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stringlengths 6
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stringlengths 16
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stringlengths 117
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A0A316ZER3 | MSGHCSASGSGSTMPLAPQPPQPRVLIVDHHDSYTLNLLPLLLRALELDGADSTSLASHVLVLPHTHPLLAPALFATHLAPHVELLILSPGPGAPQHRRDFGAARELLRSQPSLPTLGVCLGHQGLATANGGAVRAAAAPRHGTRSVLQLVPRGDMELFEGVGEGTQVVRYNSLVVDEKTLPPCLEVTAYATDAPSSATGAPEPSTHHELSASALPTGELLCSAQPGASTSAERVILALRHRTLPQWGVQFHPESIESDGGVAMMRNFVRLGEQHWAQAARSSSEADAHLQSWQQRAPLPPHLQALAGQCVARPLVPRLLPQRKCFRILERRLNAAAVWLDSARPRNPANNFSYMSSPAFSVSYDAARRCVLLRSNCRSAASAEVPLAAPSMAEQTPAPSRTASPDFGPTLPDDVGPTFWSWLDAIHEELRSQTQAHAQPHFAAGWAGYWGYEMGGEALQGVGANADRSAGNETPPLDTHRMPDAHFGWCDAVLRFEHGTSEWVASALIEEAQAPADGAQLRSLQRALASVGLQRLGRSEAQATSWFDHMQARLDELADAAAEQAHCASTSLAPLSKLQARDSAPLYKAKVEAARQHILHGESYELCLTTQFLGTLEPLSDASHKDSDHFSLYCALRKRNPAPYAAYMLMAPPARGQRAQALLSTSPERFMSIDAAGNVEMKPIKGTLSRAGWADGEEQLRGAASAQWRVEEDERRKLRLAADAKERAENLMIVDLIRADLLSFCAPASVQVPKLMQVETYETVLQLVTTVRGRIAAGDSQQQARTGSIEALQRCFPPGSMTGAPKRRSVRILQQLEAERGAASAPCKSPRGPYAGALGWLDVGSGAASFSVIIRTVVANGDALSLGAGGAVTFLSDAAREWAEVLDKAAALGVGRAP | 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: 898
Sequence Mass (Da): 96071
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A0A1V6E4C4 | MRSVPAQQKPYPALAEVAKTQPVFELSNVTGTLVGFRAPPFVKGLNVPGYHLHFLADDRQSGGHVLSLTLESGTLELASYTLFQVQLPAAPGTLAGLDLHKDRAQELKAVEQ | Pathway: Polyol metabolism; (R,R)-butane-2,3-diol biosynthesis; (R,R)-butane-2,3-diol from pyruvate: step 2/3.
EC: 4.1.1.5
Catalytic Activity: (2S)-2-acetolactate + H(+) = (R)-acetoin + CO2
Sequence Length: 112
Sequence Mass (Da): 12063
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A0A7W4UHL4 | MFDINGGELIVLLIVAVLVIGPERLPAYAEQLGRWARRARVFLRDTKERVDEELGDEVRDVDWAALDPRRYDPRRIVREALLDDVTPGRGERPGAVAGSAAAYAARTGSTTRTPRPAADLRADEPAPFDDEAT | Function: Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes. Together with TatC, TatB is part of a receptor directly interacting with Tat signal peptides. TatB may form an oligomeric binding site that transiently accommodates folded Tat precursor proteins before their translocation.
Subcellular Location: Cell membrane
Sequence Length: 133
Sequence Mass (Da): 14681
Location Topology: Single-pass membrane protein
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A0A8K0ECP7 | MIEALQVERNNPPTQTANFPRKFFEYLFYCQCVAIVLVTGYLCTNGLFLNDESLLLNDDSNFHPKKWYLPLLTSVAISAILGLLFQWFIPKYTFDTIWAIFRVISPTSTLLLGMLLIGIGDQRGLGVGIMMLLFSFVQFFYGCHVNLGFQYAINLLSICLEFSPPGKNGLLLLSIFTGIFYSSFFVAGMGGVKATRNRVDDYIFVPVILASQFWTMQVIRNVMVVTVSRVKYMNYSRRFQLNTYDEFRNSTVKNSMGSVCIGSILVPVFGFVDASSRAVNSLADDGVDCLFCCAGCFSGLAAKLKRLGNEWGFVQVGAHNKGIIRASMDTWDLLQNNALEGLMGLIRSDLTESFCFFSGVAGGAICGLVSGGWALVVHKNYALEVSLYAFLIGYFMVRIAMAWPHACVLAYYVAYAAYPRTQAFVNDNTIPNRIAVIQRHQNAGPRVTLTQEEVDAIQNPPIPQDLTEHAPE | Function: Choline transporter.
Subcellular Location: Cell membrane
Sequence Length: 472
Sequence Mass (Da): 52528
Location Topology: Multi-pass membrane protein
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A0A1G2NFG5 | MKLIILGLGNPGEEYEGTRHNTGRMLVDVLAKKMKSADWSFDAKTKTWASVYKDKKNEIIFLKPDTFMNKSGAAVSSVISSPKKAETLIVIHDDLDLPIGTIKMSWNRGSGGHRGVESVKRAVKTEGFSRLRIGISKAAAKGGVKKPQGEKDVGDFILGKFKPLEEKALLLASKKIFSVVETFLERGRDQAIAVANTR | Function: The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis.
Catalytic Activity: an N-acyl-L-alpha-aminoacyl-tRNA + H2O = a tRNA + an N-acyl-L-amino acid + H(+)
EC: 3.1.1.29
Subcellular Location: Cytoplasm
Sequence Length: 198
Sequence Mass (Da): 21702
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A0A336LVK1 | MKLLSIKSVFSTVFIISFFLSTVLAIRCYQCSSATDMKGVDSCGAYKAFNRTQHIAIECNSDESHMPGSFCMKVVNQSPRGFIWDGRWRQVIRRCASVADTGVTGVCNWGVYENGVYWEECYCAEDSCNKGTAQIVFGPLVLALATIIYIFN | Function: Required for homeostatic regulation of sleep under normal conditions and after sleep deprivation. Important regulator of the Sh K(+) channel, acting as a signaling molecule that connects sleep drive to lowered membrane excitability, possibly by enhancing K(+) channel activity and thus reducing neuronal excitability.
