
Sequence Length: 716
Sequence Mass (Da): 812... |
A0A927Y1C2 | MAFRLIDLDNWERKEYYEHFISQVVCTYSVVVNVDITCLKGQKLYPAMIWLLTKTVNDMPEFRTCLTGEGVGIYDDMHPMYTVFNKENKNFSGIWSYFDEDYDTFLRSYEEDAEKYSKSTRYAPKDGTPSNSFNISMVPWVEFTGFNINVFDDGKFLLPIFTMGKFFERDGKRLLPLAIQVHHAVCDGYHVGAFVQRLQEYIDKF | Function: This enzyme is an effector of chloramphenicol resistance in bacteria.
EC: 2.3.1.28
Catalytic Activity: acetyl-CoA + chloramphenicol = chloramphenicol 3-acetate + CoA
Sequence Length: 205
Sequence Mass (Da): 24078
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A0A943XSK7 | MQKLIVILGPTASGKTDLAIQVAKALDGEVVSADSMQIYREMHIGTARPLPQEQEGIAHHLLGFVEPDAAYSVACYQRDALQVIDEILSRGKQPILAGGTGLYLNSILYDLDFTQTEPNQALRNKLEEQYQENPALLHAKLAQLDPIAAQRIHPNDKKRLIRRLEILEDAGGKQPYEFRKPQSRYQIQQIGITKPRETLYRDIERRVDAMFAQGLEAEVREIFRKYGADISAFSAIGYKEFLPYFAGKATLEETAQLIKQNTRRFAKRQLTWFRREQQVRWFSTEDFAGKEALVSAVISHIIKGAHDE | Function: Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A).
EC: 2.5.1.75
Catalytic Activity: adenosine(37) in tRNA + dimethylallyl diphosphate = diphosphate + N(6)-dimethylall... |
A0A3D4S7S8 | MRKLFLDKIDGDTITLSGDDHKHIAYSLRMRKGDEITVCADGVDYTAIIREMTKTSTIAEITGKARSVSEPSIELTLFFGALKGDKNDYVVQKCTELGVKEFVPFISDFCAVTSESVKIERLSRIALEAAKQSGRGFVPTVSSPVKFNDLSDLLRGYDTVVFPYEQENELPIDDYLKKSARGKTAVVIGSEGGFSRKEADVLRKIAGGSVTLGERILRADTACVAVVSVVMYAFGEWRRNK | 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
S... |
A0A2G6PKL6 | MAFDYAGVPTILLGSQSPRRLALLEGMGLRCEVLRGDFDERAASDSHPTGGMHLAEFLALGKLRAIALRAGCRAGGGILLTADTVVMLDGERLDKPQDEAQALERLMRLSGREHEVVTGLALSYRGRITSLSETTHVQFAPFDERYARAYIASGSPYDKAGGYGIQDWFGLGAVVAIRGSYTNVMGLPTHRVHHYLMANFT | Function: Nucleoside triphosphate pyrophosphatase that hydrolyzes dTTP and UTP. May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids.
Catalytic Activity: H2O + UTP = diphosphate + H(+) + UMP
EC: 3.6.1.9
Subcellular Location: Cytoplasm
Seque... |
A0A7C6R5W7 | MPYTIALVGNPNSGKTSLFNAITGTAQHVGNWPGVTVEKKEGIFYYDNNEIILVDLPGIYSLSPYTPEEIISRNYIIESTPDLIINIVDATNLERNLYLTTQLAELGRPMVIALNMVDMLKSKGIEIDIKALQKLLGIAVCPVSASKGRGIEELVETCIALIKESKNKKKAATIKANAPKSSRIMLEPQKSTFGVFDWKIKSAISAIEDVISNIDYAKKAPLFMAVKLFEGDTHSVRKLNLNAQQQRLINSILQSVPETEYVDRQMMVADQRYKYISNICKIAVKKHKTDEYTMSDKIDRVLTHKFLSIPIFFAIMLLIF... | Function: Probable transporter of a GTP-driven Fe(2+) uptake system.
Subcellular Location: Cell membrane
Sequence Length: 693
Sequence Mass (Da): 77047
Location Topology: Multi-pass membrane protein
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A0A8K1J1U3 | MANNSARYVPFARKYRPKNFKELLGQEVLTKTLSYCINNKKLTGALLLTGIRGVGKTSSARIIAKTVNCTSLLNDDLNNAFPCESCKNCESFNNNNHPDIIEIDAASRTGVDDVREIIESSEYRPLLGEYKIFVIDEVHMLSKNAFNALLKLIEEPPPHVIFIFATTEVQKIPLTVLSRCQRYDLRRLSIEEILVLLKNIAQNENLKLEEEALKIIALKSEGSARDATGILDQASSYIHNVSQQNDIITAESVNKMLGLVQISTILELIRLIIEGNTKEALKLLEEIYMNSSNLEHFVEQIADLIASLTKEKVIAGFHEP... | 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: 518
Seq... |
A0A2V2DM90 | MERSVTVTELNDYLKAVMDGDGNLKMLCVEGEISGFVAHSSGHYYFTLKDGASAVKAVMFKGYSRFCEFAPKNGMSVMAIGDVSVYPRDGVYQLYVKRMLQAGVGEVFLAYEELKRRLEKEGLFAPEMKKALPHFPERIAVVTSPTGAALQDIRNVLKRRYPLAEIALYPVLVQGERAAEDIVEKLAQMDRESGADVAILARGGGSVEDLFVFNDERIARAVFACSTPLISAVGHETDFTLVDFVSDKRAPTPSAAAEIAVPDIMELLQQLSSYEDRMFSALASQTNYYVSAADGAAERMARTFLSVLDKNRTRCSEADM... | 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... |
A0A2G6PHL2 | MALYRSVIRPLLFRIDPERIHHLLMGALRVGLSLPLLPKLLRWRLYYRAEALASTHSGIFFPNRVGLAAGFDKGAELVDRLRSLGFGFAEVGTVTPWPQPGNPRPRIFRLPEDGAVINRMGFNSVGLAAVVHRLARRRPYRIPIAGNIGKNTDTPNGRAVEDYVTCMRELYPLVDFFVVNVSCPNVEHLSDLQSCEGVTPIVAALLRQREEMRYHKPIYLKLGPDEPEESLVAVARATLRMGIDGFVLTNTTRSREGLRSPGARVEAAGMGGLSGAPLRLRARERVRILREAVGKDVPIIGVGGVFTGPDALEMLKAGAS... | Cofactor: Binds 1 FMN per subunit.
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; orotate from (S)-dihydroorotate (quinone route): step 1/1.
Function: Catalyzes the conversion of dihydroorotate to orotate with quinone as electron acceptor.
EC: 1.3.5.2
Subcellular Location: Cell membrane
Catalytic... |
A0A2V2DUI9 | MQMNKIGIIVNPLKDPGLLYLNEVARRLEKADFTYAVSCCDYESKEKYPFCSAEECFMGARLVLTLGGDGTLLRAAPYAARYRVPLLGINLGHLGFLAEMERNEIDQLAAILSSGYQYSERMMLNVQILRNNCCCGEAIALNDAVIRSRIGKPAHIVVADDESDLIDYFCDGFIVATPTGSTAYSMSAGGPILEPRSRAIVVTPICPHTLGSRSLVFGETLQQIYMKVTNADLIQAHLECDGAEIGVLHNGDLVCVSRHDTPLQLVRLHNKSFFKVLNEKISRRMS | Function: Involved in the regulation of the intracellular balance of NAD and NADP, and is a key enzyme in the biosynthesis of NADP. Catalyzes specifically the phosphorylation on 2'-hydroxyl of the adenosine moiety of NAD to yield NADP.
