ids stringlengths 6 10 | seqs stringlengths 16 1.02k | texts stringlengths 117 4.4k |
|---|---|---|
A0A1M4T529 | MRTLFFQQMNLQKKLAIILVLFIFAPITIIGIFYNVNAQRYVSNQIDQDTSQTVTLVKENTDLLLQNYETQIKSIYQNEEIIRQLQANKTDIKKGNEEIYLFLRKFIRDNESIESIYLFPSRFNQLFFWDYKGSNYFIHQWKNHPEWQKSITKSNGKIVWIKTYRSPPNRYHSKNNYYFLGGFQIKNISNALEPLGTILFNVRTEAFDQIMNDIEVSKNGFILLVDPMGNIIWHRNTSIIGENIAHLEAFKKLSKKNQAFAYQKLNGIVYRVGMIQSKYNQWQYLSFIPTGDIEDKTKDIKKYTLIILLIIISIFSLLAW... | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Membrane
Sequence Length: 600
Sequence Mass (Da): 70331
Location Topology: Multi-pass membrane protein
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A0A293LK75 | MASDLSAEGVPSVAYHAGLDDARRNQVQRLWIDDKVRVVCATIAFGMGIDKPDVRFVMHHSLPKSVEGYYQESGRAGRDGRPAVCILFYNYGDMHRIRRMVEQDVSNPAARQTHLTNLWHVVNFCENRTDCRRAQVLHYFGENFDREFCRRNPHASCDNCSSRGRWVTRDVTDAARDLVRCVQGFNGTNVTLNHIVDIFRGAAIKKIIEMGHNKLPLYGKGKGYSRMDAERLARKLVLDGFLKEVSTINHLDMAISHVRVGNRAPELVQGNAKISLAVEKESKASESSVAVQELPADAEMDKLTESCHNELVEMVKSLAR... | Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
EC: 3.6.4.12
Subcellular Location: Nucleus
Sequence Length: 491
Sequence Mass (Da): 54833
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A0A0S8IV55 | MRIAVDAMGGDRAPGEVVAGTVLAAREFTDTEFLLVGDETSVKEELDQHDGGAFPSISIVHAEQVLSMDDAPIVAVRAKRNSSATVSVKLVAEGKAEAVVSAGNTGGTVAAAAVFLKSLGGIKRSGIAATFPTRFGTTTVIDVGANIHCRPIHLLHYGVMATIYAQQMLDIENPRVGLLNIGAEDRKGNELVRETRELLEGHPRVDFVGNIEGYDIHRGVCEVAVCEGFLGNVILKIAEGLSASLVDDVEERLKKAFPGDTDKYAGVVHELRRRNDAAEYGGAPLLGVDGICIIGHGSSDARAIYNALRVARGFGGKHVN... | Pathway: Lipid metabolism; phospholipid metabolism.
Function: Catalyzes the reversible formation of acyl-phosphate (acyl-PO(4)) from acyl-[acyl-carrier-protein] (acyl-ACP). This enzyme utilizes acyl-ACP as fatty acyl donor, but not acyl-CoA.
Catalytic Activity: a fatty acyl-[ACP] + phosphate = an acyl phosphate + holo-... |
A0A8C0FQ31 | MTVELKRKKKNPLACGETLKLEVCGSCFLALFIWLLILFYLTLFQIHPKKGKFLAAKAQEMGLPVGTPAILPIITALKNGESVTFEGKELSPEELCTPADPGPVFIVLECPHEGFVDAVCENETFQRYQEGLPENQVALVIHMTPESVLRDSRYQQWLERFGPGTQHLVLNENSSAVHNPRSYKIQTQLNLIHPEIFPLLTTYQSKEEKAVCSVPIVRGECLLKYHFRPQQEWQRDAVTVCDHDAFVSEALDLPDFQTRVKECKESLSAVPGNVCPYPEVVFLGTGSAIPMKIRNVSSTLVNTSSTRSLLLDCGEGTFGQ... | Catalytic Activity: Endonucleolytic cleavage of RNA, removing extra 3' nucleotides from tRNA precursor, generating 3' termini of tRNAs. A 3'-hydroxy group is left at the tRNA terminus and a 5'-phosphoryl group is left at the trailer molecule.
EC: 3.1.26.11
Subcellular Location: Mitochondrion matrix
Sequence Length: 628... |
A0A3G9J2V9 | MNWMEKELELLAEDSLERFLRDSAPVPECPGYTVRGERLLLNLASNDYLGLAQHPAIIETMREMLLTEGGGSGASRLVTGNRPPYGRLEEALATWQNSEAALVFANGYMANSGVIRALMGRGDVVFSDQFNHASIVDGIVLSRAEHARYRHNDKDHLKLLMNKHRDKRRKLIVTDAIFSMDGDQARLRELVELKCEYGAMLMVDEAHSGGIYGERGEGLCYELGLHNEVDIHMGTFSKSFGVYGAYVCGSRNLIRWLINKARPLIYSTALPPSLVAGVSTALDLVKVDYWRRERLFSASRLFRSSLCEAGFNVINGDSPI... | Pathway: Cofactor biosynthesis; biotin biosynthesis.
Function: Catalyzes the decarboxylative condensation of pimeloyl-[acyl-carrier protein] and L-alanine to produce 8-amino-7-oxononanoate (AON), [acyl-carrier protein], and carbon dioxide.
EC: 2.3.1.47
Catalytic Activity: 6-carboxyhexanoyl-[ACP] + H(+) + L-alanine = (8... |
A0A3R7VNQ6 | MLNFNKTFLKNLHVIKIDPFKDIRGEFARFFCEKDFKEIGLSKKIVNVNYSKTMNKGDVRGMHYQKSPYAEIKIVKCINGKIYDVAIDMREDSDTYLQYFGIELSQDNNTMLYVPEGFAHGFQSLTDNAEIIYFNTQFYKPEFEKGVNIIDPRIDIKWPIQIANQSEKDKKIKFIAN | Pathway: Carbohydrate biosynthesis; dTDP-L-rhamnose biosynthesis.
Function: Catalyzes the epimerization of the C3' and C5'positions of dTDP-6-deoxy-D-xylo-4-hexulose, forming dTDP-6-deoxy-L-lyxo-4-hexulose.
EC: 5.1.3.13
Catalytic Activity: dTDP-4-dehydro-6-deoxy-alpha-D-glucose = dTDP-4-dehydro-beta-L-rhamnose
Sequence... |
A0A4Y6EML0 | MEEYRNLNAELNLYDESGKIQFDKDKEAARAYFLQHVNQNTVFFHSLEEKTNFLVENRLWDQEVVNRYPFEDFKALFKQAYAHKFRFQTFVGALKFYRGYALKTFDGKRYYERFEDRVVMTALTHSNDYEHAKRLVDHIIEGRFQPATPTFLNAGRTDAGGPTSCYLLRVEDNLESINRAQSDAAQLSKRGGGVALSVTNIREAGAPIKGYEGKSSGVIPFMKVLEDTFSWIDQLGQRQGAGAIYINAHHPDVMKVLDTKRENADEKIRIKTLSIGVVIPDITFELARNNDDMYLFSPYDVEKEYGVPMSDISITEEYER... | Pathway: Genetic information processing; DNA replication.
Function: Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides.
EC: 1.17.4.1
Catalytic Activity: [thioredoxin]-disulfide + a 2'-deoxyribonucleoside 5'-diphosphate + H2O = [... |
A0A8C4ADI5 | HPLKMTSVRPFCFILQGLLLVGFYQVESGNVLVIPGEFSHWHNMRVIVEELVERNHSVTVLVSTASNTVKYAKEEGFKFQFFSVSREEHEFSAMWDEMTDIWVQFKNSTILHTVSRVIDLMKNVSAFEICEAMIKNETVMGTLRQSKFDVVLYDPFTPCGDLLADMLNVPLIVVMKMFFGYALERICGQMPSTPSYTPTHPVRFSDRMNFPERVQNFLQHVMLTTIFYTLTHVQLNPLYSEIKGEPITFCDSIGKAEIWLMRSYWNWDYPRPFPPNFVFIGGYHCKPPKPLPKDMEDFVQSSGDDGIVIFSLGSIYKNQN... | Catalytic Activity: glucuronate acceptor + UDP-alpha-D-glucuronate = acceptor beta-D-glucuronoside + H(+) + UDP
EC: 2.4.1.17
Subcellular Location: Membrane
Sequence Length: 533
Sequence Mass (Da): 61628
Location Topology: Single-pass membrane protein
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L0DVN6 | MSHRYTIALDVMSGDHGASVVMPAALGALQETPDIRLVLVGDEAVIAAHMRHWPEPVKPRAEILHASQTVGMEELPAVALRNKKDSSMRRAIDLVKQGDAEACVSAGNTGALMATARYVLKTLAGIDRPAIATALPSLFGHTHMLDLGANVDVEAAHLYQFAVMGSVLVTAIDNNDAPRVGLLNIGSEAIKGNDRVREAAHLLERSSLNYIGFVEGNDVYCSDVDVVVCDGFVGNVALKTSEGVARMILENIRGEFKRSWLTRLRGLVALPVLSRFRSRIDPRRYNGASLLGLQGIVIKSHGGADALAFQNAVRIARKEA... | Pathway: Lipid metabolism; phospholipid metabolism.
Function: Catalyzes the reversible formation of acyl-phosphate (acyl-PO(4)) from acyl-[acyl-carrier-protein] (acyl-ACP). This enzyme utilizes acyl-ACP as fatty acyl donor, but not acyl-CoA.
Catalytic Activity: a fatty acyl-[ACP] + phosphate = an acyl phosphate + holo-... |
A0A1F7TKA3 | MLPRLMRGVLVFALLGAAIGLVAGAAGGIAYYRKVARELPDVELLRTYRPSLVTRVFDQHGGLVREFFVERRFLLPLEEIPQTVIQATLATEDSRFEDHPGIDVIGIARAALRNLSGGEIVQGGSTITQQLAKTLFLTPERSLDRKLREAVLAIRIEGRFNKREILNLYLNQIYYGHGAYGIEAAARVYFGKGAKALSLPEAALLAGLPRAPSAYSPFRSLDRARRRRTHVLRRMYDEGYIPAMERDLASRAPVFLAKAPPSGGEAEYPVEQARRQVERQFGSQRLYRDGLHIHTTINSDIQHEATLALRRGLREVDRRR... | 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-alanine.