Subcellular Location: Cell membrane
Sequence Length: 152
Sequence Mass (Da): 16931
Location Topology: Lipid-anchor
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A0A6H5I8Y1 | MSSGEKIEEQTHQQQQRQYNQIRQRKGEEEDADNEAKGAGGDEATTSDIDSLKDNALKDRQSGGFYFGQPLIWLNIVAISLFHVAALYCFLTFPYIQRPLTFLWAVVIAVTTSFGVGAGVHRLWTHRSYKAKTPLRIILLCCYCMAGMNPLYDWVRDHRVHHKFSETDADPHNSNRGFFFSHVGWLMMKKHPEVIRKGRQIDMSDITNDPVCAFGQKFFLPMKILFCFVLPTLVPVYCWNEDWYYAIASQVFMRYSYVLNVTWCVNSVAHMFGGRPYDKTIAPVENKLISCATGGEGWHNYHHVFPWDYKASEIGHPTIDLSTVFIQTFAKIGWAYDLKEPTADLVKSIAANKGDGTYAEVEEPMTRQ | Subcellular Location: Membrane
Sequence Length: 368
Domain: The histidine box domains are involved in binding the catalytic metal ions.
Sequence Mass (Da): 42137
Location Topology: Multi-pass membrane protein
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R6TWB4 | MKIEEKYELVLKAYQNAYAKYSKFKVGALVIVKNGVFFLGSNIENASYGLSNCAERSALFATYSNGFQKDDIEELVLIGKSNDFLYPCGACRQVICELMNLDAKVTLFRLDKKYKEIKVRDLMPFIFDESELHAK | 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: 135
Sequence Mass (Da): 15431
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A0A5K7YEP6 | MIHPTAILSPGANVADGVEIGAYSIIGDDVTIGKGTWIGPHVVIDPHVTIGPGCRIFQYAAIGAIPQDLKFGGEKSVVKIGPEVTIREFVTIHRGTETGGGITEVGEKSFLMAYTHIAHDCRVGKMVVLANNTTLAGHIVIGDHATVGGLVAIHQFVRVGDYAFVGGKSAVVKDVPPYVIAAGDRAVLHGLNRVGLKRHGFSNQALSALKKTYRILFRYGLTLNEAIERVHAEVEMVPEVETFIGFIKASSRGVTR | Pathway: Glycolipid biosynthesis; lipid IV(A) biosynthesis; lipid IV(A) from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and UDP-N-acetyl-alpha-D-glucosamine: step 1/6.
Function: Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.
Catalytic Activity: a (3R)-hydroxyacyl-[ACP] + UDP-N-acetyl-alpha-D-glucosamine = a UDP-3-O-[(3R)-3-hydroxyacyl]-N-acetyl-alpha-D-glucosamine + holo-[ACP]
EC: 2.3.1.129
Subcellular Location: Cytoplasm
Sequence Length: 256
Sequence Mass (Da): 27268
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A0A191HW39 | MIVGITGGIGTGKSFVASYIKEKGYPIVSSDEISSVLMKKGNQNYLNIVDAFGKAVLLSNGEINRKKLGQLIFSNKEDRALLNKITHPNIIEELKKQGTAHKLVFLEIPLLFEANLEYMVDEIWVVACSEDIQINRIVKRDEITQKEALLKIRSQYPLAEKKKKAHFIINTNESKKNIYKEIDQLINRLEKKNKWIL | 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: 197
Sequence Mass (Da): 22513
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A0A3A1Y7L6 | MNMSLLKKFFSFFSNLDFITLAIIIALAGYGTLMVYSATSGSIGYMDRKIVQVLLGLGVIFIVANIKYSIVQSFALPFLAFTCLLLVLTLIFGITSKGATRWLNIGIRFQPSELAKLAVPVYLSCFLGQQEGPMNWRRLIISSLAVAIPSGLVILQPDLGTTILVALSGLVVIFLAGLSWRIIIVGIIALIVIAPIFWEYGMHDYQKVRVLTILNPDADPLGAGYHVNQSKIAIGSGGITGKGILQGTQVQLNFLPEAHTDFIFSVLSEELGLVGVTVLFSLFFFLILRMFWLATIATNKVAQLLCASQGFILSIYVVVNVGMVSGLLPVVGVPLPFVSYGGTSFVSLCVTFGLVMGFYNQTQREKNSFKQSVTNKY | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Peptidoglycan polymerase that is essential for cell wall elongation.
Catalytic Activity: [GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)](n)-di-trans,octa-cis-undecaprenyl diphosphate + beta-D-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-di-trans,octa-cis-undecaprenyl diphosphate = [GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)](n+1)-di-trans-octa-cis-undecaprenyl diphosphate + di-trans,octa-cis-undecaprenyl diphosphate + H(+)
EC: 2.4.1.129
Subcellular Location: Cell inner membrane
Sequence Length: 377
Sequence Mass (Da): 41038
Location Topology: Multi-pass membrane protein
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A0A5K7YV73 | MACIVQKYGGSSLSDVDKIMQVARMIAGVKATGMDVAAVVSAMGKTTNGLVEMARSISSKPARREMDMLLSTGERITMSLLCMALNELGVASVSLTGSQCGIITNHRHNDAQVIEVRPFRVMDEMAEGKVVVVGGFQGVSYRRDITTLGRGGSDTTAVALAAAIDAERCEIYSDVDGVYSSDPSVVADARHLPEVSYPVMQEMSAAGAKVLNAQAVQFAKEKKIAIYAGSTFDRRRETVVRKLPTGQVAGVQAVVSEKEITRVRISGDRALVDFRWALDFLEGEQVPVKEVHAADVSADPLPSQVSFVVSASNIYGWKDIRDRLVQRLGASVRFDAHLSALSLIGEGLNRTNATLIEALALLENHGIVVAAATTTSFRISLLVPREKIDAGVRLCHGHWISKMS | Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 1/4.