Catalytic Activity: ATP + NAD(+) = ADP + H(+) + NADP(+)
EC: 2.7.1.23
Subcellular Loc... |
A0A2G6PIN5 | MERDGRALHGAEGDYRLVVDAGNSSTKLGIYAGRRQVLTTRCTEGLADRVERLLAEYPVARAIISSVAQREEELRALLGASIPVHVLSHRSTLPFRVGYSTPETLGRDRLAAMAGAAFEFEACPLLVVDLGTAITYDFLDAAGVYHGGAISPGIGLRLASLHEHTARLPLVERGEDSPLVGGSTADCLRSGAVWGVVAEVEFYHRKLAEQHGELKLILCGGDADFLHRRLFYCNFVRPNLVLDGLNRLTECNA | Cofactor: A monovalent cation. Ammonium or potassium.
Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 1/5.
Function: Catalyzes the phosphorylation of pantothenate (Pan), the first step in CoA biosynthesis.
EC: 2.7.1.33
Subcellular Location: Cytoplasm
Catalytic Activity: (R)-pant... |
A0A3D4S676 | MDVLSTLKKEGFVFSKKYGQNFITDERLLGSIVDDAGITSADTVVEIGAGAGTLTAAIAKKAKRVIAFEIDRSLEPVLGATLKGYDNVEVIFDDVTKWQEAEFDALTDGKYKVVANLPYYITTPLLFMLLDRKKPPVSLTVMVQKEVAERICATEKKGDYGALSVSVGVRADAVITKVVGREMFTPPPNVDSAVVRVDMRGETGALDDKTLFSLIRVAFAMKRKTLVNNLSAGYGMSKDEACRLLTSVGVDVRARAEELSCRKFVELADALYLSRSQR | Function: Specifically dimethylates two adjacent adenosines (A1518 and A1519) in the loop of a conserved hairpin near the 3'-end of 16S rRNA in the 30S particle. May play a critical role in biogenesis of 30S subunits.
Catalytic Activity: adenosine(1518)/adenosine(1519) in 16S rRNA + 4 S-adenosyl-L-methionine = 4 H(+) +... |
A0A927XZK0 | MDLNKKKRLILAAAVLFAAIAVGVAVVVALTGSGANEGGQPMIGPSGQPVATDYVAIEVEGYGTITAELYGDMAPITVKNFLKLVDEKFYDGLTFHRIISGFMIQGGCPLGTGMGGTEPIKGEFAQNGVANPLKHERGVLSMARTAVDMNSASSQFFIMQQAAPSLDGGYAGFGKVIDGIEIVDALSRFSVIGDRNGILAAENQPVITSIRRIEKP | 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: 216
Sequence Mass (Da): 22648
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A0A8T3TXY4 | KMIAVIVYIIIGIALLVLSLVQSKQENGASAAIMGGTRDSFYEKNKNRTQEARMDNAIVALFAVFVILSLALYFI | Function: Involved in protein export. Participates in an early event of protein translocation.
Subcellular Location: Cell membrane
Sequence Length: 75
Sequence Mass (Da): 8237
Location Topology: Multi-pass membrane protein
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A0A3D2CKL6 | MTVTLLYSPFEKGNKEAAEAAAKLLFEAGAQVQCLKGMLDLPFLKQIAGKEIYRADAALVLGGDGFIMHNAKNCAHRNTPVRGINRGHLGYLADGEEFTAEEAERLVARSFYTEERMMLQVQRNDEISAALNDVVLMREGIAGVVEIEVLSDGESVGIYRCDGVLVATPTGSTAYSLSAGGSVVDPALSCLCFTPVCPHSLSAKPIIFAPEKKLTLRNISRRERRLSYSCDGEKPGVLLYGEELTVTAGREKVRFIRMNQSSFCATLHKKLSEIG | Function: Involved in the regulation of the intracellular balance of NAD and NADP, and is a key enzyme in the biosynthesis of NADP. Catalyzes specifically the phosphorylation on 2'-hydroxyl of the adenosine moiety of NAD to yield NADP.
Catalytic Activity: ATP + NAD(+) = ADP + H(+) + NADP(+)
EC: 2.7.1.23
Subcellular Loc... |
A0A928RN60 | MTINFEGVGHRYKKVIKDVYNKALEITGNNVDGLEATISFVDSATIRSYNKEYRQVDKETDVLSFPMLNINYSQKVSDFVEETLPNGALYLGDIVICKKVAKRQAKEYCHSLKREISFLALHGLLHLLGYDHIEKEDEVVMMEKSDEVLSSLGIKREKNV | Cofactor: Binds 1 zinc ion.
Function: Single strand-specific metallo-endoribonuclease involved in late-stage 70S ribosome quality control and in maturation of the 3' terminus of the 16S rRNA.
EC: 3.1.-.-
Subcellular Location: Cytoplasm
Sequence Length: 160
Sequence Mass (Da): 18275
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A0A927RKZ4 | MKNIEEIINYKFNNIELLNTATYHSSFAHKYSLKNNERLEFLGDSVLGLIVTEYLINEYSLKEGELSKLRAKIVSCENLSKNITENKLDEFIKVSPESLIKSEAIKGDFFEALLGALYLDGGVSICKSFVYKFLIKNKDNIDNLMNETLDYKTKLQELVQAKKGKVNYYTTDEIGLDNDKTFEVKLYINDKFATKAKGKTKQKAENLCAKIACENLSKFI | Function: Digests double-stranded RNA. Involved in the processing of primary rRNA transcript to yield the immediate precursors to the large and small rRNAs (23S and 16S). Processes some mRNAs, and tRNAs when they are encoded in the rRNA operon. Processes pre-crRNA and tracrRNA of type II CRISPR loci if present in the o... |
A0A947Z961 | MNTFGTLYVVATPIGNLGDMTQRAREILATVDVVVAEDTRLTGGLLQKLGIAPRSMEALYKDRERERTEQVLGQLLEGRKVALCSDAGTPGISDPGALLVGRAMEEGVLVVPIPGVSALTALFSVSGFSGTHFWFEGFLPRKGKDRALRLSWLQRLTEPYILYEAPHRIVETLEDLNALDPEGVITVGRELTKLHEEIFHGTIGEALAHFSQGETRGEFVLAVKGTPVEDQLTHLPAMEDEVARLLAIGLSTRDTAAVLAPLYRVPKKQVYELAMGLKQN | 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: 280
Sequence Mas... |
A0A2H0WD10 | MSAQVLQGISVSPGFALAPAVCWHPVAVEIRAEKNTDASKEWSYFQSCLPRVQQQLQDLIKKTAQELSDEEAQIFESQYLFTEDPEILSDLETEIRQNSWKSIWAVEIVFEKYAQMMAAMSDSYLRERALDLRDLKSRLQVALSLGPQALQQDAQALNEKCILIAQDLTPSDFASMDKKKVQGLVLEANQRTSHTVILAKTYGIPTLVGVVQVFEKIKNKDLLALNATRGTLYLNPSDQTKNEIQSLMERDQVEKKELQKYKDQPILNREKEIVHLEANITSVHDLPLAAAQGAEGVGLFRTEFLFLERATAPSEDEQFE... | Function: General (non sugar-specific) component of the phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS). This major carbohydrate active-transport system catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. Enzyme I transfer... |
A0A947Z8D7 | MRFGKTAVICAASISGSVPDWMRGKGRGWVTAEYAMLPGSASGRIGRKVQGRSTEIQRLIGRALRAAVDLEALGERLITVDCDVLQADGGTRTASITGGYLALALAVQKLKLNGELTGDPLRTPVASVSCGIYQDTAILDLNYEEDFGAAVDMNFVMDGEGKLVEVQGTAEERTFTVEELGEMLSLAKKGIGELLALQQKILG | Function: Phosphorolytic 3'-5' exoribonuclease that plays an important role in tRNA 3'-end maturation. Removes nucleotide residues following the 3'-CCA terminus of tRNAs; can also add nucleotides to the ends of RNA molecules by using nucleoside diphosphates as substrates, but this may not be physiologically important. ... |
A0A061EQV6 | MHFSLQFSLPPVITALSPRSKSFSHQPHHHRIKKLTSHVPKSPLCSTTECALIHQCKEEEEEAFDGRVEDQTLPLGLRPEALPRHVAVIMDGNRRWARLRDLPVGSGYEAGVRSLRKIVELCCEWGIKVLSVFAFSSDNWFRPKVEVEFLMSLFERGMQEDTGIFLRENIRISVIGDLARLPEALQELIINLEEATKNNARFQLIVAVSYSGHYDVVQACQRLALKAKCGLIEPSDINESLIEQELVTKCTEFPYPDLLIRTSGEFRVSNFMLWQLAYAELFFAQSLWPDFGEAEFLKALLAFQKRQRRYGG | Pathway: Protein modification; protein glycosylation.
