ids stringlengths 6 10 | seqs stringlengths 16 1.02k | texts stringlengths 117 4.4k |
|---|---|---|
A0A970L1A0 | MRRYRVSYFIGQALQGIWRNGVMSFASIAVLMSCLVVLGAFTLLVVNINTNLENLDEANKIIVFLDYNLTEEQIVDIERQIKKIKEAETVKRITADEALRSLAKRAGENALLYDDYFKDNPLSDSFEITYDDVKDLTTIEFELQSIEGVRKYRDQRYIVNLISDIKSGVLFVFLWFLVMLFIVSVFIIINTIKLSVYSRKNEISIMRYVGATGWFISLPFILEGAIIGLFASIIAYFVEEYLYKSLVGSLGISIEIITLIPFSELAGGILAVFIIIGVTTGIMGSSISLSKYTKK | Function: Part of the ABC transporter FtsEX involved in asymmetric cellular division facilitating the initiation of sporulation.
Subcellular Location: Cell membrane
Sequence Length: 295
Sequence Mass (Da): 33354
Location Topology: Multi-pass membrane protein
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A0A970TT47 | MLLKVKDVSEVQNTIMEHFGGFVVESEEVGLLEAPGRVAAEDIKAVYSVPDFNKSVVDGYAVRARDTFGASDSLPALLDMAGEVMIGSNADININVGSCAYVPTGGMLPEGSDAVVMVEDTEDLGSGSIAVYKPIGPWENTISRGEDIKAGGVVLEKGTVIRPQHVGVLASVGLERVPVFKRPRVSIISTGDELIPPGEDLQPGKIWDINSYSLAAAAAEDGAFPILGGIVPDDRATIKTKVMDALTKSDALLISGGSSAGARDYTAEIINELGRPGVLAHGISIKPGKPTIIGGVDGKPVIGMPGQPVSSLVVYNVVVS... | Pathway: Cofactor biosynthesis; molybdopterin biosynthesis.
Function: Catalyzes the insertion of molybdate into adenylated molybdopterin with the concomitant release of AMP.
EC: 2.10.1.1
Catalytic Activity: adenylyl-molybdopterin + H(+) + molybdate = AMP + H2O + Mo-molybdopterin
Sequence Length: 409
Sequence Mass (Da):... |
E0NM54 | MQGILVVNKRQGITSHDCIYILRDLLGIKKIGHSGTLDPMATGVLPMTIGKATRVSSFIQDSEKEYIATIEFGIETDTEDITGNIINRSDKIPTKEEILEILPKFTGVIEQIPPMYSAVRLGGRKLYKIAREGKVVDRPKRKVKIYGLELLGTNPYKVKINCSSGTYVRTLISDIGKSLGTFATMTSLVRTKVGPFIVEKAITIDDLENMTKEEIEEKFYPTEFALRNMPRYNVPKSFFERLINGVKFFDDRMEDGKYSVYCRDEFIGIGEFIDGRLRIKVLR | Function: Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs.
EC: 5.4.99.25
Catalytic Activity: uridine(55) in tRNA = pseudouridine(55) in tRNA
Sequence Length: 283
Sequence Mass (Da): 32093
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A0A971JY77 | MQLLIAIDGPSGAGKSTVADLLASRLGIAHLDTGAMYRAFAWQALQEGLDTLDERAMSELTARSTVEVRFVNGKQHTYVNGRDVTVLIRTPEVSMGASNSSKFPLVRCWMVRMQQALAQNCSMVLDGRDIGTKVLPTATLKVFLTASPQVRAKRRFEELQIMGASDTYEDVLEDVIRRDHQDTTREVDPLRPAEDAVMLDSSNMTQAQVVDEIERLLRLKNSTSAIPQEKPKDINRQSKEKAEHFKGRFSIFYRIIQALSWLVFHTIVPVRYHHVDKLQLDAPFMLISNHLSMLDPFLIGWKCKRYQLFFLGKKELASNP... | Catalytic Activity: ATP + CMP = ADP + CDP
EC: 2.7.4.25
Subcellular Location: Cytoplasm
Sequence Length: 453
Sequence Mass (Da): 51054
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A0A6I7QMY7 | MTDNTTGSPIRKETFFCRKRTLNCRGKIINLSSPVVMGIMNITPDSFYDGGRHTRPWDAIKLAEKLLDDGAHILDMGAASSRPGAAMIDPAEEQERLMPALKAVLKQFPEAIISVDTYHASTARIAIDSGAHMINDISAGSMDDNMFHTVARLQVPYVIMHMQGRPDNMQKNPRYNHLVKEVAGFFSERINKLRDLGVHDIVIDPGFGFGKTLEHNYQLLANLDYFAIFDLPVLVGFSRKSMINKVLNTSPDKALNGTTVLNTIALQKGADILRVHDAKEALEAIKISGFLKKQQ | Pathway: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 7,8-dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate and 4-aminobenzoate: step 1/2.
Function: Catalyzes the condensation of para-aminobenzoate (pABA) with 6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPt-PP) to form 7... |
F8ABZ7 | MVNLPTPLIILLAFVLDLLFADPQVRWHPVRVIGQVAEFFCRFFYSLGRLGGLLTLLFTSIVFVGGVSFTVCLFPPLEILWLYFFIAPTSLQKEVLKVAEALQENISLARKRLSFLVGRETKNLDTSQCVRAAVETLAENFTDALVGPLFWYMVGGIYGVAFYKVCETLDSMYGYKTKKWLRFGYFSAKFDDILNFLPARLAGLFIVLASGLTGQNLWRAFRTMLADAHKHDSPNSGYTEAAMAGALGIELGGPVVYQGQFFEKERFGKPLREREVSDIFLAGKIIRLATFLIVATIVFLEVFLWKLGYPNLIELIMNEL... | Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis.
Function: Converts cobyric acid to cobinamide by the addition of aminopropanol on the F carboxylic group.
Subcellular Location: Cell membrane
Sequence Length: 326
Sequence Mass (Da): 36659
Location Topology: Multi-pass membrane protein
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A0A3D4MVW2 | MEKPVTLDAPLTSLPGIGPQRAALFARLNVRTVGELLRLYPRTYEDRTRLVSIASLEAGTPACFEAAVVTTPRTNRIPKPGSRMLEVTKFTVADDTGRLNLTFFNAAHSAGALRIGERYCFYGVLTGDYAAYGMTNPLFEPCDGPAHVTRRILPVYPLTAGLTNSMVLRAQAQAVSRCAGLLPETLPPELLRRCGLCGAAEACREIHCPTSAAALGRAQRRLVFEEFFLFSAALAIVRSRRTAHSCPAWQTELTPFFAALPFRLTGAQQRAVDDICADVRTGRPMSRLVQGDVGSGKTMVAAAAACLAAKNGAQTALLAP... | Function: Critical role in recombination and DNA repair. Helps process Holliday junction intermediates to mature products by catalyzing branch migration. Has a DNA unwinding activity characteristic of a DNA helicase with a 3'- to 5'- polarity. Unwinds branched duplex DNA (Y-DNA).
EC: 3.6.4.12
Catalytic Activity: ATP + ... |
A0A971VRW6 | MVILAVDYGEARTGLAVCDKNEVLATPLSPVVVKSTDMLIDTIIETAKQYKAELIVVGLPVNMDGSHGFRAEAVKEFAQLLKEKSGMPVEFWDERLTTMSASRLLNETDVKGKKRKMKLDSAAAALILQSFIDSRKRG | Function: Could be a nuclease involved in processing of the 5'-end of pre-16S rRNA.
EC: 3.1.-.-
Subcellular Location: Cytoplasm
Sequence Length: 138
Sequence Mass (Da): 15171
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A0A972CC76 | MDNGNPNSGNMNRETNKSEGRRNLHRRAARRPSQLGAAKDRQPEARRAPARDAQDSHPAQKTQPNIPSGRPGSDSKSGGANHRADERLPVTGSPREQLRRLELDGARLPQADIARRNTGKTDVARPVQAPLPREVQFEAPVIDPEILRRSASERQRQPDGRTVGRSKIYATSDIAETKANVARPAKPLPQRAAGSASGGKIRVGYKRADEFLPEKLTVTGDKRVITESSDIEDEEIDIDEADSEPARRGSALSSLLKAIVYIVFVLTVSAFLSFFIISIGNDIFAFVKPNIETTVTVPEFATIDNIADILSEKGVIKYPF... | Function: Functions as a peptidoglycan terminase that cleaves nascent peptidoglycan strands endolytically to terminate their elongation.
EC: 4.2.2.-
Subcellular Location: Cell membrane
Sequence Length: 607
Sequence Mass (Da): 68275
Location Topology: Single-pass membrane protein
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A0A1I1EFG4 | MGGGDAAAPIVVMGVSGCGKSTLALSLATALAWPFIEGDAYHPPANVEKMTAGIALTDADLQSWLASLVEVLRTHPQGTVLSCSALKAAYRDTLRQAHAGMRFVFLDLDEVAATQRVAARSGSHFFNPSLVRNQFDNLQRPDAEPGVLCLDAMLPQALLCQQALVWVKGEAPKPEGQRHQRPILAL | Pathway: Carbohydrate acid metabolism.
EC: 2.7.1.12
Catalytic Activity: ATP + D-gluconate = 6-phospho-D-gluconate + ADP + H(+)
Sequence Length: 186
Sequence Mass (Da): 19854
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A0A7T7JPK4 | MKTSLVATLNLLMIGLILPCLCSEDEERLVRDLFRGYNKLIRPVQNITEKVDVRFGLAFVQLINVNEKNQIMKSNVWLRLVWNDYQLRWDETDYGGIGVLRLPPDKVWKPDIVLFNNADGNYEVRYKSNVLIYPHGEVLWIPPAIYQSSCTIDVTYFPFDQQTCIMKFGSWTFHGDQVSLALYNNKNFVDLSDYWKSGTWDIIEVPAYLNTYPGVPTETDITFYIIIRRKTLFYTVNLILPTVLISFLCVLVFYLPAEAGEKVTLGISILLSLVVFLLLVSKILPPTSLVLPLIAKYLLFTFIMNTVSILVTVIIINWNF... | Function: After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane.