EC: 2.7.2.4
Catalytic Activity: ATP + L-aspartate = 4-phospho-L-aspartate + ADP
Sequence Length: 404
Sequence Mass (Da): 43404
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A0A0S7C082 | MNNPRLSIRYAQALLDLSVERGEVEAARKDMELLLRVCNENAGLKQMLSSPVINADKKISVMRALFSEKISKLSMAFINLIIRKRRESLLYQIAGKFGELYLEYKNIKTARITSAVPLQEEVRSELVSLLEEQTGSQIRLTEVVDAEIIGGLIVKIENSLFDDSIRKKLQNLRKEFSVNVYTREI | 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: 185
Sequence Mass (Da): 21132
Location Topology: Peripheral membrane protein
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A0A336MXA4 | MPVVPDTQDEELVKLRELFDEVRSLLDDKPNDEEPNERSEDATSTQGDNNTQSNGDNEVRTGNDTTTPPTDNEAEHNSSDNVSPEISGASTEYHSSNSLANSSSESLRSTVQNSPTGSIDYGPEESDDDNGEALDDNGDVSDDSAATVEYLPSDSMLRFSIQETSGSDLQIGLIEQNESSIQSDTNAQDESVQSNAQNVETVDNDSDIEEIVQPVPLIVIDSTIDNEPHEPLNANSSSNVTQDDDVVFVQQVRNDNPIVIDLSNTLDDGFAVPSSSTPLIPSRRRRRNQEPIDIEDGPTPPQRPRIPNIFENLYQEIQIRFGPSNPTPQMSFPKTPVPSTSTTSHDDESLNSTQSEPIDFKCAICLSNPRNRQPVSTFCGHIYCKSCIEACIQSTHKCPLCKKPLTMKKIHRLFF | Pathway: Protein modification; protein ubiquitination.
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
EC: 2.3.2.27
Subcellular Location: Nucleus
Sequence Length: 415
Sequence Mass (Da): 45687
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A0A2H9L8T3 | MKLIFLGTSGSIPTAQRGLPAIALRRDRELLLFDCSEGTQRQMALAGLSPMRLKAIFITHLHGDHFLGLVGLVQTMSLMDRKEKLEVYCPPEGKERIENFLRVPYYTLTFEVHVKELKPGDELRRSGYSIKTCGVDHPVPALAYALLEDQRPGKFYPQKALALGVKAGPDFSRLQSGKSVKLRDGRVVKPEQVIGPPQSGRKIVYAGDTRPCKSIIKFSEGADVLIHDCTLADELAERAAETGHSTPAGAAEIAKRAEVKQLVLVHISPRYKEDSVLLKQAKQIFSNVKVAKDLMELEVKLQGAQK | Cofactor: Binds 2 Zn(2+) ions.
Function: Zinc phosphodiesterase, which displays some tRNA 3'-processing endonuclease activity. Probably involved in tRNA maturation, by removing a 3'-trailer from precursor tRNA.
EC: 3.1.26.11
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.
Sequence Length: 306
Sequence Mass (Da): 33835
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R6Z8Z7 | MSKFIIQGGKELAGEVRISGSKNAALPIIAATVLVKGKITLYNVPNIQDVQTMFEIIRDIGGKVTKKNNKMIIDTSKINTYEIPENLMRKMRSSVILAGAIIGKYNKANFSYPGGCEIGSRPIDLHLKGFEKLGINIKEEYGEIICNAEKIEGTQIHLDFPSVGATENIILAACLAEGTTILTNAAKEPEIEDMVKFLNKAGAKIRGAGTDRVEIIGVKKLFEISYNIMPDRIEAGTYLVAGAITGGNVKIINANPNHIEPILDKLEEANCMLKIGKNCIELKAPKRIKAVDIKTMPYPGFPTDMQSIFGALLSTAKGTSIITENIFENRFKYIQELNRMGAKINVEGRTAIIKGAKRIQGTNVVASDLRGGAALVIEALTAKGITQIENIHYILRGYEDIVEKLKSLGAKIFVEE | 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: 416
Sequence Mass (Da): 45377
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A0A8E6B7Z0 | MQGQIVQRPVADGRLRDYDSALEEYEGGSSDDQDQSPSRYLTVLWRRKWILAIAGLLGLVIGFVYTFEKPRIYQSSAQVMLSRKKQPTMTEGTGPLADTRTAYLDDYVTTQLLLLKSDLILRNAAKNFEKFSLPGAASVDSAVGMLGGGLGALRDKDTAGRGGNVVMLTFRSSSQEYCARYLESIISSYQEFLQDKFDAATNIEIKQIEKTLKDMDSEIKHGEEELVEKARTEKNVFEENPEDLKKRISNAKERIDALEVRQASIAKKLALIAEFRAKDSPPKDRPLLLAQLSIQAPGTNPNGGTNNGNNSISALDALIRSTELEVGRMQSDLDYKMVPLGNNHPEALSMKSRLNFLKNQLLKMKEANGGNGGIEQDVIEFQNQLLDAEKGSNEVDLKTLKDKLERDTKLAQTVGLYTSLQTNLDEKKKRYLARKEDLERTKRNLEATKNSGGYEMTLLQPPEKSPVYKVEPNMFTGTVLGGFLGLLIGIALAALAEVTDRTFHTPDEIRTKLGVPVIAHIPTLESNLQLGTSSSQGSNGQPIADPSIICYHTPKSRSAESIRGLRTSIYFSLLGRGHQVIQVTSPNPADGKSTLISNLAVSIAQSGKKIVLIDADMRKPRIHKLFPSVSAEFGLSSVVIGEKTIKEAIQPTGIENLSILPVGQRPSNPAELLSSPAFRLVLEEIRKEYDFILIDTPPLLAVSDPAVVASCVDGLLLVIRIRPNIRPAAERARTMLRTLGVKLLGVVVNSLDDKGAQYGYGYSYGYGYNYGYGYKYAYNYDYEYADKYNLDDVIDLPAINDSPKKG | Catalytic Activity: ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]
Subcellular Location: Cell inner membrane
Sequence Length: 806
Sequence Mass (Da): 88918
Location Topology: Multi-pass membrane protein
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D3EMX8 | MQNNYMQQNIDNMLKIGTIVGPRGLKGELKVLSSTDFPERFEISEEHWISDPNKSTLQSVKLISSRYVMEKNIYIVRLQGIETRNQAELLRNYKLFISNHSIPELKKDEYHISQLINLEVYHQKTKKLIGIVTDVFTTGHDLLEIELENPSLPESDKKQKFLVPFVYEIVPIVDLVNRRIELNPPKGLLDLSIVK | Function: An accessory protein needed during the final step in the assembly of 30S ribosomal subunit, possibly for assembly of the head region. Essential for efficient processing of 16S rRNA. May be needed both before and after RbfA during the maturation of 16S rRNA. It has affinity for free ribosomal 30S subunits but not for 70S ribosomes.