Function: Catalyzes cis-prenyl chain elongation to produce the polyprenyl backbone of dolichol, a glycosyl carrier-lipid required for the biosynthesis of several classes of glycoprotein.
EC: 2.5.1.-
Sequence Length: 312
Sequence Mass (Da): 35695
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A0A2G6G7R8 | MKTVEKTGKNLEDALDLALEELGCDIDQVDYEIVENDSKGFLGIFGAKEAKIRVTKKFSIVDEINDFISKILFSLGIDLNIEINREGEVIKVNLEGENISRVIGKNGATLDALQYLTNIIVNKGQKEYTRIILDANGYKKRKIESLEGLAKAMADKAVRLRKDIVLRPMSSYERKIIHFTLQKDDRVRTKSDGIDPYRKVIIFLNR | Function: A probable RNA chaperone. Forms a complex with KhpA which binds to cellular RNA and controls its expression. Plays a role in peptidoglycan (PG) homeostasis and cell length regulation.
Subcellular Location: Cytoplasm
Sequence Length: 206
Domain: Has an N-terminal Jag-N domain and 2 RNA-binding domains (KH and ... |
A0A2N6AVL7 | MKQNSSEKKHVVIGITGGIGSGKTTVTEYLSKRGFPVVDADAISRNLMYEEDTAFEVIDAFGKGILDSHGNIDRKKLREMVFCDKRLLVRLNSIFHPKIRERIEKDMADLKKEGNDVIFLDAPLLIENNLDRMVDEVWIVSCSKETQIKRVMKRDDSKRTEIEQIIKRQMPLEEKLKHADVVFENEGSIADLGEKIEDALKELVKRI | Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 5/5.
Function: Catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A.
Catalytic Activity: 3'-dephospho-CoA + ATP = ADP + CoA + H(+)
EC: 2.7.1.24
Subcellular Location: Cytoplasm
Sequence Le... |
A0A927ZLZ8 | MTEKKAKKKETLTFEQAMEGLETAVSNLRRDDLSLDDSMAEFRKGMELYERCSELLQDARQQVAVYTKETDSLEDF | 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... |
A0A927NYK5 | MSGLFYGSGVALVTPFFRGEIDYVRLGALIDWQISEKTDALIICGTTGEASTMTDEERMDTIAFAVSRAQGRVPVIAGTGANDTRRAIVLSERAEAVGADALLVVTPYYNKANADGLVRHYTGIADHVSIPVIAYNVPSRTGVNLTPHIMVELARHPRIQGIKEASGNIAQISELAHLAGDGLFIYSGNDADTLPILSLGGRGVISVAANIVPRRMHDLVMHFLKGDFAESQKIQLALIPLMQALFCDINPIPVKAALSMMDKIMDELRLPLTSLNADKRAQLKSILADFDLLPKK | Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 3/4.
Function: Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).
Catalytic Activity: L-aspartate 4-semialdehyde + pyru... |
A0A8B6EI08 | MDLSTYAPRFPKPGETMIGHKYVVGFGGKGANQCVSAVRLGCKTAMVGKVGNDDNGNKTINNFKSNGVITDYMAVTDQSSTGIAAITIADTGENSIVIVPGANLLLTDVDVTALEDMIKGSKVVVCQLEVGLSATLETLKLARKHNVRCILNTAPAQSGLSNDFFVLSDILCANENEAEMMTGLPVSDVAQAEAAIDVLLGKGCQYAIITLGEKGTVFASQDNRKPTYIPATKVKAVDTTGAGDAFVGSLAFYLATRPDLTFENAIQRSSIIASISVQSPGLLGFGNIQQQLLQSADARHRRELVQQEFRRGEEDRQVRA... | Cofactor: Requires a divalent cation, most likely magnesium in vivo, as an electrophilic catalyst to aid phosphoryl group transfer. It is the chelate of the metal and the nucleotide that is the actual substrate.
Pathway: Carbohydrate metabolism; D-ribose degradation; D-ribose 5-phosphate from beta-D-ribopyranose: step ... |
A0A971BKF6 | MKDELVRALAYGGNVAVLAANTTRLAGEAQRVHGTWPVCTAALGRALTGAILMASSIKHPEGSVSLVFSGNGPAGNVVAVARPGAEAKGYVENPRVDLPLNDRGKLDVGGAVGREGTLTVVMDTGRGEPYCGKTALVSGEVAEDIAAHFLFSQQQPTLSYLGVLVAPDMRVLRSGGVLMQPLPGCPGEIVGRLEAQAEALTSFGDAIFGGAGAEEALGSILPDAGLRVLERTEPRWRCGCSPERMEGALVALGPRALEEIIEEDGGAELNCRFCNRSHRFDGPALKGFLEAAFQA | PTM: Under oxidizing conditions two disulfide bonds are formed involving the reactive cysteines. Under reducing conditions zinc is bound to the reactive cysteines and the protein is inactive.
Function: Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversi... |
A0A7C6H982 | LMRERNPVEYALFMEEAGAPAISVVTEQEHYGGSLKLLEKIAEKTLVPVLRKDFIKTKQQIKDSKKAGADAVLLITSILDRNQLIELIEFSLANGLEPLVEVGNYTQMQMVNELNVSFIGINNRNILKYEIDNGDVGMTELLGQYKKPDTFLLSESGIMGKADVMRAISAGADGVLVGTAILQAENPVRKYKQLAYPYTDIKG | Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 4/5.
EC: 4.1.1.48
Catalytic Activity: 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate + H(+) = (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + CO2 + H2O
Sequence Length: 203
Sequence Mass (Da): 22450
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A0A943V4W7 | MENHKPFIKYVPNLLTVFRLLLVPVFYYAFWRPGFLLPDRFLACLVFVTAVLTDWLDGVIARKYDASSNFGKLMDPVADKLMTIMALFCFYVSGLVDWLFLAIVILKELAMIVGGYVLLTYHIVVYSKMCGKVAACLFYLAIVMTFFTALWPWNTYVLYAALALMIYSFFFYLRDGIRQLKQRKKEGKTLKGHEKLQ | Pathway: Phospholipid metabolism; phosphatidylglycerol biosynthesis; phosphatidylglycerol from CDP-diacylglycerol: step 1/2.
Function: This protein catalyzes the committed step to the synthesis of the acidic phospholipids.
Catalytic Activity: a CDP-1,2-diacyl-sn-glycerol + sn-glycerol 3-phosphate = 1,2-diacyl-sn-glycer... |
A0A4Q4W3T1 | MGFSKLATEIYTVSYLILFAILGTLARLGLQALTYYPRAPVIFSSVWPNFAGSLVLGYLSEDRKLFRHEWGVPTYDQHISRAKQKNADEENGESLFTQPAVDLPAAKKAHMATKKTIPLYIGLATGFCGSFTSFSSFIRDIFLAMSDDLASPDVSASSIPRNGGYSFIALLAVVIITVSLSLSGYFVGAHMAITLEPFTPSFPFRLTRKVLDPFAGLQRHGAVELRSPWCSPHSVVYYGITHLCASTPA | Function: Fluoride channel required for the rapid expulsion of cytoplasmic fluoride.