EC: 2.4.1.129
Subcellular Location: Cell inner membrane
Sequence Length: 833
Sequence Mass (Da): 91167
Location Topology: Single-pass type II membrane protei... |
A0A6G7PRS1 | KDIGTLYLVFGAWAGMVGTALSLLIRAELAQLGAFLGDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGISSILGAINFITTIINMKPPAISQYQTPLFVWAVLITAVLLLLSLPVL | Pathway: Energy metabolism; oxidative phosphorylation.
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytoc... |
A0A9E1MP33 | MNKARITAILTAVIIMLFQVCPTTAQPAPSNSPKPSATQIDTNISDSPESTEVPEKPSFPEPHAKAALLYDMKGGRVLYENNASEKNFPASVTKIMTALLALEKGNLSDIVTVSSSALADITYLHSRINLKSGEQMSLENLLTALLVSSANDAANVIAEHISGDIPTFVALMNQRAAELGMTNTHFANPHGFHDDNHYTTASDIAIMTREALKNTKFCELVKIKVTSIPATNKSNERKISTTNHLISKYRNTFHFYPYATGVKTGATVEAGNCLVSTAEKNGVSLMSIVLGCENADSEENAYSFVDSKAMFEYVFENYES... | 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... |
E1BCG5 | MPALARLRRLCRHVSPQAVLFLLFAFCLFSVFVSAYYLYGWKRGLEPSADAPEPDCGDAPPVAPSRLLPLKPIQAATPSRTDPLVLVFVESLYSQLGQEVVAILESSRFKYRTEIAPGKGDMPTLTDKGRGRFALIIYENILKYVNLDAWNRELLDKYCVAYGVGIIGFFKANENSLLSAQLKGFPLFLHSNLGLKDCSINPKSPLLYVTRPSEVEKGVLPGEDWTVFQSNHSTYEPVLLAKTRSSESIPHLGADAGLHAALHATVVQDLGLHDGIQRVLFGNNLNFWLHKLVFVDAVAFLTGKRLSLPLDRYILVDIDD... | Pathway: Glycan metabolism; heparan sulfate biosynthesis.
EC: 2.8.2.8
Subcellular Location: Membrane
Sequence Length: 882
Sequence Mass (Da): 100961
Location Topology: Single-pass type II membrane protein
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A0A371SJQ9 | MIQQKGLSDYIKKGINLSKELSRPVLISQVKEMKNIDPLLFFSAGKRTPFETRSFWSNPTNDTIIVGLGEAYTISDNESTERFDAIEKQWKRLVRHSIIIDDFAPYSTGPILMGGFSFDPLKKRTELWDYFDDAKFVLPVIMLSYYKGSTYITTNIICDPTGTSFGGSDLEQLEVLLEESYKFQKNNSFTKEEVQPQEWMDSVRNATQKVQNGEVEKVVLAREIKLHFDNPIEADAVLARLKEEQPMSYLFAIEYKNSCFIGASPERLIKKKGEEFLTTCLAGSIRRGKTPSEDKQLENELLHDPKNLHEHDVVVQMIKN... | Pathway: Quinol/quinone metabolism; 1,4-dihydroxy-2-naphthoate biosynthesis; 1,4-dihydroxy-2-naphthoate from chorismate: step 1/7.
Function: Catalyzes the conversion of chorismate to isochorismate.
EC: 5.4.4.2
Catalytic Activity: chorismate = isochorismate
Sequence Length: 463
Sequence Mass (Da): 52170
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A0A1Y6CNP4 | MFDSGFLALTQNVGLLALLVVAYGGLACAVAALPAAVRQLLLGGLFGLSGLLLMAFPFETGSGLIFDGRAVPLLLAGPFGGGPLAALAAGLLVAAGRLAIGGDGVLPSLVVALAVVALSSGLWLLRSRGGRFDAGILALGGLAASAALFAGLFLLGRETAVGLVAGLGPAYLTTVAGATALFGYLLLLDDRRREALAGAEAARRAADLANASKSRFLARMSHELRTPLTGILGMVDLMARDATPQARQGYLEALRGSGRILLTLIDDILDLSGLEGGGLTISPGEVSLHRLTFDVVSVFEPRAQAKGLTLRLVIDEAVPE... | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Membrane
Sequence Length: 759
Sequence Mass (Da): 78279
Location Topology: Multi-pass membrane protein
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D4K908 | MKIIYKDGHVDECPQDQELHVIRHTAAHVMAQAIKRLYPQADFAFGPATENGFYYDVDLGDQKLSDEDLANIEKEMRKIVKENLPIKPFILPRAEAEKLMEERQEHYKVEHMADLADETEFSFFQQGEYVDMCIGPHLTYTKALKAFKITQQSGAYWKNDKENKMLTRINGVAFRNQEELDAWEKEQQEARERDHRKIGKEMGLFMTDDLVGRGLPMFLPAGYTVWQELENYIKEKERARGYLHVMTPCIGTVNLYKTSGHWDHYRENMFPAMEMEGESYVLRPMNCPHHMMIYANRPHSYRDLPMRIGEIAHDFRYESS... | Cofactor: Binds 1 zinc ion per subunit.
Catalytic Activity: ATP + L-threonine + tRNA(Thr) = AMP + diphosphate + H(+) + L-threonyl-tRNA(Thr)
EC: 6.1.1.3
Subcellular Location: Cytoplasm
Sequence Length: 594
Sequence Mass (Da): 68572
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Q13G68 | MAFAMAVALHLVALYFLTARQVDIHLASEQQPGATTISVSLVAAPPVPMAAPVAQTVAAVPPRAEPQRHAKATKVLATHRDSKATTAQQARAPQTVPTSPAPVTKQVMPPVSSPAALPSALSTAQAAAAHPDDGKLMSLPKVIGASSLNQLGCRIPRPTYPARARRLGESGVVRLRIRIAVDGHLADVQVVQSSGFPDLDTEAVHAVSAGSCEPYRENGVATAVTAEQPVAFDLDP | 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... |
A0A0S8J5E4 | MTFLGFAYYVANWPKVTDFVIETETEMKKVTWPTYREVLAATVVVIVVVIILGAFLFGVDRIVLEPLFKLIGILPKMSAG | Function: Essential subunit of the Sec protein translocation channel SecYEG. Clamps together the 2 halves of SecY. May contact the channel plug during translocation.
Subcellular Location: Cell membrane
Sequence Length: 80
Sequence Mass (Da): 8981
Location Topology: Single-pass membrane protein
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G1K1P6 | MYSVLYELQPFPDNYVDRRFLEELWKNIYAQKYQYWAVVFESSVVIQQLSSVCVFVVIWWYMDEGLLAPQWLFGTGLASSLIGYVLFYLTDGDEGRKKSERTRRADLKGAQVFITFTYGFSPVLKTLTESVSTDTVYAMAVFMLLGHLIFFDYGTNAAIASCTLSLNVAVFASVCLASRLPRSLHAFIMAMSAIQIFALWPILQKKLKACTPRSYVGVTLLFAFSALGGLLSLSAVGAILFALLLVSISCLCPFYLIHLQLFKENIYGPWDEAEIKEGLSRFLS | Pathway: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor biosynthesis.
Subcellular Location: Membrane
Sequence Length: 284
Sequence Mass (Da): 31985
Location Topology: Multi-pass membrane protein
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A0A944FYD4 | MLNFNKSQGLGNDFIIIDNRDGYFSDLGALAQKLCPRAISVGADTLLVIENSETCALKMRTINADGSEAQMCGNGIRCFAKYAYERGLVSTDKFSIETKAGIITPKLNISNGLIESVTIDMGAPLFERSAVPMKGDGRFIDGELVADGKSYVASSIFMSIPHTIVFADDPYAIDIASVGPAIERHKLYPEGTNVNFVKIIDRNTMQSRPWERGCGATLACGTGACAAAVVGFVTGRTERNVEVKMALGSLFIDYRTDGRVYMTGPAVSVYDGKIDI | Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; DL-2,6-diaminopimelate from LL-2,6-diaminopimelate: step 1/1.
Function: Catalyzes the stereoinversion of LL-2,6-diaminoheptanedioate (L,L-DAP) to meso-diaminoheptanedioate (meso-DAP), a precursor of L-lysine and an essential component of the bacte... |
A0A943XD75 | MNRFDYHMHCSYSFDSEAKISDQLLAARRMGLTEICFTDHVDFDELKKPYPRPLPDLDARRREIESLAKDFPDITVKHGAEISLSDASAAERAEAYLEGKNLDFVIGSVHAVNGVETYYEDYMAGRTKQTAYYDYLDAICKGIKPCKMMNVLGHYDFVAKFTDYADRRMTLDVSKELFYEIFKLLIERGKGIEVNTSAWKDDPCWGLDVLKLYRELGGEFITTGSDAHIPKNVGRRLDEACALAKEAGIPYIASFDKMKPIFHRL | 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: 265
Sequence Mass (Da): 30288
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A0A3Q1M6Q6 | MMTRNSPTQRWLTLATSWMRVATLRTLSKVYGPVFTVYFGMKPTVVLHGYEAVKEALIDLGEEFSRRGSFPVIERNVKGHGIVFSNGKTWKETRRFSLMTLRNFGMGKRSIEDRVQEEARCLVEELRKTNGLPCDPTFILGCAPCNVICSIIFQNRFDYKDQTFLNLMKTINENIKILGSPWIQVLNIFPVLLDFFPWSYSYKKLYTNTAYVKNYVLEKTREHQASLDINNPRDFIDCFLIKMEQEKHNHQSEYTFENLTITVSDLFGAGTETTSTTLRYGLLLLLKHPEVTAKIQEEIDRVIGRHRSPCMQDRTHMPYM... | Function: Cytochromes P450 are a group of heme-thiolate monooxygenases. In liver microsomes, this enzyme is involved in an NADPH-dependent electron transport pathway. It oxidizes a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics.