Subcellular Location: Cytoplasm
Sequence Length: 195
Domain: The PRC barrel domain binds ribosomal protein uS19.
Sequence Mass (Da): 22629
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A0A6P2AP84 | MLSFKNPYTFPITLWALSRLWVLLGLLGIAPLLPAPPGGEQALFHWSAFAGWDGFFYENIATTGYSYVADGQGHNVAFFPMLPLLIRGGMALGLPFEVAGVLITNSAFLISLILLYQWLRERQGEEVARWGAIALAWCPFSLFSTVIYTEALFLVFSIAALAAFDRGHHWQAALWGACTTATRLPGLAIVPALLIIAWRERRGIGAYLAALSTGVGAALYSLFCWFEFGEPLAFLKVQKAWNVPDHFYGQGWLIMLGEVFLGPANMGESGFQDPLYPLAVLVLMGLAIWVGRSPFRGRVYVGGALFVIAWLMAGDSLLNICMILGSMVLLWRYRREIPAIALVYGIFSFIGILSSGRTASLERYSYGIVTVAIAIGIWLHHHPKLARFVVSFSGLMLLLYSIRFAQSLWVA | Pathway: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor biosynthesis.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 411
Sequence Mass (Da): 45371
Location Topology: Multi-pass membrane protein
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E6SHZ8 | MTYRIAVLPGDGIGPEVTREAVRVLEAVGAAAGIRFEFAEAPVGGAAVDATGDPFPPETEQLCMAADAILLGAVGGPRWDREPVPRRPESGLLRLRKAVGAYANLRPVRVHPALAGRGPLRPEVVGGGVDILIVRELTGGLYYGERGVQQEPFGERAYDTMVYTTPEIERIVRMAFQLARGRRRRVISVDKSNVLETSRLWRRVTEAVAEDFPDVELEHMLVDNAAMQLVRNPQRFDVLVTENTFGDILSDLGAALAGSLGLLPSASLGLPGRPPLFEPVHGSAPDIAGRGIANPLGAIASAAMMLRHAFGLQREAQAVEEAIDDLLAAGPWTPDIAPPGAPVASTEDVGRAIARRVRERLAPGPLEPLGPVAGRDGRGTQDGRGSQDGSGLAGDPVAAVWIAGEYGFRPLPPDEPAPPAAAPAATGTVRAGDPATGASRDAMTPDALANGPTAAGGTAADTATGTNGTATRSESPVRTPARRGTGAGTTRRRARARKGA | Cofactor: Binds 1 Mg(2+) or Mn(2+) ion per subunit.
Pathway: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 3/4.
Function: Catalyzes the oxidation of 3-carboxy-2-hydroxy-4-methylpentanoate (3-isopropylmalate) to 3-carboxy-4-methyl-2-oxopentanoate. The product decarboxylates to 4-methyl-2 oxopentanoate.
EC: 1.1.1.85
Subcellular Location: Cytoplasm
Catalytic Activity: (2R,3S)-3-isopropylmalate + NAD(+) = 4-methyl-2-oxopentanoate + CO2 + NADH
Sequence Length: 500
Sequence Mass (Da): 52069
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I1T0W1 | SGXIGSSMSIIIRXELSNPGFLINNDQIYNSIITTHAFIMIFFMVMPIMIGGFGNWLIPLMMGAPDMAFPRMNNMSFWLLPPSLMFLIWSNIINQGVGTGWTIYPPLSLNNNHEGPS | 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: 117
Sequence Mass (Da): 13061
Location Topology: Multi-pass membrane protein
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A0A832RN25 | MLNVIELKQQNLINIMKAKGFLKEWKVERAIRITPRHIFVPTEYIEHAYEDRPLPTKSLQTISQPSVVAKMTQLLDVQENNKILEIGCGSGWQSAILSKLTNGKVFSIERIPEIVEFAKKNHRTAYIQNVEILQGDGTLGLPVSAPFDRIIVTAACKTVPEPLLAQLNDGGILVAPVGEIFSQDVVVIQKLGGKFKEIKRESGFIFAPLIGKFGF | Function: Catalyzes the methyl esterification of L-isoaspartyl residues in peptides and proteins that result from spontaneous decomposition of normal L-aspartyl and L-asparaginyl residues. It plays a role in the repair and/or degradation of damaged proteins.