Subcellular Location: Membrane
Sequence Length: 249
Sequence Mass (Da): 27240
Location Topology: Multi-pass membrane protein
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A0A3D4LKR4 | MQYNRIKNLNMNGMPKICIPVTGATENEILDEFNELNNASMDLVELRADYFEFVQDQSKVIELLKKIRKVYDKPLLFTLRTKKEGGVSYIDADYYFKLNDSVIESKLVELIDIEFFSQAEKVENTVNLARKNNVVTILSSHDFLKTPPEEEIILRVSKMMDCGDIAKIAVIANSEEDVLTLLSAALKLKKEKKGPFIAISMGPLGIISRISCELFGSCMTYASHKAQSAPGQIDVTFVKELIKIMHI | 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 (DH... |
A0A0T6A764 | MDEAIKKLLTRGGAKLGLALTEAQIEHFITYLTELKRWNRKANLVGFRTDEAVVRHGILESLTLLKAFEVKPNLRLIDVGTGAGLPGIPLKIAAPDLAVTLVEAMRKKVSFLRQVCRLLQLRGISVLQARAESLHRDPAHREAYDLVTARAVTRLPETVALCTPFMNREGRLVLPVGLRWLREAETIRRPDIKIERVLHLSSDRDIIIIVRAGTVPRETGVEARPERVT | Function: Specifically methylates the N7 position of a guanine in 16S rRNA.
EC: 2.1.1.-
Subcellular Location: Cytoplasm
Sequence Length: 229
Sequence Mass (Da): 25679
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A0A917FSF5 | MDAITIENFRADTTIGVHDWEQQQKQPIIVNLRLECDCQEAADSDNIADALDYFTLTEHLKAFLAHNKCALIEYLAQQLIDEIFKVFPKVMAIDLHLQKPEAINNALVGVKLHRQR | Pathway: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate from 7,8-dihydroneopterin triphosphate: step 3/4.
Function: Catalyzes the conversion of 7,8-dihydroneopterin to 6-hydroxymethyl-7,8-dihydropterin.
EC: 4.1.2.25
Catalytic Activity: 7,8-dihydr... |
A0A7S7ESY2 | MTKLLVFAGTTEGRTLLEALSRQLSRQTYENGLSVFACVATEYGKELLQDGLDGIHIHAGRLTQSEMTALMKEHCFDFVIDTTHPYARVVSESIRMACAESGCKYLRVVRAEGRTLEMERQNCLFFHSHETAANYLDENPGKVLMTIGSKELHHYTNIQDYQHRLFPRVLPMNGVLESCTALGFAGRQLILMQGPFTAEMNAAMIRQINARYLVTKDSGEAGGFNEKYEAAVETGAQLLVIGRAEAEEGLSLKDLVEFLDETCGLTVGDAFMPYSTQLLEASDETQQGDTENAVAEKQNERRTPEQQKQDTGSWFPFFTK... | Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis.
EC: 1.3.1.76
Catalytic Activity: NAD(+) + precorrin-2 = 2 H(+) + NADH + sirohydrochlorin
Sequence Length: 463
Sequence Mass (Da): 51564
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A0A0M9VN32 | MSWLAPASLILVGGVWGTLARLGLVALNQYDGQSIAPLIWAQGVGCLVMGWASHKTTKAAIEASFAPAFPMLTTGFAGCCTSFSSWVLQVFEAFANTEHFDRHGLHNVMDALTQTAATLGIGIASFWAGRAVGDSFPADRWLRLHVPKRYSLLLSLLAGVLTWVGAALLCGLYAPFRHVTWSLVFCPLGAWLRWQLARLHTPPSVDKKIPMHHVLSWPIGTFLANILGTMVLCGALIGQQYGHITALPCGVLQGLQDGFAGSLSTVSTFISEAVALRPLRTSFAYLFVSWSCGVILSLLLVGVPTWTLPNAHFAPCVP | Function: Fluoride channel required for the rapid expulsion of cytoplasmic fluoride.
Subcellular Location: Membrane
Sequence Length: 318
Sequence Mass (Da): 34183
Location Topology: Multi-pass membrane protein
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A0A1V9ZXH0 | MKPHAVNTVQSLLDDGLQAKEAGRLRQAARIFNKIIIEDDTTQDKLVYQAYLHKYKLECEFLAYKSARDTTCRMITRFCGAHEPYLLKAQAESKLNKPYDAVASSLVGLAHNPIYQPLLSNLETFRDTLRSTIAGSTADKAKQRLLKDEPPYDLGVVDLPDLFVSVEQLRTVPSRYELYHGLSPDMFKRFEALETSPKDFMLVNKDISESLCTAASLAPRLSNLAKEIMSLTFLQTFYELQPGKTITQYERDCSIILSRAVYQLETLPFEMNCAFIFDVDDTALSSYSYMKSVKYQAIPQTQHNYLIKFNPPVNSIVHKF... | Catalytic Activity: a D-aminoacyl-tRNA + H2O = a D-alpha-amino acid + a tRNA + H(+)
EC: 3.1.1.96
Subcellular Location: Cytoplasm
Sequence Length: 870
Sequence Mass (Da): 98897
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A0A942Q1A9 | MRILALALALVSASALIAGGLVYASIVRDLPDLEGPPAGRDQTSVITDRNGEVLATLFAEQNRTDRPLAEIPQALRQAVIATEDSRYYEHRGIDPIGIARALWVDIRTRSAAQGGSTITQQYVKNAFITPEKTLRRKISEAILAYRLEQRYSKDRVLELYLNTIYFGHGAYGVESAAQVYFGKPVDQLDLAESAMLAGVIKSPGRFSPYLEPEAAVLRRNTVLRQMTDQELITEEERAAAADAEPVLAGLSGRNVIAPYFVEYVKAQLVEEYGSDQVFRGGITVTTTLDITMQRAAEEAIAEALDSPDDPSAALVAIDPK... | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Cell wall formation. Synthesis of cross-linked peptidoglycan from the lipid intermediates. The enzyme has a penicillin-insensitive transglycosylase N-terminal domain (formation of linear glycan strands) and a penicillin-sensitive transpeptidase C-term... |
A0A9E2BQ18 | MARLVLGVGGGIAAFKSAQLASLLRKRGHRVRVILTPAAARFVTPLTFESLTGEPVYHDLWNPPRYGDPDEALGEAHIHLSRWAEGALVAPATADLLGQLASGQARDGLTAFLLAFGGPVFLAPAMHHRMWLHPAVQEGVERLKRWGYRIFGPVKGPLASGEEGLGRMLEPAELADLFEDHLHGRDMEGKRVLVTAGPTQEPLDAVRHISNPSSGKMGYALAQAAFGRGAEVILVSGPTSLPDPYGVEVIRVRRAVEMYEEVARRFPEVDILVAAAAVADHRPKGMQAGKIRKEDLPFQVELEPNPDILKEMGLRKKPGQ... | 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 se... |
A0A972EFQ1 | MKDVGKISIIGLGLMGGSFALALKNKGFKGTITGYDISKNCVKKALRSQAIDVAAENLRDAVIDAEVVVIAVPLGKYETVLGETGKYLSSNCIVTDLGSVKMQALEMADRLLPKYIHFIGGHPMTGSERGGFEAADPFLYENAYYFLTPEDDTPADAIKTIESMVKNLGAYTVCLSPSQHDLIVSRISHLPHILAITLVNFIDKNMGISHLPFVGGGFRDTTRIASGDPNIWKDILFTNKGEIIKSIESFQLLLDEFKYCLEHDKDENIIQFLRNAKSIRDGVPHHGRDYMSPLYEITVSIEDKPGTIAELTQLISSNNI... | Pathway: Amino-acid biosynthesis; L-tyrosine biosynthesis; (4-hydroxyphenyl)pyruvate from prephenate (NAD(+) route): step 1/1.