Subcellular Location: Cell membrane
Sequence Length: 389
Sequence Mass (Da): 44967
Location Topology: Multi-pass membran... |
A0A350J968 | MNFFITMEHVALYRQFRPKTFDEIVEQKAPVAALKQSVRTGRIGHAYLFCGQRGTGKTSIARVFSRAINCENPKDGNPCNECPTCKGILDGSLMDVIEIDAASNRSIDNIRKICEEVTYSPSKASHKVYIIDEVHMITTDAFNALLKTLEEPPKHAVFLFATTEPHQIPATILSRCQRFDFRRISQEAIEGRLRYISDQEKIDIDDDALRLIASLSDGAMRDAISILDQAASAADNKKITAADIESMTGTVNTDFLAAMAEILIEGRYDELLIKCDELARSGRDTIQFTLDLAGFFRNLLIVRTVPEPWNLIPASPATYT... | 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: 396
Seq... |
A0A927T1Z1 | MASKRDYYEVLGVSKSATDDELKKAYRKLAKKYHPDANPDNKQEAEEKFKEVSEAYENLSDPQKRRMYDQFGHDGPQGFGGGNGGYYSYSSSGFDGFGDFGDLGDIFSSFFGGSGFGGRTTTRQRNSGPKKGRDLKYSMDITFEESFLGVKKDISIYREEDCETCHGNKAKPGTKAERCTTCGGTGTVRQTVSTILGQMQTTKTCSACGGEGEIIKEKCPECKGRGKVRKQVKIKVTIPAGISDNQTVVLRKEGEAGTKGGERGDLYIVVRVKKHSIFTRQNDNIFCEIPITFTQATLGADLKVPMVDGKSEVYRIPEGT... | Cofactor: Binds 2 Zn(2+) ions per monomer.
Function: Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction... |
A0A1U9NQX2 | MAESGKRFGWLSTLAGAVVVIAAAFGLRFLFAPGLVDRKSGYREVMGTFAQVVAVAEDGAVAKEAVEAGWDALVRVDELMSGYKEDSDVSRINREAGDGPVKVDEAVVEVIEEAVRYSEMTDGAFDVTVGPEIELWREAEKKGEVPNDEEIATVRERVGYEKLEVDEEANTVEFAVEGMRIDLGGIAKGYGIDAAVEAMKEAGAVGGMVDVGGDIRVFGVRGEKDEVGEWNIGLQNPVVEKGVLAVLKLQDAAIATSGDYRRYVEIGGKRYSHIFSPAEGGSATELTSVTVIAGEAVEADALATAVSVMGMEKGLQLVEG... | Cofactor: Magnesium. Can also use manganese.
EC: 2.7.1.180
Catalytic Activity: FAD + L-threonyl-[protein] = AMP + FMN-L-threonyl-[protein] + H(+)
Sequence Length: 351
Sequence Mass (Da): 37254
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A0A9E6AGF0 | MDRVLVTGGAGYIGSHACKALSRAGFEPVTFDNLSTGWADAVKFGPLEEGNLLDRARIDAVFAKHQPIAVMHFAALSQVGDSMKDPGLYWRENVTGALNLIEAAVAADCKRFVFSSTCATYGDQDGVVLDEDSVQIPINAYGASKQAIEQILSNFEATYDLQHVIFRYFNVAGADPDGEIGEFHRPETHLIPLILQAIDGQRPALTVFGTDYPTPDGTCIRDYVHVSDLVDAHVSGLKWLIDGKGSRAFNLGTGSGFSVREVLENARRATNRDVPIEYGERRPGDATSLVSGSSRASSELGWTPHRSNMKQMISDAWQWH... | Pathway: Carbohydrate metabolism; galactose metabolism.
EC: 5.1.3.2
Catalytic Activity: UDP-alpha-D-glucose = UDP-alpha-D-galactose
Sequence Length: 327
Sequence Mass (Da): 35696
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A0A947YXX6 | MPLKQPGKLYVCATPVGNLGDVTERLKTTLRTVDAVAAEDTRVTSSLLNHLGIRTPKLISCFDGNETKRSQEICNLLEDGLSVALVSDAGTPAVSDPGYIVVKAVTEAGFECISIPGPSALTAAISCSGIDSSHFHFEGFLPVKGSERKKRLEYIVQTGETVILYESPHRIHKTIGDLAAVYPPDTQVTIGRELTKIHEEFIRGTIESLNSSESVITERGEFVIIIGPSQQISTNTLPLLEKQVIRFLDAGITPKVISTLLVDFYSVPKRDIYQLCIEYNSEK | 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: 283
Sequence Mas... |
A0A3C0PAB7 | MKEKIEQLKMEFDKVIKEHNSMEKIDELRVAYLGKKGKITELMQGLKDVIAEQRRDVGIAINNFKQYVEGLIENKVKEAKELELQKEINNAERIDITIPSGERCGSLHPITVVQKEVEEIFKSMGFVVEDGNEIETEFNNFDAVNVPRNHPARDMQDTFWLDNGEVLKTQTSAGQNRILRKYGAPCKVIFPGRCFRNESVDASHENTFFQLEGMMVGRDINVANLIYFMKTMLSKVLKKDVDVRLRPGFFPFTEPSFELDVTCPFCGGKGCPTCKQGGWIELCPCGMIHPEVLRMGGVDTNKYQGFAFGLGLTRLAMMKY... | 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: 342
Sequence Mass (Da): 38949
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A0A947YZL3 | MSKRIRHHVNPLSMSYLDFEISPPELSGHFTEVEIGCAEGEFLFERYGDCPDHQVIGLEIRRSLVDEINDKSRNFGLKGISAVFCNVNTHMTELFPAGSVDRFFVNFPDPWFKKDHHKRRIVSPALVADLISCLRSGGEIFFQSDIFDLAMDAMAVFEENGPPQIRNVSGEWSFMKENPFKTMSRRERFVTEEGLRVWRMLYRLSC | 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: 206
S... |
A0A359JLC6 | MESDSTRYFNRELSWLEFNNRILFESRDTKNPLLERLKFLSITASNMDEFYIVRVASLRDLLSVKYDELDISGRTVKQQLSEIDEKARAQMALMYSTYTRSLVPSLKNHNIFISDYRDLDDHAKEVCDDYFRSTLYPILTPMAVDASRPFPLIYNRQLNLCVLIDETEEEKQARLAKQEKKGKVIDPEYRFATLQVPTVVPRLFEMHLSTGICFVPIEGIIQANLSSLFIGSSVLASGFYRVMRNADLDIDEDEAEDLLKEIEEQVRKRRFGEIIRMEINEDLDPRLLKLLTTSLKISKKDVFPVGGPIDLTFLMKVVGK... | 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)... |
A0A970RV93 | MKRDILVIFGGNSTEHDISVITAVEALNSMPIKGYNVIPIYIRDSVWYTGSRLFEIKSYIDFNPKGLNIVCVSGGKVYKAGHYKKFAGFCDADCAVLCTHGGDGENGSLQGLLEMNGIPYTSCDVRTSALCMDKHLTKLALNAMGVDTVEGREIVLPHGEGVIDEIESEFGYPVMVKPAEQGSSIGLTFAKNRKALEEGLTVAAAFGKRALVEKGLTDFAELNVAVATLNGKIEVSEVERPISANEFLTYGDKYMGGGKGMADLKREFPAKIDEKTAKYLKSTAKSVYEHLGLFGVVRMDFLKKDKVYLNEINTLPGSLA... | Cofactor: Binds 2 magnesium or manganese ions per subunit.
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Cell wall formation.
EC: 6.3.2.4
Subcellular Location: Cytoplasm
Catalytic Activity: ATP + 2 D-alanine = ADP + D-alanyl-D-alanine + H(+) + phosphate
Sequence Length: 365
Sequence Mass (Da): 40... |
A0A2G6PJ39 | MLQLLLTQWVDGYELGLILRILALLYCLTIAASVLMVILDRRNPTKTLLWVWVLILLPIMGLVFYIFLGQNLRRRLTARRYPDSRREVEDRFGTATIPLSEIPPQHDVLETHAYIATLLDHQGEAPVLGSNGVELYHEGEVAFASLLEDIRHAQDFIHMEYYTFTDDALGQRIAAELIERAGQGVDVRIIYDAVGSWGLSKSLLARLQEGGVRIYPFERVIFPLLGNRINNRNHRKIVVIDGTMAYMGGMNIAQRYITGSSIGQWVDTQLRIKGPAAHALHRIFLRDWAYVSGEAPSPDYCPIPVEGGNTPVQIITSAPE... | Function: Catalyzes the reversible phosphatidyl group transfer from one phosphatidylglycerol molecule to another to form cardiolipin (CL) (diphosphatidylglycerol) and glycerol.
Catalytic Activity: 2 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol) = a cardiolipin + glycerol
EC: 2.7.8.-
Subcellular Location: Cell membra... |
I4YFH9 | MDFSTPILNMLMNSRRSHYDPIDDQEQDIQETVELNPRHTDDDDGPPASILVEGEQRNSLDDNPPIKYTHSQQDTPLPLHQHRPVSRGMSPYQLAMWKWVNVQNLDKFLQDAYSYYLNKGIYCIVLTKALNLATVGFVFLFSTFLFGCIDYSAISHDGSLSDIVIPHCASSFSFITWIWLLAFGIFYIYQVLTFILSLKPLVDMYRFYTHILRIPNTDVKTISWEEIVSRISHIRQSNPLTAISSVGVSHGPVAKLDVLDVANRIMRQENYLIALFNKDLLNLDLPIRNKLLKKVLSFATSNGLTKTLEWNLSFALLGHV... | Function: Phospholipid scramblase involved in autophagy. Cycles between the preautophagosomal structure/phagophore assembly site (PAS) and the cytoplasmic vesicle pool and supplies membrane for the growing autophagosome. Lipid scramblase activity plays a key role in preautophagosomal structure/phagophore assembly by di... |
A0A7Y3HP51 | DYTICFEELFDVVNYFVVNVSSPNTPGLRELQDKGALLSLLQELQTLNNAKPNPKPILLKIAPDLTNEQLDDIVEVCTESKLSGIIATNTTISREGLKTSVNRIEEIGAGGLSGASVTERSTEVIKYIRKRVPQDFVIIGVGGIMNAEDALDKIKAGADLIQLYSGLIYEGPSLVKDINKKLASYYQSIS | 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.