Catalytic Activity: [protein]-L-isoaspartate + S-adenosyl-L-methionine = [protein]-L-isoaspartate alpha-methyl ester + S-adenosyl-L-homocysteine
EC: 2.1.1.77
Subcellular Location: Cytoplasm
Sequence Length: 215
Sequence Mass (Da): 23936
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T2IHI9 | MAETAIQLSQKAYPQVRERDSFIKAELEREEATFLKTLERGEKLLAEIISKTEKQGQISGVDAFTLYDTFGFPLELTQEIAEESNLTVDIEGFEVEMKQQQERSKAAHETIDLTVQGSLDKLAEHIHPTEFLGYTDLQSTAKVEAVLIEGKSVETATAGTEIQIVLDKTPFYGESGGQIGDRGFLTGEDLVIRVDDVQKESGIFVHFCRVERGQVSVNEHLKATIDRSCRRRVQANHTATHLLQAALKKVVDDSISQAGSLVDFDRLRFDFNCLRAVTSEELQEIEDLINTWIAEAHDTEIEVMPIETAKEKGAIAMFGEKYGAEVRVIDVPGVSMELCGGTHVRNTAEIGLFKIMSESGISSGVRRIEAVAGPAVLEYLKVRETVVKDLCDRFKIKPEEISDRITTLQSELKTTQKELEGVKQELAIAKSDQLLNEAESIGEFKLLVSDMGEMDAKALQTAAERLQQKLGEGAVILGSIPSEEKVSLVAAFSKKVNKEKQLQAGKFIGQIAKICGGGGGGRPNLAQAGGRDPSKLSEALSTAKQQLKEGLQ | 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: 552
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): 60583
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A0A2D5YRM4 | MVFILNDLEITLSEEQTENTPEVLDNTSSNQETKTKEKPKAWTKEWFLYETWSWIYIFFIVFGFRSTFIDHYHIPSGSLLPTNAIGDSIVVNKMSYGFKVPFSEFFGTYSDWLGLDKRWEPIYFGEQEVPERGDIIVFEFPRDKSILFVKRTIGIPGDVIEIFDNDLYINGKKIEREVVKDDAKYRELYDPKPGFDPEQMVFYRQKIGDKEFITGQDSRKKADPPQKYIVPEGHVFVLGDNRDFSADSRYWGTVPLELVRGKAFFVWMSLVYPWSQEPFHFRPSRIGTRI | 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: 290
Sequence Mass (Da): 34119
Location Topology: Single-pass type II membrane protein
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A0A0J1FPU1 | MRGDIIVHGGNLRKAQENYGLHDFIDLSANINPFGPPQGVWESLNESLKEIVSYPDPECLALRTALASHLELPLEEIMVGNGAGELIFTIVNALKPRKVAIPLPTFSEYERAARSVGAEVCYITLGAEGWNGCHLTKEQWAETLKDCDLLFLCSPHNPTGSVLQRDSFAQILKLCAEMDCKILFDESFFDFLPPGQYTSARSYLRTYKHLIVLYSLTKFYSIPGLRLGAAFADRSLLTQFEGFRDPWSVNVLAQKAGISALKDQKYSDEVRNKIEASRSYFYHEFEAACFNYLRIYPSAVNFALLKVLDSSISELIPYLGKRGILVRDCRNFSGLQGDFMRVAIKDIPAMQNLIEALKGFYL | Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis.
Function: Decarboxylates L-threonine-O-3-phosphate to yield (R)-1-amino-2-propanol O-2-phosphate, the precursor for the linkage between the nucleotide loop and the corrin ring in cobalamin.
EC: 4.1.1.81
Catalytic Activity: H(+) + O-phospho-L-threonine = (R)-1-aminopropan-2-yl phosphate + CO2
Sequence Length: 362
Sequence Mass (Da): 40694
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A0A1M5HJI9 | MSDLDTRTGAGAGNDTGDHAGDHVGNDGGQRRWRAAMMNNYGTPQLTLVRGEGAHVWDADGNRYLDLLSGIAVNALGHGHPAVVAAVTDQLGRLGHVSNFFVAEPTLELAETLLDLAGLHGEAKVLFCNSGAEAVEAAFKIARRTGRPKVVAAEGGFHGRTMGALALTGQPAKRAPFEPLTPGVVHVPYGDADALESVVDGETAAVVLEPVQGENGVLVPPDGYLQRAREITSRHGALLVLDEVQTGIGRTGTWFAFQHAGIVPDVITLAKGIGGGLPLGVCVGVGRAGELLEPGQHGTTFGGNPVCCAAGLAVLRTIRDEGLLDHVSRLGKEIANGVEELGHPLVAGVRGVGLLLGVMLRHPVSAAVAAHARKAGYLLNNVQPDALRLAPPLVLTEADVHQFLADLPAVLDAALPSSSSEATS | Cofactor: Binds 1 pyridoxal phosphate per subunit.
Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 4/4.
Catalytic Activity: 2-oxoglutarate + N(2)-acetyl-L-ornithine = L-glutamate + N-acetyl-L-glutamate 5-semialdehyde
EC: 2.6.1.11
Subcellular Location: Cytoplasm
Sequence Length: 424
Sequence Mass (Da): 43722
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A0A963PWZ7 | TAVLREALAANAGATGPLAALAALGGFEIATMVGSVLQAASERRVVVVDGFIASAAVLVASRIAPPVLQRCVFAHRSGERGHARMLQLLGAEPLVDLGLRVGEGSGAALAWPLLVSACAILNEMASFESAGVSDKG | Pathway: Nucleoside biosynthesis; alpha-ribazole biosynthesis; alpha-ribazole from 5,6-dimethylbenzimidazole: step 1/2.
EC: 2.4.2.21
Catalytic Activity: 5,6-dimethylbenzimidazole + nicotinate beta-D-ribonucleotide = alpha-ribazole 5'-phosphate + H(+) + nicotinate
Sequence Length: 136
Sequence Mass (Da): 13674
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A0A1H8E142 | MKAGVRIGIYGGAFDPPHNAHLGLARAAVEQLELDILYVIPTGQPWMKQRRLTAAEHRLAMARLAFESVPEVRVDDCEVQREGTTYTIDTLHELQQRHAVQGDTEITWYLVMGQDLLHSLPQWQRAEELLRSVTVAVLQRPDAEQTAVEQELAQVRAQLPELRTVQLHLPASDASSTRIRAGMQQRMSDNSANRLAWLQSLVPPSVAQYIERHQLYGTSTPDGH | 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 = deamido-NAD(+) + diphosphate
Sequence Length: 224
Sequence Mass (Da): 25212
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A0A1F3SQ30 | MSSLNSMKRQSCVFKARVLHEEKNCYEVKIESEVVRAVVSGKMRHDALVPSQLPAVGDYVMCTYEPHNSLARIEEVLPRSTHLTRKVAGDAYSEQILASNLQVVFYLTSLNMDLNLRRLERYLIMIRDGKITPVVLLSKADLVDAQTIEQAVKDVKAVAPSVEVYAISSQHTASMDELKKYFVPEATVAFLGSSGVGKSTLTNFYLGREVQTTQEIGEERDKGRHTTTSRSLFFLANGCAIIDTPGIREIQLWEGDSTGVDELFADILDLQGRCQYSNCGHQHEPGCQVQLAIEEGRLDRARLKSFLKLAREQSYMQLKLNATTRRQQKEIWKKRGRTYRRGRKAEWNLQG | 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: 351
Sequence Mass (Da): 39733
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A0A6N8UA04 | MMKMKPLNGSGCILSKEQPKICVPLTPSDEKELKQQLEMIHRQSADIDLIEWRADYWQGELKDGLSAVSNQLQNIHKPVIFTIRTAAEGGEKDIALSEYEHMIRMSLKFPCFMMYDLQLMLVKQKADRMRMLLDDLHRHNKWIILSYHDFQATPSNEQMLAILNEQEALGADLVKLAVMPQTEMDVKRLMEVSSLFTQTHETMAITISMGELGVKSRIQLKETGSCISFATASAASAPGQLPASSLRKLLQTQ | Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7.