EC: 1.3.1.12
Catalytic Activity: NAD(+) + prephenate = 3-(4-hydroxyphenyl)pyruvate + CO2 + NADH
Sequence Length: 366
Sequence Mass (Da): 40463
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A0A9E2BN64 | MKDLVLVVGLGNPGPQYHSTRHNAGFLCLDEVARALGIAFHPHPRREALVAEGRFGGRPFRLVKPLSYMNRSGPVVAEFLQESPVPVEDLWIIHDDMDLPLGTIRLKRGGGSAGHRGVDSVMAAIGPDFARIRIGVGRPPEGVAVVDWVLSPPMGEEAEAFQDGIRKGAQALFAVYEHGWEEAMNRFHRRR | Function: The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis.
Catalytic Activity: an N-acyl-L-alpha-aminoacyl-tRNA + H2O = a tRNA + an N-acyl-L-amino acid + H(+)
EC: 3.1.1.29
Subcellular Location: Cytoplasm
Sequence Length: 191
Sequence Mass (Da): 21017
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A0A353EY34 | MNQNRDPQTERELFREEPTVEEATPAAPTGKKSWLFTLLFVLIAALTFWAVTAQIKDFSFSDFAGYIGGANPAWLIAAVACMLAFILLEGVALLDITHSFGYRKNPAQGFLWSAGDIYFSAITPSATGGQPASAYFMIKDGIPGMVTAVALVVNLVMYTLAILAIALICLCLRPQLFLQFGTFSRILIVVGVVIQVVLAVFFVMLLKKERTLHRICDAFLRLLARLHLLRKPEEKRAKLRNYMEDYARYAQMLKGHGRMLFSAFLFNFLQRAAQIAVTSFVFLAAGGNPAQAFDIWVLQGFVVLGSNCVPIPGAMGVSDY... | Function: Catalyzes the transfer of a lysyl group from L-lysyl-tRNA(Lys) to membrane-bound phosphatidylglycerol (PG), which produces lysylphosphatidylglycerol (LPG), a major component of the bacterial membrane with a positive net charge. LPG synthesis contributes to bacterial virulence as it is involved in the resistan... |
A0A927NN70 | MLTIEMVKNCSHVHFVGIGGVSTSALAQWLVANGKKVTGSDKTKSVFTNKLQSLGVQVDIPCENNLLCGCDFVVTNSAISNDDSEVVLAKKLDIPVFNRNQLLGVVFDSFSKNVAVCGMHGKTTTSAMIAHCLAVAGRNPTAFVGGICKDFGNNFLQGSSDFCVAEACEYKCNFLTLHPQILCMLNLDLDHTDCFKDISQVKQIFGQFAKNLKRGGTIVKNGDQKEFDDIEGVSFGITRQSDYMATNLVQKCGCYSFCAQKHGRLYSKIKLQVAGVHNVFNALCAFATLDLLGVPRTVISRGLHTFSGVERRCNVYKGKT... | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
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: 447
Sequence Mass (Da): 48978
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A0A927P408 | MNRPQLLSMYEAELLEAVGGGFRAKQVLEWVRRGAPFSEMSNLPKALREELEEKFISNPVTIREAIQEGETEKYLYALPDENIIEGVKLKYHYGSTLCVSTQVGCAMGCAFCASTLDGCVRNLTAGEMLGQIVAVNRRLEPSGDKLRNAVLMGSGEPLANYDNTVKFLRLLREYGMSLRGVSLSTCGLADRMRAFAEEDLPITLCVSLHAPNDEIRKRIMPVARTYAMDDVIDACRNYVGKTGRRVIFEYTMIDNVNCSLANADELASRLRGLQCHVNLIPLNPVKERNMKAPSLRDQDAFMHRLEQKRVSVTRRRALGS... | Cofactor: Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs.
EC: 2.1.1.192
Catalytic Activity: adenosine(2503) in 23S rRNA + 2 reduced [2Fe-2S]-... |
A0A1J4VSK5 | MVPGGVFMFNLILKVREEILNEKPISYEDALMLTKATAVEIPYLAATANEVRQKFVGGHIESCALSNIKSGNCSEDCKFCAQSGHYKTDSPVYSQISVEDMVSQAKSAEAMGATEFCLVSSGWGATHEKDFTAILEAVRRIKAETGIFVDCSLGFLTGEQMQQLKEAGLYRNNHNLEASKDYFEKVCTTHTYAQRLKHAQMTRHYGIHPCTGGIFGMGESPKDRIDLAFELKKLGADCVPLNILNPRRGTPLGDVEMLKPLEIIKYIAIYR | 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.
EC: 2.8.1.6
Catalytic Activity: (4R,5S)-dethiobiotin + [sulfur carrier]-SH + 2 reduced [2Fe-2S]-[ferredoxin] + 2 S-adenosyl-L-m... |
A0A5P8NQF2 | MFDENFKGVLKYYTDTVFQKEQEIDRHVKLLSEYQKALDESAIISKTDKDGNITYVNDKFVQLSGYSAQELIGSKYSIFKHEDMPQEYFEDLWFQLENAGIFRGTIKNNKKNGDYFYVDVTIVKIVDAYDDSVEYISIANDVTKLIDARLEAQRASQAKEYFLSNMSHEIRTPLNAILGFVNLLIEQDTSKQHRKYLEIILNSGENLLSIINDILDFSKLRSGEFTIEPKVFSIHNEISHTLELFVASANSKDITITSFIDPNIPKELYADSLRIKQILSNFLSNAIKFTPVGGYINIEATCKDKILKVSVSDNGIGINK... | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Cell inner membrane
Sequence Length: 763
Sequence Mass (Da): 87336
Location Topology: Multi-pass membrane protein
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A0A947YWT6 | MNKALIFLFGATGDLARKKLLLAIGNLYAEGYISSDSQLICISRRNFTTKEFIDFANINNNPIVSIVKYIKMDFQNPDPIELIDIKNKFSKENDSFVQLSYLAVSPDYFLQMVDVLKKLDHEEHRIVFEKPFGKDLSHAKELNEKVQENFPEEKIFRIDHYLGKELVQNIFNVRFGNRLFEAIWCRQYIDSIQITVAESTGVEKRGSYYETAGATKDMYQNHLLQILSLVCMEPPLDMNPESIRDRKTELLRQIRKIDNKDVVFSQYDEGFIDLEPVNSYCQEDNVYEGSKTETYTATAVFVDNERWMGVPIFLRTGKRL... | Pathway: Carbohydrate degradation; pentose phosphate pathway; D-ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step 1/3.
Function: Catalyzes the oxidation of glucose 6-phosphate to 6-phosphogluconolactone.
EC: 1.1.1.49
Catalytic Activity: D-glucose 6-phosphate + NADP(+) = 6-phospho-D-glucono-1,5-lac... |
A0A3C1B2U8 | MPNNTNRNRSRQASERSQGSSAGSIAENRQSAEVTAPSLPVKRSPRRKPASQTLETRKPAVQPKQVQQPSAAQQPRPKQQHSQQHRQKSAKQNVVNQASSSLLKIIPLGGMREIGKNLTVYEYDDNIIIVDCGIAFPEEDMPGIDVVIPDFSYLIRNKEKIRGIFLTHGHEDHIGALPWLCKDIKVPIYGNRLTLELVRLKLEDRGTGVTGVTLHPIKDGVVIPAGPFSVEFIHVNHSIADANALAIRTPAGIIFHSGDFKIDYTPINGGPIDLARIAAIGQEGVLAMVCESTNVERPGHSSSESKVGETFADLFGKAAG... | Function: An RNase that has 5'-3' exonuclease and possibly endonuclease activity. Involved in maturation of rRNA and in some organisms also mRNA maturation and/or decay.
