ids stringlengths 6 10 | seqs stringlengths 16 1.02k | texts stringlengths 117 4.4k |
|---|---|---|
A0A2E1ZNX3 | MKINRLFKMIMLLLIFSTAAACSSTSEEEPASEVTQGSESGIDATTRRAQELEEEARARAAAAEERMRRSALANRVFYFDFDVSDFRQADRDILNFHAQDLAANPSKRVRLEGHADERGTREYNLALGERRSNNILNYFVVNGARRNQIETVSYGEERPADRATSETAYQRNRRVEIVVQ | Function: Part of the Tol-Pal system, which plays a role in outer membrane invagination during cell division and is important for maintaining outer membrane integrity.
Subcellular Location: Cell outer membrane
Sequence Length: 180
Sequence Mass (Da): 20510
Location Topology: Lipid-anchor
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A0A8T7AFX0 | MTSNKPTPISRFAPSPTGNIHLGNVRTALFSYLLAKHLHGDFILRCEDTDQERSDEAFLQQQQRDLRWLGLDWSAGPDMDSAHGPYRQSQRFEIYDGFYKDLIEKGIAYACFCSPQELKMMRKAQMQSGRPPRYSGTCRHLSADEVAAKFTNGEKASLRFRVPSDETMQLHDLVVGEKTYHSNDIGDFIIRRSDGTPAFFFCNAIDDSLMGVTHVLRGVDHLTNTPRQLMILNALNLRAPEYGHISLVVGADGGPLSKRDGSTGVKDLREAGYLPEAIVNHLARLGHHYANNDLMPLAQLAKEFALEHCGRSPSKHDPVQ... | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the attachment of glutamate to tRNA(Glu) in a two-step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu).
EC: 6.1.1.17
Catalytic Activity: ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-g... |
A0A8T7B3Q6 | MNSVGFIGGGNIATALISGLRQQAADMTVMVFDPNPAATQKLVASQQVLMASSNKALTEQCDVIVLAVKPKIIDMVCKDIATVVSNQTLIISLAAGTRVDTVSAYFENAVAVVRAMPNTPAAIQQGITALFANTDATIDQRQQAELIMSAVGQVLWLEDENQMDVVTAISGSGPAYVFWLMENMLRSAKELGLNEQHAQQLVLHTAAGAAAMPMQQQIEPESLRKAVTSPGGTTEAALNYLNSHQAADTFRQAIHAAFRRSQELGKKE | Pathway: Amino-acid biosynthesis; L-proline biosynthesis; L-proline from L-glutamate 5-semialdehyde: step 1/1.
Function: Catalyzes the reduction of 1-pyrroline-5-carboxylate (PCA) to L-proline.
Catalytic Activity: L-proline + NAD(+) = 1-pyrroline-5-carboxylate + 2 H(+) + NADH
EC: 1.5.1.2
Subcellular Location: Cytoplasm... |
A0A2E9EEZ0 | MNKLDILTFPDPRLRKKAQPXERFDENLKDMAKKMLYTMYADKGIGLAATQVNYHERLIVIDVSENQDEPIYIVNPSYEVLDSSPESSKEGCLSIPTFQQEVXRAKKIELSYQDLDGNPHKLTAEGLFGYXIQXEIDHLNGXLIVDYASSLKRSRIKAKLLKIKDGQX | Function: Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions.
EC: 3.5.1.88
Catalytic Activity: H2O + N-terminal N-f... |
A0A2E8ZY15 | MSNLIRIATRKSPLALVQANRVKELIEKRLKDTTVKLITRSTSGDTVSKAKFKKSGGKGLFLKELEELLLDGDADIAVHSLKDVPAVIDKKFIITTIDIREEAADVLISKQFNKITELPDKSIIGTSSPRRIAQIRNKYKNIEIEEIRGNVQTRLAALSNDKVDAVILAAAGLKRLSLSDKISQYLPKDDYVPAAGQGVLCIQAIKNKEYVLKTLKGLVVDEVDRCASEERDFISQFDGDCFSPIAAHCYIKNNKSTLIGYVSSTDGNRFIKTKIVENVNEMRGIGKKLAKIMIEQGAKKILGTK | Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 2/4.
Function: Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps.
EC: 2.5.1.61
Catalytic Activity: H2O + 4 porphobil... |
A0A2G6LD41 | MTNEKITEATTVKTTEKTYEVAIAELEKILSQLENNDLPLEAAIKQFESGVALIKHCQAILDNTEQKIKGLMDTPPESIADSTTAE | 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... |
A0A947FL82 | HDQSIIESILHALDPQPGENIVEIGPGRGALTYPLLQRCETLTAIDLDRDLVPILKQQASRFGTLEVINADILEFELSSIPDGGDFRLVGNLPYNISTPLMFHLLESAQDIRDMHFMVQKEVALRIVAHAGEANYGRLSVMLQYRCDCQYLLDVAPSCFKPPPKVDSAVIRMTPFSEPLQDVGDYRNFSSIVQSAFGQRRKTISNSLKSILDRETIIACEIDPGLRAENLAISDFAKLSRACTA | 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(+) +... |
A0A2E6QYG8 | MKTNSENFNEKFLSDFKQIYLNPSKIDYYLKNNSDYIEEDIKRKFTKLNLDHNYAIYSIGGFGRGEIFPSSDVDISIIETNRPKNYSNLEIFISSLWDEGYKVGHSVRSIKDIKKITKSDLSEFTSYLTRKPILSDRNLDNLVSKTLSSLWTSAKFHKAKFLEQNNRHREFFLSSSNLEPDLKESPGSLRDFHSALWILQHCYSLKTFDDILNFSFFKDEFLIARNAYNFIKVLRFITNLFTKNNKLDFETQIEIAKRTASGKLNLSNKALVERMMAKYYEHAHYISHFNTLVYQFFEEKKYSFKNKKGLYRNGSKVGFT... | Function: Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher ... |
A0A2E3WWL8 | MTESKKATGEEFSTSLKKVGREYAEALILAILIALFFRTFVVSVYRVKSVDMAPTLFVGDVVVGYKFPFSKFGSDPLGELQRGDLVLFSCPGRKSARCLSRVVGLPGDEVLMHRGRLSINGVELNYSIPDEITEEWLSQPNFSQFDLLVEKDLEAIDSDRRIFVRTGSLLEPQQQTVPPGEVFLLSDYRNSDQSSFHWGVVKHQAISARAVGVLFSLRWPLDPEETPLFPGLRWDRWFLRL | Catalytic Activity: Cleavage of hydrophobic, N-terminal signal or leader sequences from secreted and periplasmic proteins.
EC: 3.4.21.89
Subcellular Location: Membrane
Sequence Length: 241
Sequence Mass (Da): 27289
Location Topology: Single-pass type II membrane protein
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A0A920L372 | MDSAAQSQEKEQKPQQTSKQQAKPAIAPGQMRVIKRNGSVVSYDAEKIAIAITKAFLAVEGGAAAASTRIHNQVNELANAVTRTFNRRMPSGGTLHIEEIQDQVELELMRSGEQKVARAYVLYREERKQLRQQQEPQKGTKEEIKITLENGDEDTLDIDRLEAMVAEACEGLEGTDSALIIEEANKNLYDGVTEDDARTSLVMTARTLVEQEPNYTYVTARILLDNIRTEALSYLGMQKQATQSEMKDLYHQAFRNFLGKGVENEILNPELLEMDIERLGKAINPERDNLFTYLGLQTLYDRYFIHDSETRYELPQVFFM... | Pathway: Genetic information processing; DNA replication.
Function: Catalyzes the reduction of ribonucleotides to deoxyribonucleotides. May function to provide a pool of deoxyribonucleotide precursors for DNA repair during oxygen limitation and/or for immediate growth after restoration of oxygen.
EC: 1.17.4.1
Catalytic... |
A0A849WJY7 | MKSNVEKLSSLQRKLNVEVPSTTVQSSYERIFNDIQKEVTIKGFRKGKAPLSAIKSMYNSKVKQDVVQDLIQMHYVKALVEHKLDPISYPEFEFDDLSEEKNFSFSATFDIRPEISLKKYENLSVEKEILKFDDAQVDKVVENLRNSKATYEDLATTRPAQLGDLSVIDFEGFVDGQPLEGGSGKDHRLELGSKQFIEGFEEGIVGMNIGEEKTLKLSFPTPYHSKDLEGKAVEFKVKLTGIKTKQLPELNDEFIKAANTGVNSVEEFKKVVKQDLEASDKKRVEDAFKNRLLKTLVKENPVDVPSSLLKDQKLALIEDF... | Function: Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase.
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
EC: 5.2.1.8
Subcellular Location: Cytoplasm
... |
A0A2E2HEH5 | MEALQALTINILALLVTLGILVTIHEFGHYWVARRCGVKIECFSIGFGKSLFSWWRGDTEYRIAVLPLGGYVKMFGEREGDISEAEKAYAFNFKSLPQKTAIVAAGPLANLVLAVFLYWIMFMTGVSGIAPVVGNLNAESPAEQIGMQRGAEIVSIDGQTTRTWQQVRVALLNRLGESGTINIVYSPEDSDLIRENNIRIERWLIDQAEPDVLGALGITPWRIDIPAVIGQVVEGSRAEQAGLQPGDEIVAVEQQELNGWLDWVDTVRNNPEQDLQISVLRDGMRLSLGIRPEMSINNNGEQSGYIGAGVSAPEEIPSLP... | EC: 3.4.24.-
Subcellular Location: Membrane
Sequence Length: 459
Sequence Mass (Da): 50488
Location Topology: Multi-pass membrane protein
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A0A8T7AD45 | MQASFWLNKWQQHEIGFHQDDYHPALVKHFPKLESGAKILVPLCGKSKDMLWLEAQGYQVVGIELAESAVCDFFSEHGLNFTRTEQGETIHYQCTEKNILLIVGDFLALDESILSANSFDALYDRAALVALPAEMRTAYAQQCHALLKHEAKIMLINFNYDQSAMQGPPFSIDRAEIEALWHGRLSLIESFSMLRERSKFMDKGLAYMNEETWLT | Catalytic Activity: S-adenosyl-L-methionine + a thiopurine = S-adenosyl-L-homocysteine + a thiopurine S-methylether.
