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stringlengths 6
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stringlengths 16
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stringlengths 117
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A0A949EYS6 | MKDKIIVCESGMENTGYIRDLYKRGIRVFLIGSYFMQSKNLAHDLSDMEARLKRENLI | Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 4/5.
EC: 4.1.1.48
Catalytic Activity: 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate + H(+) = (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + CO2 + H2O
Sequence Length: 58
Sequence Mass (Da): 6812
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A0A7V1BU08 | MASLAQLTNELEPELARQVFTHSSWAPERTLSYERLEFLGDSVLGLCISTDIYSRYPEYNEGELAKVRAYVVSRHTCAKVGEQLDLSRKLIEAAKQADAANITSLAANANVLAAMVEALIGALYLQFGMEVVLGAVLEVFNEHIEYAASEHIDFKTELQEEAARRNLEVNYEVVAVEGPPHSRMFTSEVSIGGRVMGSGRGRTKKVSQQGAAKEALNALRVRGEADS | 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 organism.
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphomonoester.
EC: 3.1.26.3
Subcellular Location: Cytoplasm
Sequence Length: 227
Sequence Mass (Da): 24876
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A0A933UL92 | MRPRDVGSHGVGDPPLNVDQYDGVAAETLLDSAAAASEADVEQAAAADLATAAAIRKFRRRVAIGVGVLLALFAMRAWVVEPVRVRESSMLPTLHDGDALVIDRLTYQFRDPEVGEIVTAHIDATDADVVKRVVAVGGDTIGIDDGELVRNGEVVDQSYAKLDQMGGYFWGPITVPEGFVFLMGDNRLESSDSRNYGPVPVDDVDGRYVARFWPL | 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: 215
Sequence Mass (Da): 23213
Location Topology: Single-pass type II membrane protein
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A0A7V1H0W5 | MLTVGLTGGIASGKSTITKYLSDLGAVCVDADLIARDAMVEAPVYSKLVEHFGPNILSEPGEIDRAALAAEVFSDPDQLRVLNGLVHPVVIDRIKEVLGAWSRERHGIGIVQVPLLIEAGMTDLFDVIVVVITTPEMQVNRLTASGLSFEEAEARLRSQLPGSARLPFADLTIINKASLELLKEQTAILYDKLKSLGPGEKEGETTTFSG | 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 Length: 210
Sequence Mass (Da): 22523
|
A0A933PJ64 | MQVIRVLVVDGSRTARTATAETLATDPGVEVVGTADTGPMAFAKTATLKPDVVTLDSEVNDGDLVRTVKALRSTHPPVVVVLVASPTDAGTRTTVEALDAGIADYVTGPPEPRTAIAVQKMVLAHLLPRVKALTGLAPPIPRRRRPELPPAARRRAAPAGRPWPDAPPTAPAPGARTDRISPELAEMLAASGVELAPGSPRALKPPRTRPPTVVLIGASTGGPEALAEVVRGLDRNVRTPVLVVQHMPAGFTQLLAERLDRLTHLTVREAVDGARADPGHLLVAPGGRHMELHRAGSGLAVRLTDAPPEQFVRPAVDVLFRTGAHACRDGVLAVVLTGMGRDGEAGARVVQEAGGTVIAQDEATSVVWGMPGCVARADLADAVLPLPLIGGEVSARLARRI | PTM: Phosphorylated by CheA. Phosphorylation of the N-terminal regulatory domain activates the methylesterase activity.
Function: Involved in chemotaxis. Part of a chemotaxis signal transduction system that modulates chemotaxis in response to various stimuli. Catalyzes the demethylation of specific methylglutamate residues introduced into the chemoreceptors (methyl-accepting chemotaxis proteins or MCP) by CheR. Also mediates the irreversible deamidation of specific glutamine residues to glutamic acid.
EC: 3.1.1.61
Catalytic Activity: H2O + L-glutaminyl-[protein] = L-glutamyl-[protein] + NH4(+)
Subcellular Location: Cytoplasm
Sequence Length: 401
Domain: Contains a C-terminal catalytic domain, and an N-terminal region which modulates catalytic activity.
Sequence Mass (Da): 41734
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A0A4Q7DNC8 | MRKLLVANWKMSSGLSVLEKLADEIVGISLRKNVRSVICPSFPYLHAINQVIEGSSVFLGAQDCSMHNAPSHTGDVSAAMLRESGCKYVILGHSERKRSYNETSGHIASKLRMVLDEGLHPIVCVGESMEDRKEGKTLSVIMEQISEAAIQGVRKMTVAYEPVWSIGTGVIPTVDDVEEVVKHIEHLVGGDVSVLYGGSVNAHNCHELMKCNRIGGFLVGKASLNFESFKEIYASLALAM | Pathway: Carbohydrate biosynthesis; gluconeogenesis.
Function: Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D-glyceraldehyde-3-phosphate (G3P).
Catalytic Activity: D-glyceraldehyde 3-phosphate = dihydroxyacetone phosphate
EC: 5.3.1.1
Subcellular Location: Cytoplasm
Sequence Length: 240
Sequence Mass (Da): 26143
|
C2CH62 | MVELAPSILSCDFSKLQEDLDATKDTGLKMIHIDVMDGLFVPNISFAFKIIKDIRDKNDYFFDTHLMIVDPIRYIDRFVEAGCDRLTIHYEASDSPLEAIKKIKACGIEAGISLKPKTACEKILPLLAYVDAVLVMSVEPGFGGQSFMEESLDKVKFLRKYIDENKLSCKIEIDGGIKTENVRRVIAAGCDEIVSGSDIFAKEDIRGQIEKYYQIFNEDSH | Cofactor: Binds 1 divalent metal cation per subunit.
Pathway: Carbohydrate degradation.
Function: Catalyzes the reversible epimerization of D-ribulose 5-phosphate to D-xylulose 5-phosphate.
EC: 5.1.3.1
Catalytic Activity: D-ribulose 5-phosphate = D-xylulose 5-phosphate
Sequence Length: 221
Sequence Mass (Da): 24901
|
A0A931QD41 | MEPLGDVTAALLAPDAQATAFLVARREGVLAGRLCAEEVLRQVDASIEVAWAADDGDRIVAGQRLATLSGSLASLLTAERTALNLLGHLSGVATLTARYVDAVAGSVQIWDTRKTTPGLRALEKAAVRAGGGVNHRGNLSEWVLLKDNHLAMLGITEAVGRARAMWPGRTVQVEADHFGQLQEAIAAGADLVLLDNMTPDEVRRCVAERGEATRPLLEVSGGVSLDTVLDYASTGVDLISIGALTHSAPVLDIALDIDVEGDVGQTHPYVPER | Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; nicotinate D-ribonucleotide from quinolinate: step 1/1.
Function: Involved in the catabolism of quinolinic acid (QA).
EC: 2.4.2.19
Sequence Length: 273
Sequence Mass (Da): 28706
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A0A077M4D9 | MSEAPVAAGGLLVGRIGGAPVRIGASWLLLAALVVIVIGPQIAQSRPDLGPLAYAVALASAVLLLVSVLLHEAAHALTARGAGLRVHAIVADLWGGHTTFEGHSLRPGSAAVIAAAGPLTNAVLGVASLVAERGMTSGVPRHLVYGLAVSNLLLAGFNLLPGLPLDGGQLVESAVWAASGSRPRGTVVAGWCGRVLVLVVAIYWVALPVLRGEGLSMSLVWGLLIAGFLWRGATVAIQSGTVLGRIESVRVADLLIRVPGVTETTAVERVWAEPAGAAVVHDPSGAPVGLVTRQMVEQLPPERRATTPVSAVYVRMPPSWVVDADPDDPVVDVVRPMAEAGLSLAAVRSGGRIAGVLRVEDVDPILRGSAPPPR | Cofactor: Binds 1 zinc ion per subunit.
Subcellular Location: Cell membrane
Sequence Length: 374
Sequence Mass (Da): 38336
Location Topology: Multi-pass membrane protein
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A0A964ZRS0 | MLKLAINDETSSNTPLRQELSTGGFLELDEAISYAAKNKIIWRYFNSYGSPEDLQIKQFIAVEPFKSNFDKLIKQVKTWIEQGFLVVISLEGIGILERYRDIFVDGDIAVALVDNLSADLSPDKLYLTSTLIRHGFIDQEQMVVFLTEADITGNRDLRAAGSRMPSKRKASIDPLELKSGDYVVHEQHGVGRYLELVRRDVAGISREYLVIEYASSKKGHPADRIYVPTDSLEQITRYIGGEAPAVHRIGGGDWIKAKSRAKKAVKEIAGELIRLYAARTSSPGFAFSPDTTWQRELEDSFAYVETPDQLVTINEVKEDMQRPYPMDRIICGDVGYGKTEIAIRAAFKAVQDAKQVAVLVPTTLLAQQHLATFTQRYSGFPITVSALSRFASTKEINETLAGLASGGVDIVIGTHRLLSEDVVFRDLGLIIVDEEQRFGVEHKEKLKKLRASVDVLAMSATPIPRTLEMAITGIREMSTITTPPEQRHPVLTYVGAYDEKQVAAAIHRELLRDGQVFYIHNRVESIDDVASKIRRLVPQATVAIAHGQMSETSLEQVVVGFWNREFDVLVCTTIVENGIDVANANTLIVERADLFGLSQLHQLRGRVGRSRERAYAYFFYPIDRAMSEVALDRLSTIAQNTELGAGMRVALKDLEIRGAGNLLGGEQSGHIADVGFDLYMRMVGDAVNEYKAGFIEGGQELVECKVELPVTAHLSAEYVPSDRLRLDLYRRLADTKDEDEITKIGEELSDRFGSLPREAENLLRIARLRTYLKEKKIQDFAVQGRYVKIAPLVPNESLELKIKRLYPGSIVKSVTQVVMIARPQSAAWVSESEEIGDTSLIDWAVELAKTLLERPLGK | Function: Couples transcription and DNA repair by recognizing RNA polymerase (RNAP) stalled at DNA lesions. Mediates ATP-dependent release of RNAP and its truncated transcript from the DNA, and recruitment of nucleotide excision repair machinery to the damaged site.
EC: 3.6.4.-
Subcellular Location: Cytoplasm
Sequence Length: 858
Sequence Mass (Da): 95779
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A0A965IZC6 | MNYSLVIVESPTKVATIQKILGPSFVVASTRGHFADLPERKGAVDIEHAFAVQYRLTEKGAKTIAELRKQLDGASELIIATDADREGEMIGHLAVEFLQPTVPVKRVRFNAITADAINEAMANPTVIDERLVMAARSRRVLDHVYGFHLSPELWRTVRPGLAAGRVQSPALHMVVKREKERMAFVVSEYHGIDMTVTGDPAVTASLRTVDGSEVAASRHFDAAGKPKSGVLVLGAETATDLVRRLEGAAVSVVSVEPKAYRRRAPFPYITSSMLQDAASRLKLGSKATQSALQSLFEAGHITYPRTDSPHMAPQAIAAARATAIQLFGEENVPEKARHPKAKKSNAQEAHEALRPTNMSRRSVKGVGTNAQRIYEMIWRRTVASQMIDATGTTTTVSFAVTAAGAGEQCVFTASGTVIDVPGFRLVYVPQTEEEPPMPAFAVGQPCTADQFTAVAHATRPPARYTEGTLIKALEEEGIGRPSTYTAIMQSLRLRYVWSKKGDPALIPTISAFAVDQVMGICFAELIDYRFTSQMEDRLNDVVAGDLEYENLLAAFWSAGDGTWTPLEKLIVNGKTLFDPKKTPVLSFGMHPTLGEEVVLRAGRAYKSRGRTVGRPYLACGKKTVSIADETELDQLTPDVAFARLLETREPRVLGEHGGHQVEVLRGIYGPYLRWNGRNVKLPKNLDAGTVTLDDVTGLLE | Function: Releases the supercoiling and torsional tension of DNA, which is introduced during the DNA replication and transcription, by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(5'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3'-OH DNA strand. The free DNA strand then undergoes passage around the unbroken strand, thus removing DNA supercoils. Finally, in the religation step, the DNA 3'-OH attacks the covalent intermediate to expel the active-site tyrosine and restore the DNA phosphodiester backbone.
EC: 5.6.2.1
Catalytic Activity: ATP-independent breakage of single-stranded DNA, followed by passage and rejoining.
Sequence Length: 700
Sequence Mass (Da): 76324
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A0A972KEI2 | MTETGAPGHKPAEVDARSSRRRLLAIGGVLVVVDQLTKWWATTALADGPIDVVWTLRFREIGNTGAAWSIGKDLGPFLGILILIIIIAMYFFRSRIDSGRPFVAYSVIFGGAIGNVLDRLFRGEGWLRGAVVDFIDFQWYPVFNVADMSVVVGSLSLIALTWRSGSEDDTVETGPEAASQQADQPT | Pathway: Protein modification; lipoprotein biosynthesis (signal peptide cleavage).
Function: This protein specifically catalyzes the removal of signal peptides from prolipoproteins.
Catalytic Activity: Release of signal peptides from bacterial membrane prolipoproteins. Hydrolyzes -Xaa-Yaa-Zaa-|-(S,diacylglyceryl)Cys-, in which Xaa is hydrophobic (preferably Leu), and Yaa (Ala or Ser) and Zaa (Gly or Ala) have small, neutral side chains.