EC: 3.1.-.-
Subcellular Location: Cytoplasm
Sequence Length: 652
Sequence Mass (Da): 72049
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A0A923UQX7 | MSSIHIQGMRFRAYHGCIAEEALSGTDFEVSVLAHMPMVKAASTDNLHDALDYCAVYELVKEEINIPSKLIEHVAGRIYNRMKQFDYITECHVQVSKLNPPVNGYITQSTVVYNGE | Pathway: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate from 7,8-dihydroneopterin triphosphate: step 3/4.
Function: Catalyzes the conversion of 7,8-dihydroneopterin to 6-hydroxymethyl-7,8-dihydropterin.
EC: 4.1.2.25
Catalytic Activity: 7,8-dihydr... |
A0A2H0SKP5 | MKFLAKLQASIARKKSNVCVGLDSRYDRIPDAFKNGAGVAESILAFNTSVISQTYQLAAAYKSNLAFYAGFGSDGLKGLELTNRYLRQHHSDIPVLADCKRSEMGASVSLVKQEIIEWLKFDCVMVTPWFGFDTVEDYLDDPQIGVCVYVHDSNPSAAEFQELKLSSGQRLYEYVAERVAGHWNRNGNVFVEAGATYPWALQRVRQIVGEEMVMLTAGVGAQGGKPEDLKGAFGRHGNALLVNSSRGIIFADDPAAAARELQKQLDRCKED | Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 2/2.
EC: 4.1.1.23
Catalytic Activity: H(+) + orotidine 5'-phosphate = CO2 + UMP
Sequence Length: 271
Sequence Mass (Da): 29865
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A0A943PV04 | MAKKKDFESSLKRLEEIANQMEKDETTLEKSLKLYKEGVEEATFCASFLKDMEQEVSILQKDSKELFKLTPFYDMEED | 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... |
A0A2G6NY93 | MNQIIIKPYKLCGELVAPPSKSYSHRALIAAALCDAPSTIDNIVLSQDVRATKEALSAFGAKIHSFEKSCRIVPMPLTRPRTAIDCRESASTLRFLLPLALLVEGGCSFTGRAALIGRPLDDYVELFKAHDCIVDYDGKLPISLKGSPLQGEISISGAVSSQYISGLLFALPLSGAAATIKLTEPLQSRDYVAMTIDVLAQYGIKVESLASGWHLAAKQRYRATDYRVEGDYSNAAFWLVAATLGERIVIRGLNPNSLQGDRRIVDIINRMGGDVKASDDALIANPAQTHGIDLDISNVVDLVPVIALLAALSKGQTRLY... | Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 6/7.
Function: Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-ph... |
A0A5Q2FDG8 | MAPQDTLTPARTVDTVDLVALADRILAGGKVTRGEALALLGTPDGDVLGLVQAAGRLRRHWFGNSVKLNYLVNLKSGLCAEDCGYCSQRLGSEADVLTYSWLSTQEAVAVARTGMDAGARRVCLVSSGRGPSNRDIDRVSAIIDGLKEEDPDLEICACLGLLKDGQAEKLAAAGTDAYNHNLNTAESHYDDICSTHTYEDRADTVRKARQAGLSPCSGLIAGMGETPEELVDVAFALRAMDADSVPVNFLMPFEGTPLAGTHALTPLDCLRILAMVRFVNPDTEVRIAGGREDNLRSLQPLGLEVANSIFLGDYLTSEGQ... | 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 ra... |
A0A2V2DSS2 | MENYRTDLAVEIMNKIGGAREGAEVESADGRGGTKINRVRITSEAAARDIGKPIGNYHTVDYVELDSETYEYREEISKDIAAEIDMVAGGIREKKYETVLVAGLGNRDMTADALGSYVCERIFVTRHIKAEIPELLEDGSLGVAVIAPGVFGVTGIETEEVITSVSKRIEADLVVLIDSLAALEPRRIGTSVQISDTGIIPGSGVGNKRTPLNSPTLGADVIAIGVPMVTYATTIAKDASGLERLDETMMKKYENMVVTPKNIDEIVEKSAETLAMAIDRAINPGIARDFIELIRR | PTM: Autoproteolytically processed. The inactive tetrameric zymogen termed p46 autoprocesses to a smaller form termed p41, which is active only during spore germination.
Function: Initiates the rapid degradation of small, acid-soluble proteins during spore germination.
EC: 3.4.24.78
Catalytic Activity: Endopeptidase ac... |
A0A455UKK5 | MFIWMGEILFRSGLADNMFRGLSPWLNRLPGRLLHTNIIGSGMFAAVCGSSAATCATVGKMTLPELERRGYDSNMAIGTLASASTLGLLIPPSIVLIVYGVVTEQSISRLFMAGIGPGLMILALFMSYLIVWALLKGNREGLTGEDESGMSFGEKLRNTWSLMPILLLIGGIIFSIYGGLASPTEAAAVGVVLSIVIARFNGHFDRAIFKSSLFAAVRTACMIAFIIAGRLS | Function: Part of the tripartite ATP-independent periplasmic (TRAP) transport system.
Subcellular Location: Cell inner membrane
Sequence Length: 232
Sequence Mass (Da): 24772
Location Topology: Multi-pass membrane protein
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A0A8D8FA35 | MDDSDSDDTCELLPIFIDQLLRGSVDGKPFTNAEIADNAYTIIFGGNEPSALSVANTCLFLALYPRVQQQLYTEILQIIPDKSCAITHQTLHDLPYLDMVLKETLRLCPAIPNIARETTRTVSIDGRRIPAGTMFLISFYALHRRGDFWGDTVTEFDPERFHPDRGGYQRHPFGYLPFSGGARNCIGWQYAQSSMKI | Function: May be involved in the metabolism of insect hormones and in the breakdown of synthetic insecticides.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 197
Sequence Mass (Da): 22210
Location Topology: Peripheral membrane protein
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A0A7W4EV70 | MPSLKDIRIRIASVKSTRKITSAMKVVSAAKFHKAQDAQSHFQRYVDAYQYALGQAMHYCPGYDAPLMGVQNPDAPVALLLLTSNSSLCGAYNSSVASLALAEIYRLRQLAESQQAKSKQARAKDAQPTLADAVKVYTFGRKGYDTLKREGVVPVENDTALVDKPSFQQAAVLFDSLATDFLAGKISGVRLCYNRFRTAASQEPVVEPLLPVTVSLPQEALNSRVEYIFEPSAEQFFNYALPQYAKLLLYTSFMNNFVGEHGARMTAMTQATDNADSLIDELTLAYNKARQTAITNEILEIVSGADALKNT | 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: 311
Sequence Mass (Da): 34154
Location Topology: Per... |
A0A355JCM8 | MILLAPSILSADFSRLGEEVSAVEAAGAQYLHIDVMDGHFVPNISFGAPVMKSIRKMSQMVFDVHLMISDPLRYIDDFAAAGADIITFHIGCSSDIDETLDKIKSHNIKCGLAVNPDVPAERLFPYRDKIDMALIMSVFAGFGGQSYIDGVNAKIQAARTFFGPDFDIEVDGGINLTNKTVPIANGANVLVAGTAIFGAQSPKEAVCSFLNETEIDN | Cofactor: Binds 1 divalent metal cation per subunit.
Pathway: Carbohydrate degradation.
Function: Catalyzes the reversible epimerization of D-ribulose 5-phosphate to D-xylulose 5-phosphate.