EC: 1.14.14.-
Subcellular Location: Endoplas... |
L0EIX2 | MDMGQPTLVRWIEIDSPVGPLVLLKADGRLCRVEFGRMEERRAALTAWAAEHGLAGDFRHAPDDPLLKEAAAQLAAYFRGERFRFELPTAMYGTPFQKAVWAALAAIPYGEVRSYKAVAGAIGRPSAVRAVGGANNRNPLPIIVPCHRVVGADGSLVGYAGGLDAKRRLLELERLAANVARPLANVL | Function: Involved in the cellular defense against the biological effects of O6-methylguanine (O6-MeG) and O4-methylthymine (O4-MeT) in DNA. Repairs the methylated nucleobase in DNA by stoichiometrically transferring the methyl group to a cysteine residue in the enzyme. This is a suicide reaction: the enzyme is irrever... |
A0A1Q7S1Z7 | MHPLEQLRDDALREIESARDERALETARLKYLGRSGTVSAWGEQMKTLAKEEKPVVGKLLNEVRNAVTAAIDIRAQQFRSQKETGGLAKIDISLPGTPHELGALHPLTQMLERSIEIFRRMGFALADGPDVEDEWHCFDALNTPPEHPARNEQDTFYLPDGRLLRTHTSTVQIRTMQSAPPPIRVIAPGAAYRRDEVDATHSAQFHQIEGLYVDENVSVADLKGSLEFFMRELFGADTAVQFRPHYFPFTEPSLEIYVKSKALKKGEQWIEVAGSGIVHPAVFEAVNKARGDKAYDPEKWTGYAFGLGMDRLAMILFDIP... | 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: 337
Sequence Mass (Da): 38017
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A0A2M8C375 | MRILAIDFGEKHIGCAIADSNGHVATKLPTLEVVSMHDAVSRVGIVVKSEHIDLVVLGLPLSFQFEQTPMCEIVRTFANALAAATGVRIAFVNEILSSDLSKQFMHAQKDHSVSAQILLQDYLDKTDERIT | Function: Could be a nuclease involved in processing of the 5'-end of pre-16S rRNA.
EC: 3.1.-.-
Subcellular Location: Cytoplasm
Sequence Length: 131
Sequence Mass (Da): 14360
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A0A1T4ZT52 | MAKLKSTLPNMLLSLTIICAGAGAILAGVNDFTKAPIAASKAAALENAIKEVTPPFDNNPTQEAYKAVSADGDSLLIYPAKKGGELIGVAVESSTQKGFSGEIKVIVGFDVEGKLFNYSVLQHAETPGLGSKMQEWFRTDKNKQNVLGRSLADGNLTVSKDGGDVDAITAATISSRAFLDAVNRAYSAYAGTQKWDGESGATSVGTDTETTSQTVTEKEGDKHE | 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: 224
Sequence Mass (Da): 23465
Location Topology: Single-pass membrane protein
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A0A9D9E3P8 | MKIKNLKKPFTIRLVIAAAVTAAVLAAFAIYAYIVLNKPIGGESHLLYINEMTTRQSLYDELAPVYGTRNAKLVDTMLKVRRRRPDRYPGCYILTADMTPLQLFRLLTMGDDSTVNYTFNNIRTKQELAETTSKYLNLPADTVLAMLNDTVLCKSLGFDTVSIVSMFLPDTYQVYRCSAPYAFMKRMKREYGKFWNDTRKALAKNAGLTPYEVSILASIVEEETKIPEEMNRVAGLYINRLNKGMLLQADPTVKFAVGDFSLKRILNKHLETDSPYNTYKYPGLPPGPIRIPSKTALNAVLNFEKNNYLYMCAKEDFSGR... | 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: 347
Sequence Mass (Da): 39566
Location Topology: Single-pass membrane protein
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A0A9D9IA42 | MFFITALDFTASVKLFEHLQNRGNELLIKAGRKIMKSVRCPFVLIITCDRAELISEEKVSPEILERALSVSPIEAAACRYSISPEDSVRHILLLATGILSPLFGEDTIQGQLTSGAECARLIGSSSPALDKLISSAVSFSRRVHCSRKIRVIDRTIIEKTAETVKDCSKILIVGSGECARLVAERIKGCHEVTMTLRDADKTYLVPDGVRPSSYDDRIKDAEKAEAIISASSGLYHTFTSEELAELDDNKILIDLASPPDLPDYPGVIRIIDMDIDLPERNGVIAYVSSEAEKEEESFYAYIEKSKAMPDLKEEADALSY... | 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... |
A0A9D9E545 | MSTIKEIKGRISSTRSSEKITGAMKMISTAKLRKAENSLRQLKPYREQLRSAIVHLLDSDGDYPSPLTEKRPVQKMAIVVIGSEEGLCGAFNMYLYKALEERIATLRKEYGEKLALDIYPLGKRLTLALAHIDGVAMKNVSYLDAKSDTTVIRNFTDDLISRFLTKEIDAVEVIYPYYKSMAAQPVKIRTLLPVDASKLAGSAKKDETSGPYIYEPSQEKIFNTLLPLFVRIDMQESIYNGRTSEQAARVIAMQSASDNAKKLLEELQLDYNKLRQQGITNELLDIVGGSMQ | Function: Produces ATP from ADP in the presence of a proton gradient across the membrane. The gamma chain is believed to be important in regulating ATPase activity and the flow of protons through the CF(0) complex.
Subcellular Location: Cell membrane
Sequence Length: 292
Sequence Mass (Da): 32767
Location Topology: Per... |
A0A370CQ50 | MIVTLTPNPSVDRTVFVDDVVLGSVNRSDRSWSEPSGKGVNVALALHAHEVPVRAVVTAGGSTGAQLQQMLKGAGLDTVVVPIGGEIRSNISLTQPNGCVTKINEPGPTLTAEETDRLLRAVADHVRGASWLVCAGSLPAGLPTGWYGELVELGHRHGVHVAVDTSGQALVESLDAGPDLVKPNVHELAEVTGQAPQTLGDVIEAAQQVRRLGARTVLASLGGDGAILVDAAGAVWGNAPVERVVSTVGAGDAMLAGYLSCPDGRSEALAAALQWGAAAVQVEGTLFSPKASGAEVTMTATIDPSRPLRDPEPAHTVGEG... | Function: Catalyzes the ATP-dependent phosphorylation of fructose-l-phosphate to fructose-l,6-bisphosphate.
EC: 2.7.1.56
Catalytic Activity: ATP + beta-D-fructose 1-phosphate = ADP + beta-D-fructose 1,6-bisphosphate + H(+)
Sequence Length: 340
Sequence Mass (Da): 35141
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A0A1I4UJ60 | MGDSAKMGSDGKPEAFHQTPELDQPPELGQTPAIIGLTGGIGSGKSTVVRMFGELGVHWVDADDVAREVVEPGTPGLGQIAEHFGQDILTAEGTLDRAQLRQIVFANLEERTWLEGLLHPMIREELIRQLKPEGYALPYVLLVSPLLLETDQHNLVSRIIVVDVPVETQIERTMARDANERDQVERIIAAQMPREKRLEKADAIIDNDRPMDDVERQVRELHEKFLVDFG | 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... |
A0A2X3GUZ9 | MNHHLAKVYGQAEVGAPPMSVPHIDTRIIDGKRVVLFGPFATFSTRFLKNGSLWDLLASTNTSNILPMLNVGLDNFDLVKYLISQVMQKDKDRLAALCEYYPEARKEDWRLWQAGQRVQIIKRDAKKGGVLRLGTEVVSDDEGTVAALLGASPGASTAAPIMLQLMEKVFKDKVNSPEWQAKLKAIIPTYGIRLDGNPAEIEKALAWTSEVLELKYEPAGAVDEVPQAELKPLRGGKPMADIAL | Pathway: Carbohydrate metabolism; tricarboxylic acid cycle; oxaloacetate from (S)-malate (quinone route): step 1/1.
EC: 1.1.5.4
Catalytic Activity: (S)-malate + a quinone = a quinol + oxaloacetate
Sequence Length: 244
Sequence Mass (Da): 26851
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A0A943EGX7 | MPNVSEYGMKLNPNKEHAEVVLKKLEANQGYCPCLPVKNKDTLCPCKYLRKFQACRCGLYVRGDVE | Function: Catalytic subunit of the ferredoxin-thioredoxin reductase (FTR), which catalyzes the two-electron reduction of thioredoxins by the electrons provided by reduced ferredoxin.
EC: 1.8.7.2
Catalytic Activity: [thioredoxin]-disulfide + 2 H(+) + 2 reduced [2Fe-2S]-[ferredoxin] = [thioredoxin]-dithiol + 2 oxidized [... |
A0A136MTL2 | MFIDRIRIKVIGGKGGDGCVSFHREKFVPLGGPDGGNGGRGGDVIFYVEPGENTLVSLHSRPWYAAEPGGNGSTNNKTGADGESIRLPVPPGTTVSDSVTGELICDLVDETQEAVVAAGGRGGKGNAHFATPVHQTPRRAEPGKPGVERNLLVELKVVADIGIVGFPNAGKSTLLNAITKARARIGDYPFTTLHPVLGTLELDMAEEAQLLHIRNEKGIQSKIRPRIILADIPGILEGAHQGVGLGLEFLRHIERTKVLLFVLDVSIHREHEPVNAYQALIHEIASYNPDLLLKPRLIALNKVDDPLDEGEIPEIVQSLQ... | Function: An essential GTPase which binds GTP, GDP and possibly (p)ppGpp with moderate affinity, with high nucleotide exchange rates and a fairly low GTP hydrolysis rate. Plays a role in control of the cell cycle, stress response, ribosome biogenesis and in those bacteria that undergo differentiation, in morphogenesis ... |
A0A136N353 | MQATSSPYNTGLPAGDSHTTTAVVLLNLGTPESPDPKSVQKYLAEFLGDPEVISLPGGMKWATPLLAHLIAFFRAKPSSANYRMIWTEEGSPLLAITRRQAALLEEQLGDGYCVEVAMRYGQPSLEGVFDRLLEKGIRRLLILPMYPHFSRPTTGTALALAYRLLERKGLRWEAHLFSSWHDEPSYHQAQARHIRDYTAAHGLSAEDTHLLFSAHSLPVSYIQKGDPYQNEIQSSLEGIHACLCWPKEKISVAYQSRLGPVEWIGPSTEHTLRGLAEKGCRKVVVCPISFTADCIETSHEIGIEYRRLFENELGGTLFLV... | Pathway: Porphyrin-containing compound metabolism; protoheme biosynthesis; protoheme from protoporphyrin-IX: step 1/1.
Function: Catalyzes the ferrous insertion into protoporphyrin IX.