Catalytic Activity: (S)-dihydroorotate + a quinone = a quinol + orotate
EC: 1.3.5.2
Subcellu... |
A0A943JXR8 | MAKLISKRYAVALFELAKETDKIDLFNSQVELIYNSIKNDKEFLTVLNHPRISGGEKFNLFQNIYKDNISEEILGLISIVVNKNRETEILEILETFLELVKDYKGITTAYVFSAIALNDEQLTKIKENLSKNLNKEIIIEASVKPELIGGLLINVDGKVIDNSIKRNLDDIKKSLINN | 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... |
A0A9E2BN17 | MVLQITGWATILFLLLASGLAVAASRTPLPPVDLPEASRLYDRHGRLIGSWFEENRTPVSSSQIPPLLKAAVVLMEDERFYEHHGVDPFGIARALYRNLRAGKVVEGGSTITAQLAKNLYLSPERTLSRKIKELLLTLKLEQQFSKDQILTLYLNTIYFGDAAYGVETASEYYFGKSVSELTLPEIALLAGMPRSPAAYSPRTHPDRAKARRDLVLDRMAQKGLITPKERDQAKAQPIQVARLAQPLPRSGYLMDYIRSEIATRYPEIAARLSRGGYRIFTTIDLDVQEAAAAALERLPVAGETAAGVRQPQGAILAVDP... | 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... |
A0A9E2GWV0 | MDTPRKHNFFAGPAVLPESSIKKAQEALWNFAGTGAGILEISHRDKAFDAVLEDTKVRAKRLYNIPEDYEVIFVQGGASMIMAMISMNFIHEGDKAQFIDTGTWASRAIKEAKRSKGNVEVLWSGKDTNYTYLPDLNTLKFDDDACLVHMCVNNTIRGTEFPDFPRIKAPLFADMSSDFFSRPINVKDFAFIYGGVQKNLGPSGCAMCIVRKDLLARVPENLSEMLSFRKYVEENSIYNTPPVFTIYMIDLAFQWLEEEIGGLGNMQKINQEKAALLYDLFDASEGFYRPTVTVKEHRSLMNITFRLPSEELETKILAEA... | Cofactor: Binds 1 pyridoxal phosphate per subunit.
Pathway: Amino-acid biosynthesis; L-serine biosynthesis; L-serine from 3-phospho-D-glycerate: step 2/3.
Function: Catalyzes the reversible conversion of 3-phosphohydroxypyruvate to phosphoserine and of 3-hydroxy-2-oxo-4-phosphonooxybutanoate to phosphohydroxythreonine.... |
A0A3C0NNM2 | MRWIEVCINTPGEEIDARCEELAALGAGGFVIENEEDFREFLENNHQYWDYVDKELEDSFSGVSRIKTYLADDEDGRRVLSAIRRACGEVAVSFVEDSDWENNWREYYKPIEIGEKLVVVPEWEEIPAGGRIPLRLDPGLIFGTGSHPTTRMCLAALEGYAAPGKRVLDLGCGSGILAIGALNLGCESAVGCDIDPKAPDVACANAALNGIGAGRFHVYAGDILSDASMRRTLGGGYDIVLANIVSDVIIPLSAIAGAFLAAGGVFITSGIIEGRQDEVAAALRANGFAISAHRCEEEWHCFECVRV | Function: Methylates ribosomal protein L11.
Catalytic Activity: L-lysyl-[protein] + 3 S-adenosyl-L-methionine = 3 H(+) + N(6),N(6),N(6)-trimethyl-L-lysyl-[protein] + 3 S-adenosyl-L-homocysteine
EC: 2.1.1.-
Subcellular Location: Cytoplasm
Sequence Length: 307
Sequence Mass (Da): 33159
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A0A940ARY0 | MKVRQILDKTEYTYIAGNMDLEVNGCAMDNRQVQPGDAFVAVIGQKTDGHKFISGALEKGASLIVIEESRREALSEELKNLVGETGAAIVAVNGSRRAAAEIAMQYFGYPSSQMQIFGMTGTKGKTTSTYILHEILERAGRSCGLIGTVENKIGSLAEKSKHTTPEAWQFQSLLRRMKDQDVSDCVMEVSSLGLKFFRTYGVRFEVGVFTNFLNDHISDGEHETEEDYFRSKLMLFDNCRIALVNKNTRRLDEVLAYAKVHTEKVYTYSISGDADFSVRGIRSGEQDGVPGMDFTLVTPTYQEKMFVPLLCDFNVDNALC... | PTM: Carboxylation is probably crucial for Mg(2+) binding and, consequently, for the gamma-phosphate positioning of ATP.
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Catalyzes the addition of an amino acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosyn... |
A0A4U8YJ13 | MRDEMKSSGGRRLLFWGLFAALTLSAGMAFASSGGGHAAEAKHWLTTDTARVLNFVVLMGFLFFVLRKPVSSALSGRIGSIRDELDTLEQKKADAEKTLAEYETRIATLESEVEVILGQYREQGEAARTRIMEEAKLHAAKLEEQAKRNIDHEFKAARTDLKAEIMALALEKAESLIQEKINTDDQEKLVDDYLNKVVVQ | 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: 200
Sequence Mass (Da): 22331
Location Topology: Single-pass membrane protein
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A0A929SRZ9 | MIIGIDGPAGTGKTTIAKLFEEKYNIKYINTGAMYRALAYKCLQNGIEKDDEEKILKILKDIKIEYVKKSVDGKILTSIILDGKDITEEIHRVDIAPIASDISKIVKVREYMVDLQRKIANEYVKNGEDVLLEGRDICTVVFPDADLKIYLDADTKVRAKRRLEELKQRGISQNLTLEQIIESIEKRDETDKNKTVGALKRTENQKYIDTTNRNIDDVITEILEEVERVRKENVR | Catalytic Activity: ATP + CMP = ADP + CDP
EC: 2.7.4.25
Subcellular Location: Cytoplasm
Sequence Length: 235
Sequence Mass (Da): 26988
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A0A095YUE7 | MKKSIAIIFGGCSSEYPVSLHSSYSVIKNLDDEKYDKHLIGITEDGCWYYFDDDIDKINDDTWHKGNIKKAFISPDRKDAGIWIADENRFIHLDAVFPVLHGKNGEDGSIQGLLQLAGIPVVGCGIEASVLCMDKYIAHRIANDVGVRTPKNIMIHEWDNPMEMKKEILKLGLPLFVKPIKAGSSLGMTKVHEEKDLVPAIEEAFKFDNQVICEENIEGFEVGCAVIGNKDLSVSPVDEIELFVDWFDYGEKYSQLKSKIHLPARIEDKLAKEVQNTALKVYRALCCEGYARVDIFIRTSKQNSDDSGKNISQNHMQEIL... | Cofactor: Binds 2 magnesium or manganese ions per subunit.
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Cell wall formation.
EC: 6.3.2.4
Subcellular Location: Cytoplasm
Catalytic Activity: ATP + 2 D-alanine = ADP + D-alanyl-D-alanine + H(+) + phosphate
Sequence Length: 359
Sequence Mass (Da): 40... |
A0A316LVB7 | MQYYTETMQPITVSQLNQYLKEKLEYDDALKTICIEGEISNLTLHTSGHIYFTLKDANAAIRAVMFRGYRASLKFIPANGMHVLLIGDVALYERNGSVQLYVQRMIQEGIGEVYFQFEQLKQKLAAEGLFDEAHKKSIPKYPEKICLVTSPTGAALQDMRNILRRRYPLAKIELCPTGVQGQDAVQEILRALFLADQKNADIILLARGGGSLEDLYVFNNEEIARAIYSANTPIITGIGHETDFTIADFVADLRAPTPSAAAELAVPNQQDILLDLLHMENRLSTAVASLIQTAAEKVKRAENTLNNGFSAKHTVLTQHL... | 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... |
A0A316MDQ1 | MSSERNDLLRYEETVARWLDRNRIGLRGKTVLAAFSGGADSAALLLLLNAMRARDGFSLCAAHVNHKIRGAEAERDARFCETFCAQRGIPFRLLTGDAPRLAAERGTGMEDAARVLRYRLLDKAAGEMHADWIATAHTADDHLETVLLNLARGGAARGLSGIRPVNGRIIRPFLPLERADTERIVSLFGASYVTDSSNASDCYARNRLRRSVVPVLRDLNADVCRGALENSRILREEDEFLDSLAAAALTEVEAAGALSARGLTELPAPLRARAARLWAEQAGITLDRRKTEAVLALAGAQCPSAVCDLGGGRVCRRNYD... | 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)... |
A0A7C6XRU8 | MLFKLTFKRGGIHPKDMKELAKDSAFEEMPTGAKVYIPLVQHIGAPCTPSVQVGDYVKVGQNIGLANGYVSANIHSSVSGKVLGFEARENAAGKRVRHIVIENDYKYDEVFFEPLENPTKEEIILRCKEAGIVGMGGATFPTHVKLEPKTPIKALIINGSECEPYITTDYRLMLEKPVEILKGVDLVKKALDTKQVFFGIESNKGEAIKNIIKHATDEQLSVFELKTKYPQGGEKQLIYALTKESVPNGGLPSDIGYIVLNVSTCLALYEAVCLGKSSYSRYLTVSGKGIKRPANLHVRIGVPYEEVVEYLGGTNEFVKI... | Cofactor: Binds 2 [4Fe-4S] clusters per subunit.
Function: Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane.
EC: 7.-.-.-
Subcellular Location: Cell membrane
Sequence Length: 434
Sequence Mass (Da): 47762
Location Topology: Peripheral membrane protein
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A0A1G1RPM1 | MKALVKPTRYLQGQIQALSSKNYTTRYMLVSALAEGTSIIHFPAHSEDSDAMRRCLKDLGAAIVENDHQMMITGFGKNPLPVKELNVGNAGAVLRFLMSIAALSQDVTFVNTYPQSLGKRPHDDLIQALEQMKVRIEHQQGKLPITIYGGNPRGGSIQVSGSVSSQYLSSLLFLTPMLVDDSEIEVLHDLKSKVVVRQTLEVLQEAGINLQYTDDLMHYAIPGMQQYQAKEYTVEGDYPGSAAILAAAAVTSSDVTVLRLKEESLQGEKAVVDVLKAMGVQLTHEGNKVTVHGRKQLQAGEFDGDQFTDGVLAMVAAAVF... | Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 6/7.