EC: 5.1.3.1
Catalytic Activity: D-ribulose 5-phosphate = D-xylulose 5-phosphate
Sequence Length: 217
Sequence Mass (Da): 23318
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A0A7W4EWM8 | MEHTLIIAGLVAVAYLLGSIPTAVWIGKRFYGIDVREHGSHNAGATNTIRVLGLRTGLIVFVIDLAKGYCAVSLSLLAGWLGSSPQLHTLLGIGLGLAAIAGHIFPLFAGFRGGKGVATICGVALALHPWAALCALGVFAIVLIATRYVSLGSMLAGLSYPIFLFFVFQSRNIPLLVFGCVIALLLLLTHRANIKRLLHGEESRFKPSGKGTMGK | Pathway: Lipid metabolism; phospholipid metabolism.
Function: Catalyzes the transfer of an acyl group from acyl-phosphate (acyl-PO(4)) to glycerol-3-phosphate (G3P) to form lysophosphatidic acid (LPA). This enzyme utilizes acyl-phosphate as fatty acyl donor, but not acyl-CoA or acyl-ACP.
Catalytic Activity: an acyl pho... |
A0A3D5MLW1 | MVAAKEMTYLDHIAELRRRLITVVVTFVLAMVATFPFAGDIIDYLTAPVKDGLVVLRPAEAFYAHLQVSLAVAVVVNIPVLLYQLLAFIFPGLTPSEKRWVWLSIPPVILLFVGGVLFAWFTVVPIIYRFFMGFTSEALQPFISVGNYISFVSGIVLPFGIVFELPVVIALLTGMGLVTPSFLLRYRKYAVLIIFVMAAFLTPPDVVSQGFLALPLIGLFEASIGVSKVIHRRRQRALARLEAELAAEEAAVEGASGTGR | 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.
Subcellular Location: Cell membrane
Sequence Length: 260
Sequence Mass (Da): 28529
Location Topology: Multi-pass membrane protein... |
A0A927NPY0 | MARIKIKLALIGANVGNSFSLDIHRFILDKWGYDCEYELISVAVDEFPNAVRRLIGDFDGFNVTIPYKREIMAYLDEIVGDAFEVGSVNTVVCDERKGYNTDGVGFSLALERAGVELLNKRVLVLGAGGAGRSVAKACKDKGAQVWAYRRDREKLKEFCLELGVNECQGLENAEFDIIVNATGVGSKVDLGVSPIGDSAFEKAEWAIELAYNPSETEFLRLAKSKGANTLNGFAMLFFQAYYADCLYLKKTPSKREMDELYKEWIYEIFNH | Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7.
EC: 1.1.1.25
Catalytic Activity: NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH
Sequence Length: 271
Sequence Mass (Da): 30296
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A0A927XYF2 | MAQDTFSEFLAELKEKNDIVSVVSSYVPLTRKGRHHWGCCPFHNEKTPSFSVNEDLQIYKCFGCGVAGDVIKFVQEKERIDFNGAVKILADRVGMEIPKFNGSDTQADKKRSELLSIMNAAQEYFVANLSKPMAAAANDYIAKRGLSKKVVESFGLGYAPEGWENLKTYLVGLGFSADSVNETGLLTVGDKKSYDKFRNRIMYPIIDEKGNIISFGGRIIDPNDTPKYMNCPQTLLYDKSNTLYGLNIAKNYARAAGSLIIVEGYMDVISMHEYGYNTAVASCGTSLTQQQARKIKRYVDKVYIGYDGDGAGQKATLRGL... | Cofactor: Binds 1 zinc ion per monomer.
Function: RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication.
EC: 2.7.7.101
Catalytic Activity: ssDNA + n NTP = ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate.
Sequence Length: 608
Domain: Contains an N-termi... |
A0A927VRV0 | MKRLAVILAVIIGITGFGGAFAAEPVYADVTVPELTAEAAILIDGYSGQVLYTKNEHAKLEPASTTKMITCLLGLENLEMNQILIGDADTAFVDGSKIFFLEEERMTVEQVMNSLMTVSANDAAVAIGKAVSGDLDTFAQLMTERAKELGALNTTFKNPNGLHAEGHLSTAYDLAMIAKGCLENDEFRKLCTTYKYYIPATNKQDERYLYNTNRLIYDDVNTVQVNGVNRICKYEGAIGVKTGTTPEAGACLVAAAEREGTLLIAVVLKSTDMGRYADAISLLDYGYANYYGVKAADKELEIFDPVPVKRGSVRDVEIEL... | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Removes C-terminal D-alanyl residues from sugar-peptide cell wall precursors.
EC: 3.4.16.4
Catalytic Activity: Preferential cleavage: (Ac)2-L-Lys-D-Ala-|-D-Ala. Also transpeptidation of peptidyl-alanyl moieties that are N-acyl substituents of D-alanin... |
A0A2M7SY21 | MPKTAHMHISPAAHRYATALFLAAEDVKATQLLENQAHTLLAALKDSALEAVTSPTLGRTQRIKLVQMVVKTLKPHALLEGTLGLLTQKGRLNLLPEILTDFTAQTAAGAGIVPVEVETATPLTESQVLQIKMQIKAATSARDVTLTQTLRPRLIGGFRAFYQGKVWDASVSGGLEALKQRLRSTLSAHQKPMF | 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 c... |
A0A972ALK3 | MKLFYDYHVHTVFSEDSSMGMEEMCLGAIERNIVEIAVTDHLDIDYPDRDFQFDLDYAAYSTAIDHAREKYHGRLNIIKGIEIGLQAHILDECAAFLEGKDFQFVIASVHAVSGMDLSGDEYYRQKTKKAAYIEYLEALLACIKNFKAFNVVGHVDLLRRYGSYRDKSMKHSDFGDLLDLVFEELISTGRGLEINTSGFRYKLQSTLPDLDLLKRYRELGGEILTIGSDAHTPHHLAYYFSAAYQVVKKAGFDYITRFPNGEPEFVKI | Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 8/9.
EC: 3.1.3.15
Catalytic Activity: H2O + L-histidinol phosphate = L-histidinol + phosphate
Sequence Length: 268
Sequence Mass (Da): 30660
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A0A943PBQ2 | MDKIFKGKTIDEAVKNACEALGVSEDNLFYEVVDLPAKGFLGIGSKLASIKIPGTDDPESYINDYLKELFSKMGVSDYNQIVEIKDENIVNIRLEGEEIGYYTHKNTDIVDSLQFLLALSLNREFENKNYKVTLNINDYKEKTTSRLESLAVKTAKQVLRNKRKVTLRPMSAYQRRIVHSKLHEFENITTFSIGEEPNRRVVIAYDGPDRALPRDSEGKPVFEKKGSDKKTSGRKNHGGRVSEKNGSGNYGKDFFEKDHKGGAERENSGSVKISERGGGKPFDPGALGHSLSSRGRADKKENSSSSEPRVEKVKILYPGP... | Function: A probable RNA chaperone. Forms a complex with KhpA which binds to cellular RNA and controls its expression. Plays a role in peptidoglycan (PG) homeostasis and cell length regulation.
Subcellular Location: Cytoplasm
Sequence Length: 333
Domain: Has an N-terminal Jag-N domain and 2 RNA-binding domains (KH and ... |
A0A965Z7P6 | MNSINTILASRQKILIFGFGREGKSTYRYIRSRFPQKMLTIADEKSHPDLFSCLSADPYLMVQTEEKCFNNLSQFDLIIKTPGIPLFKLTGAHKEKITSQTDLFLRQYGAQTTGISGTKGKSTTASLIYHLLKVSGRDTIFAGNIGIPAFDMLPQITPETTVVMELSAHQGEILHAAPHVMILLNLFQEHLDHFGNFGNYKQAKLNFCTFQKPGDYFIYLTEDPELIQCAGTVDGVHYIGISESFSENGYSFKDEKITGRGLVMEKYICALKGKHNRKNIAAALAAAHILEINTDTLQTGLASFSPLKHRMEFVGEINTV... | 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-... |
A0A927NTK0 | MVVIAWIIRILLILVSIGLVVLVTMQKAKQAGLGSLAGGDSFSLKGKSKGKEAALNKFTWIGMIVFVVLSIALAVIAKTM | Function: Involved in protein export. Participates in an early event of protein translocation.