Catalytic Activity: 2 H(+) + heme b = Fe(2+) + protoporphyrin IX
EC: 4.98.1.1
Subcellular Location: Cytoplasm
Sequence Length: 346
Sequ... |
A0A2M8C2M0 | MVHTIAMTSTITQLGQSRVELKISVPTGEFQSFVDAALKDFTAEAEFPGFRKGKAPAQLVQEKIGEFALYEHAAKNAAMKFFADAVTEHSLDPIGKPDVEVLKLAPGNSFEFKAVFFVMPDVKLPNYRSIAQSLKPEYHSVSVSEDKVQEALAWLQKSRRTYTDVSRPAQTGDRITCDFTILENSKHVEHETQKDFMFVIGEARVLPGFEEKIIGAAAGITTSFTLTIPDNYWNKDIAGKIVNCNVVIKKIGQTHNPILDDAFAKSISKFETMDALRANIAKGLEAEEKEKEQQRFRTLILKRIDEKTEIDTPALLVERE... | 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
... |
A0A0D6QHI1 | MMEREVTGHRPRASKSAKKLAKKGLSVERYFTTPGVDPAEELAWETRTAAITGEGGATIFEQKDVEVPKSWSLLATNVVASKYFRGQLGTPARERSVRQLVSRVVQTIGAWGRKDGYFATEGDAVAFEAELAHLIYRQKMSFNSPVWFNVGVEEHPQCSACFINAVGDSMDSILKLAHTEGMLFKYGSGTGSNLSKIRSSKERLSGGGEASGPVSFMRGFDAFAGVIKSGGKTRRAAKMVILDVDHPDVVEFVNCKADEEKKAWALIEAGYDGGFNVRGGAYDSVFFQNANHSVRVTDAFMRAVLEDREWKLTARTDGEA... | 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 Activity: [thioredoxin]-disulfide + a 2'-deoxyribonucleos... |
D4KAY7 | MSRFLSPALSAVTPYTPGEQPQDQQYIKLNTNESPYLPSPRVVAAVSEAEVEKLRLYSDPACAQLLRTAAAHFGLQPSQVMPGNGSDENLFFALRAFCDESHPLAFADITYGCYGVWCGLLHIPAHIIPLKEDFTLAPADYHGLHETIVIANPNAPTGLCLPRSAIEGILQSNPDSVVIVDEAYVDFGGESCVPLIDQYENLLVVQTFSKSRQLAGARLGLAMGNAALIADLNRVKFSLNPYNINRLTLKAGQAALEDTAYFEKTRAAIMDTRAWTMQQLTDRGFTVLDSHANFVFASTERINGGVLYKKLKENGILVRH... | Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 7/9.
EC: 2.6.1.9
Catalytic Activity: 2-oxoglutarate + L-histidinol phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate
Sequence Length: 353
Sequence Mass (Da): 38853
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A0A372BWH0 | MPPESSSGSPIAQTVSEALQHARNRLSDRLETDLLACKALGCNRSWLYAHGKDLIDTRALERFENLVAARIQGKPVAQLLGSREFYGRDFRVDECVLVPRPETELLIDITLNLLLPESARVVDVGAGSGCIALTLAAERPGWQITATDISAEALAVATENRDRLGLDRVEMVCGDLLEPVGECRFDLIVSNPPYVADEDPHLELGDVRFEPRRALAAGPDGLEVIRRLVPDSWDRLQRGGWLLIEHGHDQAASVRALLERAGFADVLSHHDLAGIERVTSGMKPE | Function: Methylates the class 1 translation termination release factors RF1/PrfA and RF2/PrfB on the glutamine residue of the universally conserved GGQ motif.
EC: 2.1.1.297
Catalytic Activity: L-glutaminyl-[peptide chain release factor] + S-adenosyl-L-methionine = H(+) + N(5)-methyl-L-glutaminyl-[peptide chain release... |
A0A8C4AZG8 | LLQLPSCCMLTMITEVQTKELFRRADAVCFDVDSTVIREEGIDELAKFCGVGDAVTEMTRKAMGGSMTFKTALKERLSIIKCSREQVNKLITDHPPQLTPGIKELVDVLHQRGVNVFLISGGFRCIVEHVAAQLNIPFSNVYANRLKFYFNGEYAGFDETQPTSETGGKGRVISLLKERFSFRNIVMIGDGATDLEACPPADAFVGFGGNVVRPPVRDGSAWFVTSFGELLKELEKI | Pathway: Amino-acid biosynthesis; L-serine biosynthesis; L-serine from 3-phospho-D-glycerate: step 3/3.
EC: 3.1.3.3
Catalytic Activity: H2O + O-phospho-D-serine = D-serine + phosphate
Sequence Length: 237
Sequence Mass (Da): 26176
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A0A1R0Y4X4 | MPILIPLDQAADCSLQSIGAKAWRLGVAGREGLAVPDLMVIPHECMEAHRSDLQVYLSEELHKHFDLDHTVFAVRSSSNAEDLSYASAAGIFESVLGVRGMEEIISAVEECNRALHSETARKYMQRLENDCLQMNIIIQELITPRRAGVLITGRPGSDQFIAEGAWGLAVDIVSGMTNPDFLTASLQEGRNYTVRKGGQMTVCLPTVDGKGIYYREKSRIELDSEIFDEAFIIQLAAVADRVRTIFGGDQEVEWAEDNNGKLWLIQSRPFANKNSLRAPG | Pathway: Carbohydrate biosynthesis; gluconeogenesis.
Function: Catalyzes the phosphorylation of pyruvate to phosphoenolpyruvate.
EC: 2.7.9.2
Catalytic Activity: ATP + H2O + pyruvate = AMP + 2 H(+) + phosphate + phosphoenolpyruvate
Sequence Length: 280
Sequence Mass (Da): 30966
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A0A1V5QQE6 | MGNLGLTEILLIGVVLLLFFGPSRLPELGKALGKGIQEFKKASREITDSVKDDVKEGSEAGKK | Function: Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes. TatA could form the protein-conducting channel of the Tat system.
Subcellular Location: Cell membrane
Sequence Length: 63
Sequenc... |
A0A939SUG5 | MLLVSLLLLWLAIAKKFEPLLLLPIGFGGLLSGGRAGAHRPRACWLTTTRRSWR | Function: Catalyzes the decarboxylation of oxaloacetate coupled to Na(+) translocation.
Catalytic Activity: H(+) + 2 Na(+)(in) + oxaloacetate = CO2 + 2 Na(+)(out) + pyruvate
EC: 7.2.4.2
Subcellular Location: Cell membrane
Sequence Length: 54
Sequence Mass (Da): 6028
Location Topology: Multi-pass membrane protein
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A0A3D8GNL6 | MLANIGHVLNQVLVVLFPIWFYHLFFHKNGKKENGLKPRLLIVLSLSLVLTLTFSVNYSDKLIYDLKLIPIIIAFLYGNPLTGSILLVIAMVYKILFQNGEPLITVLNFTIAGVLLAFISKKFRDHSLRFKVIAISTVHWIITFSREIWLIVTKHTNEIGLVFIFSFIAWLTLMSVVFIFENLKKQMEMEEKVHRAERYNVIGQLAASVAHEVRNPMTAVRGFLQLMKKDDNLTDSQRRYIDISIEELNHSQAILSEYLSLAKPANTDLGILDLQYELHKIIELMKSYTNLQTISITSSIEEGIFIKADSSEIKQVFVNL... | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Membrane
Sequence Length: 416
Sequence Mass (Da): 47121
Location Topology: Multi-pass membrane protein
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L0EHA2 | MKRVGLMGGTFDPIHIGHLLAAETAREQCGLDEVWFIPSRTPPLKSGAPSASGEDRLEMVRLAIAGQPAFKALDLELRRPGISYSIDTVHELSARCPGCSFAYIIGGDRVNDLPRWHRIDELAASVAFIGVARPGHPVDIGSLPESLRGRVRIIPMPQLDISSSAIRALRREGRSVRYLVPDGVHDFIVRKGLYGS | 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... |
A0A944AKB0 | MSTTKQARKTLKYLNLPYGDKSITHRALICAALSDGKCTLTNAALNADTYATISCLNAIGAKITVSGGGKIEVNPVLTPNTDVVLNCLNSGTTARMLAGVAVGLNIHATFIGDESLSKRPMQRIIRPLTAMGGRIEEKEGCLFEVFKHGELHGIDYEMPSPSAQVKSAILLAGLFVKGKTSVREAFATRNHTEMMLKRFSADVSCADGRVSVSGCFPLKATDVDIPNDFSTAAVLIAMHATDPDGVLISDVGLNPTRTAFLEWLRLGGAEVNVTVKGNASGENVGDVYVNASVLRAVNSTYALSNKMIDEVPLACLMAAT... | 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: 670
Sequence Mass (Da): 72484... |
A0A831TLP4 | MRSILKYPTKLFTLIVLCFFGFNVFFLLASGIMFYSTYTDLAYREIKETKIDLLDATSEKLSNYVSGIEDTALFLVTNEMIREYLSSRPENFFDFRSKTKDIYEHFQKMLSVKIGVHSIELYTDRYSGFVPVQDRFLFSLEDADQQGWYQHLAVADGFWIPSHPYDEIAGSMEIVSYVHRIIGNRGDTLGIIKINIPDRELFRILSKQYPAPGSGDYYVLMDTVGNYITSTIPSELSYKFDNYEITNGEDFARMFYEDPSRLEEGMISGRVYNTIHSESSSPHWKLIQLIPTDVFLESRKELQLLTIGLLVLLIVISIPI... | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Membrane
Sequence Length: 608
Sequence Mass (Da): 70605
Location Topology: Multi-pass membrane protein
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G9N5Q1 | MDKIEQLRREIAEKEAELVQLRAQLVDAEKLSAGIENDKDEGEGEWKWPLAESDYERYSRQMIVPNFGLQGQLNIKHAKVLLVGAGGLGCPAAAYLAGAGVGTLGLVDGDAVEASNLHRQVAHSTDRVGMMKVDSAVTYLKGLNPTITYRAHATHLTPQNAEEIVSQYDLVLDCTDHPTSRYLISDICVLLSKPLISASAFQTSGQLIVLNNPPGKGPCYRCVFPKPPPPESVIGCGEGGIIGPVVGVMGVLQALEAIKLLVRGDHLKSRAGDEEAVKQVGMLLFSAMGDVPFRTVRMRGKRKGCFACAGDDSALTLNEL... | Cofactor: Binds 1 zinc ion per subunit.
Pathway: Cofactor biosynthesis; molybdopterin biosynthesis.