EC: 3.4.23.36
Subcellular Location: Cell membrane
Sequence Length: 186
Sequence Mass (Da): 20258
Location Topology: Multi-pass membrane protein
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A0A249KGD5 | MIAMKASEIASVIQGTLHGDDVTVTEAAVINSAEATPGSLFLAIKGEKVDGHDYVADARSHGAVLTISTKSVEGSHIVVSDVVVALGKLAQHVRSNLLNLTVIGITGSQGKTTTKELLATVLSSAAPTVAPHGNFNNEIGAPLSLLHCTEATKYCIIEMGARHKGDIAHLCSIAQPNIGLVLKVGTAHVGEFGSVKAIAETKSELVASLHEEGIGILGTYDEFTPKMAALHKGKNITFGEGPDCDIRATDIEVREGRAHFDLVTPEGRSAVGLRIVGLHQVANALAVASVATVLGFSLDQIAGGLSTAESAAKWRMEIHELPSLVLINDAYNASPEAMAAALQTLVLFAQERGGESWAFVGKMNELGESSDADHAGIGTLASELGIDHLVCVGAPIYGAKIAADSATSVHLCADKAEALTVAANINPGDVALVKASRSEKLEELAESISAQWLEKMKESEENA | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Involved in cell wall formation. Catalyzes the final step in the synthesis of UDP-N-acetylmuramoyl-pentapeptide, the precursor of murein.
Catalytic Activity: ATP + D-alanyl-D-alanine + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-2,6-diaminoheptanedioate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine
EC: 6.3.2.10
Subcellular Location: Cytoplasm
Sequence Length: 463
Sequence Mass (Da): 48149
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G8NC27 | MYEAVIGLEVHLHLKTRTKAFCGCEAEYFGQAPNTHTCPVCLGLPGSLPVPNRKAVEFGLKLALALGSRVPERLLFHRKNYFYPDLPKNYQISQYDLPLGQGGSLPLGGRAVRIKRLHLEEDAGKSLHLEGRTLLDLNRAGSPLIELVTEPDLHTPEEARLFLQRIQALVQTLGISEASPEEGKLRADVNVSLRRPGEGLGTKVEIKNLNSFKSVQRALEYEIRRQTEILRRGERVKQATLGFEEGSGKTYPMRTKEEEADYRYFPEPDLPPVPLPRAWLQEIRASLPELPWEKEARYQGLGIKPQDAEVLAYTPALARFLDQALALGEASPQALANWLLADVAGLLRERGLALEETRLTPKALARLVALFERGEVTSRVAKTLLPELLEGQDPEALVRERGLRVVADEGALRRVVAEVLAAMPEAAESVRQGKLKALEALLGQVMRRTRGQAKPEVVRRLLLEALGVG | 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 activated phospho-Asp-tRNA(Asn) or phospho-Glu-tRNA(Gln).
EC: 6.3.5.-
Catalytic Activity: ATP + H2O + L-aspartyl-tRNA(Asn) + L-glutamine = ADP + 2 H(+) + L-asparaginyl-tRNA(Asn) + L-glutamate + phosphate
Sequence Length: 469
Sequence Mass (Da): 52076
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A0A9D0U2W4 | MKITGIGTDIVQIERIKRANKRHSSFVKRILHPNELAIYHDHVQQDHYLAKRFAAKEAFSKAVGTGIRGDIQWMDIETKNDTLGKPFFQFHGATQHYLQQVGISESHLSLSDELEYAIAYVILIGH | Function: Transfers the 4'-phosphopantetheine moiety from coenzyme A to a Ser of acyl-carrier-protein.
Catalytic Activity: apo-[ACP] + CoA = adenosine 3',5'-bisphosphate + H(+) + holo-[ACP]
EC: 2.7.8.7
Subcellular Location: Cytoplasm
Sequence Length: 126
Sequence Mass (Da): 14399
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A0A938J3F1 | MIPIPLAELEQAMGAPVSGVDIAVRGISVDTRTVVPGDAFFAIPGARVDPHQLLADAESAGAAALVVERTASEVSVPTIVVENSLEALGHFAHWYWRNRLTCRTIGITGSSGKTTTKDLIAQVLRSYGPTVWPEGSLNTEVGVPLTIVAADQHTRFLVLEMAMRGLGHISYLTRIAAPDVAVVTNVGHAHVGLLGGIDQVAIAKGELVEGMNPDGVAILNADDSRVIAMHTWTRARMVTFGLSSSADIRGERVRSTARSLQFDVIDQRTGERTAVGIEYIGEHNVSNSLAAIAVGIECGMTLMSAAEALNGAQPRSAMRMELVPGAQGVTLINDAYNANPESMKSALTAVVQMNGRSWAVLGEMRELGEFSEALHADVGRHAAESGLDHLVCIGEGTRPMHEAASDRGVESLWLPSTEEAIPVLRARLTPGDVVLVKASRSVGLDRIVTALAQDEGGAAG | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Involved in cell wall formation. Catalyzes the final step in the synthesis of UDP-N-acetylmuramoyl-pentapeptide, the precursor of murein.
Catalytic Activity: ATP + D-alanyl-D-alanine + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-2,6-diaminoheptanedioate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine
EC: 6.3.2.10
Subcellular Location: Cytoplasm
Sequence Length: 460
Sequence Mass (Da): 48487
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A0A972H788 | MKAEAVARRPQVAEPGDSTTIRGLRERLSKTRSVLGQQLSDLIGRGTLDDSFWIDLEDSLVAADVGVSVATEAVRNVRSTTPETGEEARDGLVTHLTSLFAGRERGLNLGRKLSVVLVVGVNGSGKTTTIAKIAAQLGDQGKTVVLGAADTFRAAAADQLKTWADRLGIEIAMGEEGADPASVAFSAVRLGQSKGADVVIVDTAGRLQNKANLMNELAKVQRVIAREAGAVDEVLLVIDGTTGQNALTQAKAFNEVAGVTGIVVTKLDGTARGGVAIAVEQQLDTPIKYIGVGEQVADLVAFSPEDFVDALIGA | 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).
Subcellular Location: Cell membrane
Sequence Length: 314
Sequence Mass (Da): 32668
Location Topology: Peripheral membrane protein
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A0A0G1EYA0 | MPIKSIGSKKIRDILYRMREALHAEEDGAAIAAPQIGESLRIFVVSKKITKTKDLVFINPEIIKASKKKKKVEEGCLSIRWLYGQVKRSEKVTIRAYGETGKQFERGASGLLAQIFQHEMDHLDGILFIDKAENLREIPPAKNIKFVFFGSSQFSRYVLEELELAGFSPALNITSARDPLPIEELKNIQADVFVVASFGKILRKELIELPGYKTLNVHPSLLPRLRGPAPIQGAILEEEELGITIIRMDEKVDHGPILARAKVLITPWPDHYHVVEEKLGRASGKILGA | Cofactor: Binds 1 Fe(2+) ion.
Function: Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions.
EC: 3.5.1.88
Catalytic Activity: H2O + N-terminal N-formyl-L-methionyl-[peptide] = formate + N-terminal L-methionyl-[peptide]
Sequence Length: 289
Sequence Mass (Da): 32379
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A0A938J1V0 | MPGAQERVLRRRIGSVQNTKKITRAMELIAATRVVKAQQRANEARPYAEHITQVIEDLSASGADVDHPLLRQAEQVSRVGVVVLGADRGLAGAYNSNVIKTAEREIMAARAEGLSYDLVTIGRKSKAYFQFRNYPITASFEGFSEKPTFEAAADIAARVISLFTAEGGCDRIILVYTRFISMGSQEVVVRRFLPLQTVSRIAEEGDAKAVAGFEFEPSPAAVLESLLPRYVESRLFSALLEAAASELANRQRAMKAATDNAQELIVKLTRKMNQVRQDAITTEIMEIIGGAEALAEDRDEPGDLILSHLDSDPFPRHSGSGHHTAPDRTIPDPD | 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: 334
Sequence Mass (Da): 36572
Location Topology: Peripheral membrane protein
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A0A944YG85 | MHVKLDEIEKCIGYSFQDKKLLVLALTHPSYNEHDRTRPDNQRMEFLGDSILSAILTEALFIAFPKENEGSLSRKRAVFIRGSSLAKIAYQLRIHKYLLMSTSELKNNGNQRSSTLEDAIEAIIGAIFIDGGIKDAKKCVLNWFGDLPKKLVKDQPSYNPKGQLQEFLHEKSIASKVQYRISKEAGPAHQKNFEIDLIVGKKTLGSGTGSTKKEAEEEAAKQALSKLKFKQ | 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 organism.
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphomonoester.
EC: 3.1.26.3
Subcellular Location: Cytoplasm
Sequence Length: 231
Sequence Mass (Da): 25937
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A0A966NY47 | MTTSFSAKLRAAWSARDSMLCVGLDPDLSRLPNGIDKSPRGVLEFCRAIVESTADVVCAFKPQIAYFAAIGAERELEELCQHIRTNHPEVVLILDSKRGDIGDTAALYAREAFERYGADAVTVNPYLGTDSLEPFFAHTGRGTIVLCRTSNAGSGEFQNIDVDGAPLYEHIATTAATKWATRGDVALVVGATYPTELARVRAIVGDLPLLVPGVGAQGGDVEAVVRAGRDSTGYGLIINSSRAHDC | Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 2/2.
EC: 4.1.1.23
Catalytic Activity: H(+) + orotidine 5'-phosphate = CO2 + UMP
Sequence Length: 246
Sequence Mass (Da): 26213
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A0A938FKH9 | MLSESFCRHVLRRQSWSPTRSGWGSTRGPHWGATTATFSDESTPHSQRGRLVPISWWPADFSASRIRRLHSAVRRSRGHRVASDQPFLQHARVAVAFLTRVPVRHGEEIAMGRVARWFPVVGAGVGVLSAAVLAASREILSNQVSAVLAVITGVLVTGGFHHDGLADSADGLVGGWSPEQRRQILKDSRHGTYGVLALVLQIILQVSVLADLDTRKAVCAVVLMHCLGRAAAVSVMHAGNGITEGLGANYVAGVRKLDMSIALGLGVVFGFVVAGWQGLVPFVVALVVARLGVTYAVKRIGGIVGDVLGGVEQISESAVLLSVMAIVGIGGDFGWS | Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis; adenosylcobalamin from cob(II)yrinate a,c-diamide: step 7/7.
Function: Joins adenosylcobinamide-GDP and alpha-ribazole to generate adenosylcobalamin (Ado-cobalamin). Also synthesizes adenosylcobalamin 5'-phosphate from adenosylcobinamide-GDP and alpha-ribazole 5'-phosphate.
Catalytic Activity: adenosylcob(III)inamide-GDP + alpha-ribazole 5'-phosphate = adenosylcob(III)alamin 5'-phosphate + GMP + H(+)
EC: 2.7.8.26
Subcellular Location: Cell membrane
Sequence Length: 336
Sequence Mass (Da): 35582
Location Topology: Multi-pass membrane protein
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A0A9C8EZC3 | MFSLPSIKIGKILGFNIEINYTWFIIFIIILFQFTLIFDAELASLPISVLAGLITSLLFFSSLLFHELCHSYVAKLNKLPIKKITLFIFGGVAEMTEEPSTPAIEFKMAAAGPLASIFLSGFFYGFFILANILNLGNVLISPLYYLALINFMLAIFNLMLGFPLDGGRLLRALLWYFLKDIKFATKVASMVGQILAYLLMFVGFMSAIQGRIGGIWFILIGWFLNQAAQGSYQQVVLQSALSGIKVSEIMAPNVLTVSPSITLDEIVSNYFLKYRFGRFPVVEGDKFLGVVTLHDVKEIPRERWATTTIGEIVHSSDKLLTINVNNDAVHALMQMAREEIGHLLVVNEKNDLVGLVTRTDIIRLIKVKTELGM | Cofactor: Binds 1 zinc ion per subunit.
Subcellular Location: Cell membrane
Sequence Length: 373
Sequence Mass (Da): 41667
Location Topology: Multi-pass membrane protein
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A0A2K9LHI7 | MSIDLSQFHQVFFEESFEGLQVMESSLLDLDCENVDSETINSIFRAAHSIKGSSSTFGFTEVAEFTHVLETLLDQVREGSRQLLPDHVDLLLQSVDCLHSMLTALQAKEAVDTEQSKVLIQAFNDILEGREPTSSTDASAAGAADVATSQMAPTLEAESAEEVTWNIKFVPDGNLLRTGNEPLRMFRELAELGELDVKANLSKLPDIPVLNPEECHLSWEMYLTTVKPKSDIEEIFEWVVDESDITILATAGLFGELPSQSSVVDLDAGALPGGVPAEQAVEQPESEKLPKKDIKAPTQKAAAQKDSGKSSESTSIRVSIEKIDSLVNLVGELVITQSMLGQLGNEFDMDKLQKLQEGLAQLEHNTRELQESVMRIRMLPISFTFSRFPRMVRDLSKQLGKKIDLKLLGESTELDKTVMEKIGDPLVHLVRNALDHGLELPEERRAAGKSETGTITLNAFHQGGNIIIEIIDDGKGLNSERILAKARANGVIGESEILTDEQIQELIFQPGFSTAEKVTDVSGRGVGMDVVRRNILELNGSIEVRSVAGKGSTFTIRLPLTLAILDGQLINIGNQTYIIPLVSIVESLQPNMELVNHVAGGCDVFRLRDEYIPIIKLCEVFGVDPISDNLSESLLVVVEVGNSKVALVVDDLLGQQQVVIKSMESNYKKVDGISGATILGDGTVSLILDITDLIHMAGVRQQSKNGLKLVSSKIRAA | 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: 717
Sequence Mass (Da): 78254
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A0A938ACM9 | MSTASATRPRVLSGMRPTGQLHVGHLLGALGNWVRMQDDYECIYMVADLHALTTGYEDVQGIRAKGTEMVADWLAAGVDPERSIVFRQSDVPQHAELAILLGMITPLSWLERVPTYKGQIDELGEHLLTYGFLGYPLLQTADVILYKATRVPVGQDQLPHLELSREVVRRFNHLYGPVFPEPEAIISDAPLLLGMDGRKMSKSYGNAITLASSDEEIDKQVMSMVTDPQRIKKDDPGNPEICNVFSWQKLMGASDAEITEIFEGCTTATLGCVADKRNLAEKVKALIGPIRDRREQLMADPAELEAILEEGAERARAIAGPVLAEATAAMGL | Function: Catalyzes the attachment of tryptophan to tRNA(Trp).