EC: 2.1.1.67
Subcellular Location: Cytoplasm
Sequence Length: 215
Sequence Mass (Da): 24607
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A0A8T7B3G1 | MWWRFDINKAVRALRNNQLIAYPTEGVYGLGCRLNALDTIDRIINLKQRPKDAGFVVIGSSFEQLSKLMSSTLHEDARKRLLRDWPGPTTFIVPASRTLPWLVTGGRKTVALRQTAHPVAKALCKKLGEPIISTSVNVRDDEPARSAKAVKAMFPNQIDFVLQGPLGSLKGPTEIRDLWSDEIIRSR | 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. Catalyzes the conversion of L-threonine, HCO(3)(-)/CO(2) and ATP to give threonylcarbamoyl-AMP (TC-AMP) as the acyladenylate intermediate, with the release of diphosp... |
A0A9D8FA78 | MLKPPSLFYRLLSILLLFVWLIHAILHALKFKQFSYISQRLGFTTKTTDDALIWVHAASVGEVNLMYPLCQSLIDKKHRLLITTSSATGLQQVKKLFSASLQSQIIPIDFLPISKLFIARNNIKLALIAETELWPETLYQTAKNSIPILHINARLSKKSRQAPLLIRQTLKNTLQYFSHHFVRYPTDVNHFKSMAVKNDKITVMGNLKYVQTADKHEMPPNLVGQEYLLAASTREGEEQLITKLLHNNTHWPLLVIAPRHPKRAKQILMSLEPYQLNIAQRSKADKITSETQVYLADTLGEMAALFQHAHLVVMGGSFTD... | Pathway: Bacterial outer membrane biogenesis; LPS core biosynthesis.
Function: Involved in lipopolysaccharide (LPS) biosynthesis. Catalyzes the transfer of 3-deoxy-D-manno-octulosonate (Kdo) residue(s) from CMP-Kdo to lipid IV(A), the tetraacyldisaccharide-1,4'-bisphosphate precursor of lipid A.
Catalytic Activity: CMP... |
A0A7C1TTW3 | MIEVYVSLGANLDDPRAQVMQAIDDLALLPQSRLLAVSSLYRSAPMVLPDQVKTGIPVQPDYINAVAKLETALTPHTLLDELQAIEQTHGRQRDGQRWRARTLDLDLLLYGNQQLDNERLQVPHTGIAVRNFVLYPLGELAPQKLQIPGVGKLADLLDRCSPKGLEKITL | Pathway: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate from 7,8-dihydroneopterin triphosphate: step 4/4.
Function: Catalyzes the transfer of pyrophosphate from adenosine triphosphate (ATP) to 6-hydroxymethyl-7,8-dihydropterin, an enzymatic step ... |
A0A9E5ADY5 | MILGERPRPQAAMREPPRPIRWGRWLLAAGAIVLVIGVQRLVVRLADPDVFPIRRVTVDGEFRYLAAQHIEALVVGAVRGGFFQVDVAQIRAQLLREAWVRDATVQRVWPIALHVSIREQQPVARWGEASLLSAAGEVFTPDPKTFPNGLVQLSGSTGTQAEVLAVWQRARATLKTLGLTATALRRSDRGAWQLELADGTLLLLGRHVIDQRLARFVRAYPRVLKDHWARIAAIDLRYTNGFSLRQRAGLSASGAATTP | Function: Essential cell division protein. May link together the upstream cell division proteins, which are predominantly cytoplasmic, with the downstream cell division proteins, which are predominantly periplasmic. May control correct divisome assembly.
Subcellular Location: Cell inner membrane
Sequence Length: 259
Se... |
A0A9D6VWY3 | MPTAATPCVLNGRGIVVMRPAHQADALCALIEAAGGRALRFPVLEICPAADPAAVQAGLVRLMRPGEYDLAIFVSANAVHYTLKALAPHTWPTSVKIAAIGAATARALAAQGLRVDIAPARDFTSEALLALPELQSVRNQRILILRGAGGREILRDNLLARGAQVDYLEVYRRATATTDPSILLEHGRAGAIDAVLIASTESLHKLLAIIGTLGIALLRTTTWVVGNERTRQLARELGLGGTMVVAADATDAAMLDALCAHFATSQPQ | Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 3/4.
Function: Catalyzes cyclization of the linear tetrapyrrole, hydroxymethylbilane, to the macrocyclic uroporphyrinogen III.
EC: 4.2.1.75
Catalytic Activity: hydroxymethylbilane = H2O... |
A0A847C0A9 | MTIQTRFPKLNDSPMIYELIQNAPPLDLNSRYLYILQATHFRNSCIVAELISDKKGEAPLLAGFLSGYRLPEDPRTFFVWQVAVGSSARGMGVAKRMALDLLRRPALSDLTEIITTITPSNGASLKLFESLARKLETQIVEEDGFDAGLFGGDAHESECLYRIGPFDLSRLSLS | Pathway: Amine and polyamine biosynthesis; ectoine biosynthesis; L-ectoine from L-aspartate 4-semialdehyde: step 2/3.
Function: Catalyzes the acetylation of L-2,4-diaminobutyrate (DABA) to gamma-N-acetyl-alpha,gamma-diaminobutyric acid (ADABA) with acetyl coenzyme A.
EC: 2.3.1.178
Catalytic Activity: acetyl-CoA + L-2,4... |
A0A2E0GR08 | MTLXIIGLNHHNASLDYREKLAFSHEEIQSCLKDLIASDEIKEAVILSTCNRTEFYLQANEEGEEYTKTWLKKNKNINKNTEDLLFSLKGEKAIIHLSRVACGLDSMILGEPQILGQLKNAYKSSVESGAITKDFSKLFDHIFRLAKKIRTNTNISNSPVSVSYAAVILANQFFSRLDNHSALLIGAGEAIELVAKHLVNKKIDKLFIANRNINKAQELAKRYGGYALDLDSLDGVIEITDLILXSTASDHYILKKFQIQKAIKNRKRKPIFAVDMAVPRDXXPEIQXIEDIYLYTIDDLQKVVLEGQNKRNLAAVEADE... | Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 1/2.
Function: Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA).
EC: 1.2.1.70
Catalytic Activity: (S)-4-amino-5-oxopentanoate + NADP(+) + tR... |
A0A0H2VYL9 | MAKEKRRGFFSWLGFGQKEQTPEKETEVQNEQPVVEEIVQAQEPAKASEQAVEEQPQAHTEAEAETFAADVVEVTEQVVESEKAQPEAEVVAQPEPVVEETPEPVAIEREELPLPEDVNAEEVSPEEWQAEAETVEIVEAAEEEAAKEEITDEELEAQALAAEAAEEAVMVVPPAEEEQPVAEIAQEQEKPTKEGFFARLKRSLLKTKENLGSGFISLFRGKKIDDDLFEELEEQLLIADVGVETTRKIITNLTEGASRKQLRDAEALYGLLKEEMGEILAKVDEPLNVEDKTPFVILMVGVNGVGKTTTIGKLARQFEQ... | Function: Involved in targeting and insertion of nascent membrane proteins into the cytoplasmic membrane. Acts as a receptor for the complex formed by the signal recognition particle (SRP) and the ribosome-nascent chain (RNC). Interaction with SRP-RNC leads to the transfer of the RNC complex to the Sec translocase for ... |
A0A967VJU0 | ASERIDPNEAPAAAVRRKPDSSIVVGIQLQKEGEADAFVSAGSTGAVMAASLFMLRPLPGIDRPAVAAMVPTSVGPMVLLDXDCKPENLEQFARLGAVYARDVLGRETPRVGLLNIGEEPEKGNELAVETHRRLAASDLNFVGNVEGREIIEGACDVLVADGFVGNVLLKFYESVAGFVFGLIRKDIAEGGPDSPADRVTRILDYAEYGGAPLLGVNGISI | Catalytic Activity: a fatty acyl-[ACP] + phosphate = an acyl phosphate + holo-[ACP]
EC: 2.3.1.274
Subcellular Location: Cytoplasm
Sequence Length: 221
Sequence Mass (Da): 23298
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A0A5Q4EV52 | MSGGFHVRTAGDPALPPLLCLHGFLGSGEDFTGLMPALAERFHVLAPDLPGHGRSRLPAEACTMAGCAAALMAWLGQQVNSPVCLYGYSMGGRLALYLALHYPERFQALALESASPGLDDERARAARRQHDEALAARLEAEGTPAFVAAWYAQPMFQSLRGQPGFAALLARRQRQAAAGLAASLRGMGTGSQPSLWSALPSLSPPVMAIVGEHDAKFREIAAQMSACHPRMELRVVPGAGHNVHMEQGATVIACLQGFFSQGRHRDP | Pathway: Quinol/quinone metabolism; 1,4-dihydroxy-2-naphthoate biosynthesis; 1,4-dihydroxy-2-naphthoate from chorismate: step 3/7.
Function: Catalyzes a proton abstraction reaction that results in 2,5-elimination of pyruvate from 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate (SEPHCHC) and the formation... |
A0A349ECG8 | LARSVMTIGAVESARVHLAFPRETVFARQQQPPTASILVRLRPGRVLDEGQVAAIIHLIASSVPKLKPEQVSVVDQYGNLLTRNGRDGANGGLNMDQLNYSRQIEERYARRVEDLLTPVWGPGRVRAQVSLELDFNTSEETAERYEPREEPRPVRSEQLLEEHNPRQNPVGIPGALSNQPPGAAVAPEVAAPQNPANPQDPAGAAQTPPTPPLPTRKEVTRNYELDKRVTQVRSGPGRVLRVSAAVVIDDRITFQEGKPVRTPVTPEEMERITNLVKQAVGFSAERGDSVNVFSATFAPSSLAALDELNAVLDEMPVPMW... | Function: The M ring may be actively involved in energy transduction.