EC: 2.5.1.19
Catalytic Activity: 3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-carboxyvinyl)-3-phosphoshikimate + phosphate
Sequence Length: 343
Sequence Mass (Da): 37624... |
A0A352A399 | MANLKYGIMGGTFNPIHYAHLFIADEVKDLFNLDKIIFMPTGTPPHKNNLNIDAFHRYTMTKLAVANNNKFTVTDIEVLNQDISYTVDTMKKLTSLHPDIDCYFITGTDAILELPSWKDPKTLLSLCKFVSVNRPNFADDTLTDKIKDITDKFGGEIFLVNGPELNISSTQIRERVKEGKTIRYLVPNEVNDYILKNKLYTI | Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; deamido-NAD(+) from nicotinate D-ribonucleotide: step 1/1.
Function: Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
EC: 2.7.7.18
Catalytic Activity: ATP + H(+) + nicotinate beta-D-ribonucleotide... |
A0A7Y2XBB4 | MELIKKYFEDLSDLQLERLTALKNLYEDWNSKINVISRKDMDSFYCNHVLHSLSLAKLDEIKKTDKVLDIGTGGGFPGIPLAIFYPETRFTLVDSIRKKTTVVRAVKDALNLNNVTVINDRFENVEDNYNIIVSRAVAPALKLIQYTKKASSKSPKYLFIKGGDLSEEKQAVLKNYKGAQWNELELNSVFAEPFFETKKVVTLDFIKGNT | Function: Specifically methylates the N7 position of a guanine in 16S rRNA.
EC: 2.1.1.-
Subcellular Location: Cytoplasm
Sequence Length: 210
Sequence Mass (Da): 23948
|
A0A2G6G813 | MNRIIRVGSRKSLLAMTQTKLIIEELKHHFPEYTYEIVEITTTGDRIQDVKLDKIGGKGLFIKELEDAMAEGRIDFAVHSLKDMPAELEGDTKIVAISKRVNPMDVLVMPVGKKISDLREDSIIGTSSIRRERQILKWRPKSKIKMLRGNVPTRIRKLDEGEYDAIVLAAAGLIRLGLSDRITYTFSESEMLPSVGQGALAIEAPKNSPILHMLEILNDRKTQLETEAERAFSKSLGGSCSTPIGALAVLSGETIELKVMYGEQEKEGYKQMVKKCKVSQRNEVAIEMAEQLRRLI | Cofactor: Binds 1 dipyrromethane group covalently.
Function: Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps.
EC: 2.5.1.61
Catalytic Activity: H2O + 4 porphobilinogen = hydroxymethylbilane + 4 NH4(+)
Sequence Length: 296
Sequence Mass (Da): 33194
|
A0A1H2RXJ7 | MHIMEGFLPPLHAAAWTAVSVPFLVIGARRIARISREQPRAKLLLASAGAFAFVLSALKIPSVTGSCSHPTGTGLGAVLFGPSVMAVLGAIVLLFQALLLAHGGLTTLGANIFSMAIVGPWVAYGCFRLARPLGLGVAVFFAAMLGNLATYLVTTGQLALAFPDPVSGFAGALTKFGGIFALTQIPLAVIEGLLTVVVVNLLVQYSRDDLNEVGFDRRSGLGPELGSAGRA | Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis.
Function: Part of the energy-coupling factor (ECF) transporter complex CbiMNOQ involved in cobalt import.
Subcellular Location: Cell membrane
Sequence Length: 231
Sequence Mass (Da): 23854
Location Topology: Multi-pass membrane protein
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A0A3D5ZN73 | MTQYKRILVKVSGEALSGGGFGVSADGVAKVAQEIASVAKAGVQVGVVVGGGNFWRGRTSVDMDRGIADNIGMLATVMNGLALCDALTTAGVKAKVVSAVNIDKIARTATIPEVKALLDGGTVVVFAGGTGAPYFSTDTAVVLRACECGAQAVFCAKAVDGIYDSDPSVNPGAKKYDTLTYDKVLADNLKAMDATAIALAREFGVQIVAYGKDEPNGLVRILSGEKLGTVVR | Pathway: Pyrimidine metabolism; CTP biosynthesis via de novo pathway; UDP from UMP (UMPK route): step 1/1.
Function: Catalyzes the reversible phosphorylation of UMP to UDP.
Catalytic Activity: ATP + UMP = ADP + UDP
EC: 2.7.4.22
Subcellular Location: Cytoplasm
Sequence Length: 232
Sequence Mass (Da): 23748
|
A0A316NB32 | MYKIGIDLVDISRMQKCLENPRFLTRVFSVGEQAHICPNGRPNAQSAAANFAAKEAFSKALGTGVRGFFLNEVSVLRHENGEPYLSLTGRAKAIADERSLSFTVSLTHEAGSACAVVIACADSRALPALTDARIQRLRQHFGADFSGGIPLERGLIASVFPRRDAYSHKGSYGKLTIVAGCRNYRGAAALCTHAALRSGAGVVTLASVPEAVDAVASKLYEAVYRPLPENEEGTLSTLAIPLLLEQIKGCSALLIGCGLGWNEDTTAVVCTLIEEADCPIVLDADGINCISSCIDILRTAKRRMIVTPHIGEMSRLCRKS... | Function: Catalyzes the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. Together with NAD(P)HX epimerase, which catalyzes the epimerization of the S- and R-forms, the enzyme allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or ... |
A0A947YU38 | MSYVVLARRYRPQTFSEIVGQDHIVQIITNAINTSRIHHAFLFTGARGTGKTTSARLLAKALNCINGPTAEPCNVCQSCTDITDGKSVDVLEIDGATNTGVDNVRALREDIRYMPSFCRYRIVIIDEVHMLTTASFNALLKTLEEPPAHVIFIFATTEPQKIPATILSRVQRFDFHRVETQVLADHLTSVISRENFQIEPDAARLIAIQGEGSVRDSLSIMDQVLAQHPSDDVIKTPEVRRILGITDRETLINIVKHVLERNTPEILTKVHELFLNGIDIGNLTKSLVRQFRDFLIIRSIPDSGNLTDLSNEEKDLIIKI... | 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: 646
Seq... |
A0A9E1AT27 | MRKLMRSFATCFSMYSQIPMPRTKWEEDSMRYVFCFFPLIGLVIGILETGWFWIARQLEISSLLYVSVAVVLPILVTGGIHLDGYMDTCDALFSYGDREKKLEIMKDSHTGAFAVIYCGVYLLLSAGFYSGLYQSGSWIHIAVVGIGYLLSRTICGLATVWLPCAKNSGLAHMFQNNADRKTAKIALTIWFMGLICILGCLSLKAALFAIPLLGLGIIVFVSMIKKQFGGITGDLAGFLLEICELLLLLAAII | Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis; adenosylcobalamin from cob(II)yrinate a,c-diamide: step 7/7.
Function: Joins adenosylcobinamide-GDP and alpha-ribazole to generate adenosylcobalamin (Ado-cobalamin). Also synthesizes adenosylcobalamin 5'-phosphate from adenosylcobinamide-GDP and alpha-riba... |
A0A847TF28 | MKSAVTLFRIRKIDISIHWSFPLLMALILIIMALQRETLSSTLWALVGIIAVFSCVVLHELGHALTAAQYGIHTKSIMLLPIGGMASMERIPEQPIQEIKISIAGPLVNIVIAAMLLPFIAHYVPFWKYWTTFTNLNGNNFLLYLHTVNILLAVFNLIPAFPMDGGRILRGILALGTSYPRATAIAAFTGRIIAVLFIIVGLVSFNLLLPIIGFFIMVSGKAEETTTYLRYHAAGLLIRDITTTHFVTLPGGLPLQTVANVLLRNANPCFVVTDDNTPPAVVMRSDLLQALAKGHRSNPLRSIVSNNKIILQSDATVLDV... | Cofactor: Binds 1 zinc ion per subunit.
Subcellular Location: Cell membrane
Sequence Length: 374
Sequence Mass (Da): 41001
Location Topology: Multi-pass membrane protein
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A0A061EDP3 | MLNPIFPHSNKIYGSYFGPCHHMRFMALHWDHDIFPDGVGWRQEVRVHQLLHWLYLGLKFAGGGMEILRGFWNSPIGPKTTHFWGPVFNWSIPIAALLDTKKPPEMISGNMTAVMCGYSALFMRFAWMVQPRNLHLLVCHASNETVQLYQLSRWIKAQEYFLKKEEAETQGSKD | Function: Mediates the uptake of pyruvate into mitochondria.
Subcellular Location: Membrane
Sequence Length: 174
Sequence Mass (Da): 20222
Location Topology: Multi-pass membrane protein
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A0A3C1B4Z5 | MTRRLFYAVEFPEDIRQKLFQAGQELAAFADRGRWTRPENIHLTLQFLGECPAAWLPDLTDIARQAAAASHSFTMYFAGAGTFGRTSDILWIGIRPQPALSALAAHLADLLRLKELPCEARRFSPHITIGRQVRLDSRQLSAWSMPPLECRIDAISLMESTRIEEKLVYRAICREKLLL | Function: Hydrolyzes RNA 2',3'-cyclic phosphodiester to an RNA 2'-phosphomonoester.
EC: 3.1.4.58
Catalytic Activity: a 3'-end 2',3'-cyclophospho-ribonucleotide-RNA + H2O = a 3'-end 2'-phospho-ribonucleotide-RNA + H(+)
Sequence Length: 179
Sequence Mass (Da): 20367
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A0A943EVM8 | MSTFDQVKEIVANQLSIPAEKITAETTFEQVEADSLDVVEVIMSIESTFNIDLPDGDVEQFKNVGDLSNYVDKLLA | PTM: 4'-phosphopantetheine is transferred from CoA to a specific serine of apo-ACP by AcpS. This modification is essential for activity because fatty acids are bound in thioester linkage to the sulfhydryl of the prosthetic group.
Pathway: Lipid metabolism; fatty acid biosynthesis.
Function: Carrier of the growing fatty... |
D9XUE9 | MRGSRSRAPGDPGPAFPDRLFPDATFRPRPRPVGAARCAGIVADGRPLRRLPRIREREAFVGMYKALCRRPHGRSPRKGPTVAAKPVAERARRLVVLVSGSGTNLQALLDEIAATGTEEYGAEIVAVGADREGIEGLARAERAGLPTFVCRVRDYPTREEWDAALAEAVAAHEPDLVVSAGFMKIVGKEFLARFGGRFVNTHPALLPSFPGAHGVRDALAYGARVTGCTVHFVDDGVDTGPIIAQGVVEVRDEDDESALHERIKEVERRLLVEVVGRLARNGYRIEGRKVVIQ | Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide from N(1)-(5-phospho-D-ribosyl)glycinamide (10-formyl THF route): step 1/1.