Function: Involved in the third step of the chorismate pathway, which leads to the biosynthesis of aromatic amino acids. Catalyzes the cis-dehydration of 3-dehydroquinate (DHQ) and introduces the first double bond of the aromatic ring to yield 3-dehydroshikimate.
EC: 4.2.1.10
Catalytic Activity: 3-dehydroquinate = 3-dehydroshikimate + H2O
Sequence Length: 253
Sequence Mass (Da): 28623
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A0A317CBL6 | MTVYDKNKARLSFDRAAHRYDQSAKLQQQVANHLIELVKQQKTTAAVTLDIGCGTGQVTEAMCELFPQGDVLGLDFSRRMLAQTKTRLALKGFAAELICADADHPPFISNSFDLIVSSLMLQWSNNLGSTLKSYQSMLKDDGKMIFNTFTDGTLTEVKQSWRAVDEQAHTSQFLTKQDLHSIVESAGFSHVEILYDTITMTYPSVREMITEMKQIGASNAHKNRERGLTGKQRFNSFEQAFEDFRQQNGQYPCTWKLAYVICNK | Pathway: Cofactor biosynthesis; biotin biosynthesis.
Function: Converts the free carboxyl group of a malonyl-thioester to its methyl ester by transfer of a methyl group from S-adenosyl-L-methionine (SAM). It allows to synthesize pimeloyl-ACP via the fatty acid synthetic pathway.
EC: 2.1.1.197
Catalytic Activity: malonyl-[ACP] + S-adenosyl-L-methionine = malonyl-[ACP] methyl ester + S-adenosyl-L-homocysteine
Sequence Length: 264
Sequence Mass (Da): 29872
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A0A923ZU02 | MPFIQRFFLYCLLLLTLWSCNHDSTPSNPLKELSFLVVGDWGRNGTQNQQEVANQMNRTALKENAQFVISTGDNFYESGVKNVTDSQWETSFEKVYAGIGLQKDWLVALGNHDYQGNPQAQIDYSLKSSRWKMPARYFTLVKTVDEMTKVRLVFIDSNPFVKEYLKNPKAYSDIANQDTQKQLVWLDSVLTNAKEKWKIVIGHHPIYSAGFGHGNQDELISQIKPILEKNHVQMYFCGHSHSSQYLKRPDSSVDYVVAGAGSSTVELVKQESSVLFGTITPSFTLISLSNNLLRTTFVDSTGQILFNTQRGF | Cofactor: Binds 2 iron ions per subunit.
EC: 3.1.3.2
Catalytic Activity: a phosphate monoester + H2O = an alcohol + phosphate
Sequence Length: 312
Sequence Mass (Da): 35401
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A0A916JSZ2 | MPHRLSRLLSEIYWLLQVSFALFLLMTLISYSKSDPSWTHAVHVDYQIVNWGGRVGAWISDILLLLFGLSAYWCVVLLAQHIVANYQCIARHDELDKPAAPLREGGWLAEILSFILVLVASDGLEALRMWSLKAQLPQAPGGIVGNAVAYGVQHTLGFTSGTLALLLMQAIGLSLFFRFSWLSVADRVGDAIINVVVLLQLWCAKKRAYKVNRKEEVNQGGKIERSQMRIEERESVTSRPAIAMLTQSKCIENEGKATLFQEHTGNNLLPPLTLLDPSPDTREAVSANTLESNSRLIEKKLKDFGVQVSVVGAYPGPVITRYEIEPEIGVKGNQIVSLAKDLSRALSLASIRVVETIPGKNYMGLELPNQSRQIVRLIDIVSSKDYINALSPLTIGLGKDTGGNPICADLNKMPHLLVAGTTGSGKSVGISAMILSILYKASSDQVRLIMIDPKMLELSVYEGIPHLLCPVVTDMRQAGHALSWVVGEMERRYKLMSKIGGRNLASYNSKIDDLKKNSRRIPSPFSLIRDKSELLETLPFIVVIIDELADLMMVVGKKAEELIARIAQKARASGIHLVLATQRPSVDVITGLIKANIPTRIAFQVSSKIDSRTILDQMGAESLLGQGDMLYLTPGSRLPTRVHSAFVSDDEVYRVVKKLKELGELNYIDGILEGKIDSEGNTLHD | Function: Essential cell division protein that coordinates cell division and chromosome segregation. The N-terminus is involved in assembly of the cell-division machinery. The C-terminus functions as a DNA motor that moves dsDNA in an ATP-dependent manner towards the dif recombination site, which is located within the replication terminus region. Translocation stops specifically at Xer-dif sites, where FtsK interacts with the Xer recombinase, allowing activation of chromosome unlinking by recombination. FtsK orienting polar sequences (KOPS) guide the direction of DNA translocation. FtsK can remove proteins from DNA as it translocates, but translocation stops specifically at XerCD-dif site, thereby preventing removal of XerC and XerD from dif.