Catalytic Activity: ATP + L-tryptophan + tRNA(Trp) = AMP + diphosphate + H(+) + L-tryptophanyl-tRNA(Trp)
EC: 6.1.1.2
Subcellular Location: Cytoplasm
Sequence Length: 332
Sequence Mass (Da): 36425
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A0A9D8DRJ8 | MNVDPRDWASSIRAQVAQGFAYLDLLTAVDYPEAQRIEIVLVLLRPGTAEISTVTTSVDRREPRLGSLVDVLPGASWHEREIAEMFGVEFDGHPDPRPLLLAPGLGLHPLRKETVLGARAVTPWPGARSGHEEGASSGRRTRRTSPPPGVPADWLREAES | 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: 160
Sequence Mass (Da): 17474
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G3JQS5 | MSTTIIIGSQWGDEGKGKLTDIFCSQADVVARAAGGHNAGHVVQANGIYHNFRLLPSGLMVPKCQALIGTGVVFHFPTFFQELADIQEEGIKDAGERVFVSDRCHVNFDLHGAVDAAQEEELAGKAVGSMRRGIGPCYSTKAIRSGIRIAEIFNEARFEEKLRRLAAGYQKRFGGLLKYDVEDEIARFKEYRVAIQKYVVDGVLFMARAKERGANIVVEGSQAILLDVDYGTYPHVTSSSTGLGGAISGLGLGIRDIKEVIGVTKAYNTRLGLGGFPTEDAGEVGQQLQKLGGEYAAVIKQKLRCGWLDLVALRYSCMINNYDSIQLSKLDVLDTFERIKVGIAYRDRDTGAEMPSFPADHDVLERVEVVYEELPGWNTSIAKRREWAELPTEAQKYVEYIERFIGVKANQVDWNGCSARGHYYAGLIYIPGSRMKRVAWPCRSCEAILCRPLLVSAQRVSTTWRALITTSPALQPRLFFLPVPGDDARPSVAMAVADDGSGTAEDEIWALPPRRTQNPLLVWCFSPCFFETHDKAYFCQAKHRTRVP | 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 and in the salvage pathway of purine nucleotide biosynthesis. Catalyzes the first commited step in the biosynthesis of AMP from IMP.
EC: 6.3.4.4
Subcellular Location: Cytoplasm
Catalytic Activity: GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate
Sequence Length: 548
Sequence Mass (Da): 60689
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A0A173SQU8 | MKRFAVIGNPIVHSLSPCMHRANFLALGIEASYELKQVLNLEKEMKDLKQLDGFNVTLPYKQMIIPFLDDVDPIAKAIGAVNTVKNVNGKLMGYNTDVDGFFESFQGLNVKLDASILILGAGGAARAVYFALIKNGYQNITIANRTLDKAKDICDNSISLVQAGEQLESYQCIINTTSVGLIEGECPIDLKNLNSNHVVMDLIYKPKLTTLLKRAKELNCRYEFGLDMLLIQGAKAFEIWFNQEANRTMMKQQLEVELYVNR | Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7.
Function: Involved in the biosynthesis of the chorismate, which leads to the biosynthesis of aromatic amino acids. Catalyzes the reversible NADPH linked reduction of 3-dehydroshikimate (DHSA) to yield shikimate (SA).
EC: 1.1.1.25
Catalytic Activity: NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH
Sequence Length: 262
Sequence Mass (Da): 29330
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A0A938FGZ4 | MGMSGTLTIAATPIGNAGDASARLRDALVEADVIACEDTRKLQRLLNDLSLRTTARFVVYHDVNERKQAPKLVESLVDGKSVLLITDAGTPLISDPGYELIRNAIAADVQVRVLPGPSAALAALTLSGLPPDRFVFEGFLPKKSGARKTRLRDLAGDSRTFIVYETSRNLPRTLQELAEIVEPDRKVFIARELTKVHEEQIRGPLGQVIASLDGRTLKGEVVLVVEGLTRAKRLRPNET | Function: Catalyzes the 2'-O-methylation of the ribose of cytidine 1402 (C1402) in 16S rRNA.
Catalytic Activity: cytidine(1402) in 16S rRNA + S-adenosyl-L-methionine = 2'-O-methylcytidine(1402) in 16S rRNA + H(+) + S-adenosyl-L-homocysteine
EC: 2.1.1.198
Subcellular Location: Cytoplasm
Sequence Length: 239
Sequence Mass (Da): 26041
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A0A1Q7W8J2 | MDESSETTEAAETERDRIRRGEAVVPRAEQAGPDQAARDWGVGAAPGGFGSAEFGSGEYGSGATGAPDAASPDAGAPEEPAAVPAEPRAPRKWWQWLYAPFVVVWRFAFPKKPRPFIVELPFLLAIALVLAFVIKTFLVQAFVIPSGSMQQTLEINDRVLVNRFANWLGHEPNRGDIVVFQDPGGWLDSEPTKPKNFFSKTLTAVGLLPEDNGDLIKRVIGVGGDHIECKGNGAPVTVNGAPLKEDGYLYPSNLPSMEPFSVDVPSGDL | 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: 269
Sequence Mass (Da): 28913
Location Topology: Single-pass type II membrane protein
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A0A1Q7VN54 | MLSALTAAALERRRPAREQALALLATPDEDLLDVIAAAGRVRRAHFGRRVKLNYLVNMKSGLCPEDCFYCSQRLGSQAEILKYSWIAPDEAAALAAKAVDAGAKRVCLVASGRGPSDRDVERVADTVAAIKGGTPDVEVCVCLGLLKAGQATRLAAAGADAYNHNLNTAEEKYADICTTHTFADRVHTLQDATGAGLSPCSGAIFGMGESDEDVVSVAFALRDLDPNSVPVNFLIPFEGTPLGDRWDLTPARCLRILALFRFVFPDVEVRLAGGREIHLRTLQPLALHLANAIFLGDYLTSEGAPGAADLAMIADAGFTVEGREETTLPTARAEQVALRRRGAGTELPANT | 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 radical-based mechanism.
EC: 2.8.1.6
Catalytic Activity: (4R,5S)-dethiobiotin + [sulfur carrier]-SH + 2 reduced [2Fe-2S]-[ferredoxin] + 2 S-adenosyl-L-methionine = 2 5'-deoxyadenosine + [sulfur carrier]-H + biotin + 2 L-methionine + 2 oxidized [2Fe-2S]-[ferredoxin]
Sequence Length: 351
Sequence Mass (Da): 37367
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S5Z067 | MIDVHEAFNIVMNNTKLLKSEDMSLINSLNRVLAEDISSKDNLPPFDKSCMDGYALKSEDTKEKMSKFQIKGSIKAGDFSDIVLKNGEAIKIMTGAPVPKGADAIIQIEKVKVEGKELHVLEKVSPGTNIFKTGEEIKIGDVALKKGKIVRPAEIGLLASLGYTKIKCYKVPKIIIINTGDELINIDQNLMQGKIRNCNEYTLIALIKNLNAEVKSYGIIRDDKNKIFNAIKTAFEEGDIIITTGGASVGDYDFIEDVLKEIGTDIKFTSVAIKPGKPVVFATFKDKLFFGLPGNPLSVINSFESFVAPSIKKNDWKR | Pathway: Cofactor biosynthesis; molybdopterin biosynthesis.
Function: Catalyzes the insertion of molybdate into adenylated molybdopterin with the concomitant release of AMP.
EC: 2.10.1.1
Catalytic Activity: adenylyl-molybdopterin + H(+) + molybdate = AMP + H2O + Mo-molybdopterin
Sequence Length: 318
Sequence Mass (Da): 35034
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A0A0A1D1Z3 | MSKETPDGGWEPLRQAATVALTKAYAPYSNFPVGAAARLEDGSIVSGCNVENASYGLTLCAECTLVGAARMNGGGLITEFYCVDGSGAILMPCGRCRQLLFEFSTAATLVMTSSGAKTMDAILPDAFGPNNLQDANSPKYTENPKEQP | Function: This enzyme scavenges exogenous and endogenous cytidine and 2'-deoxycytidine for UMP synthesis.
EC: 3.5.4.5
Catalytic Activity: 2'-deoxycytidine + H(+) + H2O = 2'-deoxyuridine + NH4(+)
Sequence Length: 148
Sequence Mass (Da): 15509
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A0A173T1Y8 | MKKYFAAAAALAVTLTLGACSNKDEVSIKLPNGNENFITSDVYNVTKQELFNDMVETGGIVALLNQVDYDVLSTKYEIDTTQIDQMIDMYKSIYSDFDQFLALQGFNSEEEVREYLALNLYREAAVKASITVTDEEIQARYDETYKKEETTIEESSSEATTDETTTEEATTEEIPTLDEVKDSITETLVKEKMTDEVVVAALAKEREDAGFTIYNTFLQDQYKEISSTYTENKTKSDLIAKTNEKEYTVEDLYNELVPAYGLSTGISILDTHLLEDKYSYDEKEVKALIDEFKVNWGSNYYAYMAQYGLMNDEEIFNYFKLAALQDAAFAAEYPITDEQLQAAYNEYTPNISARHILVEDEETAKDLIAQLDAAEDKEAKFEELAKEYSKDGSASNGGDLGSFGKGQMVSEFENAAFALNVGEYTEEPVKTQYGYHVIYKYAEDEKPSFDDLKDELETTIRSEEYTQLKLEAILIKYRTEANVKFTDESVQKRYDAIVANIQDSLSAEEGTDNTTTEETATQSSDDVTTDDVTTDEGTDASDNTEEAAE | Function: Plays a major role in protein secretion by helping the post-translocational extracellular folding of several secreted proteins.
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
EC: 5.2.1.8
Subcellular Location: Cell membrane
Sequence Length: 549
Sequence Mass (Da): 61846
Location Topology: Lipid-anchor
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A0A2T4N023 | MIFEFFDASLLARILFIYSKINSLSSLPISIIFPFRWQDLPGRFLSVSLFRRSIWLFLKWIFMKKNKLISRLFGTKNSRTLQKVRAVLSSVNALEPKLSVMSNEELFSLSASLKERAVAQSSVEGLLPEAYALCREMSSRVMGMRHYDVQVMGGIILNDGNIAEMRTGEGKTLVASLPAYLNSLAGKQVHVVTVNDYLAKRDALLMMPLYEALGLRVGYLQSKTKGDERREIYNNCDIIYGTNSEFAFDFLRDNIAPSKENLLQKGLCYVIIDEVDSILIDEARTPLIISGEGDINQGGIDMLKNLVERTKYITVVDFEKDDAQKYSQYDVILSLKNKSVHITEKGFKEIEDELTSLGVITSSSSLYSNQNLPIVDLFTTMIRANYLFEKNKDYVVVDGKIQIINQNTGRIENGRRWSDGLHQAVEAKEGVEILPDNRSLASISLQNFFRLYEKISGMTGTADTDAFELMEVYGLDVVVVPTHKPSLRKDMPDRIYAKKSSKIKGVIDEIIKQHKSGRPVLVGTTSVEESEMISSLLKEAGESSGISGGIPHNVLNAKNHEYEASIVAMAGRPGAITIATNMAGRGTDIILGGNHKELAKSLVTEDEAASAAIKESCLAAAKEVIELGGLCVIGTSRNNSRRIDNQLIGRAGRQGDPGSSVFFVSLEDDLMKIFGGERYISVFKTLGVGEDECITHPFVDKAIRDSQGRIEKHHYSTRKELLKYDDINNMQRKEIYSVRKEWLLCEDVKSKTEDFIVGAVNSMVDSFVPAGASYEDVDFKHIENCIANHWGIENDFSSLENMAVFSAEEIRKYILDKVHAETNRIIEQVGIDNFNSLSRQVMIDIIDRFWIEQISMLDNLRAGIHLRGYAQKNPIQEYSLDSLNMFKDMIGKMKSEFLSEIFVYSNQMIRYLNQIRENAEIQQIN | Function: Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. Has a central role in coupling the hydrolysis of ATP to the transfer of proteins into and across the cell membrane, serving both as a receptor for the preprotein-SecB complex and as an ATP-driven molecular motor driving the stepwise translocation of polypeptide chains across the membrane.
Catalytic Activity: ATP + H2O + cellular proteinSide 1 = ADP + phosphate + cellular proteinSide 2.