Function: Catalyzes the transfer of a formyl group from 10-formyltetrahydrofolate to 5-phospho-ribosyl-glycinamide (GAR), produc... |
A0A972AEW3 | MKRVGIFGGSFNPPHIGHLKLVRAAAEQLALDKVLIIPALNPPHKDNSELASAQDRLNMCRLAFRNELFEISDIELRREGKSYTVDTLKEIKKERPGDKLFLIIGSDMLLSFHTWKDYREILNLATLAAAIREGESSRPLIDYKNKFLQGHNVVILEFTPIPISSTEIREGISKAEIKEFLVPEVKEYIESRMLYR | Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; deamido-NAD(+) from nicotinate D-ribonucleotide: step 1/1.
Function: Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
EC: 2.7.7.18
Catalytic Activity: ATP + H(+) + nicotinate beta-D-ribonucleotide... |
A0A972CXU9 | MEINSGIIIINKPKGITSHDVIYHVRRKLGIKKAGHTGTLDPMATGVLPVCFGNATRIIEYMESDMKTYSCEIQLGITTDTLDITGEVVSESDYSDITDAKVKKAFKAFKGEIDQVPPIYSALKVNGKKLYEYARKGEEVEIKSRKTFIEYLKIKTIDLENNVIAFDVKCSKGTYIRSICRDVGEALGCGATMTGLVRTQSGKFDIKNAIDLYDFDTISTDTINELVLPLDFSLDDLGLCIIDDESAWKFVRGQRIAERNVSLISDTKIDNRFAVYLNDKKSENFLGTAKYESENYCYKAVKVIGDINEDI | Function: Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs.
EC: 5.4.99.25
Catalytic Activity: uridine(55) in tRNA = pseudouridine(55) in tRNA
Sequence Length: 311
Sequence Mass (Da): 34790
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A0A2V2E5P9 | MILAINIGNTNFMIACDDEKTVYRYPVADLRVSDNFKDVVNDFLRCKIPGGVIISSVVPALTGTITSAIYEMFNIKPIVVNSDMHMSIDLSLYDKKFLGSDRIAVSEAVFDKTGKAGIVYDFGTATTINVVNSRGFFLGGAILPGVKMGLISLSQNTAQLPEYKDPLALPPLLGQNTADCLLSGAVYGNATMVDSMSARIKEFLQEDADVYMTGGNASFIAQACNTNIILEPNLLIQGLYSLYNKNKKEEK | 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... |
A0A970LHF3 | MRTFIGIELDTSVKEAIKSIQNRIRQSSVKGRFKHVDNFHITIKFLGEISNKDILQIDEILNKAALSNRAFELKIDKLGYFGKEESMRVLWLGLGTGLNNLRILYKSVEEGLAKKGFKKDNRAYTPHITVAQDLTLLKGFNVLRDDIDLNIIPDIGVKAVSLIKSEQIRGHRVYTPISTFKLKEL | Function: Hydrolyzes RNA 2',3'-cyclic phosphodiester to an RNA 2'-phosphomonoester.
EC: 3.1.4.58
Catalytic Activity: a 3'-end 2',3'-cyclophospho-ribonucleotide-RNA + H2O = a 3'-end 2'-phospho-ribonucleotide-RNA + H(+)
Sequence Length: 185
Sequence Mass (Da): 21069
|
A0A927SB26 | MHTVIALGTFDGMHPGHRAVISRAVQEAKQTGAKSMVYTFSSIPRALFVKAPKMLMPPDERKEEILKMGVQDVVMVDFTREIAEMTPEAFVKMLFDAYCPLAIVAGEDYTFGHRAAGNMETLKKLGKEMGFKVITAETVRVKLPDGTLGEKISSTDIRKALEENKISLAEHLFKGEIL | Pathway: Cofactor biosynthesis; FAD biosynthesis; FAD from FMN: step 1/1.
EC: 2.7.7.2
Catalytic Activity: ATP + FMN + H(+) = diphosphate + FAD
Sequence Length: 178
Sequence Mass (Da): 19730
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A0A927S866 | MTHLIERIHLGLKELGVAHTQQQTEQLFRYLDMMLGVNQYMNLTAIRDPETAIDLHLLDSATLLTVVPPHKGDRIMDVGTGGGLPGMVLAILRPDCHVTLCDATRKKVEFLNGVIETLGLTNAVAIQGRAEEIALSDDHRDGYDYVTARAVAALNLLCEYCLPLTRPGGVFVAMKGKRGLEELNEAKNAYRTLCASVPQLIRSPLSGTECCIIKAKKARPTPKGYPRSGGAMRKRPL | Function: Specifically methylates the N7 position of a guanine in 16S rRNA.
EC: 2.1.1.-
Subcellular Location: Cytoplasm
Sequence Length: 237
Sequence Mass (Da): 25942
|
A0A943UFK4 | MEHIKQDQIINIPNTLTVIRILLLPVVVWRFVVGDATGALIAYLAAMLTDALDGIIARKFNQITALGKLLDPLADKLSLVTLLGLFVSDGQIPLWVLAIILLKEAAMVIGGGVALKRGIVVYALPIGKVTTVVFVLSIVARFLSWTQIADTLLWISVALSMVALIWYAVDLMKKLGTKADSTK | 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... |
A0A943IY36 | MGTPEFAQIQLQALVTLCAEKGWELCGVFCQPDRPKNRGKRLLPPPVKEYAQGCGLSVFQPQTLRDAAATELLHRLDPTLIVVAAYGKLLPPEYLHYPRFGCVNVHASLLPRYRGAAPIQRALMAGETETGVTLMQMEEGMDTGDMLSAVHVPIEMQDNAGMLFDKLAKAGAALLTDELPKLFAGQLTPEKQDDALATYAPKIEKQEAAVSFDLPAKTLHNQIRALFPSPRAQACLVRENGEQMMLKLDESCVLDEETPPAVPPGTVVQTDAAKNIIAVACGKGVLGIVSLTPLGRGHMHAGDFIRGRKISCADRFVRSE... | Function: Attaches a formyl group to the free amino group of methionyl-tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus.
EC: 2.1.2.9
Catalytic Acti... |
A0A356AVN7 | MSETGKRILLHACCGPCAVWPVELLREEGFQPEGYFYNPNIHPDKEFKRRKETFLSYAAIKNLKTIVDDDFKQDRWEKYSPEDLSRCVMCYTLRLEKVAQFAKENQFDAFTSTLFVSPYQNHEL | Pathway: tRNA modification; tRNA-queuosine biosynthesis.
Function: Catalyzes the conversion of epoxyqueuosine (oQ) to queuosine (Q), which is a hypermodified base found in the wobble positions of tRNA(Asp), tRNA(Asn), tRNA(His) and tRNA(Tyr).
EC: 1.17.99.6
Catalytic Activity: AH2 + epoxyqueuosine(34) in tRNA = A + H2O ... |
A0A2N2I7S9 | MHLHRKPSISSAFLRFTSIISTLSILLLGALWIGDALYHFDEDSALLRQEFLEARKKEVRQEVDVFLAKVKDQRASLDDVLRSDIRARVHEAWSVADNLYRLNAASKNEKELAEMIREALRPIRYKNGRGYFFATGLDGVEQLFSDRPELEGHNLLDMRDREGKPVIRDMIRIARQEGEGYYEYLWTKPGSKDNRHRKLAYIRHFPGLDWLIGTGEYLEDVENDLKARVLRNLEYERFGDGGYFFAGTLDGISLVGPTKGRNMFEVTDANGLKIVQELARTAKNSGGFVEYELPAFENNIPHRKLSYVTPVEDWNWYIGA... | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Membrane
Sequence Length: 942
Sequence Mass (Da): 106421
Location Topology: Multi-pass membrane protein
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A0A943XV03 | YIYDANGNLITTYSGTENREYATLDEIPLQLQQAVIAVEDVRFYHHNGIDLKRILSSFVGNMSSDKTSGGSTITQQLIKNQLLSSERSYKRKIQEANLALQLEKKYDKDQILEAYLNTIPLGGTLYGVKVAAKDYFGKELNELTLRECACLAGITQYPWLYSPRRAYYVTGKVDALNLRIETVLNRMYTAGYISLEEMNEALNDEFTVLEKSSATEIYDMPHFVEYGIHDVVTHLLKARGLEDTTQNRSAIQNELRTKGYSIYLTVDPDVQHKLQDTVANYDGYYRFSGSDSVVKQSGSNGTTVEIRQPQAAAVVIDHKT... | 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... |
A0A7S9E0E2 | MRKIAIFLPLALIKFYQWCISPMLGQRCRFHPTCSFYAIDALKTHGFVIGGWLSCKRIIKCHPLHPGGYDPVPEKHDTKHSK | Function: Could be involved in insertion of integral membrane proteins into the membrane.