Function: Plays a central role in 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of cytosolic tRNA(Lys), tRNA(Glu) and tRNA(Gln). Also essential during biosynthesis of the molybdenum cofactor. Acts by mediating the... |
A0A2H5YXR7 | MSEPRSLPATPETSPWDTTEYWGPTDPEQHPAVRLVRERFPDAFQEVVVFRDEVTIRVARPALREVVDFLRTHPELRYNHLTDITAVDMLYLRERPRFDVVVQLYSIPRRQRLRVKCGVDDGEMVPSLVPIFAGANWLERECYDMFGIIFEGHPDLRRILLPEDWDEGHPLRKDYPLRGYRDYVQPGYESPAPRIRGTLRRPGP | Function: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ... |
A0A2S6RHZ9 | MASIIAVALGGAIGAVLRYIVVKFFINFSLIIMPLGVLSCNVVGSFLLGILITWSFKDPTISDNLKIFLQVGVLGAFTTFSAFALEVFYITEKGQYLIAVIYVLISVLLSIGGFFMGFNFYRLIG | Function: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Subcellular Location: Cell membrane
Sequence Length: 125
Sequence Mass (Da): 13604
Location Topology: Multi-pass membrane protein
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G3N0D8 | MASAGLQILGIVLTLFGWVNALVSCTLPLWKVTAFIGNSIVVAQVVWEGLWMSCVVQSTGQMQCKVYDSLLALPQDLQAARALCVITLLVALLGLLVYLAGAKCTTCVEDKDSKARLVLTSGIIFVISGVLTLIPVCWTAHTIIQDFYNPLVVEAQKRELGASLYLGWAASGLLLLGGGLLCCTCPSGGSRSSSHYMARYSVSAPHTASRGPSEYPTKNYV | Function: Plays a major role in tight junction-specific obliteration of the intercellular space, through calcium-independent cell-adhesion activity.
Subcellular Location: Cell junction
Sequence Length: 221
Sequence Mass (Da): 23545
Location Topology: Multi-pass membrane protein
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A0A2S8F107 | MAKFAESLILASQSPRRQLLLKEAGYDVTVITPSPHAETPPRLDETPRESVLRIAREKAEDVASRVDQGIILAGDTLAELNGRPLGKPADREHAREILRALRGHDHFVWSAICLWRRPMDEVLVDVDRTTVKMAPLSDDEIEEYLDSGLWEGKAGAFGIQDRTGWVEIDEGSLTNVVGLPMELFRQMLSRFNE | Function: Nucleoside triphosphate pyrophosphatase that hydrolyzes dTTP and UTP. May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids.
Catalytic Activity: H2O + UTP = diphosphate + H(+) + UMP
EC: 3.6.1.9
Subcellular Location: Cytoplasm
Seque... |
A0A2I7SUI8 | MEGVHRTHFATECTKELVGKRVTLNGWVHKRRDLGGLIFLDLRDRSGRVQVVFNPEISPEAVRIAEQVRSEYVLAITGKVVEREPGTVNPNMKTGEIEIQGEQVHVFNAAKTPPFMIQDDLDVDESIRLKYRYLDLRRSKMQKTMLIRHRAMQIVRQFLDQHGFVEMETPMLTRSTPEGARDYLVPSRVHEGSFYALPQSPQLFKQLFMVAGMERYFQFARCFRDEDLRADRQPEFTQIDIEASFLPTETFLSMMEEMVAKLFKETIGVEVPRPFPRLTYQEAMERYGSDKPDLRFGMELVDLSDILRDSSFKVFSGAIA... | Function: Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Catalytic Activity: ATP + L... |
A0A919HU29 | MHVGCQSGDDAIYLLHGLSRFVPHFIALNAASPWFDSTDSRFACSRLNRFSSYPDNGPMPWVADWQGFRRLFRQLSYTSMIDSMKDLHWDIRPSPQFGTVEVRVMDTPLTLAQAIHIAGFIQTLACWLLTERPFKHQPDDYLLYPFNRYQACRYGLDGTLTDVRSGEQRSIRRDPAARRPAGPFRPSAEGDGSAGGGGSPRNRRTARRSRCATLSPTAVRFPGWCKNTVRFGRHKAARRVYSAQTIERTAHVITLPAPSGAAARPPSPAPPVPSPTRR | Function: ATP-dependent carboxylate-amine ligase which exhibits weak glutamate--cysteine ligase activity.
EC: 6.3.2.2
Catalytic Activity: ATP + L-cysteine + L-glutamate = ADP + gamma-L-glutamyl-L-cysteine + H(+) + phosphate
Sequence Length: 278
Sequence Mass (Da): 31095
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A0A2J0KVG6 | MSRFYISPSSVKGKEIHVSGEEAHHILDVMRLKKGDHIITFDGEGKEYEGNIKNITQGGVLVEINDTKTLRAEENISITLAQSIPKNAKIDFIIEKATELGVGTVIPMSSARTIVKIDDKNKGSKRERWQRIAVAASKQCGRLETPEIEDLVTFPEVVKRIRNYDLALVACLGKETKNIKEVITKFKKRNLIIFIGPEGDFTKEEIEAAKKEGAELISLGERVLRVDTAAINILSILQYELG | Function: Specifically methylates the N3 position of the uracil ring of uridine 1498 (m3U1498) in 16S rRNA. Acts on the fully assembled 30S ribosomal subunit.
Catalytic Activity: S-adenosyl-L-methionine + uridine(1498) in 16S rRNA = H(+) + N(3)-methyluridine(1498) in 16S rRNA + S-adenosyl-L-homocysteine
EC: 2.1.1.193
S... |
A0A3G9J5F8 | MRFYIVFFIAILLDQVSKIWVRLHLPTGDSLEIWTGILHFTHYENSGAASSMFQGYGRLFVPVAILAVVFVLYFRRKGHLNRWLLDVGAALFAGGAIGNAIDRVLFNQVTDFIVFQSSNGIMNVADLVLNLAILLLGLDQLLKYWRNRRTRYYHKI | 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-, ... |
L0DR37 | MRCPRLLLDANLAPGRRVELPPDLLRHAVSVLRLRDGAPCQVFDGRGSEHHARLILSGRRGGAVEIGAVAAAPTTPELPLRLLQGIARGDHMDLAIQKAVELGVGEIWPVLSARSRSAAAHRGLERKGAHWHGVLRAAAEQCGRNELPRLDPPRDFAQALADLPREGLRVLADPEGVPAGVWRCQEADASAGPVTLLVGPEGGLTSEERAQGRHAGFRGLRLGPRILRTETAAIAALTTLQLLYGDLR | Function: Specifically methylates the N3 position of the uracil ring of uridine 1498 (m3U1498) in 16S rRNA. Acts on the fully assembled 30S ribosomal subunit.
Catalytic Activity: S-adenosyl-L-methionine + uridine(1498) in 16S rRNA = H(+) + N(3)-methyluridine(1498) in 16S rRNA + S-adenosyl-L-homocysteine
EC: 2.1.1.193
S... |
A0A7H9DJ67 | MDLKQEILALIQQSDYRAMSVSDFQDALGLSSADSFRDLIKVLNELEQGGVVTRTKQDRYQKSSTQQKIVKGILSQNKKGFAFLRPDDETMEDIFIPPHKIHYAMDGDTVTVEIQKSRGEHRKGKTEGEVKSIERHAIRQVVGTFSEARHFGFVVPDDKRIMQDIFIPKGHDLGAVEGHKVLVQITQYSDGTNNPEGHISAILGHKNDPGVDILSIIYQHGIEIEFPDDVLREAKAIPETIGTDEITGRRDLRDDLTITIDGADAKDLDDAIALKQLSNGHIELTVSIADVSYYVQEGSALDREAYDRATSVYLVDRVIP... | Function: 3'-5' exoribonuclease that releases 5'-nucleoside monophosphates and is involved in maturation of structured RNAs.
Catalytic Activity: Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleoside 5'-phosphates.
EC: 3.1.13.1
Subcellular Location: Cytoplasm
Sequence Length: 784
Sequence Mass (Da): 898... |
A0A136MXN2 | MPAIVVVGIQWGDEGKGKIVDVLSAEADYVVRHQGGNNAGHTVWIEGDKHILHLLPTGVIRRKKCVIGSGVVVDPKVLLQEIMQCKGKGIDLTPENLFLSPNCHIIFPYHIRIDTLREKRLGASAIGTTSRGIGPTYRDKIDRCGIRLGELADPGRFELALKTHLVMVNSFLTDFFKEAPFSFEEIYEPYQEYGAALAPFLADVPGLLNQAAARGEKILFEGAQGTLLDVDAGTYPFVTSSNTASGGACTGSGFPPHRMDGCLGIVKAYTTRVGSGPFPTELHGEEADRLRNAGPAGEFGATTGRPRRCGWFDGPLVKRA... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Pathway: Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2.
Function: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP.
EC: 6.3.4.4
Subcellular ... |
A0A7H1N285 | MQMRSSLGRVRGLGSAKEGVGHWWAQRVTAIALVPLAIWFVVSIISLTGATYAEYVAWIGVFGNALLMILTALVLFYHASLGMQVVIEDYVSGEGARIAVLLAVKFILYTLAASCVLAVVLVAMRS | Pathway: Carbohydrate metabolism; tricarboxylic acid cycle.
Function: Membrane-anchoring subunit of succinate dehydrogenase (SDH).
Subcellular Location: Membrane
Sequence Length: 126
Sequence Mass (Da): 13544
Location Topology: Multi-pass membrane protein
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A0A8C4G1D9 | MSAEHDDRDNGPEGMEPDGIIESNWKEIVDSFDDMNLREALLRGIYAYGFEKPSAIQQRAILPCIKGYDVIAQAQSGTGKTATFAISILQQIDMELKATQAMVLAPTRELAQQIQKVVLALGDYMGATCHACIGGTNVRNDVLKTVAICLFHLLLFKPSVAVFTFFSNIPYF | Function: RNA helicase.
EC: 3.6.4.13
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Length: 172
Domain: The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.
Sequence Mass (Da): 18949
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A0A1W9XVU2 | MTHRTIDEILPAIAAKALGGGPVSRDDLLAVLARSDDDLLDVVAAAGRVRRKFFGRRVKLNYLVNLKSGLCPEDCGYCSQRLGSTAEILTYAWIEAEEAARHARCAVDAGAKRICLVAAGRGPADRDIERVAETVAAIKDSTPAVEVCVCLGLLKQGQADRLREAGADAYNHNLNTSAGNYSRICSTHTFDDRTATVAAAKTAGLSPCSGAIFGMGESNEDIVDIALALRELDPDSIPVNFLIPFEGTPLGGHWELSPQRCLRILAMFRFAFPDVEVRVAGGREIRLRTLQPLALHLANSLFLGDYLTSQGQPGRDDRAM... | Cofactor: Binds 1 [2Fe-2S] cluster. The cluster is coordinated with 3 cysteines and 1 arginine.