EC: 7.4.2.8
Subcellular Location: Cell membrane
Sequence Length: 925
Sequence Mass (Da): 104073
Location Topology: Peripheral membrane protein
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A0A9E3GUE3 | MFPRAFRVARVSGIDVRLDPTLLLIALLVVWSFTGRFGGYGHGLAAAVGMAAAAALLFFGSILFHELGHALEARHRGIEVHGITLFILGGVTEMHLEAESPGDELAIAGVGPWLSLVAAALFGLIATVIPLLGADGLRAVAEVAGVIGWINLALAVFNLVPGAPLDGGRVLRAILWKLTGDRRRAVRISARAGQVVAVGLFALAFQALTTSPAGAVNGLIWGAIGWFMWTAARGELRRAEAEELLAGRTVADLATAPSPRLPLDTPLDQVAPTLARNPGRRIFAVGDDDEVVGILHLDDVMAIDPHDRGFRTTDEVMRPLDGLSFVTAETPLRDLVPALEEQPVVAVREGDRVVDVLTIREVGAALEHLAGDGPRP | Cofactor: Binds 1 zinc ion per subunit.
Subcellular Location: Cell membrane
Sequence Length: 376
Sequence Mass (Da): 39735
Location Topology: Multi-pass membrane protein
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A0A7Y9MM29 | MLQNLTGWHALIILAVIVLIFGAAKLPALARSVGQSMRILKDEVRENAGGTDTQPTDAAGDASLPHDSSDAPHSRALTTADAGGVGPS | 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: 88
Sequence Mass (Da): 8986
Location Topology: Single-pass membrane protein
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A0A9E2Q6M4 | MDAHGPGTGPADGHGLHHVERLTAFTDAVVAIAMTLLILPLLDAVSDSASAGESTAQFVRGNLTRIGGFALSFAIIAAFWRRHHRVFGRFELATEAIVRLDVVWMFTIVWLPVATALVGTMPVDRLQAVLYVGAMAVTSWVLVAIDLLVRRDRRLWGSKEPAGTEDLAAAVSTGVLFMVALAGTVLWPRIGYLPLLLLFGTQPLAGWLAPRLESRTTT | Catalytic Activity: K(+)(in) = K(+)(out)
Subcellular Location: Membrane
Sequence Length: 218
Sequence Mass (Da): 23508
Location Topology: Multi-pass membrane protein
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A0A2H9L5K6 | MALHHVFIIPDGNRRWAKANNVAIETGYLRGVEKMLDVATWCKEFSVGTLSFWGFSTENFDRSAKEKEFLFSIFEHKADELLSSKKYDEYDVSIRFLGELSKFPESLNSKFRQLEELTKNKSQYALNIFMGYGGRQELVHAVQALAGDVKSGSFSADDIDEQKIESRLYTHGLSDPDLIIRTSGEKRLSGALPWQSIYSELYFSDAYWPDFSKKDFQAAIDDFYSRQRRFGR | Cofactor: Binds 2 magnesium ions per subunit.
Function: Catalyzes the sequential condensation of isopentenyl diphosphate (IPP) with geranylgeranyl diphosphate (GGPP) to yield (2Z,6Z,10Z,14Z,18Z,22Z,26Z,30E,34E,38E)-undecaprenyl diphosphate (tritrans,heptacis-UPP). It is probably the precursor of glycosyl carrier lipids.
EC: 2.5.1.89
Catalytic Activity: geranylgeranyl diphosphate + 7 isopentenyl diphosphate = 7 diphosphate + tri-trans,hepta-cis-undecaprenyl diphosphate
Sequence Length: 232
Sequence Mass (Da): 26785
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A0A0R0M477 | MDDLSIDSVSFNDQLLIDHKTITITGFLESIKHKKNFGFLILRSFPQTIQCIFSKDILKEKYEQFTNLNQESFLRLTGYPKKLTKPIKATTIKFYELEITDLKIESSAEKLPFDLKDLNNNILKIEIKKENKKSGSAQIQEQRDEGDENNLQPDVSMKTRLDNRTVDLRSIPSSCIIRLLDETMFLFRSYLRQHSFMEMKTPKLLESGTEGGANLFEVKYFKKTAYLAQSPQFYKQMMIISGFKKVYEIGHVYRQEESNINRYLSEFIGLDLEMETDSMDTLIHFIYNLFFYIFKNIELLEEFETLKKYFPFENLVLSEQPYIIKHSECVKLLKENGHEINYTDDLSRGQEKALGDIIKQNKNVDFFIIKEYPKKVRAFYTETLKESFSENDTKYVDKKSFDKKSTDQISDDKISDNQISDDKISEIEVDPISEIEYSKSFDGILRSEEIFSGSIRIHDHDRLKQSAIDLNINPENISSYLNCFKFGVPRHGGCGVGLERLVKAMVGGKDIRLFTAFCRDPGRLGP | Catalytic Activity: ATP + L-aspartate + tRNA(Asp) = AMP + diphosphate + L-aspartyl-tRNA(Asp)
EC: 6.1.1.12
Subcellular Location: Cytoplasm
Sequence Length: 526
Sequence Mass (Da): 61202
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A0A101GP38 | MKIDRKIVERAATLSRIEMEPENVEPMVRFFRDIIGHFKVLEKCDTTGVDPFSSLEDEPCPLRGDGPVRWDIGDEALDAAPHKEGRFFQVPAIGGEGGPDEV | 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 activated phospho-Asp-tRNA(Asn) or phospho-Glu-tRNA(Gln).
EC: 6.3.5.-
Catalytic Activity: ATP + H2O + L-aspartyl-tRNA(Asn) + L-glutamine = ADP + 2 H(+) + L-asparaginyl-tRNA(Asn) + L-glutamate + phosphate
Sequence Length: 102
Sequence Mass (Da): 11381
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A0A966J8H9 | MSLAASTYDSPCGRLTLVATDTHLRAVLWPLAGEPQRCGIREEITEGSNPIIARTVEQLTAYFDDATTSFDLPLETGGTEFQRSVWTELTGIASGATRTYGEHATAVGRPTSTRAVAAAIGRNPLSIVVPCHRVVGADGSLTGFAGGLDAKRWLLDHEAGRSANLTAPSR | Function: Involved in the cellular defense against the biological effects of O6-methylguanine (O6-MeG) and O4-methylthymine (O4-MeT) in DNA. Repairs the methylated nucleobase in DNA by stoichiometrically transferring the methyl group to a cysteine residue in the enzyme. This is a suicide reaction: the enzyme is irreversibly inactivated.
Catalytic Activity: a 4-O-methyl-thymidine in DNA + L-cysteinyl-[protein] = a thymidine in DNA + S-methyl-L-cysteinyl-[protein]
EC: 2.1.1.63
Subcellular Location: Cytoplasm
Sequence Length: 170
Sequence Mass (Da): 17966
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A0A966MXT1 | RYMEFWNLVFMQFNQAEDGSRTPLPRPSVDTGAGLERILALLQGVDSVWETDLMAPLLDRACSLTGRSYRPGDYSDRDSFAMRVLAEHARSATMLVNDGVFPSNEGRGYVLRRILRRAVRYAFLLGTERLVMPDLATEAIGVMGGAYPDVARNADFITSVLGKEEERFRHTLKTGLGILDNELSAGETLSGSTAFLLHDTYGFPLELTEEIAQERSVAVDLEGFTAEMDAQRERAKAARREGSAGEGMIESYREVLEQFGTTEFTGYAEDVTEARVLAVLEVTGPDGEDLVEVFLDRTPFYAEAGGQIGDTGTISSDSGSLAVLDTTYALPNLRRHLARPTGGSLGVGDTVTASIDVDRRSAIRRNHTGTHVLHWALRSVLGEHVKQAGSHVGPDRLRFDFSHYAAVTADEVAEIERLANSQTLSNSAVRAFETTKDEAETLGAIAFFGDKYGDVVRVLEAGASVELCGGTHVRALGDIGTIKIVAEASIGSNLRRIEAVTGEASVALLQHDEAVLAEVATLVGATGGDVVDGVRRKLDEVKALNDELKALRSKLATGRASEIAGSAVDGVVVERVDVDTPGDLRELALAVRQHAALSRVVLVGATSTGGVALVAAVAPDSGVEAAGLIRDAAKAVGGGGGGKGDVATAGGKDPSGIDEALRLAREAATA | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain.
EC: 6.1.1.7
Catalytic Activity: ATP + L-alanine + tRNA(Ala) = AMP + diphosphate + L-alanyl-tRNA(Ala)
Subcellular Location: Cytoplasm
Sequence Length: 670
Domain: Consists of three domains; the N-terminal catalytic domain, the editing domain and the C-terminal C-Ala domain. The editing domain removes incorrectly charged amino acids, while the C-Ala domain, along with tRNA(Ala), serves as a bridge to cooperatively bring together the editing and aminoacylation centers thus stimulating deacylation of misacylated tRNAs.
Sequence Mass (Da): 71019
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A0A231NZS8 | MNIFNLSQYLETYLFIGAVLFCMGLMGMAFRRTFIGMLIASELILSGASVNFMAFGRFVAHDQTTGQIATLFVMAIAAAEAVVALSIIMVVYRNYRTVDADAPKELKG | Function: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.
Catalytic Activity: a quinone + 5 H(+)(in) + NADH = a quinol + 4 H(+)(out) + NAD(+)
EC: 7.1.1.-
Subcellular Location: Cell membrane
Sequence Length: 108
Sequence Mass (Da): 11842
Location Topology: Multi-pass membrane protein
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A0A920JE10 | MNEMNREMRRMSEREERLAKKADRNIGKYNNEKVSRFKRISNYMGEVRTELKRVNWPSTQILSTFTIVTIVTIITMTLLIFGMDFGFKNTLISMLSLGG | 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: 99
Sequence Mass (Da): 11600
Location Topology: Single-pass membrane protein
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A0A1I0XWL6 | MGKGASKLIDEEKAVIDRVLPRKSQFVRQAAGTRTEAQLIAANIDTVFIVNSLNHDLNLRRIERYVLSTYESGASPVIILTKKDECTTEEVDAAILQVEAAAINVPIIAISNITRDGIDELMAYLPHGHTAALLGSSGVGKSTLINTLLDKEMQGTKDVREADSKGRHTTTYREMFRLPNGALLIDTPGMRELQLWEGESAIDTTFQDVESFAAACKFNDCRHNTEPGCRVREALTNGELSEDRFQSYLKLQRELAYEKRKRDKKAQMEEKNKWKKISKHQRDHHHFRKMR | Cofactor: Binds 1 zinc ion per subunit.
Function: One of several proteins that assist in the late maturation steps of the functional core of the 30S ribosomal subunit. Helps release RbfA from mature subunits. May play a role in the assembly of ribosomal proteins into the subunit. Circularly permuted GTPase that catalyzes slow GTP hydrolysis, GTPase activity is stimulated by the 30S ribosomal subunit.
EC: 3.6.1.-
Subcellular Location: Cytoplasm
Sequence Length: 291
Sequence Mass (Da): 32938
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A0A2E6TCY7 | MYPPAPVVRKGRVVSQEPYHRLLEADRRKAHIKLLLEEITQGEVPAGGVTLELGCGHGHWLTAYAQENPERLCLGVDLITRRIERANRKKDKRDLPHLHFFKAEAMELLQAMNDSIQIDVTILLFPDPWPKKRHHKRRLINKRFLDLLAKRSRKGGQLFFRTDHEGYFTWAREALENNASWEWTPDQPWPLEHETIFQNLLPHHQSLAARIT | 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: 212
Sequence Mass (Da): 24850
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I7LFN2 | MKKNIVIIAGPTASGKTKIGIELAKKIDGEIVSADSMQIYKYMDIGSAKPTREEMQGVPHHMIDVVDPKEEFSVALYRQMAVDCIDNIIKRGKVPIIVGGTGLYINSLTYPLDFTETAKDEEYRFYLQNLAEEKGSHFIHEMLKEVDPESYNRLHPNDLKRIIRALEVYKNTGRPISEFQRESKKREIDFNLAYFGLTMDRTKLYERINQRVDEMFEKGLIDEVKKLKEMGYTKDMTSMQGIGYKEVFDYLDGYLTLEEVKDIIKQNTRRYAKRQLTWFRREDRIFWINLDEFSSIDEVLNVMINYIKEKFMII | 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)-dimethylallyladenosine(37) in tRNA
Sequence Length: 314
Sequence Mass (Da): 36870
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A0A933P4H1 | MERRSDRRNMLVDLAIVAVVGVLATLDLASSVDRVAGSPSPGAIDYILVVAASLSLFWRRRRPVTVMLFVVAMVVVLWLRGDVAMFSVLGLPAVYAAAAHAEDRARTWWALGLGIAGLLVVAGFTVLDADDGYQVGTAVSMTGFLLAAVAAGVVIRNRERIFVDTERRAAEAEADRLAEAQRAVARERSRIAREMHDVVSHGLSVVAVQAAAGREIVHTNPDKAAEVFARIEAIGRESLTELRRMLGVLREAGDDAALLQPQPGLGDLAAFVEQASLGGVTASLVVEGSERPVAPGVALAAYRIAQEALTNVRKHAGTSATATVRLVFEPQQLVVEVADDGDGAASSLAGSGGGYGLVGVRERVEVYGGTLSAGPRRGGGFLVRATLPITTDEAGDPTSTGGDR | Function: Member of the two-component regulatory system NreB/NreC involved in the control of dissimilatory nitrate/nitrite reduction in response to oxygen. NreB functions as a direct oxygen sensor histidine kinase which is autophosphorylated, in the absence of oxygen, probably at the conserved histidine residue, and transfers its phosphate group probably to a conserved aspartate residue of NreC. NreB/NreC activates the expression of the nitrate (narGHJI) and nitrite (nir) reductase operons, as well as the putative nitrate transporter gene narT.
Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Cytoplasm
Sequence Length: 404
Sequence Mass (Da): 42290
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A0A920JEI9 | MLFNSINKLYKKLDKVYVDHFKIDKFGSISLVRGEENSYSIALASIIAKVYRDNLMVDFGSKYPQYLFEKNKGYGTREHLNMIQKYGVCDIHRLSFNLGPTQQPQG | Function: Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
EC: 3.1.26.4
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphomonoester.
Sequence Length: 106
Sequence Mass (Da): 12287
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A0A923YU89 | LIDQVAANDKPAARRPPQGNRVTERLNLIGAAVVGAVNTLGEFLAFLGQTMVVLFQTVVERRPLRWNAVIHQMEVVGANALGIVGLLSFLVGIVLAQQGAVQLRQFGAEVFVVNLIGRSVIRELGILLTAIMVAGRSGSAFAAQIGSMKLNEEIDAMGSIGMSSIEVLVLPRVIAMVIMLLLLSFFGAIMAIIGGGLFCWISLAIPPTSFVQRIQDVTPISDLVIGMVKAPVFGFIIAVTGCFQGMQVSGNAESVGERTTQAVVQSIFLVIVLDAFFAVFFTALGYV | Function: Could be part of an ABC transporter complex.
Subcellular Location: Cell inner membrane
Sequence Length: 287
Sequence Mass (Da): 30475
Location Topology: Multi-pass membrane protein
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A0A7V1G871 | MAVKNFDKPFTFKGGIHPPYRKELASGKSIEVCPLANRVVIPLSQHVGAPAKVQVEKGQEVKAGQVIGQSDAFCFSPVHSSVNGTVKAVGPKLHTCGLQVEAIVIDVNKEDSSVQKLEPLSDDAKPEQIIARVKEAGLVGLGGAAFPTHIKINPPEGKSIETVLINGCECEPYITCDHRQMLEQGDELIEGLKLIIKAVGAKEGFIAIETNKMNAIELLREKTASMENIHVVAVKTKYPQGAEKQLIDAILRKRVPSGGLPVDVGCLVQNVGTTIAVRKAVKKGQPLIERVITVSGEGIKNPKNLLTRLGTPISHLIEVAGGIDGEHNKIIAGGPMTGIVQTSLDAPAIKGTSAITVLKYDSTKKVAAPEPCIKCARCVDGCPVGLLPLRIKAYAEKGLFDELEQLYASDCIECGCCTYVCPAKLPLVHWIRYSKQKLRERGDGK | Cofactor: Binds 2 [4Fe-4S] clusters per subunit.
Function: Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane.
EC: 7.-.-.-
Subcellular Location: Cell membrane
Sequence Length: 445
Sequence Mass (Da): 47717
Location Topology: Peripheral membrane protein
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A0A7V1G851 | MLNVALSKGILLDSTISVLKKSGFDTGALEEPGRRLLVKAGDISYILARPADVPIYVENGAADLGIAGKDALIESGSEALEMLDLKIGKCRFVLAQPEAGIEKKTKTYQQLGQLTVATKYPRIAKDYLDRKGIQAEIITLRGSIELAPITGLADVIIDLMTTGKTLAENKLKVVDEILKCSARLIANSVSARLKYDEIQYFIKRLKV | Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/9.
Function: Catalyzes the condensation of ATP and 5-phosphoribose 1-diphosphate to form N'-(5'-phosphoribosyl)-ATP (PR-ATP). Has a crucial role in the pathway because the rate of histidine biosynthesis seems to be controlled primarily by regulation of HisG enzymatic activity.
Catalytic Activity: 1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate + ATP
EC: 2.4.2.17
Subcellular Location: Cytoplasm
Sequence Length: 207
Domain: Lacks the C-terminal regulatory region which is replaced by HisZ.
Sequence Mass (Da): 22519
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F0R650 | MLLSVLLQAAAGVGISKLGAAIGAGIAVLGAGIGIGKIGGAAMEAMARQPEASGDLRMNMIIAAALVEGVALIAIVVCLLTLFL | 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 catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation.
Subcellular Location: Cell inner membrane
Sequence Length: 84
Sequence Mass (Da): 8143
Location Topology: Multi-pass membrane protein
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A0A2D8I248 | MNVVILGSGKGTNALAVIKASQQDQLANANIVGIFTDNPDAEILKIASQNDIVNDFLSPGFKKSIIEKNEENNWIQKISDLNPDLIVLAGFMRILSSNFINHFQNRIINLHPSLLPSFQGLNAIEQAFNKNVKITGCTVHWVNERVDDGEIIAQAPVRIMNDDELPLVRQKVQAAEHILLPWVIRDLALGTTPFPQ | Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide from N(1)-(5-phospho-D-ribosyl)glycinamide (10-formyl THF route): step 1/1.
Function: Catalyzes the transfer of a formyl group from 10-formyltetrahydrofolate to 5-phospho-ribosyl-glycinamide (GAR), producing 5-phospho-ribosyl-N-formylglycinamide (FGAR) and tetrahydrofolate.
EC: 2.1.2.2
Catalytic Activity: (6S)-10-formyltetrahydrofolate + N(1)-(5-phospho-beta-D-ribosyl)glycinamide = (6S)-5,6,7,8-tetrahydrofolate + H(+) + N(2)-formyl-N(1)-(5-phospho-beta-D-ribosyl)glycinamide
Sequence Length: 196
Sequence Mass (Da): 21754
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A0A662ZG54 | MKKNNFIKNILLTAIFSTALAGCDFASAPKDEIHADGKTMGTFFSITVVGDYPGGQKGLDKDADEVLRKINKEISTFDKDSLLSKFNNSKSTAQFRITQDMADILIESLRVGNDLDGATDITVGPLVNLWGFGPKKVEQQDRIPTDEEISAARANIGLDKLHVEISKNAAYVRKDNPDIYVDLSTVGEGYGADKLAELLDRKGVQNYMVSVAGAIRTKGVNNRGKDWVIAIEDPSNEHAVGRNVIVPVCTKGQAISTAGSYRNYISSKDGKTFSHIIDPATGKPVDHKTVSVTVVGPTALWTDAVDTGLMVKGGEEALRYANERNIAIYVVTRNAKDDGFETHYSRAMHRYLECE | 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(+)
Subcellular Location: Cell inner membrane
Sequence Length: 355
Sequence Mass (Da): 38751
Location Topology: Lipid-anchor
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A0A966Z0D7 | MQGEIAEGVLEITSTGRGYVVCEDLDEDVMVENKYLNKGLHGDTVEVLVGDKKYKNRYEGKVVNVLKRNKKVFVGVFEKNKDYGFVNTRNARMYTDFFIEKEEMKGYKTGETVAVEIKKWEKYNNSPEGRIVKSFGFESDSLDAYSILYEYGLSPEFEEEVEKEAKKIDKKISKEEEKKRRDMRKEMTFTIDPVDAKDFDDAISFKKIDKEKFEIGVHIADVSHYVTPGSIIDEEAQKRATSVYLVDRVIPMLPETLSNNLCSLRPNEEKLTFSAVFIMKKNGQVMEEWFGKTITESNHRLSYEEAQHIIETEEKTIPKQKTILNKEKKVTNSLVEAVTTLNQVAKTIRKKRINKGAIIFDKSEIKFKLDEKNNPKEVVFKTAKSANKLIEEFMLLANRKVAEKMKKGKERFVFRVHDQPDEEKLKNLQTVVKRLGYNLDLNKNNLNDSLNTLLENTFGKKEQNLIDTLMIRSMSKAEYTTKNIGHYGLAFDNYTHFTSPIRRYPDVLVHRLIEAELKNEKIKTDELET | 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: 529
Sequence Mass (Da): 61373
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A0A931ZAU3 | MSASQSFDLIVIGAGPGGYVCAFRAAQLGLKVALVDKRAALGGTCLNVGCIPSKALLHATEHVAWAKAHAADSGIKFGSVEVDLATLMKKKDAVVTKLTGGVGLLAKGRKVTVVTGTASFVSPTEIEVSPDLKLQPSTSTTRLQARHFVIATGSAPVELPFMKFDGETVVSSDHAIAFDSVPKKLVVVGGGAIGLELGSVWARLGSDVTVVEFLPKIAATFDDDIVRQFTRLLQKQGLKIETGAKVTGLRQSKIENPKSKMSASILTAERDGQTLEFEADKVLVAVGRRPFTDGLGLDKAGVSTDEKKRIAVDGRLRTNVPHIWAIGDVVAGPMLAHKAEEDGVAVAEWIAGKAGHIDWDLVPGIVYTNPEVASVGLGEDEAKKRGLTIAVGKFNFAANGRAIAADATDGFVKIIADAKTDKILGAQILGHNAGELISEIVTHMEYGGSAEDLGRTIHGHPTMSEAIKEAALAVSKSAIHAM | Cofactor: Binds 1 FAD per subunit.
EC: 1.8.1.4
Catalytic Activity: (R)-N(6)-dihydrolipoyl-L-lysyl-[protein] + NAD(+) = (R)-N(6)-lipoyl-L-lysyl-[protein] + H(+) + NADH
Sequence Length: 482
Sequence Mass (Da): 50442
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A0A3D2KPN7 | MRPITYAFVGNPNSGKTSLFNQLTGERGKIGNYAGVTVERRDGFTVSIHGKPIRLIDLPGAYSLNAYSPEEAMLASALLDKDIDGIVYVADATKLQRSLYFFTQVQELQKPMIVVLRMVDVAKRLGIVIDIDKLSQSLGCRVVACPMEGKQGILSLRVALSENQKPTEPLFRHDDGLESLLNTLDLPSRGLKIAHLWANEARYSEFLSQHPQWKTACIQTRYDYIKKVLAATVTRTSKKRLKTESIDRVLLHPIIGLVAFFAIMGSLFWAVFTLSKYPVGWIQSLFGLLATWVEGFHLHSGIQSFLIDGALGSIGNVVVFLPQILILFFFLSLLESTGYLPRGAFLVDRCLRIFGLQGKAFIPLLSCYGCTIPGIMGTRCMRSAKERLATIFVSPWLSCSARLPVYIILISILLPNNVSNWTKTALLFAIYALTTLAALLVSFVLRKTLLRGQDVCLLGELPKYQKPPWILIASEMWEQTFAFLKKAGTLILFFSLALWGLMHVPYHPHNRSQNISESVAGQVGRFFEPALKPLGYDWKIGIGILSSFFARETFISTMSIIYGLEDDNPASRDLHSLMLQQKTSVGSPVYSIPTCISLLLFFAFAQQCFTTLAVVYQETKSLTWAISQFLFMTVFAYGVAWAAQVILTHLLHQS | Function: Probable transporter of a GTP-driven Fe(2+) uptake system.
Subcellular Location: Cell inner membrane
Sequence Length: 654
Sequence Mass (Da): 73014
Location Topology: Multi-pass membrane protein
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A0A963SMW8 | MRRISASDAIFLDLETPNAPLSIGGLMVCDTSTAPGHFVRHRDILQYVETRLHLAPNLRRKLVYHPLGLDEPRLIDDPDFDLEFHVRHIGLPKPRDWRQLKILTSRLISRPMDMHRPLWEMYIIEGLEELEGVPDDAFAVLMKMHHAVFDGAAAGATMWTFMQDSPDYEPLPPEKRWVPEREPDMLGWTVSSLQEGFKQWVDNVKALPEMGKGLAASAKTGAKGGKLADSFRGMLAPKTRFQQPVTSHRVWDFVSLPMVEMQALRTALGKPKMNDLILAIIAGGMRHYLNKHGELPEKSLYSFCPINVREGNPIDGGNYVSGMRVSLATNIADPLERLRAITESSLGGKAQATAIGGDFFAHLLAMTPYPLRHRVLGEMLSMPEKFDMETPAIANVVISNSPPPRGGHYFTGAKVICSAGYGPIINLSGVFHAITGLDFESTISVTSCREIMPDIAFYMDCIRASFEEMKEAAAGMAAAAAEAGAAPKPAPAKKPAAKRKPAAKKVAAVRKPATRKAASKKSS | Pathway: Glycerolipid metabolism; triacylglycerol biosynthesis.
EC: 2.3.1.20
Catalytic Activity: a 1,2-diacyl-sn-glycerol + an acyl-CoA = a triacyl-sn-glycerol + CoA
Sequence Length: 523
Sequence Mass (Da): 57452
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A0A966JPX2 | MRLAGELVKPGVTTDEIDEHVHRMCIERGAYPSPLNYQKFPKSVCTSVNEVICHGIPDSRELQDGDIVNLDVTCYLDGVHGDTNATFAVGTISDEDRHLIRVTEECMWLGIETVKPDVPLSEIGRAIEAHARKHRMGVVRSFIGHGIGEQFHTDIQVLHYYEPRNNTLMRPGMTFTIEPMITLGSEKHRMWDDEWTAVTVDGRRTAQFEHTVLVTDTSTLARLLQTLLSRWPEHPRVELVTTDGFLYSNAELTARGILDRKGFPESYDTRRLLEFLRAVKSGEPEVSAPVYSHVIYDVLPDTQVTVHQPDILILEGLNVLQVDSRANEFVSDYFDFSIYLDADESLIEDWFVERFHLLRRTVFQDPNSFFRHFAELNDDQATALARQIWETINGRNLRENIAPTKGRASLVIEKGRDHRVTDVFLRKL | Cofactor: Binds 2 divalent metal cations per subunit. Has a high-affinity and a low affinity metal-binding site. The true nature of the physiological cofactor is under debate. The enzyme is active with cobalt, zinc, manganese or divalent iron ions. Most likely, methionine aminopeptidases function as mononuclear Fe(2+)-metalloproteases under physiological conditions, and the catalytically relevant metal-binding site has been assigned to the histidine-containing high-affinity site.
Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 1/5.
Function: Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed.
EC: 3.4.11.18
Subcellular Location: Cytoplasm
Catalytic Activity: (R)-pantothenate + ATP = (R)-4'-phosphopantothenate + ADP + H(+)
Sequence Length: 428
Sequence Mass (Da): 48983
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A0A520VXX3 | MSDFGKLLTAVITPFDNNGVLNTDTLWRICKKLVHEKSDGLVLSGTTGESPNLTKEDRKIIYSTAKDSVGDKAKIIAGTGTYSTRESIEYTKMANDIGVDGIMIVTPYYSKPSQFGILKHFEQISKNTDLPIMAYNIPGRTATLIEIETLEKLVGDIGIHSIKDAVGDLEFSKNELEVLKGKVDIYSGNDAETIEFMKMGGKGVVSVASHVVGNEIHDLINHVLND | Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 3/4.
Function: Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).
EC: 4.3.3.7
Catalytic Activity: L-aspartate 4-semialdehyde + pyruvate = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + H2O
Sequence Length: 226
Sequence Mass (Da): 24679
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A0A965IXP9 | MASNPPDSNVVRIGVLGCGNVGSAFVQLVERQADIIEARTGVRLQVVKVAVRNVSKDRGLNFADGVLVRDAHAVVDDASVDLVVELIGGIEPARELISTALGKGKPVVTGNKELLANVGHELWALSDSSGADLLFEAAVAGGIPLIRALRESLRGEPVTRVMGIVNGTTNFILTKMAEEGADYTVAL | Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-homoserine from L-aspartate: step 3/3.
EC: 1.1.1.3
Catalytic Activity: L-homoserine + NAD(+) = H(+) + L-aspartate 4-semialdehyde + NADH
Sequence Length: 187
Sequence Mass (Da): 19564
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A0A972HPP0 | MTDPNITFEAAMSDSEALMWNIEKDPWLNPSGSMLIMLDRPIHFEKFRRRMAKATLTIPRLVQKVEPGFGRFINPSWVIDTAFELEHHVRHVAMPANANSNSDLRKMATRIGQIPFDRTRPLWEMHIVDGCRDDQGALIVKVHHSITDGTGAMRMSLAYLDFERKVRMDKKIDLGSKLDEMATASGSASSTPQDAAIDMAKGLGKLAYRNLKVARGAAAEMSMWGADPERIGEMFGGATRQFESMREQLGFDGQSSGGSPLWRERSRQRHLEVLGLDLDDVKSAAKSMDGTINDLFVAGAVHGAARYHEKRQAELESLHVSFVVSXXQRRSVGFQ | Pathway: Glycerolipid metabolism; triacylglycerol biosynthesis.
EC: 2.3.1.20
Catalytic Activity: a 1,2-diacyl-sn-glycerol + an acyl-CoA = a triacyl-sn-glycerol + CoA
Sequence Length: 335
Sequence Mass (Da): 37424
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A0A522QXE2 | MPAPKSSPTGCTLPPPNTRAGSRRCCRLRAWRCGQSNAGHRRYHARCFEPCRAATTPRKPVLSLPKPNALPWLVVSVVVIGLDQLTKAVVRRALVPYAPHEVIPHILNWTLAFNRGAAFSFLSDSSGWQTWLFGILAVVVCVGLIVWLARTRRGDWRTALPVALVIGGALGNLIDRLIHGQVTDFIQVYWHAWSYPAFNVADSAITVGAVLLIFFGLFAGKHQG | Pathway: Protein modification; lipoprotein biosynthesis (signal peptide cleavage).
Function: This protein specifically catalyzes the removal of signal peptides from prolipoproteins.
Catalytic Activity: Release of signal peptides from bacterial membrane prolipoproteins. Hydrolyzes -Xaa-Yaa-Zaa-|-(S,diacylglyceryl)Cys-, in which Xaa is hydrophobic (preferably Leu), and Yaa (Ala or Ser) and Zaa (Gly or Ala) have small, neutral side chains.
EC: 3.4.23.36
Subcellular Location: Cell membrane
Sequence Length: 224
Sequence Mass (Da): 24611
Location Topology: Multi-pass membrane protein
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A0A966NNZ3 | MGFENALLQTSSANSVDDALLRTNLILPKRKKLSEINFSFNRRRVSVLTEDQELITKGAFTEVINLCKRVRVDSAIEDIGPWHTRLLAQNKRWADQGYKVIAVATRSNVETVDENMEREMTFEGILLLNDPPKEDAKDALNKFHSLGINVLLITGDSAVSAGNIAQVVGLDSSQVVTGSEIDQWDDSKLLNVLQNTKIFAEIDPIQKLRIVTALRHSGKVVGFLGDGINDAAALKLSDVSISVEDAVEIAKSASSVVLLEKNLMVIADGVAIGRRTFENTVKYVRITISASFGNVLSMALASFFLPFLPMLPTQILLLNFLSDVPALAISSDRVDPEDLGHSRRWHMKDVGHFMVFFGIISSIFDILVFSVSLSLFDATPEELRSTWFATSLITEVLAIVILRTKRSVLKSLPSRALLVVCIIVTILALTIPGLGILQIFGLPRVGLKYFLLVLVLSTGYGLLTEYAKRSTHLNL | Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Subcellular Location: Membrane
Sequence Length: 475
Sequence Mass (Da): 52277
Location Topology: Multi-pass membrane protein
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A0A381E2H9 | MFSAYYIKITKIPLILTGISPVAYWLAITTLNKIALIRYQYQYKIGEILLTAGFTLTFTAGFMAISFWANYDPAWWLPNHCPVSLFLRYFHPSNIHGYIMTSIRADKRLGQHFLRDNSVIDRLLAVIHPQPGEALLEIGPGLGALTLPLLRETGQLTAIEYDTRLIAPLTTRAASLGELHLIHADILDVDLGAIPPQPERWRLVGNLPYNLSSPILFHCLAARAHIADMHFMLQKEVVERITAAPGGKDYGRLSLMAQLWCDTAALFTIPPAAFAPPPKVDSAIVRLVPRTTPAWMIDDEATFAATVGRAFNQRRKMLRHTFAAWFSPAELTALDIDPTARPETLDGAAYARLANAHYHKEQHP | 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(+) + N(6)-dimethyladenosine(1518)/N(6)-dimethyladenosine(1519) in 16S rRNA + 4 S-adenosyl-L-homocysteine
EC: 2.1.1.182
Subcellular Location: Cytoplasm
Sequence Length: 364
Sequence Mass (Da): 40668
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A0A7W8L8X7 | MGEGHASFVLDGDEIRRGLNRDLGFSPVDRSENIRRSAEVAKLMNDSGIIVIAAFISPYREDRAMARLLVGHDRFVEVFLAADAITCEQRDTKGLYAKARAGVIPEFTGISAPYEVPTEPDLSFDTAVQSVDCVVTALFDWVKSHYC | Pathway: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from sulfate: step 2/3.
Function: Catalyzes the synthesis of activated sulfate.
EC: 2.7.1.25
Catalytic Activity: adenosine 5'-phosphosulfate + ATP = 3'-phosphoadenylyl sulfate + ADP + H(+)
Sequence Length: 147
Sequence Mass (Da): 16227
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A0A364N1B1 | MLFSNIFLPTALLAAQAAAHGAVTSYVIDGVTYPGYEGFSPASSPKTIQRQWPDYNPTMSVNDKKVMCNGGTSADLSAKVKAGGKIRANWKQWTHEQGPVMVWMYKCASDFKSCDGSGKKWFKIDQLGMTAPPLSGTNWGTAFVLKNLYWESSVPASLAPGNYLVRHELIALHQARTPQFYAECAQIEVTGSGTANPSGDFLATIPGLHIPVLGRRFGVGISIDPSSLRPGSPASSFQTPPSPLQPLLFSKLSILSLAHHLALWLPAHSDLGNPRIALGILIHIGWCSFERGVDLGDDTGDGGENVGGGLYRLDGADCVAFANVHFDLGKLDVDDVAEGFGCVFRDAEGACGVAHRISLPRIAKTAGKIVLDQQGVVRGVSNWGTFLLPKPAKKLQSTHHYGHHFIMRFDASARAQHALRRTMSLDPRLIRYSVIKMGTKFEEIKDVPGKANFREKTNGSSSTAPRFDVISDIAVSKASSTESPTPITSQSPAPATSVTSTIPDPLEQQAFFFSSMGFNEHHQMPSTGPVGSSTVEANFIGKYLGFVFPAMFPFYRPTLFETGSSWLLHLLWKRQPARHAAVGLSCYIFTQALTDVRARGDNTGDFADCRAARWEEVNAHTDRCFQSLRTELSALDKHTKLANMNRVELFECVIQALVLEMGIGKANPLRSHLAPAFGLFHDIMNPNYHCANESPQLKLVGVLLNIEEPLWTSPNSGSRIWSPTQTGFRFCAAYLAFVDVIASTALQTPPKLLSYHDTILTQTDNGIYNVTEVQVQLSGIIGHPLVFARHSTQVQILPRPLLHHSSGQTPPIFT | Function: Has endoglucanase activity on substrates containing beta-1,4 glycosidic bonds. Involved in the degradation of complex natural cellulosic substrates.
Catalytic Activity: Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.
EC: 3.2.1.4
Subcellular Location: Secreted
Sequence Length: 814
Domain: Has a modular structure: an endo-beta-1,4-glucanase catalytic module at the N-terminus, a linker rich in serines and threonines, and a C-terminal carbohydrate-binding module (CBM). The genes for catalytic modules and CBMs seem to have evolved separately and have been linked by gene fusion.
Sequence Mass (Da): 88721
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A0A5J6WL21 | MLVSMRKNGGILAIFALACTSVVAITNAVTKDRIAEQEQTQLLKIINQLLPEDSHDNNIFQSCKLMTNEALLGSSEPQRIFTATKNNKPIGYAIEGIAPKGYSGNIKLVVGINTVGKVTGVRILGHNETPGLGDKVEYRKSNWLDDFVDQTLTEENAHTWAVTKDGGDFDSFTGATITPRAVVGSVKNILTFYQSEQFSNLNNAPSCWSKS | Function: Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane.
EC: 7.-.-.-
Subcellular Location: Cell inner membrane
Sequence Length: 211
Sequence Mass (Da): 22980
Location Topology: Single-pass membrane protein
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A0A933UJ91 | MSYALLDTRTWHRTSAVVMGCTAELMFDGSSSLAPIAFDRLRELEHAWSRFLPDSELNRLHARPGQWVHVSHELFTALHWCDRLHGETEGRFDPSIRTALEAWGYDRTFREIDQSASSPTHTPPAPGLAGLELRRDDEAVRLAPGLRLDLGGVGKGLAADMVSGELILMGASGAFVSMGGDIAVAGDTPDGGWSVPLEHPDTDLPFDTHLLSDGALVMSTTRMRRWQRGGITAHHLIDPFTGAPAVTDVIAVAVASMSAARGEALAKAAVVAGSAAAVEMLDGFGVAGWVLTSDEVIRVGLPA | Cofactor: Magnesium. Can also use manganese.
EC: 2.7.1.180
Catalytic Activity: FAD + L-threonyl-[protein] = AMP + FMN-L-threonyl-[protein] + H(+)
Sequence Length: 303
Sequence Mass (Da): 32310
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A0A0R2FYI5 | MDHGAANLVDAVLEPSPVEIKKQGLYKQWGLTEDEYEYIVAQIGRLPNYTETGLFAAMWSEHCSYKKSKPVLRTFWSQNERVLQGPGEGAGILDIGDGQAVVFKAESHNHPSAVEPYEGAATGVGGILRDIFSMGAQPIAILDSLRFGEVTQPSTRRLVDGVIAGIAGYGNAIGIPTVGGELVFDKAYQGNPLVNVMAVGLLDQTQMHVGKAEGIGNEVLYVGAKTGRDGIHGATFASAEFDSARGQDRSAVQVGDPFLEKLVMDTTIKVMRELGDSIIGVQDMGAAGLVSSSAEMASKAGNGIELDLDEVPQRETNMTPYELMLSESQERMLLVVKKGQAAKIADYYAKAGLAAVVIGQVRADQRYRLRFKKEIVADVAVDFLTTPPEPVLQQRQPRRLQVVNKQQMQPDLTDASATFLALLGQSSLASKASLYRHFDSMVRTDTVIKPGSDAALVRVAGTKKGLAMTTDINGRYTYLDPKEGGKRAVAEAAANIVVTGAKPIGITDCLNFGNPDDPTIYYELAQSVAGINQMAR | Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole from N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide: step 1/2.
Function: Part of the phosphoribosylformylglycinamidine synthase complex involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate. The FGAM synthase complex is composed of three subunits. PurQ produces an ammonia molecule by converting glutamine to glutamate. PurL transfers the ammonia molecule to FGAR to form FGAM in an ATP-dependent manner. PurS interacts with PurQ and PurL and is thought to assist in the transfer of the ammonia molecule from PurQ to PurL.