Subcellular Location: Cell membrane
Sequence Length: 80
Sequence Mass (Da): 8442
Location Topology: Multi-pass membrane protein
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A0A1H9HWM7 | MCEFEKKVWNGLIECGLQLDSPAGKVIGGGQRIGVAVSGGADSVSLLLSLSQFFSPLYVITVNHNIRPASESRGDVDFVLEVCERLRREGRQIECDVVELERGAVAAEAEKRGGGIEEAARYLRYAAFGRFVTERGLDALCLAHNRNDQLETVLMRFLQGSPAEAAAGIRARRECFIRPLLGVTRREIEEYVASRGFEWRTDKTNYETDYLRNKIRLKLVPFLDENFSGWQTAVLNGAQKAAEDSRLIQSCIEKYPLVLTKDGSVELPFSDFLSAPDAVKYRLLLEACNKAGETSRIPHQFLKDVISVFNNKTANNYDYS... | 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)... |
A0A8G1G7U6 | LIPMMMNLPDMAFPRLNNMSFWLLPPSLVLLLMSMLNEGGTGTXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXVSSILASINFISTITIMTHKNVSALKISLFSWSILLTTVLLLLSLPVLAGALTMLLCDRNMNTSFFDPSGGGDPILFQHLF | Pathway: Energy metabolism; oxidative phosphorylation.
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytoc... |
A0A353W1H5 | MNRKADIGIFGGSGFYNLLPDIEEIEIETPFGKTSDKIALANYKGKTIAFLPRHGKDHSIPPHLVPYRANIFAMKELGVSCIISPCSCGSLNAEIKPGDFVISDQFIDRTNGREDTFYEGPDVKHVSPAHTYDDRLRDIAINACKHLAIPVHEKGTIVVINGPRFSTKAESRWFSMIGGDTVNMTQYPEAYLAVEMEIPVVNIALVTDYDAGLEGRDDIKPVTMEEVFKVFNENLAKLKDLLFEMIEKI | Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via salvage pathway; S-methyl-5-thio-alpha-D-ribose 1-phosphate from S-methyl-5'-thioadenosine (phosphorylase route): step 1/1.
Function: Catalyzes the reversible phosphorylation of S-methyl-5'-thioadenosine (MTA) to adenine and 5-methylthioribose-1-phosphate.... |
A0A2G9M2B3 | MLVFVVNAGSATLKYALFRNREELCSGIADRIGFGDSFVSIKQKNLGEKILLLPLANHRDALREILRILIETGAVNDLNDIDAIGHRVVHGGEMFSKSAVIDKKVISAIKKYAKLAPLHNPPNLLGIEACEKLMPGKRQVAVFDTAFHQTMPKKAYLYPIPLKYYTKGRIRKYGFHGISHEYVALEAARVLKKSIKKLRIITCHIGSGASIAAVEYGKSIETSMGFTPLEGLMMCTRSGDIDPGIILYLMKEQKLSADEIDNMLNKESGIKGILGFSSDFRDILANLGRKDKPEAKLAFDIFAHRLQKYIGAYAAVMNGV... | Cofactor: Mg(2+). Can also accept Mn(2+).
Pathway: Metabolic intermediate biosynthesis; acetyl-CoA biosynthesis; acetyl-CoA from acetate: step 1/2.
Function: Catalyzes the formation of acetyl phosphate from acetate and ATP. Can also catalyze the reverse reaction.
EC: 2.7.2.1
Subcellular Location: Cytoplasm
Catalytic Ac... |
A0A1W1Z4C3 | MNKQSGSIDLARLAVYILKRIWLVIICAAIGFGFMYWRASKAIDTYTASGTMFVTNSNPNLVNYGYTSTSDISSAVQLVNIYSEVVKSETVMQKVLEYAIEPAGENGNENDLLLSQKYPGLSTDFIRNVISMNSVHETPMVRVSCTTPYPELSADICNSVLQVAPTAIKDVVAAGEAKAQDYATIPMFANGRNDMKKGIIGALIGAVIACALLTLLFLMNHRVEKPAELTDNYTPPILSYIRRAKGEEKDAGVFLLNDKTDMDMVESYAKLRMNLLYTMSEKMRRTVLVTSAISGEGKSTIAANLAVSLALSGKKVLLVD... | Catalytic Activity: ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]
EC: 2.7.10.2
Subcellular Location: Cell inner membrane
Sequence Length: 509
Sequence Mass (Da): 56495
Location Topology: Multi-pass membrane protein
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A0A970ES36 | MADTIKNVKHKTWAEINLTALKRNYAAVKALVGDSCRVMCVVKADAYGHGAERCATALYEAGARDFAVSSIEEALALRSAFEPRLMYDARILVLGYTPPENADILAKYAIRQTVFSTEYAKALSHAAEKRGCAVLVHFKVDTGMNRLGFDAKNGAVAKILEAASYTGIVPEGIFSHFACSDEPENPMNAEQLMLFLKIDKALRERGLVLTSHISNSAAIATIPEAHLDMVRAGIILYGLEPFYPFDEEDVLGLTPVMTLKSVISHIHTVRAGEFISYGATYSPKHDITVATIPIGYADGYIRAFQNGGGVYIGDSFAPIV... | Pathway: Amino-acid biosynthesis; D-alanine biosynthesis; D-alanine from L-alanine: step 1/1.
Function: Catalyzes the interconversion of L-alanine and D-alanine. May also act on other amino acids.
EC: 5.1.1.1
Catalytic Activity: L-alanine = D-alanine
Sequence Length: 382
Sequence Mass (Da): 41641
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A0A061GFZ9 | MGTIRNHHFCSFFLFFAFLAIFPTISFSIDTLTATQSIINNQTLVSPGDVFEFGFFTLENPGEWYVGIWYKNIPVRTYVWIANRDKPLANSSGIFKLEDRNIVLLDQGQNLVWSSNITKGDNPLAQLLDSGNLVLREANINDETNHYLWQSFDYPTDTLLPDMKLGWDLNAGFNRFLTAWRTKGDPSSGDFSFKLDYHGFPEIFLWNKQRREYRSGPWNGLRFSGVPEMKPLDYISFNFVTNQDEVYYSFSITNKNLFSRLIVTPTGTLQRLTWIPDTEQWNPFWYAPKDQCDNYRECGQYGICDSNASPVCKCPKGFSP... | Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
EC: 2.7.11.1
Subcellular Location: Membrane
Sequence Length: 840
Sequence Mass (Da): 94759
Location Topology: Single-pass type I membrane protein
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A0A7L5BX33 | MTETETALATVAPGAIAKSTGTALTAAGADHAGAHPADRLEQAEKAAIVLVALGPETAARLLAGIGERRLHRFARIVNGLSEVPADVVERVIAEFLHKIEDTRSVGGGAVEARRFLSEVLDKDQVNRIMGDLNTKGRSVWSMLGDVPDVRIANWLRSEHPQVAAIALSRLSPVKAARVLERLGQAEAEDIVMRMGPAAIADPGVTARIGDVIARDFLPAAISQRNRPEPADLIAGVMNHVSAAVRDRLLAAMVDAAPKLAEAVRKVMFTFEHIPERINPRDVGLITKSVDEAVLLRALKAGGERGRATADFIFANISKRL... | Function: FliG is one of three proteins (FliG, FliN, FliM) that forms the rotor-mounted switch complex (C ring), located at the base of the basal body. This complex interacts with the CheY and CheZ chemotaxis proteins, in addition to contacting components of the motor that determine the direction of flagellar rotation.... |
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