Subcellular Location: Bacterial flagellum basal body
Sequence Length: 447
Sequence Mass (Da): 48759
Location Topology: Multi-pass membrane protein
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A0A8I5UJR5 | MGREFGNLTRMRHVISYSLSPFEQRAHPHVFTKGIPNVLRRFRESFFRVVPRECPGPAGAGGWTPAAAVVTAPPL | Function: Component of the ubiquinol-cytochrome c oxidoreductase, a multisubunit transmembrane complex that is part of the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrom... |
A0A520TM19 | MIRILFVFFLILSDQISKVLVVKNFSIGESLNILPIFDIFLILNTGIAFSLFDNGGPTGRWILVFLVFLVCLYLLYIIATENLNKYESLSLLMILSGGMGNLLDRAFRGHVIDFIHIYYETYSFYIFNLADTFITIGVMIYILNTVISYLNKNGNKAS | 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-, ... |
A0A952NX92 | MDIAWIGAANGSGSNHWGSRDGAHFLKEQLSGSDLIHLARMPIIEEDPTGFAMKALPALLDFNHRLALKTANAHRAGDFPVIVGGDHSCAIGTWSGIFARQSRKLGMLWIDAHMDAHTFNTSETGNIHGMPLATLLGRGFAPFVNLLEEGPKLDPKRTVLFGVRSYERGEAELLQSLNVRVYLMEEIFDRGFAVCFREASDRVRGGGGLPFGISLDLDALDPAQVPSVGTPVRAGLDAGELLRAFPQILGDEDLQAFELVEFNPHEDVADRGLSFVIEVLNLVQNARLDLSVAALRPYTQKRRPPAGLRP | Pathway: Nitrogen metabolism; urea cycle; L-ornithine and urea from L-arginine: step 1/1.
EC: 3.5.3.1
Catalytic Activity: H2O + L-arginine = L-ornithine + urea
Sequence Length: 310
Sequence Mass (Da): 33796
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A0A949P473 | MAGKKKGVAGKGKRGKKRSPTPKKGTFGGGKGRLRAMLSAMFAVFLLLGVGLLFLDWKLQARFDGKRWSLPAKIYARPLELYSGLSLTADALEAELVRMRYRHDPAVKEPGSYHRRGNRVHFFTHDFQFLDGLERQRKVLVTFSGDQVKVIRHLPVGNERAETLDLLRLEPMLIGGFYPSHNEDRALIQLKDVPPLLIETLLTVEDRDYFEHSGIAWSGIARAMLVNLRAGKIKQGGSTLTQQLVKNFYLTDKRSYWRKAIEVVMAMLLELHYDKAEILEAYLNEIYLGQNGAKGVHGLGLASSYYFGRSPQQLKLNQIA... | 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... |
A0A920NKD3 | MLCPGNGSGPIECIARGYITGSGWKDYQTPVAYVASNAAGFGESDRLDQPLFTPSTKAEAGLHDENISFEQGVAMLASKPCSGLKKRPFRFTEPLEIMH | Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate: step 1/2.
EC: 6.3.2.6
Catalytic Activity: 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + ATP + L-aspartate = (2S)-2-[5-amino-1-(... |
Q73LW5 | MRLAILGGSFNPIHLGHLNLAFHSYKELAYDKIAIVPAYISPFKLFCKYTEVEDRLKMIDLAIADKPYMYCELYEIEKQGVSYTIDTINYLYQKFPDIEGKIGLIIGDDLKENFFRWKDAEEIIKKTDIIIGKRTGLKGSFDPLNTEPARASVKELKNEILNISSTQIRDAVLKNKDFSSLVPKGVYDYIIEHGLYKEKGVLALGVSALMDTSDIELKTREIDRFAKSVLTESRYAHSVRVAEYARHLAKEYKKEGVSPALAYFTGLAHDICKKCSDEELVKLVEADGLGIDNVEKNRLNLLHGRASAIVLQKKFGINDE... | 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... |
A0A2A4WTP3 | MTKNNSITLGITGASGAFYAINLLKHLVNYYQNVHVVISDAGRIVLATEMDLTLPESPKKTQIALTEYCQTSSEIISVYSKENWFSPIASGSAAPKQMVICPASMGCISAIATGASNTLMERAADVVLKERGQLILLPREMPYSTIHLRNLLTLSEAGATIMPASPGFYNRPKNLDDLANFVSARVLNHLKIENEIVSPWGYKNLKDKNVDDKNKEDNQ | Function: Flavin prenyltransferase that catalyzes the synthesis of the prenylated FMN cofactor (prenyl-FMN) for 4-hydroxy-3-polyprenylbenzoic acid decarboxylase UbiD. The prenyltransferase is metal-independent and links a dimethylallyl moiety from dimethylallyl monophosphate (DMAP) to the flavin N5 and C6 atoms of FMN.... |
A0A964UAQ9 | MSRSALAGAGVLVTRARDQAGPLIAAVEAAGGAAWLLPALEIAPLPAPAQVGDAPDLALFVSPNAVRHGARFLRLPGCRYAAIGPATAEAMRQAGCPPDLVPGGGYDSESLLAADELADMTGRRVLIVRGRGGRELLAETLRARGAAVDYAEVYERRRPAPDAGEIEAVIAAWRRGRLRYVTCLSVATLRNLAELLGERGAQVLRGTTLVSASDRVLKLAVREDIAVDTLLAQGPEPSDLVRAMVFPDGEPDRAEHD | Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 3/4.
Function: Catalyzes cyclization of the linear tetrapyrrole, hydroxymethylbilane, to the macrocyclic uroporphyrinogen III.
EC: 4.2.1.75
Catalytic Activity: hydroxymethylbilane = H2O... |
A0A8T6ZWX9 | MNTKSVSGFTLLEVMVALAVIALGMAAVIKTVTTTTSNTIYLRDKTFAYWVAQNQLAEIEVTAASPKTGFTDGEEKLAGLTWHWTRKIEGTEDPDTNRIEITVRKDKDKSAQNYATLITLFFNPR | PTM: Cleaved by prepilin peptidase.
Function: Component of the type II secretion system required for the energy-dependent secretion of extracellular factors such as proteases and toxins from the periplasm.
Subcellular Location: Cell inner membrane
Sequence Length: 125
Sequence Mass (Da): 13903
Location Topology: Single... |
A0A949UG37 | MAKTELLYGFHSVKATLKKSPESVLELLTQQGRDDQRVAEILQLAENFGITVQRAKAKTLEQMLAQEHRQSDINHQGVVARCRVQPPASDQELTTFLEKLDHPPFLLLLDSVSDPQNLGACFRVADGAGVDALITTKDKAVGITPVVRRVASGAVESIPFFQVTNLTRAIRQLQEAGVFVVGTALDESACSLYEADLTGPLALVMGAEGKGLRRLVKETTDQLVYLPMKGDVQSLNVATASGICLYEALRQRIGS | Function: Specifically methylates the ribose of guanosine 2251 in 23S rRNA.
Catalytic Activity: guanosine(2251) in 23S rRNA + S-adenosyl-L-methionine = 2'-O-methylguanosine(2251) in 23S rRNA + H(+) + S-adenosyl-L-homocysteine
EC: 2.1.1.185
Subcellular Location: Cytoplasm
Sequence Length: 255
Sequence Mass (Da): 27685
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A0A2D5T6P6 | MLMHYPRKRFGQHFLTDQNVIDEIQNSINPTNEDVIIEIGPGRGAITSGLVSKSKFVHAIELDRDLIGYLKKEFNTNSSICFHQADALKFDYSKLGDKIRIVGNFPYNISTPLLFHLLKYKDCIVDIHCMLQKEVVDRMAAEPGSKAYGRLGIMLGCHLKIEPLFNVDESAFFPPPKVKSTVVQLLPLRPNKFDIQNESVFSNLVSKAFMKRRKTIQNSLKEFVDISDLNAINIDPGLRPEQISILKYVELSNYLSNRLG | 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(+) +... |
A0A2D5T8W2 | MIFLFKIILKFNFWKIFLAKKFYNRLQALSDSVKNPFSGGLKGIEKESLRVAGDGSLSTLSHPIELGSALTNNYITTDFSEALLEFVTPASKTTEEVLSNLCDIHQFTYHHLDEEFLWPASMPCHMPPDMKIPLANYGSSNIGQAKTIYRRGLGYRYGRNMQMISGIHFNYSLPKHFWAVYQDIFNDNSNKNNFKSEQYLGLIRNFKRIGWLVLYLFGASPAFCGSFNNSSSRPIELLKKRTHFEPYSTSLRMSDLGYSNQNQSRINISLNNLEEYISDLSDVLGKPEDSYNKIGIKVGDVYRQLNANLLQIENEFYSSI... | Pathway: Sulfur metabolism; glutathione biosynthesis; glutathione from L-cysteine and L-glutamate: step 1/2.
EC: 6.3.2.2
Catalytic Activity: ATP + L-cysteine + L-glutamate = ADP + gamma-L-glutamyl-L-cysteine + H(+) + phosphate
Sequence Length: 534
Sequence Mass (Da): 61240
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A0A2D9XSU2 | MRLLATFFVLVPLLIDYFSKKYIENNFDTHAIILNDFIIIDKTYNKGIAFSLFNFDSPLTNIFFSIIVIFIIVIIINFVLKNLSTFNKSEFFAWNIVIGAAIANLIDRITNGSVLDFIIIHYENIYFPAIFNFADAFISLGVFLLIINYFIYKND | 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-, ... |
A0A8T4AKZ7 | MRLIRGLSGLECWQKPSAVTIGNFDGVHYGHQQMLSRLCEKAKQLGVPSVLITFEPLPHEFFAGDKAPPRLMGLREKLQYLSAKSDLDAVLCLPFSQSLAQLSAERFAQDILLDGLSAQYILLGDDFRFGYQRQGDLALLQNLSSHSGCQVESMFSVIIGNARVSSTRVRQALAEGNVAQATHLLGRPYCLSGRVVKGDQLGRTIGYSTANIYLRRQNLALSGVFAVQLRGIGKETLVGMANIGFRPTVNGRELRFEVNLFDFTEDIYDRYVEVDIVTKLRDEQRFDTLDSLKVQLAVDEQVARDYFASSVYLSNK | Pathway: Cofactor biosynthesis; FAD biosynthesis; FAD from FMN: step 1/1.