Catalytic Activity: ATP + H2O + L-glutamine + N(2)-formyl-N(1)-(5-phospho-beta-D-ribosyl)glycinamide = 2-formamido-N(1)-(5-O-phospho-beta-D-ribosyl)acetamidine + ADP + H(+) + L-glutamate + phosphate
EC: 6.3.5.3
Subcellular Location: Cytoplasm
Sequence Length: 536
Sequence Mass (Da): 57554
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A0A932FN12 | MPAGDRAAGSFVALRTTVAWIGRLPVRAASGLVWVYQKTASPALVVLDPTGGCRFAPTCSHYARGALAEHGLIAGAGLTLRRLAKCGPWHPGGEDPVPPRARPVCNKVSAA | Function: Could be involved in insertion of integral membrane proteins into the membrane.
Subcellular Location: Cell membrane
Sequence Length: 111
Sequence Mass (Da): 11496
Location Topology: Peripheral membrane protein
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A0A938AUY5 | PSIDAESKKALVRRVFERELPEQLVNFLLVTIDKRRQRLLGKIAEHFRALVDEKEGRVHVEVTLARPMDDSSLRLLTRKLSELLGVTAVPHVRVRPEILGGVVVRTGDTIYDGSVRRQLDGMRRQLLKAKLPSGSRG | 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 catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation.
Subcellular Location: Cell membrane
Sequence Length: 137
Sequence Mass (Da): 15497
Location Topology: Peripheral membrane protein
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A0A967PK01 | MLRFLTAGESHGPALTCIVEGLPAGLEITVDGLGAELARRRSR | Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 7/7.
EC: 4.2.3.5
Catalytic Activity: 5-O-(1-carboxyvinyl)-3-phosphoshikimate = chorismate + phosphate
Sequence Length: 43
Sequence Mass (Da): 4535
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A0A0R2FWH0 | MAEIIDGRTIAKELRTAVSQQTERLAQVGVKAGLAVILVGDDPASQIYVRNKERAAKKVGVVAETLHYPTTVTQAELLTKIDYLNQNPTVDAILVQSPLPAHINEETIQAAISPAKDVDGFHPENIGRLFAGRNEFYPVANTPRGVMTMLAHEGVSLDGKNAVVIGRSILVGRPMFALLAKAGATVSLLHRGTPSALKRQLVQAADIVVVAAGHPNLLKGEDIKPGAVVIDVGINRMDDGSLVGDVDFQAVSQLASKITPVPGGVGPMTIATLLETTVELAARHHGIELEQGWQNI | Pathway: One-carbon metabolism; tetrahydrofolate interconversion.
Function: Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10-methenyltetrahydrofolate to 10-formyltetrahydrofolate.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + NADP(+) = 5,10-methenyltetrahydrofolate + NADPH
Sequence Length: 296
Sequence Mass (Da): 31391
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A0A966U5D0 | MRASAEILGNGGVVALPTETVYGLGASVTSPTGLRRVFEVKGRPFDHPLITHGASSAILDNVGENVSPIARKLAELVWPGPLSLLVPRSDSLDPLVTGGRSSVVVRVPAHDFFRRVVEALGSPIAAPSANRFGRVSPTNAEHVRSDLGHDVDLIVDGGPSVIGVESTIIDTTLEPPQILRHGGIPIEDLELLTGVEFAEASGGSRAPGMLASHYSPRCTVHLAESQAEADEILAQFPTGSSGLIDAPSSLAMYAATLFSSLRACDDKGWLHAVAVLPADVGLGRAIRDRLQRAASPS | 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.
Catalytic Activity: ATP + hydrogencarbonate + L-threonine = diphosphate + H2O + L-threonylcarbamoyladenylate
EC: 2.7.7.87
Subcellular Location: Cytoplasm
Sequence Length: 297
Sequence Mass (Da): 31017
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A0A942IIA1 | MRNEDIARIMEDIGDMLDILGENRFRVRAHRNAAQSIRGYTRPLFEVYDEGGPEALTAISGIGEHTAKRIEQLLVTGQLPYYEELKAKVPPGLIEMLNIPGLGPKKAKKIYDSLGIKSLKELVGAVEEHRLESLPGFGRKTEENVLRGIRQFETLHERILLSEGYPIAREIVDRLREQQFVERADTAGSLRRMQETIGDIDLLCASDEPASVMEFFVSMPQVAYVLAKGETKSSVVATNGLQFDLRVVAPGQYGAALQYFTGSKEHNVHLRHIAKARGFKINEYGVFDVETDERLAGATEEEVYAILDMETPPPVIRENKGEIEAAAERRLPDLVELADIKGDFHIHTKWSDGLNSIEEVIAMARTLGYKFIVISDHAEKLRIAGGLSVRELEEQMEAITALNEEHADIEILCGLEMNIDNDGEVDFGAAVLEKLDVVIGSIHGGFAQPKEKLTTRMLKALENPYINIIGHPTGRVLGRRPPYEIDIRAVFEAAARTGTFLELNSYPNRLDLKDDHLREAKDVYGCMFTINTDAHVAGNMAHMEYGVATAQRGWLTKRDVLNTYEVAEVKKLLRRKR | Function: Repair polymerase that plays a key role in base-excision repair. Has 5'-deoxyribose-5-phosphate lyase (dRP lyase) activity that removes the 5' sugar phosphate and also acts as a DNA polymerase that adds one nucleotide to the 3' end of the arising single-nucleotide gap. Conducts 'gap-filling' DNA synthesis in a stepwise distributive fashion rather than in a processive fashion as for other DNA polymerases.
Catalytic Activity: a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)
EC: 2.7.7.7
Subcellular Location: Cytoplasm
Sequence Length: 577
Sequence Mass (Da): 64642
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C1AS26 | MVMLWIACAGSAGAIARFVIDGAIKHRKASEFPWATATINVTGSLLLGFVTGLILFHGVPREIQLIVGVGFCGGYTTFSTASFETVRLIQRQKYAAGIANAVGTLTVTVIAGGAGLALASV | Function: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Subcellular Location: Cell membrane
Sequence Length: 121
Sequence Mass (Da): 12471
Location Topology: Multi-pass membrane protein
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A0A0Q8RKQ5 | MAALGRPLAAVGSAGNGAPLWPTGMIGSISHNDRLAVAAVATTEGGLRGLGIDIERVIGADQHESMLSLVVNRREHALLLKLDAGRSLPFSSGLTLAFSAKESFYKAVSAVAGRVLEFDAIQLTAIAGDGAGGQIHFQAVAAISDEWFPGRRGQAGYMALPNGDLLTSFAW | Pathway: Siderophore biosynthesis; enterobactin biosynthesis.
Function: Involved in the biosynthesis of the siderophore enterobactin (enterochelin), which is a macrocyclic trimeric lactone of N-(2,3-dihydroxybenzoyl)-serine. The serine trilactone serves as a scaffolding for the three catechol functionalities that provide hexadentate coordination for the tightly ligated iron(2+) atoms. Plays an essential role in the assembly of the enterobactin by catalyzing the transfer of the 4'-phosphopantetheine (Ppant) moiety from coenzyme A to the apo-domains of both EntB (ArCP domain) and EntF (PCP domain) to yield their holo-forms which make them competent for the activation of 2,3-dihydroxybenzoate (DHB) and L-serine, respectively.
Catalytic Activity: apo-[aryl-carrier protein] + CoA = adenosine 3',5'-bisphosphate + H(+) + holo-[aryl-carrier protein]
Sequence Length: 171
Sequence Mass (Da): 17714
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A0A520W360 | MQNNNYKLHFIGAGNIANAMISGLINSGFPSLNIYVYDKDPAKTLSLVDKFNINDHKELSFLDEGYLFICVKPADYTDLLEEIKEHIGKGVFVLSCMAGVSLERIDKDFEDNICLRFMPNMLIENSSGFIALTSRSKNLINDFISIFSEIADIREIPEDMFDVITAAAGSGPAWIYYYINSLIKAGCKNGLNEEESKTIVLSLLKGASNKLSQDTDLNQLIQEVASPGGTTEAGLKIIEEENVDEIISDVISKATKRSKELREDSN | 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
Sequence Length: 266
Sequence Mass (Da): 29480
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C6YB66 | IFGAWAGMVGTALSLLIRAELAQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPVMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSAVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAISQYQTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQ | 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-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Catalytic Activity: 4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-[cytochrome c] + 4 H(+)(out) + 2 H2O
EC: 7.1.1.9
Subcellular Location: Membrane
Sequence Length: 212
Sequence Mass (Da): 22464
Location Topology: Multi-pass membrane protein
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A0A4Q7DLZ4 | MLSRGLFVTFEGGEASGKSTQVRILEDILTNLGFDVVVTREPGGTVFAEKLRSILLDGNGVTDPLTEFLLFNAARRDHVVNVIEKAVAQQKVVISDRFLDSSLVYQGYLKGISVDLIHEISRLSIGECTPDLTILLDVDPELARSRLKQSFSHHTHYDKADIQSFTLIREGFLKLAALFPDRIVTIPGNTDSCTLSAQIANLVLERIKARDAQSLSTDTLANNKDAV | Function: Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis.
EC: 2.7.4.9
Catalytic Activity: ATP + dTMP = ADP + dTDP
Sequence Length: 227
Sequence Mass (Da): 24970
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A0A937VK18 | MNDEVRPQAGLTIAIIGVGLMGGSLGLAARSRGAADRVLGFSRSPETLANALELGAITGSCATLEDACGDADLVFVATPVRLIPEHVHAALAAAPERAVVTDMGSTKGRLMAELTHQEQRRFVGGHPLCGAETAGVAHATASLYRGATYFLTPGAHVDPGAVQRLFGFLTEIGARPVAVDPFEHDRLMALLSHLPHVIANALMTQAGEHRGARDALVSAGPSFRDMTRVAGANAHIWTDIFAENREALLASLREFRARLEEVSAAIEAEDEDRVAGTIARAARHRARLLEESSLPPADLFRLTVRIPDRPGVYRDIMVALGDAGINIEDLSMHHESAELGGVLAVYLLGEP | Pathway: Amino-acid biosynthesis; L-tyrosine biosynthesis; (4-hydroxyphenyl)pyruvate from prephenate (NAD(+) route): step 1/1.
EC: 1.3.1.12
Catalytic Activity: NAD(+) + prephenate = 3-(4-hydroxyphenyl)pyruvate + CO2 + NADH
Sequence Length: 351
Sequence Mass (Da): 37225
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A0A9D8EKX2 | LRARLSDAKFFYEQDRKCSFDFWVEKLKGVVFYSGLGSLFDKSLRLEKICSEIISLLTANDRDSGFNRPGLLKECSRASFICKCDLVTDLVVEFPELQGFVGREYAKEKGENPDVAEAIFEHYLPRYAQDILPETGAGSILSIADKLDTIAGMFIAGNIPTGSEDPFALRRKASGIILTSLGKDYNLDILKVAGFAAGLFIESFEFKNCDANSVAQDVSDFIFARYRSRLEKASRRTDLFDAVRETGCSSIRELDLRYRSLEDYIRARKSILALSEPLTRCKNIIKGKTFSDISRTLLKDDAEISLFETLLEKEKLLSEYLKENRFDEALQELEDFAGSVNLFFDRVLVMEKDENIRSNRINIIHRCTQLYYNIADFSRIL | Catalytic Activity: ATP + glycine + tRNA(Gly) = AMP + diphosphate + glycyl-tRNA(Gly)
EC: 6.1.1.14
Subcellular Location: Cytoplasm
Sequence Length: 381
Sequence Mass (Da): 43425
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A0A9D8HRK3 | MLKTFEVNVAGVKNLCEICLSCDSALMHFSTDFVFGGYTRKSPYTEDDCPAPVSAYGISKLAGEYVIKYMLDKYYICRVCGLYGHAGSLGKGYNFVELMIRLAKEGKDIKVVDDQVLTPTSTKDVTEKLYELVQTKKYGLYHMTDTGSCSWYEFACEIFRLSGLTPDISPTTSEAFASKAKRPSYSVLDNKNLRLIGLKDMRHWKDALADYINERRILLK | Pathway: Carbohydrate biosynthesis; dTDP-L-rhamnose biosynthesis.
Function: Catalyzes the reduction of dTDP-6-deoxy-L-lyxo-4-hexulose to yield dTDP-L-rhamnose.
EC: 1.1.1.133
Catalytic Activity: dTDP-beta-L-rhamnose + NADP(+) = dTDP-4-dehydro-beta-L-rhamnose + H(+) + NADPH
Sequence Length: 220
Sequence Mass (Da): 24866
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A0A942GKD9 | MKKIDVVATSKSYPVYYGKGIFLKLKFLIDKNRLNRKIFIVVDENVYSHHTTRIDSFISSIDLKVCLYSFNANEINKSAAQLNDIYSSLIENGFGMDTLIISIGGGITGDIAGFAASTYNRGVQIIHVPTTLLAMVDSSIGGKTGINFDSTKNIIGTFYQPEFILVDTDFLKTLPEEEFICGLGEIIKYSFLTGGDFLKKIKRSLSKSLKLDTKLLLNSIETCIKFKAGIVEKDERETHGLRKILNLGHTFAHAIEVERGYTLKHGQAVILGLTCSLYLSRKLGIINEKLLREYLSLLLKTKDRINLNFFYAMKIYEIMKRDKKSVNDKIKFVLIVEAGNILVDVEAPAHMVLESINNGMDHFLVN | Cofactor: Binds 1 divalent metal cation per subunit. Can use either Co(2+) or Zn(2+).
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 2/7.
Function: Catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) to dehydroquinate (DHQ).