Subcellular Location: Cell membrane
Sequence Length: 82
Sequence Mass (Da): 9451
Location Topology: Peripheral membrane protein
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A0A3D5ZSW8 | MFFHNLKIEGEGKVNYKKIARAVYKELKQKAKLKAEVVLVNEEEIKKLNAENRNVDKVTDVLSFPALDGIRNKILDPKDYPYELDGDRLFVGSVALCLEQAKRQADELGHSTEREYVYLVIHGLLHLFGFDHMTDEDKKEMRSHEKSILKRLKIEEEE | 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: 158
Sequence Mass (Da): 18415
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A0A356B1G3 | MWYNKFQIKKKATGELQVTLYLDVLFIENLVINFFLLKAVTVLLRLQCKNIRLLVGAFVGGIYVVAMVLWPDRIFFRFSSKVLLSVVIVIISFQPQSIKTFLKTLVVFLMSTFVLAGILVALDSTYTGVQIGNVLVAFLLLVMIFLLLREWIMKKYKNCEYHIRIWYSQQNITIPGIVDTGNFLMEPMTHTPVIIVEMKALELFLPEDMISIIKTGQWTEQKEERPVEDWQLRIRYIPYNTLDQKCQVMTGFAPDYVDIWGGDLPEVRKKAVIGFSKNRLSKGNAFKALINPTLME | 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.-
... |
A0A356XH68 | MFIEKLHLRIEKCKNPVCAGLDPRIGYVPEFLRRNESESNAILRYNRMLIDALMDCVPLVKLQMACYECYGTEGMELFIKTAEYAAEKGLVVIADGKRNDIGSTAEEYARAYLGSGSNPLDALTVNPYLGEDGILPFVESCRINGKGIFVLVRTSNPSSSQLQELVLANGRMVYEKVAELVENWANLPGMRREDKGYSCVGAVVGATWPEQAMKLRQIMPSALFLVPGYGSQGGTADGAAACFDNQGRGAVVNASRSILCAWQSPKWKAKYSPDQFDEAARAEALSMAADLRGAIDARSHEIKWKGVRHEGSPDA | 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: 315
Sequence Mass (Da): 34496
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A0A354UNT7 | MDFKRQKFLVFGLSLSGRAVAEKLLSLGATVFAYDDGAPRIEKTMRYLSEKGCVSALNSPENFIRNSDVVVLSPGVPIDNPLVVKAKRMGKRITGELELGYLFSRATFVAVTGTNGKTTTCSLINAALQTANEKSFLVGNIGVPLTSKSDEINALSYPVAVTEVSSFQLETLSSFTPHIAAVLNVTPDHLDRHYTFENYKFLKKKLLANLRESEYAVLNYDDEVTRNFAENARFKPVWFSTEKEVDGAYKKGDELYFYGEKVFDLKSFTLSGLHNEKNALAAIAVLKILNVKNEDIVKAFSTFKGVRHRIELIYTAGAVN... | 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-... |
A0A975CW97 | MNRTIKRVLSALVIIISITAVIIIAFSNPEMKNAWKALASMDLKWVLGLFLCWAAYAGFEGCGTWSYLRSKGYKINLGRVIGVALIGFYYSNITPSAAGGQPMQVNSLRKAGIPVAYGTTAVTIRFVSNQLTICMMTLGLLIANRTFAYNQLGGLIWAARIGWAINFIAVPLVLLAAFKRNLIQAVIEWLISLLHKMHLVRDKEATVAKITEILDSYHAAMIALIHSPGQILMQILFSALSMLGMTGSIVFTYYAFGLSGTPWYQILTMSCLLFVSASYTPLPGASGAQEGGFMAYFAGIFTDGTIGVGLLIWRFFTYYM... | 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... |
A0A894JQT5 | GSIGGLNQISLRKILAYSSINHIGWMLTSFIINEIIWIIYFLIYSFISLSIIIMFNKFNIFMLNQLFMMMNNSYIIKYFMLMNLLSLGGLPPFLGFLPKWMIIQNLSLNNFLLITFMIMMTLITLFFYLRISYSSLMINNNELNFLMIMNKNNYNNNMLINMLSFISINGMILYTIFINFY | Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed... |
A0A149VR58 | MQGLHYVIVPAAGIGARIGAAVPKQFLKIGQHTVLDYTLQALLSCVTIKHVVVILSPSHDLYKNQLDTKDERVSFITTGSDTRAKTVLNGLHYYSSFVRDEDWILVHDAARPCLQLADLERLFKELEQDPVGGILALPISDTIKQADGKERIDFTRDRKDLWASQTPQMFRYKLLKEALAQHHIDTTDEASSIEKLNLKPKLVQGSSTNIKITYPEDINIATYILKAQGRYE | Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 2/6.
Function: Catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP).
EC: 2.7.7.60
Catalytic Ac... |
A0A1H2Q8R2 | MSSLLPRSFHRSILLSVGLLMTLVVVLAILSMLIGGSVGRATEGFAAAVNQAGSLRMQSYRIGMALADARAPADLSADRVAALAEELEQRLASPRLADIIPRRAGEEIRDAYEGIRADWNERMRPLVSADIARLRVLDPGTSRDAPAMSYLAAVDGFVEQIDVLVGELERITEARLAMLRVVQAVALVLTVIVVLVTMVLVIGRVIQPLAELLECADGSRRGDFTRRTRFTGSDELGRLGDAMNRMAADLSQLYTDLEGRVAEKTRDLERSNQTLELLYGVGQVLHESPISTPMFERVLQEIRVKLRLRAVTLCLDEAPD... | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Cell inner membrane
Sequence Length: 657
Sequence Mass (Da): 71818
Location Topology: Multi-pass membrane protein
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A0A2V2F007 | MKANFHTHSVYSDGADTLTELVEAAIEKGFGALGFSEHSYTYFDESYCMSRENTLRYISEVRALQEKYRGRIALYLGIEQDFYSTESVDNYEYVIGSVHYLKKGGHFLPVDESTEDLARFRDMYYEGDIYALIEDYFAAVGAWAEKKCDIIGHFDLITKFNEKQPLFDTEHPRYKMAAQKALDKILAADKTIEINTGAMARAWRSSPYPDAKWLDYIVKKDGRLILASDCHDKKDLDFAFDTLAPYREYLSIKPFKTL | 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: 258
Sequence Mass (Da): 29782
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A0A2V2EMP4 | MMLKVTAEEIARALGYNYSGLNDKIITSVTCDSREVTEGSLFIALAGEKTDGHNYIAKAYENGAVAAVVSREIAAPANLALIYADDGVKFLQELATWVRSKIKAEVIAVTGSYGKTSTKDLLGGIFSAKNACVSKGNNNNEIGLPLTLCRAAEDTEAVITEMGMRGLGQIKFLCEIARPKYAIITNIGTVHSELLGSKENIAKAKCEILPFIPNDGAAVLNWQDKIFLEPYLKDCKGEIIWYNCNDSKEGACALARNLSSEGSSFIFKWQDYSFKIELTVAGEHNIINAMAAIVVALKCGLAIDEIQSGLKNVGLSGMRL... | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Involved in cell wall formation. Catalyzes the final step in the synthesis of UDP-N-acetylmuramoyl-pentapeptide, the precursor of murein.
Catalytic Activity: ATP + D-alanyl-D-alanine + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-2,6-d... |
A0A948E1Q8 | MEYSGKYKIIGLTGCIGSGKSTVGRLLESMGFRRVDADELSRSVMNRNLDLINQLVDEFGPSVINNSGSLDRRALAQIVFSSDLALKRLEDIVHPVIEKEALIQLGNGPWPVVFEVPLLFQTKQDRHTDLTVVVKSPVDLRMQRVIVRDSSDEASFNARNSRQNSEDWLLERCDVVILNQGSLDDLTNRVRRFADDLISDSIAGIY | 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... |
A0A7S3XC15 | MSQVRTNFCRNVCGIHLVQRTAVGNERIRHVPTVGIFPRRVETRKERWFSQLRMAAGTRSMSTEIDPVLRSMHEAIPRLDATKHKGQCGKIAVVGGCEEYTGAPFFAAMTALYAGADLSHVFCGKSASSVIKGYSPDLIVHPYLPDDEGNASGGHGVEEEEIESVSSHCANRVKEWIPKFDCLIVGPGMGRSKAMLATVAKVLPSARQAEIPIVLDADGLFLLTKDLDLIAGYEKAILTPNVVELQRLAHAAGLPHTSPEETACNLSHKLGGVTILSKGPVDFVCCKNSSLSCTEEGSPRRAGGQGDVLAGFVGLFSAWV... | Function: Catalyzes the dehydration of the S-form of NAD(P)HX at the expense of ATP, which is converted to ADP. Together with NAD(P)HX epimerase, which catalyzes the epimerization of the S- and R-forms, the enzyme allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or ... |
A0A972F7K9 | TMAATYPGVDTVLAAMSGTKGLMPALEAVKKRKRIALANKETLVMAGRIFMEAVKRHGAELIPVDSEHSAIFQCLGGKREFLSKIYLTASGGPFRGRSFEELENVQPEEALKHPNWSMGAKITIDSATLMNKGLELIEAMHLFNLKPDKIEILVHPESVVHSMVEFVDGSVLAQLGVPDMRLPIQYAISYPKRLPSPAKRLSFKENSSLNFFEPDLKAFPCLRLAIEAAKSGGNSPAILSAANEIAVSLFLQKRIGFNDIYRLVADTLSSLPYESKPSLEALLSYDRRARSFLEEKYS | Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 1/6.
Function: Catalyzes the NADPH-dependent rearrangement and reduction of 1-deoxy-D-xylulose-5-phosphate (DXP) to 2-C-methyl-D-erythritol 4-phosphate (MEP).
EC: 1.1... |
A0A965XV51 | MIEFAQAVEITMANLVSGKQGINLLENATGKILANDIFNDRDTPPFNKSAVDGYAFSLGSYSGIPMGILETIPAGKAPLQKMREGFCSKIMTGAMVPEDADCVVMVEDTYCTNGKVTIEQPKKGVSKWDNICLKGEDLRQGQLLLSKGTLLRPEHIAVLASAGIWQVPVIEYPSAAILSTGDELKEPAETVEYYQIRNSNGWQLLSQAKRAGFKATYMGIAPDSASGLEKSISAAMDKHDVVVMTGGVSMGEFDFVPDVLTSLGFEIMFDRVAVQPGKPSTFAVRYGKNGADETASKAVFALPGNPVSSYLQFELLVRPY... | Pathway: Cofactor biosynthesis; molybdopterin biosynthesis.
Function: Catalyzes the insertion of molybdate into adenylated molybdopterin with the concomitant release of AMP.
EC: 2.10.1.1
Catalytic Activity: adenylyl-molybdopterin + H(+) + molybdate = AMP + H2O + Mo-molybdopterin
Sequence Length: 405
Sequence Mass (Da):... |
A0A7C6BFH3 | MLEFLSGAIALVIVLLLMPGFIKYMRERGMIQPDYDLGPDSFKKKDKPPNMGGLIIALAVLVASLIISLVSGNINVLLLLFVAAFGGLAIGFADDFIKDVQQHHDGLRPRYKLIGQTAVGLLFSIITVNLQGSAIHLPFTKTTLDLSYAYIPLMTLLYVFMTNSANLQDGVDGLMSSVTLAGSAALGAIALIIKGGSLGDPAIAFACFALTGACLGFLFFNQHPARIYMGDTGSMFIGGLLTGATMLLRLQIWLVPLCFTMIMSSVSVIAQRLYFKATGGKRLIKMSPIHHHFEMIGWSENKIARRYTLTIIALSVLAAL... | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Catalyzes the initial step of the lipid cycle reactions in the biosynthesis of the cell wall peptidoglycan: transfers peptidoglycan precursor phospho-MurNAc-pentapeptide from UDP-MurNAc-pentapeptide onto the lipid carrier undecaprenyl phosphate, yield... |
A0A7C6XRR2 | MLESLIKKYFDKYKIEYESNKIESFVEYAKYLKESNKRINLTSIVEDEDIVIKHFLDSVIAYRKFPLNSKVIDIGSGAGFPAIPLKILRPDLDFLMVEATRKKVNFLNSTIELLSLDNIEAIHERAENIGRYEKYREKYDICTARAFAPLRELVEYLAPFVSVNGKIIAYKGPEVDKEIKEAESALEKLNLKILDVERLDLEDNKRNIIYIQKTNTLDAKYPRSHKKITTNPL | Function: Specifically methylates the N7 position of a guanine in 16S rRNA.