Function: Catalyzes the phosphorylation of riboflavin to FMN followed by the adenylation of FMN to FAD.
Catalytic Activity: ATP + FMN + H(+) = diphosphate + FAD
Sequence Length: 316
Sequence Mass (Da): 35235
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A0A849WR53 | MSKLDLSKRYARALFAVSKESGSQAKIYSQLKQVAVLTEQPETKAFINNPSVSLATKKEVFQKAFHNSQLASELVSFLELLLEKKRISAISEIVKTFEEIVDQDNGLTRGFVYSAKPLGPEVLQSLESKISNILKKKIVLTSKEDPSLIAGAVAKVGGWTFDDSLQTHLKNLNEELLNH | 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... |
A0A368C0L3 | MKFSESWLREIIDIKLNSSELSHKLTMLGHEVDSVITDGSDIDGIVIAEIVNYAKHPNADRLSLCEINYGNNNHINVICGAPNVRTGLKTALAKVGQALPDGTKIKKSKIRGIESNGMLCSAAEISLGMDQDGIIELPIDAPVGLKLNEYLNLPDNIFDLDLTPNRGDCFSVLGVARDLASSPQSKLHTKEYKKAPITSKICQTIKTPIPEICPRFASQSIKNVNNTVKTPIAITEKLRKSGIRSINPIVDVTNYVMMVTGQPLHAYDQSKIKGIVQPRFAKKDERIMLLDEQIIKLEKDTIVVSDSSGAIGLAGIMGGL... | 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: 792
Sequence Mass (Da): 88281
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A0A920S0D8 | MNEDAIEFLVTSDEHNQRIDKVVSSKLSEYSRVIIQDWIESGNILLENQIVKPSTKVQDGQQIKVVPVLKERSEIEPQKINLDIIYEDNDLIIVNKPQGLVVHPGHGNYDSTLQHGLLFHDEELRFLPRAGLIHRLDKDTSGLLMVAKNSNAYNSLNSAMQSRLIKREYRAICVGEMTSGGTVNEHLSRDPNNRIKFRVSEDGKNAVTHYRVLKKLSGYTFVGVQLETGRTHQIRVHMSHIRYPILGDPLYGKD | Function: Responsible for synthesis of pseudouridine from uracil.
EC: 5.4.99.-
Catalytic Activity: a uridine in RNA = a pseudouridine in RNA
Sequence Length: 254
Sequence Mass (Da): 28920
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A0A8T3RR76 | MQTAPLANAGDVDVPQVALVQDAEPVPATKIRAGQSGRKRSALPFKAGDVLAGRYAIVKKVATGGMGVVYQAIDRRRAEAGSVYPYVAVKVANIPNVNSVDARNALHREFARVAALRHEGIVNVTDFDRQGKHFFLVMEWLDGKSLGTILSAAAASGTRCFDRMLTTRFIENIADALACAHRQGVVHADIKPDNVFITEERDVKLLDFGNVSLAADRSGARYFATKAYASCEVLERKPPESSDDVFALGCIAYELLTGRRPLQGMNALEAEMGGLTVEPIEGIEPRIWRAIRAALSFRREGRPQDAGRFLELWHQQLPQA... | Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
EC: 2.7.11.1
Subcellular Location: Cell inner membrane
Sequence Length: 600
Sequence Mass (Da): 64637
Location Topology: Single-pass membrane protein
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A0A7C7IF64 | MATTAQSQPQIESLGHLKLPPHSTDAEAALLGGMMLDPEGQAYDKIANIVTERDFYHPENKAVFTAIQKLSEDQKLTDLLTVSDWLDSSGTFSVVPAIQYISELVDNTAGTANVGEYAKIVRDKALLRELITISNNIAQSAYKPENRSPSELVDLAEQRIFEIAERGTRNSSYLELNQTVKHLMDELDKRAQKGGGLTGISSGFRKLDELTTGFQKGELIIIAGRPSMGKTALALNIAEHTALADNNPVAVFSLEMSAEQLAFRLISSLGRVNQTSLKSGKLKDKDWDRIDGAILQMKEMPIYIDDTPSLTPVELRARAR... | Function: Participates in initiation and elongation during chromosome replication; it exhibits DNA-dependent ATPase activity and contains distinct active sites for ATP binding, DNA binding, and interaction with DnaC protein, primase, and other prepriming proteins.
EC: 3.6.4.12
Catalytic Activity: ATP + H2O = ADP + H(+)... |
A0A4R2L056 | MSAAPTLRRRLLLGLLLPLLALLGVGVVADYRTGVRLAEDAYDHALTSTAIALAARLELDKDHDLDVDLPAAAEAVLRSDPTDRIDFAVYDHQGKLISGNAGLRELAAAPGSANPAFSDAVRDGTPLRVVTYRYAGPEGMATIIVVETTRKRQRAAAQVLVSTGWPNVLMVAATLLIVFFGVRYALAPLDALGRSIDRRAPDDLGPIPLHGTPGEARPLVAALNRLMDNLRRSTALQQAFLSNAAHQLRTPLAGLQTQVELALDAVAAPDRPRLEAMREATARLVRLTHQMLALARSAPEAGAGQQCEPVDLPALLEDAA... | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Cell inner membrane
Sequence Length: 455
Sequence Mass (Da): 48030
Location Topology: Multi-pass membrane protein
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A0A3M0Y9S4 | MEKDATLEQLARDEEGFLLDPNDWHPGLMAPLAAECGLELTPERLTVIRFIRDYYERHHSVPEARILLRHLRDIWGEEKATRRYLYRLFPYGYGQQACKIAGMRKPRKLMLDV | Function: Part of a sulfur-relay system.
EC: 2.8.1.-
Subcellular Location: Cytoplasm
Sequence Length: 113
Sequence Mass (Da): 13370
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A0A3M1K8H6 | MQIMLRCRSNEVSVAAEVVLGVGSNVAPERQVPRALEALARLLAGLRVSPVYACPAVGYEGPEYWNLVCAGHTRLNLAELKHELVALERQSGRPADLPPGQPRTLDLDILLYQRNPSDPPPGNTTHAADVCAPHPDILTQAYILRPLADLMPDRSHPDTGKTFAEHWRASEKGLPMRVVPLPGDPACTGFGWTAGA | Pathway: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate from 7,8-dihydroneopterin triphosphate: step 4/4.
Function: Catalyzes the transfer of pyrophosphate from adenosine triphosphate (ATP) to 6-hydroxymethyl-7,8-dihydropterin, an enzymatic step ... |
A0A3P3WAZ6 | MGRKILLDKINIPGIKTYEVYRRNGGYASVEKALKMDPDAITEEVKTSGLRGRGGAGFPVGLKWSFIDKKSGNPRHLVCNADESEPGTFKDRYLMEYIPHLLIEGMIVSSFALGANLSYIYIRGEYMWVFKTLERAIKEAYAAGWLGKNIKGTGYDLDLHVHCGGGAYICGEETALIESLEGKRGNPRIKPPFPAVKGLWQNPTVVNNVESIASVPWIVLNSGEEYSKIGLGRSTGTKLFSVSGHVKKPGVYEIEMGMTVEEFMNSDEYCGGMIDDRPLKGLIPGGSSVPILPQHLIFKTANGEDRLMTYESLADGGFAT... | Function: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain.
EC: 7.1.1.-
Catalytic Activity: a quinone + 5 H(+)(in) + NADH = a quinol + 4 H(+)(out) + NAD(+)
Sequence Length: 454
Sequence Mass (Da): 50619
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A0A661BQV7 | MSVIGRFAPSPTGPLHFGSVVAAVASYMQAKSQHGKWLVRMDDIDTPRNQAGADSSILKSLEILGLYWDDKVLFQSHRQAAYQEALDLLTDKNLLYRCTCTRKQLQGKAYPGTCRDKGHSSDQQHALRVLCNQQAINLNDEIQGKFQQNLETEIGDFIVHRADGLVAYHIATVVDDAWQNITEIVRGADLLDSTPRQIYLQKLFNYHSPAYAHLPVAVDKQGYKLSKQYHAKPIDDEDPVTTLLLALEFLGQDPDKLLAQENVEEIIQWGIKHWSLEKIPRLDTIEVKSS | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the tRNA-independent activation of glutamate in presence of ATP and the subsequent transfer of glutamate onto a tRNA(Asp). Glutamate is transferred on the 2-amino-5-(4,5-dihydroxy-2-cyclopenten-1-yl) moiety of the queuosine in the wobble position of the QUC an... |
A0A3M1S679 | MAEYLVIRLPDDGRPEAAWAVLDDSGAILQAPVLGALEDAAPAAAGRRVIALAPARAVLRTAVSLPLRSQARIRQALPYALEEQLAEDVEQLHFAAGRGPSPGTVAAAVVRHERLQDWLAALRGAGLEAQAMYAESDGLDALPGTAVLLLEPQQLILRDGDGQLSVGDPDNLEPLLQLWLAALQDASPPHLLAYLAGELADTVPETLQSLRPRLASLEIKRLPDGPLPRLAANVVVNGGVNLLQGVYARRSELGRYWPAWRLAAGLLLALAVTATMSTALEVRRKEARAAQLQAAIEQAFRYTFPDARQVRGTRAELQSR... | Function: Inner membrane component of the type II secretion system required for the energy-dependent secretion of extracellular factors such as proteases and toxins from the periplasm.