Subcellular Location: Membrane
Sequence Length: 685
Sequence Mass (Da): 75428
Location Topology: Multi-pass membrane protein
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A0A317C6S9 | MQLLTPEQIQQASAAVNSLTPAQMVWVSGYLQGLSSNAAPDIGGLTLSPATAAAPAPAVSEKVTVLYGSQTGNSRKIAEKLHAALESRGQQATLQNMLNYRGSQLKKEENLIAVVSTHGNGEPPDEALGFFKFVNGAKAPKLDHMKFSVLALGDSSYDEFCQTGYELDARLSELGASRLSDVVACDVDYADDAAEWNDTILKLLEPSSAAVPSIDFGGQPAAASATETQYDEQNPFQAEVLDKLVLTDEGSDKSVLHLELSLEDSGLTYEPGDIVAIQSANQVELVDAIIAELSLDANEQVTIKKNTLTLREALLNKRELTHITRKQLQVYAEQSDNAELLALAQDKSQLTEEIEAADVLDVLQLWPAKLNAQALTDWLRPLSARQYSIASSEAASPEEVHVLVKHVEYDYRGRKHGGVCSSQLAASDSGETLGVSIKPNSSFKLPENEDTQVIMIGAGTGVAPFRSFLFDREAKGLEGNTWLFFGEQKFQTDFLYQTEWQQFIKSGVLEKMSVAFSRDQAEKVYVQHRILEEAEAVYQWLESGAHLYICGDMHHMAKDVHQALIDVIVQQSGRNAEEASDWLDQLIAEKRYQRDVY | Cofactor: Binds 1 FAD per subunit.
Pathway: Sulfur metabolism; hydrogen sulfide biosynthesis; hydrogen sulfide from sulfite (NADPH route): step 1/1.
Function: Component of the sulfite reductase complex that catalyzes the 6-electron reduction of sulfite to sulfide. This is one of several activities required for the biosynthesis of L-cysteine from sulfate. The flavoprotein component catalyzes the electron flow from NADPH -> FAD -> FMN to the hemoprotein component.
EC: 1.8.1.2
Catalytic Activity: 3 H2O + hydrogen sulfide + 3 NADP(+) = 4 H(+) + 3 NADPH + sulfite
Sequence Length: 597
Sequence Mass (Da): 65500
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A0A545V4D0 | MALRTTTRQLCQTLPRSSTGLRQIAVQRRHLATTSGHPVTQNAAGSKGPTAMVFLNMGGPSTTAEVGDFLSRLFSDGDLIPLGRLQSYIGPLLSARRTPKIQKQYDAIGGGSPIREWSEHQCAEMCKILDKTSPETAPHKPYVAFRYANPLTEDMYKQMLKDGFGGGKGGRAVAFTQYPQYSCSTTGSSINELWKWRHRLEGNTRAETEGAISWSVIDRWPVHPGLAKAFALNIQAKLAEYPEERRKDVVLLFSAHSLPMSVVNRGDPYPGEVAATVYAVMQQLNFSNPYRICWQSQVGPSAWLGPQTSDTVSNYIARGQTDMILVPIAFTSDHIETLYELDEEVIGESGHKDTVKRAESLNGSRVFIEALADIAKQHLHSGDACSKQMLLRCPGFAQPANATDSYRSMLDVDDPPKLPCSSMSLDELHPGSMASTKSDSDGGRSDLTAVATSASINQDQISTQICQELPIANAHTLSYSTNGSGSPPSMAPASPANGKLDLPADFGKGDNRSNPVSVDVPISAPVQDTRNIVRRKLTGYVGFANLPNQWHRKSVRKGFNFNVMVVGESGLGKSTLVNTLFNTSLYPPKERKGPSLDIIPKTVTIQSISADIEEAGVRLRLTVVDTPGFGDFVNNDESWRPITDNIDQRYDAYLDAENKVNRMNIVDNRIHACVFFIQPTGHSLKPLDIEVMRRLHTKVNLIPVIAKSDTLTDEEIASFKARILSDIKHHGIQIFEGPRYELDDEETIAENNEIMSKVPFAVVGATNEIKTPDGRAVRGRQYPWGIIEVDNEEHCDFVKLRQMLIRTHMEELKEHTNNTLYENYRTDKLIAMGVSQDPSVFKEVNPAVKQEEERALHEQKLAKMEAEMKMVFQQKVQEKESKLKQSEEELYARHREMKEQLDRQRLELEDKKQRIESGRPLEKEGKRKGFSLR | Pathway: Porphyrin-containing compound metabolism; protoheme biosynthesis; protoheme from protoporphyrin-IX: step 1/1.
EC: 4.98.1.1
Catalytic Activity: 2 H(+) + heme b = Fe(2+) + protoporphyrin IX
Sequence Length: 933
Sequence Mass (Da): 104037
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A0A1F8TAA4 | MVATAFTIGAAQEQARQALKGMSDSPGQQAQLILADLLDRPRAWILAHPEFILGEADKRSFGVALARLTNGEPLPYVLGWWEFYGRRFRLAPSVLIPRPESELLVEKALERLKLTPPPVKIVDVGTGSGCLGVTLAAEVPDIRLAVTDVSLETLHVARRNAREYGVDGRISFVQADLLEPLAGPFDLVVANLPYVPSSALRGMPAGRREPGLALDGGRDGLELTGRLLHSLPGKLSPTGAAFLEIGADQGTAVQSAAKAALPDADVQITRDLAGHDRVIEIRCGAHA | 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 factor] + S-adenosyl-L-homocysteine
Sequence Length: 287
Sequence Mass (Da): 30606
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A0A4W4F8I0 | MLQQIEEPCSLGAHAAVIVPPTWIIRVRRPQSSLKSSKKKKRTSFKRKLSKKGAEEARWKPFIVRPIPSQLMKPLLVFVNPKSGGNQGTKIIQSFMWYLNPRQVFDLSQGGPKEGLEMYRKVHNLRILACGGDGTVGWILSTLDQLQLNPQPAVAVLPLGTGNDLARTLNWGGGYTDEPICKILSHVEDGNIVQLDRWNLHVESNPEAGLEEKDEQVTDKLPLDVFNNYFSLGFDAHVTLEFHESREANPEKFNSRFRNKMFYAGTAFSDFLMGSSKDLAKHIKVVCDGADLTSKVQELKLQCLVFLNIPRYCAGTMPWGNPSEHYDFEPQRHDDGCIEVIGFTMTSLATLQVGGHGERLNQCHEVTLTTYKSIPMQVDGEPCKLAPSTIHISLRNQANMVQKTKRRTSIPLLNDQQPFPERLRIRVNRISMHDYETLHYHKEKLKEACESIPLGLIVVPGDSDLETCRVHIERLQEVQWEGWGDENKSKMLSSQRLSPKWCFLDCNTSPGVPDLLDSSDISASQLMSHSTFSAHSSCFFSLDCSDLFAWLAKLSGHAFISCSGETVLHKAASLCQRTICHYLVEAGASLMKTDLQGDTPKHRAEKAKDPELAAYLENRQHYQMIQREDQETAV | Pathway: Lipid metabolism; glycerolipid metabolism.