Pathway: Cofactor biosynthesis; biotin biosynthesis; biotin from 7,8-diaminononanoate: step 2/2.
Function: Catalyzes the conversion of dethiobiotin (DTB) to biotin by the insertion of a sulfur atom into dethiobiotin via a ra... |
A0A1Y6BGC6 | MEGAGLTIALLDSGVGGLSVLRAMTAALPDADILYLADFAGLPYGAKSDAELAGRLVGLQRRLAAEAASEAPLDALVVACNTASTLALEALRAEAGFPVVGTVPPIKTAAEMTRSGVIGLLATAATVRRPYVDRLIAEHAARCRVVRVGAAGLVPLAEAALRGSPPDPEAVARELAPLAVAEGLDAVALGCTHYPLLAGVLAAALPGVAHWIDAAPAIARQLCRVLAPRLAAGTDGVEGETPRRRFLFTGPAAGIEGLAPALAGYGFAEARPLGRADSLPPSSPAAASR | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Provides the (R)-glutamate required for cell wall biosynthesis.
EC: 5.1.1.3
Catalytic Activity: L-glutamate = D-glutamate
Sequence Length: 289
Sequence Mass (Da): 29104
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A0A0E3M8Q7 | MKDLFILAGPTAVGKTDISIKLAQKLNGEIISADSMQIYKYMDIGSAKVTKEEMQNIPHHLIDIIEPNINFNVSEYKKMAEKEIESITSKNKLPMLVGGTGLYINSLIYNYDFTEASTDYEYRQYLHNLAEIEGKEYVHSLLKEVDAQSFNRLYPNDLKRVIRALEVYKLTGKTISEFNLENDIYDIPYNVYYFVLTMNREKLYERINMRVDIMLQNGLIEEVKKLNEMGYSAEMQSMKGIGYKEILYYLDNKISLDEAVYSIKKGSRNYAKRQLTWFRKDKRVIWIDKDKFNADNEIVDNIVDIFASLKNL | Function: Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A).
EC: 2.5.1.75
Catalytic Activity: adenosine(37) in tRNA + dimethylallyl diphosphate = diphosphate + N(6)-dimethylall... |
A0A2N8M282 | MTADTLIPRPDTETLIEIALALPLPDDARVVDLGTGSGAIGVTLALEKPHWQVALVDLSEAALQVATDNARQLNAPVQCLAGSWLVPCEGPFDLIVSNPPYIDASDHHLDEGDVRFEPRSALVADDKGLADLAEIVRQASGKLVDGGWLMLEHGFEQGEAVRALLDQAGFQDVRTAQDLGGNDRVTLGRFASASS | Function: Methylates the class 1 translation termination release factors RF1/PrfA and RF2/PrfB on the glutamine residue of the universally conserved GGQ motif.
EC: 2.1.1.297
Catalytic Activity: L-glutaminyl-[peptide chain release factor] + S-adenosyl-L-methionine = H(+) + N(5)-methyl-L-glutaminyl-[peptide chain release... |
D6Z2I3 | MKVILAQHAGFCMGVRRAVETTLKLVDLRQGPIATYGPLIHNPQVLEMLEEKGVKVLEEVPADTTGTVVIRAHGVPPERKHRLEASGVVVEDATCPRVVKVQAIIDKYQKEGYTTVIVGDRDHAEVEGLMGHAGAAGLVVSRLTDLDELQLAPPYIVVSQTTQDEELFREITDEILKRFPGGKVFNTICDSTHKRQDEVREMCREIDALVVVGGRNSANTKRLAEIAHGLNCPVFLVETEDELEPDKLKKFHCVGVTAGASTPAWIIRQVVAALESIPG | Cofactor: Binds 1 [4Fe-4S] cluster per subunit.
Pathway: Isoprenoid biosynthesis; dimethylallyl diphosphate biosynthesis; dimethylallyl diphosphate from (2E)-4-hydroxy-3-methylbutenyl diphosphate: step 1/1.
Function: Catalyzes the conversion of 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate (HMBPP) into a mixture of is... |
A0A0G0J0T1 | MKFDIITIFPKIFSAKGGSYLNESILKRAQKNKLIQIKIHNLRDFTKDKHRKVDDRPYGGGPGMVFKIEPLIKAISSILRIQNLKLRIKKKIKVILFSPSGKQFDNKMAANLSKNYNQLILISGRYEGIDARIKKVLYDSGFKIQEISIGPYVLTGGELPAMVLIDAISRQIPGVLGKKESLEEKGHGIGVPVYTRPEEFIYKSKKYKVPKVLLSGDHKKIEKWLNKKTNR | Function: Specifically methylates guanosine-37 in various tRNAs.
Catalytic Activity: guanosine(37) in tRNA + S-adenosyl-L-methionine = H(+) + N(1)-methylguanosine(37) in tRNA + S-adenosyl-L-homocysteine
EC: 2.1.1.228
Subcellular Location: Cytoplasm
Sequence Length: 231
Sequence Mass (Da): 26293
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G9N3X4 | MSEPYHGYSFPHNRLKRRLTHPNKTPLVLVSCGSFSPPTSLHMSMFSVAESYAERTGFELVGSYMSPCSDTYGKSSLVPAHHRINMCRLAIEQTNSNAMIDDWETLRRDEAGRPVYTRTADVLKRLDEQLNDVLGGIQTLDGTFVRARVMLLIGADLALTMSDPKVWAPADIDVLLGYYGAFIVERPALCATQDAIQPLKKYHDNIMVVPSFQNDVSSTKARAQIRNGEVAQDLPRSVYDYIKLHHLYQSAPSKDRHVDKNGKPDLEMVSPRLPVASHR | Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from nicotinamide D-ribonucleotide: step 1/1.
EC: 2.7.7.1
Catalytic Activity: ATP + H(+) + nicotinate beta-D-ribonucleotide = deamido-NAD(+) + diphosphate
Sequence Length: 279
Sequence Mass (Da): 31314
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A0A9D1NMV5 | MYPIHEIFESLQGEGRHSGRPCLFIRFAGCNLACPWCDTDHSPRLTLSADDLLAQVEACGAKSVILTGGEPLLQPLLPLVRGLRERGIWVAVETNATIEPEPALRAALSYIATSPKLGAPIALTRADEVRLVVADGVDAAWCEAVRARLPAADYYLSPCDDGTRLRVREAITLLGRLNAADPTPPWRLSLQTHKLADIP | Cofactor: Binds 1 S-adenosyl-L-methionine per subunit.
Pathway: Purine metabolism; 7-cyano-7-deazaguanine biosynthesis.
Function: Catalyzes the complex heterocyclic radical-mediated conversion of 6-carboxy-5,6,7,8-tetrahydropterin (CPH4) to 7-carboxy-7-deazaguanine (CDG), a step common to the biosynthetic pathways of a... |
A0A2H5VP26 | MRDQYQRPAKDLRISVTDRCNFRCLYCMPLPEYAWVERTELLTFEEIVRLTRLFVRLGVEKVKLTGGEPLLRRNLEGLIAELVTIPGVRDLCVTTNGALLAEKAERLRAAGLPRVNVSLDTLDPEKFRRITQGGDLARVLEGLFAAQRVGLYPVKINAVIERGVNEEDIIPLARFALEHGFALRFIEYMDVGTVNQWRWEKVVPKAEIARILSRAFPLREVGRERESDTAVRYQLADGRGDIGIIASVTEPFCAGCTRVRLTSDGKLVTCLFSADGYDVKALLRGGASDEEILAAIRRVWEARRDRYSEERWEALRAGQP... | Cofactor: Binds 2 [4Fe-4S] clusters. Binds 1 [4Fe-4S] cluster coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine and 1 [4Fe-4S] cluster coordinated with 3 cysteines and the GTP-derived substrate.
Pathway: Cofactor biosynthesis; molybdopterin biosynthesis.
Function: Catalyzes the cyclization of GTP... |
A0A136MPP2 | MEVNTQLTQPITGFPEWLPAERLLEVRMIDTIREVYECYGFTPIETPAVEKNESLQSKGEINKQIYSLYRPNVPAEVDKETGLSLHFDLTVPLARYVAQHYGKLVFPFRRYQIQKVWRGERAQKGRFREFYQCDIDIIGEGSLDLLADAEMPLIIYEVFKALDIGQFVIRISNRKILQGLLHHWKVNGEQAEETLRAIDRLPKLKGGWQELQAWLTDELGLEGGICNALHQLLMEEETHASPLEKLRRMNVPDEIFQTGIAELQTVLESAESLNLPQGILETDLSITRGLDYYTGTVYETFLVGYEKVLGSICSGGRYDN... | Catalytic Activity: ATP + L-histidine + tRNA(His) = AMP + diphosphate + H(+) + L-histidyl-tRNA(His)
EC: 6.1.1.21
Subcellular Location: Cytoplasm
Sequence Length: 464
Sequence Mass (Da): 52752
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E1AR82 | MTLSSTTLNTSITLSIFIILILTSTFSNKNNNNVTSIRNANEDYICLLSMKTLSILAILNLLLFIVGSNTPISSSLLPWINNTSINSVLSINIDGSFIFFSTVALLVTWSIMEFSIYYMHSDPFSSNFFRLLIIFLLNMLILTAAENLFLFFIGWEGVGFLSFLLISWWTTRTDANSSALQAIIYNRVGDLGIIVLLSIALFNLGSWSITNIYSLNGSENQWWTSIILFSALVGAIGKSAQFGLHPWLPAAMEGPTPVSALLHSSTMVVAGVFLLIRITNILQPTSAFLNTTLVVGSLTAIFAATSAFRQHDIKKIIAYS... | Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor. Essential for the catalytic activity and assembly of complex I.