Subcellular Location: Cell inner membrane
Sequence Length: 416
Sequence Mass (Da): 44438
Location Topology: Single-pass membrane protei... |
A0A1F8CS09 | MEGNQIQVFISPEQLANRVKELADQISADYKNQELILIGVLKGSNVFLVDLSRELGTDRLERGRSPKLVKIGFVGTSSYGSKTDSSGEVKQTIRLDTDIKGKHVIIVEDIADTRITLEWLLKLAHAQNPASVRVCVALNKESRNQTNAKLDYVGFDIPDEFVVGYGLDLNEEFRNLPFVGILLKKS | Pathway: Purine metabolism; IMP biosynthesis via salvage pathway; IMP from hypoxanthine: step 1/1.
Catalytic Activity: diphosphate + IMP = 5-phospho-alpha-D-ribose 1-diphosphate + hypoxanthine
EC: 2.4.2.8
Subcellular Location: Cytoplasm
Sequence Length: 186
Sequence Mass (Da): 20717
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A0A9D6JIU4 | MAVVYISLGSNIERVANTRAGVAALRAHYGDLVLSSVYESESIGFAGGSFYNMVIGLQTAEPPDRVLVSDPSREMADILT | Pathway: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate from 7,8-dihydroneopterin triphosphate: step 4/4.
Function: Catalyzes the transfer of pyrophosphate from adenosine triphosphate (ATP) to 6-hydroxymethyl-7,8-dihydropterin, an enzymatic step ... |
A0A2D5PRC3 | MNFKRGFSLIEVSVSLLILSVAVMSVYQTLSSTTLSIFSLENRVIAREIANNRISLINTLEKPFNQKIRSGSLVFYGDEWEWKETFNEAPMKSYIEYQIEITKKDNSQVIYEAKGFLKKN | PTM: Cleaved by prepilin peptidase.
Function: Component of the type II secretion system required for the energy-dependent secretion of extracellular factors such as proteases and toxins from the periplasm.
Subcellular Location: Cell inner membrane
Sequence Length: 120
Sequence Mass (Da): 13882
Location Topology: Single... |
A0A933VLB1 | MRKKKASKPPKRGLPTCVDKSEPQLPRGVLHDTSLIFAQVMELHRLSRFEQAKFLCEKIIALNGGHIDALNYLGTVHLQNGSLREGIRLIGKSLEVNSAQPVAHMNQGNAFKDLGDMEEAFVCYSRAIALKANFPEVYYCRGNAYSVCVRLDEALADYDRAIALRPDYVQAIFNRGNTLKSMGRLDEALASYDRAIALKPDYAEAYYNRGYVLNDLKRIDEALLNCDRVIALMPNFADAHYNRGNALQELGRLDEAVISYDHAVALKPSYFEAFSNRGNALRKLKCLDDALASYQRAIALNPAYASAHNNQGNVLLELNR... | Pathway: Protein modification; protein glycosylation.
EC: 2.4.1.255
Catalytic Activity: L-threonyl-[protein] + UDP-N-acetyl-alpha-D-glucosamine = 3-O-(N-acetyl-beta-D-glucosaminyl)-L-threonyl-[protein] + H(+) + UDP
Sequence Length: 773
Sequence Mass (Da): 87328
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A0A2E1KDT3 | MMNKKDIDWDNLGFYAHETKSMFKAIYTAEEKWQVEGLIPYGDVSMSPASTILNYGQGIFEGTKAYRTSKDRVVGFRIEENAARFASSSERLCIPQLPEGLFLNAVQEVVKDNSDFLPTQDQGSLYIRPLAYGDGPMLGVKASNNYTFLVYATPVGSYFKSGLKMLDTILTDKYHRIATKSIGFAKAVGNYAGTLLPYKEITMDGFDEVIFLNSSDENIIDEARSANVFVLKGNVLKTPALQGSILPGITRDSTIKVARELFDLEVYEEDVTVEDLLNGDEVFFTGTAAVVAPAGSINYKNNKVQFETDYNASMTKKIRD... | Pathway: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 4/4.
Function: Acts on leucine, isoleucine and valine.
EC: 2.6.1.42
Catalytic Activity: 2-oxoglutarate + L-isoleucine = (S)-3-methyl-2-oxopentanoate + L-glutamate
Sequence Length: 341
Sequence Mass (Da): 38038
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A0A6L7SR88 | MLITIIKRDLKCVSHNLSGAIQPIGFFIIITSLFPLAVTPDPEALQSIAPGIIWISALLATLLALDTLFKEDFIDGTMDQMFIAADSLYVIAFARIISHWLFSGLPLIVMCLVIAMMLHIPAYTFDALIVSLLLGTPTLSMVGSIGAALTVGLRYSGVLLTLITLPLYIPVLIFGASCISADLAGFPWTGQAYLMGAMLVLSITLAPFATAAALRINMS | Function: Required for the export of heme to the periplasm for the biogenesis of c-type cytochromes.
Subcellular Location: Cell inner membrane
Sequence Length: 219
Sequence Mass (Da): 23403
Location Topology: Multi-pass membrane protein
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A0A2E1IC08 | MNYSSRRSGFTLIEVVVALGILGLVLGGAISAVHQYADQRVYMSAKNLSNQVAWNVLMQQYQNAEMRSSNSRRTSNAQKGRQTQYGLDWNWNLTVEPAMGKDLYRYEAKVSAVNSDRVTSALSIYIVED | PTM: Cleaved by prepilin peptidase.
Function: Component of the type II secretion system required for the energy-dependent secretion of extracellular factors such as proteases and toxins from the periplasm.
Subcellular Location: Cell inner membrane
Sequence Length: 129
Sequence Mass (Da): 14486
Location Topology: Single... |
A0A523JZL3 | MSKTWAILPVKAFDRAKTRLSSVLAGTQRESVARLMATDVLRALCNTPEIDRILLLGQGPEQEELARRFDCAYENDDPTLDVSANVTRIAQMPEIQSAKTFLLVAADLPRLCSQDFARILRGHQEGITICRAARDGGTNAFIATMPQQVKFSFGAGSAKRHALAAQAAGQKVSVLDDTAFQRDIDTADDLQYLCRQNDSCDTLKFLQRSGVVTRLNDRVAAAETA | Pathway: Cofactor biosynthesis; coenzyme F420 biosynthesis.
Function: Guanylyltransferase that catalyzes the activation of (2R)-3-phosphoglycerate (3PG) as 3-[(R)-glyceryl]-diphospho-5'-guanosine, via the condensation of 3PG with GTP. It is involved in the biosynthesis of a derivative of the hydride carrier cofactor co... |
A0A1X6P0G2 | MPQSGPAPPPPPPPPTAPRGHPWASSPPSPPPPQWVCSPLPPPPTASSPSPAPCAWRRSSSSTRASWASTLPSTCGCWRQRGGRRRRRRRGAGRGHCGHERVALWGGAVGRAGVGAPRRRGRGGGAPAGWLGDAAPPWAPVGGEADDESGGEEAPRYCTVCDLFKPPRAHHCSICRRCVLRMDHHCPFFGTCIGLYNHLHFFCFCTSTVAGGAILIALSAYLLAAARPLSRPDANRLLFAAVFGTVVAVALGVLTAWHALLLARGVTTLEWLGGARWGRGERPRGAGRSRRLRRAAAGGGDGGGGGCGGDDGRQPSTEGL... | Catalytic Activity: hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein]
EC: 2.3.1.225
Subcellular Location: Membrane
Sequence Length: 373
Domain: The DHHC domain is required for palmitoyltransferase activity.
Sequence Mass (Da): 39041
Location Topology: Multi-pass membrane protein
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A0A9E3HXW8 | MADFRLQLRWRSALLLVLAAIVTGLIYNGFGGIALVAPQDTARRALGTGLPVEDGIHLVGLDAARQFIDQAQGPVVDARSPEQYGEGHISGAVNCYVYELETYLPPLLERVALDDPMMIYCAGADCEDSRFLAQTMQELGFKRLYVYEGGFENWKQAGLAIGTGTDSTQPAATGSGVRQAADFSRYVPAWLWLAGELALLAFGVWILVLLKRGDTDSFAPGLALRVVGLVFVLASLYKIVSPAQFARIVDNYQILPPATVNFTAIVLPWLELISGLLLLAGLVRGGASLVLAGLTLVFIAAISFNLIRGVEFDCGCFGSG... | Pathway: One-carbon metabolism; methylamine degradation.
Function: May be specifically involved in the processing, transport, and/or maturation of the MADH beta-subunit.
Subcellular Location: Cell membrane
Sequence Length: 354
Sequence Mass (Da): 37971
Location Topology: Multi-pass membrane protein
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A0A974UXU4 | MSLARFRTPEANQWRIGVIDGPNMPNLGHRSEAIYGPIKSLADLQRLVAELADEIGVAVTPFASNHEGEILDFIHRTALEVDGYVINPAGLTTYGEATRHALDDTGKPVVECHFANTARHFAGVTPPYLAQQSRFTYTATGLVMGLRQYSYLGALLALTLALDDADFLAGGARRH | Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7.
EC: 4.2.1.10
Catalytic Activity: 3-dehydroquinate = 3-dehydroshikimate + H2O
Sequence Length: 175
Sequence Mass (Da): 19021
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A0A2D7FY42 | MRLEDKVIQVKQRRTAWATLSPQRTLGSAIEWLGAKQVALVSSFGTDSAVLLHMMSEINPSNPVIFLDTEFHFDETLRYLEDLVDRLGLTGIQRARIDPVSRKRLDPDQQLHRRDPDRCCQARKVEVLDRALKGFQGWISGQKRFQSSLRNDVEVLEVDVERNLIKINPLAYWSEQDIEEYLADHDLPRHPLASQGFASVGCWPCTTPLQVGESGRAGRWRGQDKQECGLHETQPLRLRNIL | Cofactor: Binds 1 [4Fe-4S] cluster per subunit.
Pathway: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from sulfate.