EC: 2.1.1.-
Subcellular Location: Cytoplasm
Sequence Length: 233
Sequence Mass (Da): 27082
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A0A7C6TQB7 | MSLLYTLGLTGASGSGKGYISEIFARRNVESLDTDALYHSLTGSNPALRDEALMEELKSEFGNDIISPDGSLCRPALRERVFNSPEKLKRLNEIAHPHVISAALSWIKEQRKSGRKYCIIDAPLLFESGMNDYCDWTIGVIADRALRVSRIIKRDGIFPEAAEKRISNQPDNEFYQTRCDFIIVNDEGHNPELQVDIILQKLNFMV | 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... |
A0A927W7C8 | MNIREYMKDHILVADGALGTMLQKYGMETGTMPDSIQIERPELLERIYREYYRAGSDFVLTNTFGSNRYKLAGRYTVEETVNAAVAAAKRAAEAEREARMAELEGRCAAGSAVGGADPKRPGPWVGLDVAPIGKLMAPAGDLEFEDAVTMFKELITAGVNAGVDLIMLETFTDIYELKAALVAAREVTDLPVFASVTFQEDGRMLMGTDPLTAVAILQDLGADVIGLNCSLGPKQMVPLVRQFLKYSKLPVIFQPNAGLPQIDENGNTVFTVGPEEYAETMLQMIGEGVAVAGGCCGTTPDHIAALRKGLEKADFRPDRL... | Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-methionine from L-homocysteine (MetH route): step 1/1.
Function: Catalyzes the transfer of a methyl group from methyl-cobalamin to homocysteine, yielding enzyme-bound cob(I)alamin and methionine. Subsequently, remethylates the cofactor u... |
A0A8T4VWF2 | MLHIDGSYGEGGGQILRTAVSLSVLTNTPIEVTQIRANRSNPGLRPQHHLALLVMKELSNADTSGLQIGSSSISFKPGDIRPGSYEFDIGTAGSMVLVFQTILLGVLLTNKEIHVRLHGGSDVKWAPSWDYFTQVFLPVLHQMGYSVSAQLNKRGYYPKGGGDAELWIHPMKKDLSAIVFESFYPDHVFGTVHLSNLPDHIAKRMKHEVVKTVVPYDITAQIQTEKSDALSPGVGLTLWTEMESGKFGSVVLGEKGVSAEKVGKKAIDCMLSDINSKATVDSFLSDQILPYVVLAKANSLFYVRLLTGHFKTNLWVLQQF... | Function: Catalyzes the conversion of 3'-phosphate to a 2',3'-cyclic phosphodiester at the end of RNA. The mechanism of action of the enzyme occurs in 3 steps: (A) adenylation of the enzyme by ATP; (B) transfer of adenylate to an RNA-N3'P to produce RNA-N3'PP5'A; (C) and attack of the adjacent 2'-hydroxyl on the 3'-pho... |
A0A3D4MSZ7 | MTKPQSTAAYVLRLTLTLFLITVIVAGLLAFVNYLTADTIAEHTAEAARSAMTQVLAADDYTELPVSDAQAATGVTAAWSAGEAGTVVRLTTNGFGGAIDLMVGVDNENRVTGVAIISHSETASLGANCTREDFRAQFAGKTGELAVSKDGGDIDALTGATVTSRAVTRAVNAALAYAGEVQK | Function: Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane.
EC: 7.-.-.-
Subcellular Location: Cell membrane
Sequence Length: 183
Sequence Mass (Da): 18784
Location Topology: Single-pass membrane protein
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A0A316M4I5 | MQKQEKLNELRAAKHVNILAIETSCDETAAAVVRDGREVLSNVLYSQIEIHKQYGGVVPEIASRNHVEKLPYIVHGALEQAKLDWDQVDALAVTSGPGLVGALLTGVSYAKALAYALDKPLIAVNHMEGHISANYITHKQLEPPFICLIASGGHTNIIKVTDYCAYEILGSTRDDAAGEAFDKVARVLGLTYPGGPNVQRLAEQGNPDCYVFTKPFHGESHLDFSFSGIKTAVINLVRGFEVRGQEYRKADVAASFQKAAVNLLIENVFEAARRTGIKKVVLGGGVSANAALRARALQQENYQVYLPDLRYCTDNGAMIA... | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Is involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, togeth... |
A0A3D5WSQ6 | MKLLLSTSNEDKTRELKSLLEPLGHTVYTLKDYGLKIRVEAKDITFFQNALLKAQAVSKVVDIPVLGDESGLVVPALNGEPGVYSARYAGEVHNNVANIQLLLRKMENITDREAYMQTVLVLMYPDGKYYYGEGSAKGSITRSRRGLNGFGYDSVFYSPQLKKTFAEASFVEKQSVSHRLQAVNDLFRKVNENVGAMNSKK | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Pyrophosphatase that catalyzes the hydrolysis of nucleoside triphosphates to their monophosphate derivatives, with a high preference for the non-canonical purine nucleotides XTP (xanthosine triphosphate), dITP (deoxyinosine triphosphate) and ITP. Seems to function as ... |
A0A380NLN0 | MSRIAVIGGGLTGLTAAYYLSQAKPDWQIDVFEQENRFGGKIKTKRVDGYVVEVGPDSYLARKQSMTDLINELGLGDTIVTNATGQAFIYDRGAMYPLPGGAIVGIPTEFVPFAKSTLLSWPGKIRAMQDYFKSPYPTEGDVSIGDFFKYHLGQEMMDKLIEPLLSGIYGGDIYELSLDATFPEFHSLERKHGNMVKGMLAARKQRASSHIKPSGQFRQLTGGLESIIDALVGQMPANVTLHKSTPVTSIEKTKQGYVLGGTVKSPYNEVIITTPPQSYQAWFSEDKKFSELMNMDLSSCAIAVMAFDRANFDASLDGTG... | Pathway: Porphyrin-containing compound metabolism; protoheme biosynthesis.
Function: Involved in coproporphyrin-dependent heme b biosynthesis. Catalyzes the oxidation of coproporphyrinogen III to coproporphyrin III.
Catalytic Activity: coproporphyrinogen III + 3 O2 = coproporphyrin III + 3 H2O2
EC: 1.3.3.15
Subcellular... |
A0A0D3M4E0 | NVGFKAGVKDYKLNYYTPXYXTKDTDILAAFRVTPQPGVPPEEAGAAVAAESSTGTWTTVWTDGLTXLDRYKGRCYHIEPVAGEENQFIAYVAYPLDLFEEGSVTNMFTSIVGNVFGFKALRALRLEDLRIPHAYIKTFQGPPHGIQVERDKLNKYGRPLLGCTIKPKLGYPAKN | Cofactor: Binds 1 Mg(2+) ion per subunit.
Catalytic Activity: 2 (2R)-3-phosphoglycerate + 2 H(+) = CO2 + D-ribulose 1,5-bisphosphate + H2O
EC: 4.1.1.39
Subcellular Location: Plastid
Sequence Length: 175
Sequence Mass (Da): 19441
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A0A927SPL5 | MKKTFISFLTIILLITPTLAITNKPVINATSAIAIDSNSFRILYEKNAFSKKPMASTTKIMTIIIAVENNNLDEIVTISKKAAGTGGSSAHLKAGKQIKLEELLYGLMLNSGNDAAVAIAEHTADSVENFAKLMNKKAIELGALNTNFVTPHGLDTNNHYSTAYDMAIIAAYALKNPIISEIVNTTSKDMKFTDGTSVFLSNTNKLLSLYNGANGVKTGYTAMAGRCLIGSATQNNWQVITVVFGEPTSSSRLNDTIKLLDYCFDNYSLVDLCELYTPQFKINIKKGKKINVTPKYANSLVLPLTKSEEKSITIKKSYSD... | 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... |
A0A927SYU7 | MLLFDLLNNILNKNEYEVFPDNMLDIDVKGISSDSRKVLKGYVFASINGTKADGAQFIPDAISHGATVVLTQDRNDAVYCDRAYVIVVNDVRLVLGKMAVKLYFNSSLPLDIIGVTGTNGKTTVSHYVSSILNECNIPSAVLGTLGASANGIKTPSDRTTPDAISLCEYVSDFARHGAKVLSMEVSSHALELKRVCGVHFKVSIFTNLSEDHLDFHSDMESYGKAKAKLFEQCDVAVINIDDEFGKKLSSSVNCRSVTYSLYDDNADYFASNVVHSVTGSKFVLNSKSAQYSVSIATPGDFSVMNALAALAACREYGIEL... | PTM: Carboxylation is probably crucial for Mg(2+) binding and, consequently, for the gamma-phosphate positioning of ATP.
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Catalyzes the addition of meso-diaminopimelic acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in... |
A0A970EZK3 | MSAANHLMEEIKLENDIRILIADSSPEFRAILKESIGAEQGMSIVGETSNGLEVQTLIDKKSPDIVLMDVVLSGLDGLGVLKQLSQRRMEKKPAVIILSYFLNEHTISEASDLGAKYFMLKPFDINSLIEKIRSFCAHPKAISIEKGRQIRNVNLEAMVTNIIHEIGVPAHIKGYLYLREAIILAVKDMDIINAVTKVLYPSIAKTFNTTASRVERAIRHAIEVAWDRGDIETLQNFFGYTVSNTKGKPTNSEFIAMIADRLQLQLKTGS | Cofactor: Binds 1 Ca(2+) ion per subunit.