Catalytic Activity: a ubiquinone + 5 ... |
A0A942RTQ2 | MIEINNLTKQKINPFLIKKFIAQALKILKIKKSISLVFVGLALIKKINEKYRQKNEITDILSFIGADNYLGEIIISLKQAQKQAKQAQHSLMTEIKILIIHGILHLHGYDHHYKKDYKLIVKKEKQLLKILKV | 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: 133
Sequence Mass (Da): 15468
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A0A507CBF5 | MGRKRDGAVSPVSAEPPRYDPEVIGPQANRRCRDIIFLALFIVYWVGMFVVAALAIRTGNPQKLIAPTDSKGQYCGWNNALINSSLADLTNYPYLYYINPLSPLTTDSVCVAACPTVTAISTTTTAICDMNVTLPLTLSTLSTAVSAGLCSAFTYQSDIVLNRCMPSANVSADIWNAAASSFSISLGGTNITLQSLVSSERGDFVLAISDIVKTWPYILGGAGVSLVSSFLFLILMRWFVGLFVWITIIAANVVVDGFAVWLYFYWRARATAFYAIPVASQQNVDKWEMYAALGVFIAMCVLGVVLFLVTIFMRNRLRVG... | Function: Probably involved in transport through the plasma membrane.
Subcellular Location: Cell membrane
Sequence Length: 659
Sequence Mass (Da): 73166
Location Topology: Multi-pass membrane protein
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A9VAB8 | MMTKQNSSSFCMCLSLKLSPLSSLSLSLSNSQTLKLSLSNSLSQTLSLKLSLSLSLSNSLSQTLSLKLSLSLKLHSSHTLTLSLSCSSVKAVETAATLDERDAYGATPLHWACFSGYAPLASMNLDIVVLALLMAGADPNSRNQKGATPVHWAAFSGSLNALFALRAHGANMSVIDTDGNSALHRAVQRGHLMPCKFLLDRPMYRFKMDPLMANNEGWTCVDTAERYNLQDIRTELMKVVKSQNNRLSNPNNLYYGYMASTLVCFALWFGFLWPATDERLYGLNRVCFALLVVWLLNWYRTSSMDPGTVRCSVPRAELKR... | Catalytic Activity: hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein]
EC: 2.3.1.225
Subcellular Location: Membrane
Sequence Length: 483
Domain: The DHHC domain is required for palmitoyltransferase activity.
Sequence Mass (Da): 53758
Location Topology: Multi-pass membrane protein
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A0A7S0CDG4 | SELTMCTDVDRNDKSRICVPGSVKVIGRRQIEMYSRLIHTVDHVEGYLRKEFDALDAFLCHTWAVTVTGAPKTWAMKFLEKVERSPRCWYGGAVGLVGFDGGLNTGLTLRTVRVKKGVAEVRAGATLLYDSDPHDEELETELKASAMIDAIVQSSPSTTTTIDTVATTANNQLEPLQKPGEGKSIVLIDHEDSFVHTLGNYLRQTGAEVKTFRSGQSALDAIEMLVHTGKKPDMVVLSPGPGNPSDFALDKSVALLTKHKIPAFGVCLGLQGMVEAFGGTLGVLSYPMHGKPSMVNLTPSGMKEDSIFASLPDSFEVARY... | Pathway: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 4-aminobenzoate from chorismate: step 1/2.
EC: 2.6.1.85
Catalytic Activity: chorismate + L-glutamine = 4-amino-4-deoxychorismate + L-glutamate
Sequence Length: 505
Sequence Mass (Da): 55231
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A0A7Y0KJ35 | MLAQGGSSQNFLLPNGTFFFELILFVVVFVLLAKFVVPPIRRAMEERAERVRQLQRDREEADEKYQEAERRHAEVLSEARNEASSIRDEARATAREQAAEQRAQAEREISDVRQRGERELEDQRSRARGDLQQRLPDFARTLAERILGRSISDETSARSTIDSYVGSIGSSEPAGTTSGSSADGAGTSTVAAGSSGSGTGEG | 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: 202
Sequence Mass (Da): 22107
Location Topology: Single-pass membrane protein
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A0A6H0A2Y2 | MLHGSARFKDNRNLIVQLNDGGERVVAFDRCLIATGASPAVPPIPGLKDTPYWTSTEALVSETIPKRLAVIGSSVVALELAQAFARLGAKVTILARSTLFFREDPAIGEAVTAAFRMEGIEVREHTQASQVAYINGEGDGEFVLTTAHGELRADKLLVATGRAPNTRKLALDATGVTLTPQGAIVIDPGMRTSVEHIYAAGDCTDQPQFVYVAAAAGTRAAINMTGGDAALNLTAMPAVVFTDPQVATVGYSEAEAHHDGIKTDSRTLTLDNVPRALANFDTRGFIKLVVEEGSGRLIGVQAVAPEAGELIQTAALAIRN... | Function: Resistance to Hg(2+) in bacteria appears to be governed by a specialized system which includes mercuric reductase. MerA protein is responsible for volatilizing mercury as Hg(0).
EC: 1.16.1.1
Catalytic Activity: H(+) + Hg + NADP(+) = Hg(2+) + NADPH
Sequence Length: 360
Sequence Mass (Da): 38144
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A0A424NDR7 | MKKRISIIGGGVSGLGAALLAKSKNNHVFLSEKNQLNNKIKQILKSNYINYEEGHHSNNLFSSDLIIISPGISDNSLIVKQIKEKGIPIISEIEYGFENTDSKIIAVTGTNGKTTTCLMLKHIFNQTALNVLLAGNVGNSLCHELSLKNNYDIIVLEVSSFQLENINKFQPHISVILNISDDHLDRYSNFNEYRKSKFMITKNQKKEDYLIYNYDDKCLKDLKTNANKIPFSLEREFENGIFFKKNKININLKNKKMTIDQLSLKGKHNIYNSMAAAISARVFEISDSLIRKSLQDFQNVEHRLESVLKVNNIEFINDSK... | 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-... |
A0A4Y8WQG3 | MKERRIGVYAGSFDPFTIGHANIVRRALEVVDELHIVLGHNIQKHSFHTVDDRLEDIRGLYADNPRIVVVSHQGIIAQYASQHDAILIRGLRNVADLESERAMAEVNKERFGVETFCLFSESKYSYVSSSLVRELAAFGEDYSEYIPKREEIYGY | Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 4/5.
Function: Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate.
Catalytic Activity: (R)-4'-phosphopantetheine + ATP + H(+) = 3'-dephospho-CoA + diphosphate
... |
R5LY22 | MTEISFNVYYTIALAVLALMLGDFIKKRIYVLRKFCIPTPVVGGVLVALLITALNLSGTASVSLDSSFNEFFSLLFYAGIGYTASWKLLKKGGPQVILFLVLSSILVVFQNGLGIVICHIMGINPLIGMACGSIPMVGGNGTAAAWGPILESAGLDAGTTIATAAATFGLVAGALLGGPIGRFLIEKKHLKPGLETKEMKFGDKEEEAEIDEKRMTAAAYQILLTVGLGTLISYLLELTGLEFPASVGAMTAAAILRNIADHSDKLDLKLPELSIISNISLLVFLALSMMTMELWKLIDLAVPMFLILLAQMILITLYGI... | Function: Catalyzes the sodium-dependent transport of glutamate.
Subcellular Location: Cell membrane
Sequence Length: 395
Sequence Mass (Da): 42117
Location Topology: Multi-pass membrane protein
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A0A1G0H1L3 | MTYLALARKWRPKQFNEIVGQPHVVKALTHALSQNKVHHAYLFTGTHGIGKTTLARIFAKCLNCETGITATPCEKCAHCQEIDSGRFPDLYEIDAASRTKVEDTRELLDNIPYAPLKGRFKVYLIDEVHMLSGHSFNALLKTLEEPPSHVKFLLATTDPQKLPATVLSRCLQFHLAKMMPEQIETQLAFILESEKIAFEKDALPFISYSANGSMRDALSLLDQCIAYGNGKITASETQKMLGLSDQIEMVALLKAIHANNAEGALTLTKNWAEKGVNFTRCLSELLTQLYQIAVLQSIPQATLQISNPELKNCAREMSRE... | 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: 522
Seq... |
A0A1G1XTK1 | MLAKKYRLAKEKDFKKIIASGRSFFSPSFRLRYLATNLDFSRLAVIVSAKISKKATVRNRLKRQMREIIRLNLKQIKPGYDILVYFKNQALGKDYHELEQEFISALKKLRLV | 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... |
A0A0Q6GX74 | MTPWTAPTSPHPVRATVALPGSKSITNRAFVLAALASGPSTVTGALRSRDTDLMIEALRTLGTTVEPTGDDGTTVLVSPGPRRGGDVDCGLAGTVMRFVPPLAALSVGRSRFDGDAHARTRPQQTILDALRAVGVAVDGDRLPFVVDGTGSVRGGTVQLDASGSSQFVSGLLLSAAQFDEGLTIEHIGAPVPSMPHIDMTVEMLRESGIRVDTPADSGVANTWRVYPGVVAPVDRAIEPDLSNATPFLAAAAVTGGEVRIPRWPARTTQPGDAFRHILSEMGAEVTLTDTALTARGPASLRGIDVDLHDIGELTPTVAAM... | Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 6/7.
Function: Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-ph... |
A0A7W5GW83 | MEPFVVLEDVAVPFDKPDVDTDQILPARFMRRPRTEGYDQFLFRDLRFRQDGSEDPEFVLNQPPYRQARILVGDRNFGGGSSREQAPWALLDYGIRCVIAADFGDIFNVNALKSGLLPVQVDIAVCARLRQQLHERPGAVLRVDLPSQIVTGPDGATYAFRIDAFRKRCLLEGLDDVGLTLRHEAELDAFERDYREKFSWLFPERS | Pathway: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 2/4.
Function: Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate.
EC: 4.2.1.33
Catalytic Activity: (2R,3S)-3-isopropylmalate = (2S)-2-isopropylmalate
... |
A0A1M4TTQ6 | MELVLASGSPRRRELLSQLGLHFTPVNYQVDETITNCSLTPEKIVQELSIRKAKAAQQDFTDALIIGADTIVFDGISILGKPKDQHEAIQMLTQLQGKEHQVYTGITLIELVDGVVKECKSGVRMTRVWMRTLLKSEIEEYVLTGEPMDKAGSYGIQGIGATLIDRIDGCYFNVVGLSLVLLQDLFRQIDKSMNQFR | Function: Nucleoside triphosphate pyrophosphatase that hydrolyzes dTTP and UTP. May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids.