Function: Catalyzes the formation of sulfite from adenosine 5'-phosphosulfate (APS) using thioredoxin as an electron donor.
EC: 1.8.4.10
Subcellular Location: Cytoplasm
Catalytic Activity: [t... |
A0A2E6YZF6 | MRLLDRYLIREWLFPFLICLIGFMVLWIAFDLIEELDEFAGLGVAEIARYYWVTLPGNFFVVVPVALLLSLMYSINQHSRHHEFIAIRNAGVGMFRMSAPYLLVGLLLSAGMYWSNEKWLPSGLRQGEIIKSTRAEGGENALGPEWISDVKFRNDEARRSWQIPRFNRATGEMRGEGNNPVIISWKWDDEQPKREIMAASGRWENAGWTFQEVRDYKPTEGFPEAHAITWHKTLRLGEFDETPMQIEGELKIAPLFDKRAHKRWSVSLAEIDSYRRIHPNIAPEKKAILNAQYQARLAEPLTCLVVVLIAIPFAAPSGRR... | Function: Part of the ABC transporter complex LptBFG involved in the translocation of lipopolysaccharide (LPS) from the inner membrane to the outer membrane.
Subcellular Location: Membrane
Sequence Length: 375
Sequence Mass (Da): 42620
Location Topology: Multi-pass membrane protein
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A0A975B991 | MIKLGIDIHGVSDADQEFFSELTKLLVQNGHEVHILTGSEHTQAFENHLKNDLKLYWTHLFSITSFHLKSGTEVSSINGNPYMEEDMWNRTKAQYCKKHGIQLHLDDSAVYGKFFQTPYGKYYSNQQPETRKKIAVIGGSFNPVTQGHISMAEAVLDAVHDIYQIWLMPAFRHPFEKHKEYCPERIKMIRLIESEKIRYFGYEIDNKLFGETFATFTRLLDDPDYKNLYDFHMVIGSDCVLDFDRKWKHAGLLSKLIKFIIIPRPGYDLENYKGLLSCHPHIILGSVKTPDISASKVRKHIRQNKSIKGLVPDAIETYII... | 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... |
A0A661EGZ3 | MVFYIMIARLTGLKAWVHQRISAVFLMLVMPYLIWQIWINITDYQSLQIFVSSIFNQILLVITAIFLLIHSWVGLRDILLDYIWNDKILTFLLSFVATGLLVIFIWFLTLLFF | Pathway: Carbohydrate metabolism; tricarboxylic acid cycle.
Function: Membrane-anchoring subunit of succinate dehydrogenase (SDH).
Subcellular Location: Membrane
Sequence Length: 113
Sequence Mass (Da): 13432
Location Topology: Multi-pass membrane protein
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A0A945SNI3 | PEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPETSSESMEDEPVEEIEEESNLPEGESAPASAAEAYVDAVYESSQLNNRRPKYPLKARRKGMEGVVTLQVEVSVLGEPSEISILNSSGYRLLDREARRTVSRWRFHPATQGGQPVTSLVEVPIRFQLKG | Function: Interacts with outer membrane receptor proteins that carry out high-affinity binding and energy dependent uptake into the periplasmic space of specific substrates. It could act to transduce energy from the cytoplasmic membrane to specific energy-requiring processes in the outer membrane, resulting in the rele... |
A0A938Q130 | MSWFGKFVGGAFGFMLGGPLGAILGASLGHQFDIGMISFQCPELLRPGDQHRVQMAFFTATFSVMGHIAKSDGRVSPEEISFANRIMDQLYISGDMRNTAINLFQQGKSTDFPLDDVLDQFYKECHRRIDLIRMFLEIQIQEALADGSLDNKEEHVLLHICNRLRISQFEYERLKVRVMAQQRFNQYHQQQYQQRSDNRYQYQRQRQQHQSERPSRSKLQDAYEVLGLTPSASDEDVKKAYRRLMSQNHPDKLVAKGLPEEMMKLAKEKTQKITKAYETIQQARKK | Function: Regulatory DnaK co-chaperone. Direct interaction between DnaK and DjlA is needed for the induction of the wcaABCDE operon, involved in the synthesis of a colanic acid polysaccharide capsule, possibly through activation of the RcsB/RcsC phosphotransfer signaling pathway. The colanic acid capsule may help the b... |
A0A920J262 | MPDDNSFVKEQLNSFGDGKILVVDANGIDTVALLGDMIAEAGVKNGWSGIVINGYIRDIDIVKTLDIGVQALGTVPVKSEKKNQGTLGGEISFGGLTFKPGNYIYADNNGLLLSNTELDLS | Function: Catalyzes the aldol cleavage of 4-hydroxy-4-methyl-2-oxoglutarate (HMG) into 2 molecules of pyruvate. Also contains a secondary oxaloacetate (OAA) decarboxylase activity due to the common pyruvate enolate transition state formed following C-C bond cleavage in the retro-aldol and decarboxylation reactions.
EC:... |
A0A2Z6A9J9 | MQVIFAPWLGKMSDRFGRRPVLLLSLIGASLDYLLLAFSSALWMLYLGRLLSGITGATGAVAASVIADTTSASQRVKWFGWLGASFGLGLIAGPIIGGFAGEISPHSPFFIAALLNIVAFLVVMFWFRETKNTRDNTDTEVGVETQSNSVYITLFKTMPILLIIYFSAQLIGQIPATVWVLFTENRFGWNSMMVGFSLAGLGHSVFQAFEPLIGC | Function: Resistance to tetracycline by an active tetracycline efflux. This is an energy-dependent process that decreases the accumulation of the antibiotic in whole cells. This protein functions as a metal-tetracycline/H(+) antiporter.
Subcellular Location: Cell inner membrane
Sequence Length: 215
Sequence Mass (Da): ... |
A0A6P1MC47 | MYSASDLRKGLKIEIDGDPCVITDFQFSKPGKGQAIYRCKIRNLNTGNSFEKSYRSVDKVKKAALESRDFTFSYEAGDDYIFSDNETYEEVHLSAEQLGDQRFFIVEDMQVEILFHNNKALDITLPNFVEKAIAETEPGARGDTATNVTKPAKIDNGYEINVPIFINEGDIVRIDTRTGEYSDRVAKG | Pathway: Protein biosynthesis; polypeptide chain elongation.
Function: Involved in peptide bond synthesis. Stimulates efficient translation and peptide-bond synthesis on native or reconstituted 70S ribosomes in vitro. Probably functions indirectly by altering the affinity of the ribosome for aminoacyl-tRNA, thus increa... |
A0A432EMY1 | MHIGLTGGIGSGKTSVARLFAEHGAPVLSADESARAVVRPGSPLLQRIREAFGSRVMTETGELDRQAMREMVFADADARRRLEAIMHPAIRDHLHRQTETIHAPYLIIEIPLLVESGHGIETDRVLVVESPQDQRVDRVRKRDRIDSDAVRAIIRSQATDDDRAARADDIIANDGSLNDLARKVKELDLLYRQLAQSHNGAP | 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... |
A0A3D5DJN1 | MPRSEIEAEIQRLRGAVQTAKQDLRAVREQIPTTTAPDIANFIDTHLLMLEDAAITFDSERLIEARGCNAEWALKMRRDALVKVFDEMDDPYLRTRKDDVDHVVTRIQRILANHEQKKYEMDGNHLADIVVVTDELSPADAILMKKNGVAAFVTRYGGATSHMSILVRSLGIPGIVGVHGIHQYISEKELLIVDGDEGVVVADPDTVSLSHYRGQQSERRRHAESLEHLREVQAITSDGVEIELHANVELPGDFVAAQNVGATGVGLYRTEFLYVNRNDIPNEEEHFRAYRELINSVQGLPVTIRTLDMGADDDITIEGS... | 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... |
A0A924V5F0 | MKKAVSQSKSKAKVIQKKAKSKPVRKKKKDTFKEHPLSSSEMFNNREIGWLNFNLRVLAEAKDPQNPVLERLKFLAISSSNLDEFFMKRVGGLKRQIAYGLSPKSSDGQTPKKQLAMIAKALEPMLKSQQEIYHKLRLELHKENVHVETFDQLNESERVHLKKYFLNHIYPILTPLSVDPGHPFPFISNLSTSLGISLVQEGKDADEKIFARLKIPKLIDQWVQIRGTQKYIHLIDIVKQYVNELFPEMKVMGTVVFKVTRNADSDREDEDAEDLLATIEEELRQRRFAEIVRIEFGSCTDEWLKTFLIKELDFKNEDIH... | 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)... |
A0A534CLU0 | MNLIWYALWFVVAVSLLVTVHEFGHFWVARRLGFKVLRFSVGFGKPLVRRVAGADRVEYVIAAIPLGGYVKLLDEREGPVAPEDLARSFTRRPPWQRIVVLLAGPCFNILFAVLLLWGMFWASGVTEVKPVVGDLAQGSIAARAGLRSGDEIRAINGSAVTGQRDVVFGLLDAMSSRGEAALAVRAADGAVHTVTLSVPDAAQRRRLTEPAELFRGLGFQFWAPPIPAVLGQVMPDGPAARAGLKAGDQIVAIEGAPVSDFREIVARISAHPGETLAITYRRGGVEQTARVAVAAEEAGAKRIGRIRVMQPQGITYPASM... | EC: 3.4.24.-
Subcellular Location: Membrane
Sequence Length: 457
Sequence Mass (Da): 48940
Location Topology: Multi-pass membrane protein
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A0A924V5K6 | DVIKKAYRKLAMQYHPDRNPGDKAAEDKFKELAEAYDVLSNTDKRARYDQFGHQAFSQGMGGGGAGGFHDMGDIFSQFGDIFGDIFSQGGSSGRQQNARSKNSPRRGADLRYLHQMSLKDVLTSSEKEIEFDTEEQCAECTGTGGEKGSAAVTCKTCRGAGQVVRQQGFFSMATTCPTCLGAGETVDKACKPCQGKGRVKAKRKIKVTIPAGIDNGTRLRVTGEGEGGYRGGPAGDLFVEMRVEDHDVFEREGDHLFANLDVNYLQFLLGGEETVEALDGDIKVEIPRGSSPGDRIKIAGRGVPSLRGSRRGDLHYTINV... | 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... |
A0A920IUN6 | MQQNLHHSLYGPFRDAVGSLNNLANASKATYQMDSRNIDEALHEVALDLNEGC | Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 1/4.