EC: 4.2.3.4
Subcellular Location: Cytoplasm
Catalytic Activity: 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate = 3-dehydroquinate + phosphate
Sequence Length: 366
Sequence Mass (Da): 41128
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A0A944GTP5 | MSDDQDKDSKTEEPTEKKIQDAIEKGNTPTSKEAPVFASFLAVLLIGSFVLSSSVSSLAAQLMQMIDKAGGYKLGNGADALLLSHAISLEIGRFLAPIVTIIALAGLTSAFMQNKPRLVLHRIKPDGSRLSPIKGWNRIFGAQGFVEFLKAVFKFSTVSAAAFLQFQASQTGLVSAMFSDPSTLPELILQISMKLVSGVCIVTIVLVAVDIAWSRSHWRKNLRMSKQDIKDEHKQAEGDPIVKARQRSLARDRARNRMMSAVPKATLVVANPTHFAVALRYDSDSMAAPVVVAKGQDLIALKIRQIAEENEIPVIEDRELARSLFASAEIDRMIPAQFYRVVAEIICYVYSRRVDAVV | Function: Required for formation of the rod structure in the basal body of the flagellar apparatus. Together with FliI and FliH, may constitute the export apparatus of flagellin.
Subcellular Location: Cell membrane
Sequence Length: 358
Sequence Mass (Da): 39287
Location Topology: Multi-pass membrane protein
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A0A2G9ZD74 | MPIMEKFVIHGPNKLEGEVDVSGSKNAALQLIPATLLADSPSTITNVPDILDIRNILDIIKILGAKVDFSNNELTIDPTTLKSCELPEKLVGKLRASIMLAAPLVNKFNSCQIPYPGGCVIGKRPLNYHFDAYRALGYNVTEKESSYKIEKGNPTGTTININFSVLATGNTIMAAVYAKGETVIKLAACEPEVSILIEFLNKMGADIEWIDNHIIKIKGTTSLHGTNIKNMPDRIEAGTFAIAAAACHSEIIINDFYSSHNDALLFKFREANVKYEIEGNKLHIKKGTFIKPVKIQTKEYPGFPTDLQAPFSILMTQAEGISEVFETIFEGRLGYLHELEKMGAKVIIKNSQFANIDGPTPLYGTHIDSLDLRAGATLIIAALTAQGESIINNIDIIDRGYENIEGKLVDLGANISRVASNLITLKS | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine.
Catalytic Activity: phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine
EC: 2.5.1.7
Subcellular Location: Cytoplasm
Sequence Length: 427
Sequence Mass (Da): 46616
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A0A2D1C2X2 | MIFFFLFFFCFFLFFLGKQFFKGFNSYFFMNTMKEYECGYGELDSINYSYLYQFYFVSISYMVFDMEIVFFLPIFFSLGFVNYIFLGGMLFLFMLILGLLWEMFYNIF | 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 of complex I.
Catalytic Activity: a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) + NAD(+)
EC: 7.1.1.2
Subcellular Location: Mitochondrion membrane
Sequence Length: 108
Sequence Mass (Da): 13363
Location Topology: Multi-pass membrane protein
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A0A0D5MFC7 | KDIGTLYLVFGAWAGMVGTALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPVMIGGFGNWLMPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGISSILGAINFITTIINMKPPAITQYQTPLFVWAVLVTAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFF | 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-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Catalytic Activity: 4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-[cytochrome c] + 4 H(+)(out) + 2 H2O
EC: 7.1.1.9
Subcellular Location: Membrane
Sequence Length: 226
Sequence Mass (Da): 24264
Location Topology: Multi-pass membrane protein
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A0A2H9L6Y9 | MEGQTGQTEDNIITYPGGFKANGMNCGIKFKNNDLGAIVSEQECTVAGMFTTNRVKSESLMYSMPIVKKGRARALLVNSGNANTCIGKQGVKDARTAAKALARQLGIGGKEVLFFSTGIIGRPLPVGKIIECMPALTSGLSDNAMPVAQAIMTTDTTQKIVAEEADIDGKKVKFVGIAKGSGMISPKLATMLCFIATDANISQEGLKKTLAASVNTTFNRITIDGDTSTNDSVVVMANGMAGNSQIGCDGELFAKFGNALHSVCAKLARMLIEDAEGATKFLTITVKGSPDTRSAEGIAFAVADSKLVKTAMFGNNPNVGRIIAAVGYAKVKFRVKPDKVALRVNGIECFREGKLLYEEARAIDLKGRFIEIEIDLGSGNEEATIWTSDLSFDYVKINAEYN | Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; L-ornithine and N-acetyl-L-glutamate from L-glutamate and N(2)-acetyl-L-ornithine (cyclic): step 1/1.
Function: Catalyzes two activities which are involved in the cyclic version of arginine biosynthesis: the synthesis of N-acetylglutamate from glutamate and acetyl-CoA as the acetyl donor, and of ornithine by transacetylation between N(2)-acetylornithine and glutamate.
Catalytic Activity: L-glutamate + N(2)-acetyl-L-ornithine = L-ornithine + N-acetyl-L-glutamate
Subcellular Location: Cytoplasm
Sequence Length: 402
Sequence Mass (Da): 42730
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E7RXN7 | MMCNTQPTPAMPSTANATPQPFAELGPNTVLAALEEIGLRCDGRLQALNSFENRVYLVGLEDGGSRVAKFYRPGRWNRDQLLEEHRFAHEIAAAEIPLAAPLHRDALMAPDLLDEEEDPEDDAAVADTLFESHGFYIAVYRRQGGRVPELDNIHEGPAMRERIGQFIARIHQVGARHGFLHRPPLDCGLDGWRSIERVTECAWLPPEVRHQWEDLARQCCTLVEARLHPTLASPGVADFTRIRLHGDCHLGNLLWTEAHGPHFVDLDDCRSGPAIQDLWMIADAAGQQDAETGDDATSQAMHELLAGYKQIRPFERRELALVEPLRTLRIIRHSAWLAERWEDPAFPAAFPWFGSVRYWQGQIISLQEQLAQLRGL | Function: A protein kinase that phosphorylates Ser and Thr residues. Probably acts to suppress the effects of stress linked to accumulation of reactive oxygen species. Probably involved in the extracytoplasmic stress response.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
EC: 2.7.11.1
Subcellular Location: Cytoplasm
Sequence Length: 376
Sequence Mass (Da): 42381
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A0A0C3BZD8 | MPSRKAKNRKGAASSLNAEHNQRPVSGFFPFARYVSVVGVHTTLLAFVALFLPRVPRDPLRSPSPSPFLEGLTRDPVLTVMWICAGAIPLQGWWAGWVRKWWIQFSIKGTDAEKRLEENERDRNKFSTLKNAWLATVATSFVVYAVVVLFGAPLLRLVPFRFALTLCSSLLTVTIYTRIFWHVLCLF | Pathway: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor biosynthesis.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 187
Sequence Mass (Da): 21208
Location Topology: Multi-pass membrane protein
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A0A968CA29 | DLLDTPNHLLTTDLSGVEALTDEQRSDLTGRSMVVRRAEVIPVECVVRGYLYGSSWREYRDGGGPTTEHLPDGLRMADRLPEPIFTPATKATSGHDENITEAETRSLLGDELYERLKRTSIDIYLTAANFAAERGVILADTKFEFGWAGDELLLIDEVLTPDSSRYWPKDQWSPGSAVPSYDKQYVRDWLDSVGWDHMPPAPTLPAEIVTETRAKYVEAYERITGKRFDDYPTQT | Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate: step 1/2.
EC: 6.3.2.6
Catalytic Activity: 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + ATP + L-aspartate = (2S)-2-[5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamido]succinate + ADP + 2 H(+) + phosphate
Sequence Length: 235
Sequence Mass (Da): 26516
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A0A0F4IL53 | MHDAYDVLCVGYGPANVAVAVAFEELWPQARVKFIEREPGPYWQRAMLLDGSDIQNNPLRDLVTPRNPRSRYTFTNFLHEQGRLFKHLNLPSHYPLRKEYARYVQWVAQNVGADVDYGREVTGIDVTATGDGPLVEVSTADGTTYRGRSVVVAPGRTPNVPEVFSGVPAPHLFHTSQFLPNIADLERDFDGTLAVVGASQSAVEVVLDLIARFPAARIVNVMTGFGYRLKDTSPFSEEVYFPEFVEYYFHASEEGKKRLRDQLRPTNYSAADADVVSALYMRMYEDELDGRERIRLCTNRRVEAVERTPEGVALDLSEHITGERERIHADRVVLATGYLDLGITGRTEQLPPLLKDLTQVLGVTDGRPLSVGYDYGVVPHPAFEREVPPIFVNGLCESTHGLGDAGSFSLLALRSQAIVESLERRLVAERGAADLVAAQASGSEI | Pathway: Siderophore biosynthesis; mycobactin biosynthesis.
EC: 1.14.13.59
Catalytic Activity: L-lysine + NADPH + O2 = H2O + N(6)-hydroxy-L-lysine + NADP(+)
Sequence Length: 445
Sequence Mass (Da): 49379
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A0A7D5FJM5 | NIISILNIRIIYDTINIKKFLKMTLIELIWTITPALILIAIAFPSFRLLYLLDEVTSPTVTIKVTGHIGLKFIINNLKHFLIKRIYKINTFLYLQSYANIEKSHIVKKLIVKNLSKNRHNALNLYHNNLLLSKSSHSIFIRNPMTIRVPNRISDKFLPLSSTNFTTFKNFHTRCRAINRIGPHNIDVISILVGLLLGDGYLNNRSGEGARMAIKQSIAHKEYLFNLYEFFYNRGYCTSLPPRLYIRNIKGKEKNYYGFEFNTFTFRSLVWLHKLFYKNGKKVIPSNISELLTPLALAVWIMTNGYIKENSNTNLGIISRSSTLQIYSVFNSIESNNILINVLKKNFYINSYLFKDKKGTYIINIDPNSIESTFNLIKPFIFPSAYAKLGLTFPLLEYNNPEIEKSLIYKENSNKSGIYRWINKITGNTYIGSSSNLRLRFYSYFSIHWMTKKVETSNSLIYSSLLKHGYSNFKLEILEFCDKQELASREQFYLDYFKSSYNILNLAYSSLGYIHSQESKIKIKDAMQNWLSKGENLELVRNNILKLNLEKGIKVEVLDTYTNITTHYDSIRQAATFLNCHLKTLLEKEKLSSKNKSSNNSKTQFIFRGKYFIKILRASNSTFYPTDDIYTEYKTLIENKSLKEEFNGQNTNLEISENLLSKDGILKDQDQKEKREYDYLERRSIEVLGLDQIASPGELELEKAKQKYKDAFGKKIMVKNIITGSSKEYNSISEASKELKMDRKTIRNYISSKKIFKNIYSFSL | Function: Mitochondrial DNA endonuclease involved in intron homing.
Subcellular Location: Membrane
Sequence Length: 763
Sequence Mass (Da): 88811
Location Topology: Multi-pass membrane protein
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A0A8D5FJ44 | MGAKVKTMERRGATWTERVYLIEICKGMATTFRHFLRNLLDNSKLYVRHYPEVQPEIPVRWRGRHRLTTHEDGTVKCVACFMCQTNCPANCISIEAGERLDGKTEKMPVKFTIDLLECIYCGYCVEACPLDAIRMDTGIFSVTGYNRDSFVLSLEELLQTPGAFSEEEYKKGGA | Cofactor: Binds 2 [4Fe-4S] clusters per subunit.
Function: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.
EC: 7.1.1.-
Catalytic Activity: a quinone + 5 H(+)(in) + NADH = a quinol + 4 H(+)(out) + NAD(+)
Subcellular Location: Cell membrane
Sequence Length: 174
Sequence Mass (Da): 19832
Location Topology: Peripheral membrane protein
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A0A522RYH0 | MRVGARGQGGRVAVVQVLLWLIVLVVAVAVAWAGITYRHFTHTPLTVTRAGQTVEIAKGTGFNGIVGQLHADGVTRAPRVLWQVLAWRLRVVSKLHAGEYALVPGMLPVTLLQNMAAGRVLHRRVTLVDGWTFTQVRQALERAPKLAHALRGLPDDAVMARLGVKELAPEGEFMPDTYDYVLGMSDLDVLRRAHAAMQAFLATQWAQRDPSIPLQQPYQALILASLVEKETAVPSELPRVAGVFERRLKIGMRLDTDPSVIYGMGGAYAGTLHKADLETDTPYNTYMRNGLPPTPIALPSRAAIRAVLHPASGNALYFVAKGDGTHQFSATLAEQNAAVKKYILDKTHNR | Function: Functions as a peptidoglycan terminase that cleaves nascent peptidoglycan strands endolytically to terminate their elongation.
EC: 4.2.2.-
Subcellular Location: Cell inner membrane
Sequence Length: 350
Sequence Mass (Da): 38209
Location Topology: Single-pass membrane protein
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A0A172W3N2 | TLYLIAGAWSGMVGTGLXMIIRMELGQAGSLIGDDQVYNVVVTAHAFIMIFFMVMPILIGGFGNWLVPLMLGAXDMAFPRMNNMXFWFLIPALIMLLSXSLVENG | 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-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Catalytic Activity: 4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-[cytochrome c] + 4 H(+)(out) + 2 H2O
EC: 7.1.1.9
Subcellular Location: Mitochondrion inner membrane
Sequence Length: 105
Sequence Mass (Da): 11504
Location Topology: Multi-pass membrane protein
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