Function: May play the central regulatory role in sporulation. It may be an element of the effector pathway responsible for the activation of sporulation genes in response to nutritional stress. Spo0A may act in concert with spo0H (a sigma factor) to control the expression of s... |
A0A948E0X0 | MVRFFKNSNYDFMGGRKKAAAISMTVIGISVLVMIANLFIPGRGSILNWGIDFLGGTQIQLEMPKDSNKEAIAKAMDSLGYKDFDVVKFGSAKRYYIRMRSFSSLADDKKIAIENAFKAKYTTNFFRVRFSESGDSVKVRFFKPVDLKEFKPILDQLGINHKLPKVRLSQEAIEYKAKVKRNEKAVWEKDHSADLDFAEVTGVSPMKNEYTITLNSISEKLQTELNGKFGFKLDNNAEGGVKVLSVESRGPQVGRRLRVNGILSLLYAIGFILLYIVIRFDLKFAPGAVVALVHDVMITVGIFAALYIEFSLPILAALLT... | Function: Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. SecDF uses the proton motive force (PMF) to complete protein translocation after the ATP-dependent function of SecA.
Subcellular Location: Cell membrane
Sequence Length: 489
Sequence Mass (Da): 54952
Location... |
A0A975CTX4 | MRLFTAIQPLPGFRAALEDLQQRLREAGVTGKYREPDGLHLTLAFIGEWPEDITELLPVVQKPFCVTLSHLGIFPEANVLWAGVEPCEELDLLAKQVRHCLADAGIPFDRKSFSPHITLARKPFVPEKVILSEIQVPRVSMIVDDVSLYRSDRGKDGMVYTVIGSSSENAEW | Function: Hydrolyzes RNA 2',3'-cyclic phosphodiester to an RNA 2'-phosphomonoester.
EC: 3.1.4.58
Catalytic Activity: a 3'-end 2',3'-cyclophospho-ribonucleotide-RNA + H2O = a 3'-end 2'-phospho-ribonucleotide-RNA + H(+)
Sequence Length: 172
Sequence Mass (Da): 19269
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A0A356F1E3 | MGQKLDDYKKSQVKIFGFSWETKKFWLTIGLSLGVLLGLIALTLFGVNISWYGVMIGIGFLIALVLAQQLFKERDLSSEYPYTLIWWIFPLSIIGARIYFLIFDGSFTGIMDVIRVWDGGLAIYGGVIGGFLGLVISCLVHKVNIISTTDCVAPVLSLGQAFGRIGCIFGKCCYGVAVTNRSLQWFPIALYVHGGYHYATNFYESILDLALFFGLTVLLRKVKIKGIVTFAYLFGYGLIRFILEFFRDQAQTLYLGSFPVSQIVSIVCVIAGVVGISILLLVNNKKSPKKTEK | 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,... |
A0A972CWB7 | MKLERNKEDELRVINESCNAIMVIEISSHRVIFFNKAAENLFYNKMQVGIKCQELFFGRRTPCEDCMIDNMKYGRKEIFHADTGRHLEIVLKKIPWEGKETVVAYINELTSSKEFEKTKDELLELIDNVPLGMGVFKCNALKEIVPIKVSKSIKDKWGINVEINVNIEKQFKNFNIHSDDKRQLKIDINKATKNLSHSFDGVYRCFNINEGEYRHVRITASGIKTGASDIIFYVSFIEVDKEYRALGVCEKNQRDVDLIFELADMNYWEYCFSEDKAKHVMMHGELTNLDYDMENWPETVIEKEIVHPKDAQIYRSQFLE... | Function: May play the central regulatory role in sporulation. It may be an element of the effector pathway responsible for the activation of sporulation genes in response to nutritional stress. Spo0A may act in concert with spo0H (a sigma factor) to control the expression of some genes that are critical to the sporula... |
A0A9D5M4B9 | MNRFRLAPMCGVTDHVYRGICVRLGCEQTCTEMISAMGYCCAPNQRATQELMIRNPVETRLIVQLFGKDPAIVAEAARRMEDTGRYDGIDLNMGCPAHKVASSGEGAGLMLHPDIAFKMMRQTVEAVSLPVTVKMRLGWDDRHLNAPEMAQMAQEAGIREIAVHGRTRVQQYAGEADWEAIREIRSRVSIPVIGNGDLFTAEDGIRKLEEGYADGIMIGRGAMGNPWIFRELQQLAAGREKTDVTLDEREEMIRTHYEAMLEAKPDFVAVREMRKHISWYIHGLRGAAQIRNRINRMAEPDEVLTAMHLYFEELRQAA | 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: 318
Sequence Mass (Da): ... |
A0A2G6G9Z2 | MAIFIKIIYFILVFSAIVFVHEFGHFIVAKMYKIEVEQFMLGFGPKLIKFKKGETLYSFRAIPLGGAVMLAGETGESDSPNTFKSKARWKQFTVMLAGPFMNFVFAILLLFAVYSFSGQPSNLVTYLNDNSPAMKAGIILGDRIVKFDDTKISNWNDIVEFIKNSKGEKISVTVKRDNKLISNIVVTPEKNIKEDRFIIGVSSNEKSISMAAVSTKNTFVFMSTSIVKFIPKLFSDKKMLKELSGPIGIANVVGKASDAGIMSILVLTAFISINLGVMNLLPIVPLDGGKMFILLIEMCIRRKLSEKVENLISYSGLALM... | EC: 3.4.24.-
Subcellular Location: Membrane
Sequence Length: 337
Sequence Mass (Da): 37570
Location Topology: Multi-pass membrane protein
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A0A970ESE1 | MKYPTVCENKLFSAAYSKGKKHTGRYAVVYALRDRYPKNTAVSRLGLTVTKKRGGAVVRNRIKRVLREAYRAVDTKYGVKGGYIIIIVARDAAAKAKTPVVAADLATSFDALGLLLRGETSSSDADVKISENTGEKTDETVHFSVNESTISDLDKISSENTRDVEEADGADGSNKAKEQ | 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... |
A0A971BX24 | MTTLTAFAMDTYMTVSVRGIDSFEAAKAAGELIEEYDSLFSVSGSGSDIAAINSAAGEPVNISSETLRQITASIEVSGRSGGAFDITVEPLADAWGFSGGSEYRIPSDLEISQLLDKVDYSRIQISGNTLSIPDDMKISLGATAKGYTSDALVALFGSYRVDGAVISLGGNVQTFGTKKDGSEWIIAIQDPNDPERYTGTVSVSETAVVTSGNYQRYFESGGKRYGHIIDPATGYPVQNGLLSATVICHSGLLSDCLSTALFVLGEEGAKSYYETYGGFDMILITSDGRIIVTSGIAGSYTQEKNSPYILEVF | Cofactor: Magnesium. Can also use manganese.
EC: 2.7.1.180
Catalytic Activity: FAD + L-threonyl-[protein] = AMP + FMN-L-threonyl-[protein] + H(+)
Sequence Length: 313
Sequence Mass (Da): 33147
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A0A7D9CY96 | MATNITWHGNITHEERATLIKKNGITLWLTGLSASGKSTIACALETYLLQQGVQAYRLDGDNIRFGLNKDLGFSEKDRNENIRRISEVAKLFADSCTVALTSFISPYRKDRDAARKLHDDAKLPFIEVFVDAPLEVVEKEIRKVYIKRQEKELLRTSRA | Pathway: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from sulfate: step 2/3.
Function: Catalyzes the synthesis of activated sulfate.
EC: 2.7.1.25
Catalytic Activity: adenosine 5'-phosphosulfate + ATP = 3'-phosphoadenylyl sulfate + ADP + H(+)
Sequence Length: 159
Sequence Mass (Da): 18097
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A0A099KVY7 | MKNKTKRYSIRRYLTLHVVAWTLAMTIIPAAWVYYDTAKEVEELFDASLAQSARVLHGMIGRDGIEKHHGSMLEALLNKEKDPHSIQHDYEKKISFQVIDDTGLILRSASAPDHPESDLERGYTYIELGQYEWRIFILYSKVDDWHLVVGERMDIRDELIHHIALDHAIPLFLLTPFFVLIVSLVIRKGLKPLEVIANDVQEKNYSSLEKLSYKTEPEEVSGLISAVNTLFDNLSEQYDRERRFSSDAAHELRTPLAALMIHTENILEDNNDITLDASIINIKRSINRLSHLVSQLLSLSRADTQLIADDFTDVDIIKTV... | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Cell inner membrane
Sequence Length: 457
Sequence Mass (Da): 51634
Location Topology: Multi-pass membrane protein
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A0A947Z598 | LALEDALTNYQRPKMEEFDDNSHIVIRMPNTLDGLYFEQVSLIWGKNFIISIQEREGDCLDGLRQRIRTGVGRIRKSGVDYLVYAIIDAIMESYVPLIISLGEQLEVIEEGILAGHNRRSMELPHRIRKELHYMRRICIPTRELLVPLYREESRLVQAATRPYFRDCADHVMQIIEMVEVEKEFCTQIIDLHAMGLNQRMNEIMKMLTLISTIFIPLSFVAGLYGMNFATDKSPFNMPELKWYFGYPMVLSLMLGITLTLLVFFWKKGWIGDNRPDDK | Function: Mediates influx of magnesium ions.
Subcellular Location: Membrane
Sequence Length: 278
Sequence Mass (Da): 32429
Location Topology: Multi-pass membrane protein
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A0A927W087 | MEGIINLLKPAGMTSHDAVSFLRHLLGERHIGHTGTLDPMAVGVLPLCVGNTARLIEYMDGDQKSYRCEFLLGLETDTLDVWGKILEDRRGAFAMPGREAVEAALEPLRGTILQVPPAYSALKVNGKPLYKYARSGGEVPQVEARTVTIHSLQLVSYDEEQGRGVMDVTCSKGTYIRSLCQELGDTLGCGAAMSFLARTASGPFTIQEAVTLAQLKESWESCLLPSDAGILWMGELTLREGRDRWFSNGGYLTDRDLTGKKEPDDAHRRSGEEQEGPFKKYYKVRSHGGRFMGTVVWNEEEQQFKADKVICREVDQ | Function: Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs.
EC: 5.4.99.25
Catalytic Activity: uridine(55) in tRNA = pseudouridine(55) in tRNA
Sequence Length: 316
Sequence Mass (Da): 35035
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A0A7C6P0G3 | MAYFPFFVDLKGKECYVFGGGAVASRKALALLEFEAEVTVVAPKVCDEIWQRREKVMVLLREYREEDLDHAFFVIAATDRAEVNARISKACDERGLMVNRVDQPESGSCLFPAYIRQGDITVGVTTSGKSPVVAGRIKKLVESQIPAYYQGLVQVLGNCRELVKQRVPSERVRARIFKRLVDLGEEKEGNLTQEDIEVAIKQEAGSE | 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: 207
Sequence Mass (Da): 23174
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