EC: 4.2.1.24
Catalytic Activity: 2 5-aminolevulinate = H(+) + 2 H2O + porphobilinogen
Sequence Length: 53
Sequence Mass (Da): 5873
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A0A920P3T4 | MRKALLWASTNPFLAERLPRMRFVKRATSRFMPGESWEEALTEADRLSTRGMGTLVTLLGENLDSIDQADAVLDEYLGVLQDVSDAGVDLEISVKLTQLGLDFGPEVAQERLSRLAEATQSLVWIDMESSDYVDVTLEIFRNVMSTNRNLGLCLQSYLRRTEDDLDNLLPLDPSIRLVKGAYNEAREVAYPDKREVDEHYFTLSRTLLKARLNGGMARPVIATHDTRMIESVNRMAVELGADKDDYEFAMLYGIERQEQNRLVTSGHVVRVLISYGSSWFPWYMRRLAERPANVWFVAKQLFR | Cofactor: Binds 1 FAD per subunit.
Pathway: Amino-acid degradation; L-proline degradation into L-glutamate; L-glutamate from L-proline: step 1/2.
EC: 1.5.5.2
Catalytic Activity: a quinone + L-proline = (S)-1-pyrroline-5-carboxylate + a quinol + H(+)
Sequence Length: 303
Sequence Mass (Da): 34663
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A0A6L7SVA2 | MAGLIPREFIDDLMQRTDIVDVIDSMVPLQKKGQEYMACCPFHDEKTPSFTVSPQKQFFYCFGCGESGSAIDFLMKYQNLGFIEAIEDLSSRAGLEIPHSATASEFTTSHGHANRLLEIVDKANLWFQEQLKVNPDRKTAISYLRSRGLTARIILEFGIGYAPDSWNGLFNELGKTPTNVESLVTAGLISHKQDVQGRDRHYDRFRGRIMFPIEDSRGRIVGFGARDLTDKGPKYLNSPETPLFHKGRELYGLHRARRAIGKQNRSIVVEGYMDVVSLVQFGIENAVAALGTATTPYHVQRLFRLAPDIVFCFDGDQAGR... | 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: 591
Domain: Contains an N-termi... |
A0A945T5H6 | MLQKVIVVDENNKKVSLKEKNAVHIDGDLHRAFSIFVFNQGGELLLQQRSLEKYHSAGLWTNSCCSHPLLDGAGSEEAESRLRDEMGFSCELKKVTRIKYNLRLKCGMIEHESNDIYQGVYDGEVLINPEEACDYKWVNFSEVLDDLSRNPQTYTEWFKYLLLETPLGSALSASITVQSAQRDG | Cofactor: Binds 1 Mg(2+) ion per subunit. The magnesium ion binds only when substrate is bound.
Pathway: Isoprenoid biosynthesis; dimethylallyl diphosphate biosynthesis; dimethylallyl diphosphate from isopentenyl diphosphate: step 1/1.
Function: Catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isope... |
A0A972KUF9 | MKKKRASLSRRDFPAAAKIVAILRENPQPHKTIKRILQETREILHHAQSDGASSTNIISLWTWFIDQLLVNIWNFVHTPEPNANCGSLIAVGGYGRNELHPSSDIDLMILLDEKASNNIDNTFTESSKRFLYILWDIGLDIGHSVRTVAECKEAAVDLTVVTNLMEARLLFGSMALLQQMQAAIGPDQIWPADQYFHAKLQEQRVRHIRFGETAYKLEPNIKESPGGLRDLHMIAWATMRYFNATSLEELVQHEFLTRNEYQTLIRCRNFLWRIRNGLHFLAGHREDRLLFEYQRELATEFGYSDKHGNLAVEQLMKRYY... | Function: Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher ... |
A0A972GYB5 | MFDIGFWEITLILVVALLVVGPERLPKLARTSGLWLGRIRSMVQTVKTDIDRELAAEDLKKTLSKQADSIGIHDIIEETKESFNEIKDSMAGLDNTLNENLSESSTPAVADKKDVQAIDEK | 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. Together with TatC, TatB is part of a receptor directly interacting with Tat signal peptides. TatB may form an oligomeric binding... |
A0A923PYX2 | ARAGHALADRILALPEFRDALPELRIGIWCGPGHNGADGRIIAGVLAKKFNVQLLVGAAWSVENFEWIIDACFGIGLNRNIEPDVAKQIRWINRGKAKIISVDIPSGLDANRGTIFGEAIRATYTLTLLPAKPGLFLNEGTACAGKICGVSISLPKNIFNAEADSVFLIGPRAAKKLLRTRRATGNKSSFGHLLVVAGSAGTDGAAILTAEAAARMGCGYVSLCTSSSEIFRSARPDFLRLTPEEFLTSDLKKYSAVVIGPGLGVTEQSQKMLSHLLGSHKKVLVDADALTLLSKTKTPPLPPEWLLTPHAGELARLLDS... | Cofactor: Binds 1 potassium ion per subunit.
Function: Bifunctional enzyme that catalyzes the epimerization of the S- and R-forms of NAD(P)HX and the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. This allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that... |
A0A2G6DZF9 | MLGAGAMGMLFSRVLLDNNCQVTWLVRHMLETHRWASLRSPVLVESEHMLAPLRPVLLSDQKNTGEIPYLLVTTKAFDVKRGIARIAHRTTPNTQILLMTNGLGVREEIESLLPSATIYNGTTTAGAYRATPQRTVLTGRGDTRIGHADGSSSAPDWFADFASELINPVWSDNIQRDLLMKLAINCAINPLTAVLGCNNGKLENPKNYPRFCAVCEEISTVLAASGYTDIASSVFERALAVVRSTANNRSSMLQDVRAGKKTEIDYITGYLLAMAERQQVPAPHNTRLFKEINARATPH | Pathway: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantoate from 3-methyl-2-oxobutanoate: step 2/2.
Function: Catalyzes the NADPH-dependent reduction of ketopantoate into pantoic acid.
EC: 1.1.1.169
Catalytic Activity: (R)-pantoate + NADP(+) = 2-dehydropantoate + H(+) + NADPH
Sequence Length: 299
Sequen... |
A0A2D5PQ62 | MNQDSLINILSMSDHGVYVWIVVVVLFVILGSTIILLNRKIRQAKQEINEEA | Function: Required for the export of heme to the periplasm for the biogenesis of c-type cytochromes.
Subcellular Location: Cell inner membrane
Sequence Length: 52
Sequence Mass (Da): 5925
Location Topology: Single-pass membrane protein
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A0A534BD33 | MASGQTLSDEDAMQLVLEPGFSTAGAITQQAGRGVGMDVVATEIKRLGGALHMETKAGEGTVFTIRLPLTLAISHALVVRVDEEYYALPLPTVEGVLRLSKSVVTSHLGRDAPAFDYGGQKYRFQHLASFVGLPPSELPGQDVTIPVVLVRAGEHS | Function: Involved in the transmission of sensory signals from the chemoreceptors to the flagellar motors. CheA is autophosphorylated; it can transfer its phosphate group to either CheB or CheY.
EC: 2.7.13.3
Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
Sequence Length: 156
Sequen... |
A0A8T3QB15 | MQSEVENLSGLSRKIKVTVPQQQVQEEVDKRIKDLAKTVTRKGFRQGKVPKTVVEREYGPAVRQEVIQDILWQTLQQAFKEQNLYPAGTPQIELKNIEVNAPLQYEASFEVFPEIKLDIEDITIEKPATKIDEAHVTDVIEKLRKQNINWKEVDRAAAPGDLVVIDFEGFIDNLAFEGGSAKDFRLELGSKMMIPGFEEPILGAKAGDAVEAEVVFPEDYHAKQYASKPAKFAVKINKVMEAELPDLNDAFAADLGVSNGSLEGLQTEVRQNLENELERRIRDKVKVQIIDKMLAKNEIDVPQAAVEEEIKRLQKMMQKQ... | Function: Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase.
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
EC: 5.2.1.8
Subcellular Location: Cytoplasm
... |
A0A2D5I3V1 | MNKRPVNINLLKIKLPLTAMLSITHRVSGIIIFFLVLPVTVYGLFQLSNSQDSYNAITLFFHNNYLFKSIIIMLIVVLKYHIFTGVRHMLMDFHIISHSLASSQKSSVVTLVLFIIDALLTIWVLV | Cofactor: The heme is bound between the two transmembrane subunits.
Function: Membrane-anchoring subunit of succinate dehydrogenase (SDH).
Subcellular Location: Membrane
Sequence Length: 126
Sequence Mass (Da): 14401
Location Topology: Multi-pass membrane protein
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A0A2D5LC47 | MNLNAWLDYIANQHQQSIDMGLSRTEEMVGRLQLQQPAPKVVTVAGTNGKGSTITALESLLVGAGLRVLSTLSPHVVRFNERLRLNGAELSDAEICAAFSAIEQARQQAPVIALTYFEFSALAALWCARENQVDVALLEIGLGGRLDAFNVIDADIAVITSIGLDHEKFLGNTRDAIGAEKAGILRSGQRVVLGADMPESVLARCRELKLQPLCAGADFVVNEDPGRTAWDLSWGDERQVNLPLGNLAPSNIALAHQAALGLVQVSGAQLAATAAQAFIPGRMQQVTHRGRLLVHDVSHNPAAAKFLCRQLAQRNLRPKQ... | Pathway: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 7,8-dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate and 4-aminobenzoate: step 2/2.