Catalytic Activity: H2O + UTP = diphosphate + H(+) + UMP
EC: 3.6.1.9
Subcellular Location: Cytoplasm
Seque... |
A0A136MLH1 | MSVTREEVRHIALLSRLDLSEAEIDRFTAQISQILDYAAKLNELDTANVEPTFHAVPLENVFREDVPGQPLPLADALGNSAATRGSFFEVPKVADGS | Function: Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an ... |
A0A136N2E2 | MMDPYHQPRNSEKGCFSFSCGCCSGGCLATVLLGSLSVLLFAYGYWVGMVDHPGEFAYVHVLRNDMSPTIQPGDWVLVDRDYYADEPIQRGDIVWLASSGESESESKQLLRVAGLPGESVTFSASGELLIDGNVFTRHPMLAERDFRKDKKVPDPVKLNENEYYLLGDNRDEARDCRSIGPVPVKNLRGMAISILFPPNRVARVDGKN | 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: 208
Sequence Mass (Da): 23106
Location Topology: Single-pass type II membrane protein
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A9V4Q6 | MKAVLVLGLALLVALAAAEDVITLTESNFESTLKQHDLAVVEFFAPWCGHCKRLAPEYEKAAGILKKSDTPVALAAVDATEHGSLASRFGVTGYPTLKIFRKGELSADYQGPRDAAGIVKYMEKQAGPSSKRKCFLIDNASMFSSLDSGMARAFLKTADAERENFRFAHTTQSKALGQYGKDVVVVFRPQKLSNKFEEGHVVYSGKAKNTLIKEFIMDAITSPGGIMTPDHRPFFFASKPLLVVYYDLDVKMNPSRAKYIRNRVLKVAQDVTSDLTIAVANKADFAQDVQQLGLDEFSVAAGIWGEGSTKYRLDEEWSMD... | Catalytic Activity: Catalyzes the rearrangement of -S-S- bonds in proteins.
EC: 5.3.4.1
Subcellular Location: Endoplasmic reticulum lumen
Sequence Length: 466
Sequence Mass (Da): 51106
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A0A354DK65 | MLIYKNGEVHHEQHIRLPQDDEVGFIRLLRPSTEEIKHFLGEVFACHPLVIEDCVFLERQRPKVDTYKNHALVMFSSLLEDLAFSKMGIIIGKNYIIAIQLEVIPALDELREQFLKIPEHMEHPGLVLYHLLDQCVDQYMSITDSIEDKVESLETSLYENPTGKLSQEIFHLKRRLHGIRRTFVEERDVLGTLMHTQFPYTREETNLYLMDVHDHLNRVVDSVDSFREALTSILELQVSLKGDRMNEIMKTLTLVSTFFLPLTFIVGLYGTNLRLPEYRWNLGYPYLWLVLIGTTVVMFLYFKRKNWW | Function: Mediates influx of magnesium ions.
Subcellular Location: Membrane
Sequence Length: 308
Sequence Mass (Da): 36314
Location Topology: Multi-pass membrane protein
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D6Z0V9 | MMAENSANSPVGQPPEVKSHSGSPVPGGLRALPRRGCLLLVRFYQLVISPLFPPSCRFVPTCSEYALEAITRYGVLRGCYLAFRRILRCHPFNPGGFDPVK | Function: Could be involved in insertion of integral membrane proteins into the membrane.
Subcellular Location: Cell inner membrane
Sequence Length: 101
Sequence Mass (Da): 11133
Location Topology: Peripheral membrane protein
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A0A139WUM7 | MRRLAIFGGTFDPVHWGHLILAEAALHQVPLEQVIWVPSFNPPYKQAATFEHRVEMVQQAIADNPKFAVSLVEQSHPVSSFAINTLINLSADHPDTHWYWIIGLDAFQTLPRWYRGQELAQLCEWLIAPRLLSGETITQSEIICKQVVQKLTKQTFNIHWQLLNIPFVGLSSSLIRNMYNDGRSIRYLVPETVRAYIDNHKLYTNG | 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: (R)-4'-phosphopantetheine + ATP + H(+) = 3'-d... |
A0A944FXC5 | MKKTCKKTNCKLESVYDFIVDFNDKNGYCPSLRQIGEKLGISTPSLVKYYLDMLEKNGKIHRGAPPRRIIIVPQKSERKKSEKIPSVDGVAVDKKQIETENVFYCPIVGSVAAGLPILATENISDYYPLPTNSFNKDDTFMLKIVGDSMVNAGIFDGDTVIVDRTKEAENSKIVVALIDDSATVKRFFRKEDRIVLHPENESYQDIIVNSDQNFIILGVIVGLIRKF | Function: Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually ... |
A0A9D9E511 | MTLINSQFLKVVKDEVGSKIEHRVNIFKTLNPDVSLIRLDSGDVVRPLPPCAVNALVKASKEMGNASTFKGRAPAQGYSFLIEAIAKHDFRSRKIKIDTDEIFINDGSKEDISGIGDILCRDNRVGVIDPVFQTYVESNVIGNRAGELGDSGQWSHVIYLKSGKETGFMPEFPVVRPDVIYLCYPNDPTGCVMTKPVLKSWVDYAIKNKILLLFDATYEAFITDPDIPHSIYEIKGARRVAIEFRSFSKSAGFTGLHCGYTVIPNDIEGYSFSAESSARLNTLWMRRQTIKSYAPSYIIQCAAASLYTEEGRREIRDNVN... | Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; LL-2,6-diaminopimelate from (S)-tetrahydrodipicolinate (aminotransferase route): step 1/1.
EC: 2.6.1.83
Catalytic Activity: (2S,6S)-2,6-diaminoheptanedioate + 2-oxoglutarate = (S)-2,3,4,5-tetrahydrodipicolinate + H(+) + H2O + L-glutamate
Sequence ... |
A0A3Q1M464 | MCVYDVNVRLAVAGPPADHILPPRSYIQCQGIPQGSILSTLLCSFCYGDMENKLFPGVQQDGVLLRLVDDFLLVTPHLTRARDFLRTLVRGVPEYGCQVNLRKTVVNFPVEPGALGGAAPLQLPAHCLFPWCGLLLDTRTLEVHGDHSSYARTSIRASLTFTQGFKPGRNMRRKLLAVLQLKCHGLFLDLQVNSLQTVFTNVYKIFLLQAYRFHACVLQLPFSQPVRSSPAFFLQVIADTASRGYALLKARNAGASLGARGAAGLFPSEAAQWLCLHAFLLKLAHHRVTYSRLLGALRTGGCGRAQGGLFGQVGGSRSPQ... | Function: Telomerase is a ribonucleoprotein enzyme essential for the replication of chromosome termini in most eukaryotes. Active in progenitor and cancer cells. Inactive, or very low activity, in normal somatic cells. Catalytic component of the teleromerase holoenzyme complex whose main activity is the elongation of t... |
A0A354DKG6 | MKIKLKLQKFIKKIFSPSVKVYELSKKNVDHSIRLQLVLVFGLCLIISVFFMKIVGNFMNNSPRNARIDYSAGIKHISDTAYEISSFFKEQKVSKNDSSKINTVVKIQDQDSSIKVLICDLEGNVLYHSSNAAEKKIDVYSILKNVMDRDDKVHYKNGKGVIVYENKEYDSLYPISFTDGYGYVVVKGIPYGTVVYDKYDNSLLAVLFAFAAFIISFYFITSRKMQYIESVSSGLYEISKGNLDYRIKKVGNDEIASLADNINDMAEKLKNKIDKERQIEKTKNDLITNVSHDLRTPLSYIKGYSEAMIEGVVTEEEQKK... | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Membrane
Sequence Length: 511
Sequence Mass (Da): 58051
Location Topology: Multi-pass membrane protein
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A0A4R6SW55 | MNITQEKINDLNAVVKIKIAPEDYTEKVDKSIKEQAKKSNLPGFRKGMVPAAHIKKMFGKSILVEEINSLLSETLNKHLTDNKVEILGQPLPVIDDTKDFKWDNTDEFEFNYELGLAPVINVDVTSKDKFVKYSVKADEETLAARIKNIRRSYGKMTNPEVSADDDVLYAELAQLSPDGSVFEGGINHTGSIRLDQVADKKILKSLIGLKKDDVVELDLQKTFDKNEVIIAKLLDIAEEDAKELQSKFQVTIKNVNRLEESDLNQEFFDKLFGAGEVTDEAGFTTRITEEVESMFQQDADRKLQNDIYTKLIESVKIELP... | Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
EC: 5.2.1.8
Subcellular Location: Cytoplasm
Sequence Length: 448
Sequence Mass (Da): 51310
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A0A377KJI3 | MPLQQLLDRAESTNQLPKTILYSLNPNDYPIITALMGCFQKEAPGKLQLGSGWWYNDTRAGMREQLTQFADGSALGNFVGMLTDSRSFLSYTRHEYFRRVLCEFIGEMVERGEAPEDVELLGNLVENISYHNAQHYFGFFD | Pathway: Carbohydrate metabolism; pentose and glucuronate interconversion.
EC: 5.3.1.12
Catalytic Activity: D-glucuronate = D-fructuronate
Sequence Length: 141
Sequence Mass (Da): 16154
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K2JS69 | MTDQKNLILAIGVSLAILLGFQYFFEFPKMQEQQQAQTSEQIAQQARELDASRPSPAAPGADVTAGTVTAANQPQTREQVIAASPRIRIDSPRLRGSLSLTGGRLDDITLRDYHVNPDKSSPNITLLTPRGLPQPYYAELGWVAGAGSSGIAVPGPDTVWQADRDVLSPGQPVTLTWDNGQGLRFEKRVALDSDYMFTVTQRVTNESGQPVNLHSYALASRGGTPQTSGFFILHEGLLGVFDGTLKEVDYDDIQEDKQVEMPSTGGWIGITDKYWLVALVPDQQEQVKARFLHTTRNNDDRYQVDYLDAGREIAAGATLE... | Function: Required for the insertion and/or proper folding and/or complex formation of integral membrane proteins into the membrane. Involved in integration of membrane proteins that insert both dependently and independently of the Sec translocase complex, as well as at least some lipoproteins. Aids folding of multispa... |
A0A943XNA9 | MKFSELVSEKTRLSLPSDPDIGGIASDSEKAAPGCLFVCIEGMHSDGHSFIDEAASRGAAAFVISQSHPEAEEKLTSAGMPFAVYADTREAEAVITSRFFGDPWKDMKIFAVTGTNGKTTVVSLLDAIFQAAGYSCRTVGTLTGRLTTPDPAVLYPALRSFADSGTQYVFMEASSHALALGKLTPIRFACGIFTNLTPEHLDFHGDMEHYAGAKAKLFASSDRAVINADDCRSQYMAERSHSPLLCSVKRSDTDFYAKNITNCGVYGIRYDLMTTDLVFKIRSGIPGLFNVMNTMEAAAAALSEGISPEVIRGAVCGFSG... | 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... |
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