Function: Functions in two distinct reactions of the de novo folate biosynthetic pathway. Catalyzes the addition of a glutamate residue ... |
A0A6P1MBX3 | MKEFQGLEKRIGYRFKDKQLLKASLTHPSYRYENPDVESDNQRLEFLGDSVLGLLAADALMKVHPEAPEGELTKFKSALASGASLARVAADLDLGGSLRMGRGEEAAGGAERESNLEDALEALIGAIWMDGGLKAVRRFFDRHIFQVLENTEPAMLNPKGTLQEFAQKKGFGIPEYSVVEESGPDHDRRFKVKVTVSTFVFRGDGRSRREAEKVAAEKAVRSLVQ | 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... |
A0A962XDM9 | MRLLIKPPLAGGLLLMVVAVLALSACGRQDPVSQGRINAFGSTVDLTLIGVDRGRADEITRILAKDMQAMETAWSATGDGPVPRINRMFNESDEPFAAPPSVLPLLRLSQRLSAASDGLFNPAIGHLVRAWGFQGRPADCLRPPPSDLIATAVSGAPSMQDIRIDGIRIASANHLVKLDFRDIQKGLAIDKTIARLQELGVDNASVAIEGNLRAIGSRDGHPWSVPVRGPDGGGILATLKLIGNEAAFTAGNYRRNFTWDGKIYHDIIDPRSGYPAEETASVTVLHADATTADAAATALFVAGPRDWHRVARQMGIRYVM... | Cofactor: Magnesium. Can also use manganese.
Function: Flavin transferase that catalyzes the transfer of the FMN moiety of FAD and its covalent binding to the hydroxyl group of a threonine residue in a target flavoprotein.
EC: 2.7.1.180
Catalytic Activity: FAD + L-threonyl-[protein] = AMP + FMN-L-threonyl-[protein] + H... |
A0A2E8K9N5 | MFYALYEQLAAINLFEWAGLVSGLLCVWLLIKQNIWTWPIGLVYSLVSLAVFMQTKLYSEFVLHIYYAGMNAYGWYYWSRSDPQDASLELPVARTDRLTGAVLFVTVAICVPLLAEFMQQFTDTDMAYADSTITILSFAAMWMTARKLIENWYIWLLVDIIATGVYIIKGIELYALLYCIYIGMALAGLVAWRASLLSRQQLQVETGPDSNHGDEKPVRVPL | Function: Required for nicotinamide riboside transport across the inner membrane.
Subcellular Location: Membrane
Sequence Length: 222
Sequence Mass (Da): 25282
Location Topology: Multi-pass membrane protein
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A0A6L7JPP5 | MFLGPPGSGKGSQAKYVIDEYAIDHISTGELLRSAVSEGTSLGNQIADIMQQGGLVPDQIVLQLISDYLDSSDLSKGFLFDGFPRNSNQAEQLQVILAERNVPLLFVLHLQVDPIAVVKRLSGRRNCSNCGRIYNIYFDPPQVEGQCDDCGSTGVLFQRADDNEASIRNRLDVYESETAPLLEYYERAELLVTVDASGDLDEVAEAVRQVIRTELCKS | Pathway: Purine metabolism; AMP biosynthesis via salvage pathway; AMP from ADP: step 1/1.
Function: Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism.
Catalytic Activity: AMP + ATP = 2 ADP
EC... |
A0A521R8G5 | MSCNPAAANRRIKSYVLRQGRITPAQKKALTEYLQRYAIRAGASPLDLNEIFGRSAPRVLEIGAGSGEFTLCEAALHPENDYLAAEVHAPGIGRLLQGIAAGGLTNIRVIDQDVVVALQGLIPEDALDQAMIFFPDPWPKQRHHKRRLINREFLDLLVTRMRAHGRLYLATDWQELAEEIRTLGDAHPRLWNLAGPGYFAPRPAWRPETRFERRGKRLGHEVYDLVYCLR | 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: 230
S... |
A0A525CG08 | MVAHLEQIISIAGQAGAAILNYYNGHREIVAEYKEDHSPLTEADKEANRIITDGLIKLASDIPVVSEENALLPYSVRQNWKTYWLIDPLDGTKEFINKNGEFTVNIALVENGRVVLSVVYAPAIGVFYYGDKNKGAFRRESGITKKITVRKANPDNFIAVGSRSHKDSRSAELLNKIDVVTEKSVGSSLKFCMIAEGVADIYIRTGKTSEWDTAAAQGILEMAGGKVIREDGAELLYNQKESILNPGFIALGVVPDRIEKSLLPW | Function: Converts adenosine-3',5'-bisphosphate (PAP) to AMP.
Catalytic Activity: adenosine 3',5'-bisphosphate + H2O = AMP + phosphate
EC: 3.1.3.7
Subcellular Location: Cell inner membrane
Sequence Length: 265
Sequence Mass (Da): 29183
Location Topology: Peripheral membrane protein
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A0A6L7JRF5 | MSASRKRKRLGQHFLVDTQVIDEILLLIRPQINQTLVEIGPGRGALTDHLIRSSAELHAVEIDPDLVQELQKLFSPDALTIHHADALKFDYSSVKCENQELRIVGNLPYSISTPLMLHLVKFTDIIEDMCFMVQYEVAERLTARCGTSSYGRLTVCVTRAFEVETIFHVEPDAFSPPPEVRSSVIVMRPKPLIAFDSDSERIFSELVRLAFGKRRKTLRNSLNGVIDVAMFQETGIDAGLRAENLSVENFMELAKCAVARDSKRKTKVMTHHD | 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(+) +... |
A0A8T7I8F5 | MRLIEHKTVVILGAGLTGLSMLRFCLESHASVTVMDSRQAPPLLKEFEAYQHDVELIFGAFNKSLLTDADYILVSPGVDLNNVPMARDELEAKMLSDIELFVFEATAPVVAVTGSNGKSTVCDALGFVLNTINRKTVVAGNIGVPVLDLLGKDIPEFYVLELSSFQLDLVKSLKAKVACILNVTEDHLDRHGSMAAYVNAKQKIYQGSELCVYNFNDPLTKPRLESHSSRKYSELTFGFDQNADIRVVLSEQGFSVNSESRMYLSEAETKLKGAHNGLNIAAILAILSALELPVDQDAISAIKNYSGLAHRCQEVETNDG... | 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-... |
A0A2E7GAQ5 | MSFKLNLYTPQRLIGSKIEVISVTVPTTEGQLQFLEGHAHEAGLMDTGLFSYQTAQGEFTGVISTGFYRFEEGILTVSAETLEYSAEIDLDRAKRAEAKSEEKMNSSDLEFENFEKYERKLQRALVRQQAAGK | Function: Produces ATP from ADP in the presence of a proton gradient across the membrane.
Subcellular Location: Cell membrane
Sequence Length: 133
Sequence Mass (Da): 14994
Location Topology: Peripheral membrane protein
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A0A976KHI1 | MTVPTRAVAHPPVNQSFPRQLRLTRAREFEQVLRRPDARLKAGPLRLNFVFNRMHHARLGLIVGKKAVARASARNRIKRVIRERFRKAQNELPAVDVVIRVIGPVSRSHLHRYVDRLLAELESLPDNAQRP | 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... |
A0A3D1EIP8 | MVSLSRLACCDAEGVLVMQSQCARRSDACSILWHTRIEDSPGYTMTANDPDTAREALTSPLPIPLYDAAVTRLVDAAAMRDVAAGGMGLEGFELMRRAALAARDLILREWSPLASVSILCGKGNNAGDGYLLAALLAEVGIAVVVVPAVLESELTGDALAANVFFREHIGLPKSLCKIASREALDELEPDLIVDAILGIGFRHPLAEPLIDIVNWINAQACPVLALDMPTGVEVDTGFGSVAVQADVTLTFITQKVGLHTGIGKAFAGRVICDDLAVSAVRQQYPATTHLHHWRARRLPALSVTAHKYQRGRVLLFGGDL... | Function: Bifunctional enzyme that catalyzes the epimerization of the S- and R-forms of NAD(P)HX and the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. This allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent h... |
A0A2E6IZ44 | MKKVVIFSSGTGGHVYPAYTLAEKYLSEGYDIIWVGTTHGLENKVVKNKKIQIEHIHASGFRGKNFLEKIKSIFYLGYSLYESFKILRNHCPCLIIAFGGYVSLSGILVSFVMRIPRIIHEQNAIAGTANKINYFLSNRVYETFPGSFKSLNNKILHTGNPVRSSFQKCRQPEEIYLENQFHLKILVMGGSLGSSFLNTTIPFALSHFPTQNLAVKHICGHGKLSNLQKKYIEYNLDAEVLEYSDNIDELFNWASLVVCRSGSTTISELASIGRACVLIPFPYATDDHQYKNAEYLSNNSAAITLKQSDDFIENFVTTLN... | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Cell wall formation. Catalyzes the transfer of a GlcNAc subunit on undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide (lipid intermediate I) to form undecaprenyl-pyrophosphoryl-MurNAc-(pentapeptide)GlcNAc (lipid intermediate II).
Catalytic Activity: di-t... |
A0A962U493 | VCTIETPEGPNIGLINSLAVYARTNKYGFLETPYRKVENGKVIDQIDYLSAIEEGRYVIAQANATLDAKGKLVDDLISCRHQNEFTLSTPDKIEYMDVSPKQIVSVAASLIPFLEHDDANRALMGSNMQRQAVPTLRAEKPLVGTGMERTVAVDSGVTVVSKRGGVIESVDAARIVVRVNDDETIAGEPGVDIYNLTKYTRSNQNTCINQRPLVLVGDEVARGDVLADGPSTDMGELALGQNLRVAFMPWNGYNFEDSILISEQVVKEDRFTTIHIEELTCMARDTKLGAEEITGDIPNVGEAALAKLDESGIVYVGAEV... | Function: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
EC: 2.7.7.6
Catalytic Activity: a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1)
Sequence Length: 795
Sequence Mass (Da): 88029
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