EC: 2.7.1.107
Catalytic Activity: 1,2-di-(9Z-octadecenoyl)-sn-glycerol + ATP = 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphate + ADP + H(+)
Sequence Length: 634
Sequence Mass (Da): 71430
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A0A924MMJ7 | MTTLNELSIQTPDDWHLHLRDGAAMAAVVPFTARQFGRPIIMPHLRPPL | Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 3/3.
Function: Catalyzes the reversible cyclization of carbamoyl aspartate to dihydroorotate.
EC: 3.5.2.3
Sequence Length: 49
Sequence Mass (Da): 5533
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A0A6H5IFD8 | MGGGVGLSVHGKYRVATEKTVFAMPETAIGLFPDVGGSYFLSRLKGKLGLFFGLTGYRLKGADVAFAGVATHYTTSDKLESLTQELTSRSTEVDQILEPYLPKNLNHQFCLAPYLDVIDECFSAPTVEEIISKLNYLIGTYQVPYMSIMDGITMGGGVGLSVHGKYRVATDRTLFAMPENLIGLFPDVGSSYFLPRLSGKLGLFLGLTGYRLKGADVLHAGIATHYVPSEIIDQVAHDIILNNTRVEDILKPYSTADNQEYSLSPHLKTINDCFSPSTVEGIIERLADEKSEWAKNVIETLSKLSPTSLKVTKKAFDEGIKKNLAECLSTEYRLVWACLNRNSDFYEGVRARLIDKDQTPKWNPKVLRKVTNEQIEKRFQFLSPRDELALP | Pathway: Amino-acid degradation; L-valine degradation.
Function: Hydrolyzes 3-hydroxyisobutyryl-CoA (HIBYL-CoA), a saline catabolite. Has high activity toward isobutyryl-CoA. Could be an isobutyryl-CoA dehydrogenase that functions in valine catabolism. Also hydrolyzes 3-hydroxypropanoyl-CoA.
EC: 3.1.2.4
Catalytic Activity: 3-hydroxy-2-methylpropanoyl-CoA + H2O = 3-hydroxy-2-methylpropanoate + CoA + H(+)
Sequence Length: 391
Sequence Mass (Da): 43408
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A0A4W4HHH9 | FLLHASYLYDLRTVFSEYFKELEEESIRDNFVIIYELLDELMDFGYPQTTDSKILQEYITQEGHKLDTGAPRPPATVTNAVSWRSEGIKYRKNEVFLDVIESVNLLVSANGNVLRSEIVGSIKMRVFLSGMPELRLGLNDKVLFENTGRGKSKSVELEDVKFHQCVRLSRFENDRTISFIPPDGEFELMSYRLNTHVKPLIWIESVIEKHSHSRIEYMIKAKSQFKRRSTANNVEIHIPVPTDADSPKFKTTVGSVKWVPENSEIVWSIKSFPGGKEYLMRAHFGLPSVEAEDKEGKPPISVKFEIPYFTTSGIQVRYLKIIEKSGYQALPWVRYITQNGDYQLRTQ | Function: Subunit of clathrin-associated adaptor protein complex 1 that plays a role in protein sorting in the trans-Golgi network (TGN) and endosomes. The AP complexes mediate the recruitment of clathrin to membranes and the recognition of sorting signals within the cytosolic tails of transmembrane cargo molecules.
Subcellular Location: Golgi apparatus
Sequence Length: 347
Sequence Mass (Da): 40045
Location Topology: Peripheral membrane protein
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A0A6H5JAQ3 | MEVCYYKTNSYLQETQDLLSHLEKSSNLSAEDREEIEQKIKEKFEKINSNFDQLDILASKVPLTMRQSAKMKVDQLKYDARHLSAAFDSWKYMNFQRQREASEREELLSRQFTTNDHVDIMIDHVVQHNTSVRNAVNGVDNMLEHGSDILDNLRSQRTTLRGAHKRLIDIGNTVGLSNTTMRLIEQRVRSDSFVFFGGIFVTILVLFIVVYYFL | Function: Involved in transport of proteins from the cis/medial-Golgi to the trans-Golgi network.
Subcellular Location: Membrane
Sequence Length: 214
Sequence Mass (Da): 24975
Location Topology: Single-pass type IV membrane protein
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A0A4V3D5Y4 | MCKQNRMKRLTNDRGFTLVEMLIVLVIISVLIVLTVANLSKNKSVAEGKECEALKTVIGNQMEVYEIDIGEPAADITVLMDGGYIQSNTCSNGTIYTIQDGSVVGGETSSG | Function: Required for transformation and DNA binding.
Subcellular Location: Cell membrane
Sequence Length: 111
Sequence Mass (Da): 11917
Location Topology: Single-pass membrane protein
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A0A7Y4ZCP4 | MSKKAIILLSGGLDSITVLALAQQQGFDCYALSFDYGQRHNAELKAASEIAKAYQVKEHKIVKLGLGSIGGSALTDENIQVPDTLQVGIPVTYVPARNTIFLAFALGWAEVLKTRDIFIGVNAVDYSGYPDCRPEFIKAFQQLADLATKAGAEGEHFTIHTPLISLSKAEIIKLGIKLGVDYTPTVSCYSADDQGRACGICDACRLRKLGFTASDIPDPTRYQPEQSHLDYPNGRGQYQSQ | Cofactor: Binds 1 zinc ion per subunit.
Pathway: Purine metabolism; 7-cyano-7-deazaguanine biosynthesis.
Function: Catalyzes the ATP-dependent conversion of 7-carboxy-7-deazaguanine (CDG) to 7-cyano-7-deazaguanine (preQ(0)).
EC: 6.3.4.20
Catalytic Activity: 7-carboxy-7-deazaguanine + ATP + NH4(+) = 7-cyano-7-deazaguanine + ADP + H(+) + H2O + phosphate
Sequence Length: 241
Sequence Mass (Da): 26191
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D3ENU4 | MIYPRKRFGQHWLKDNTVLERIIKSAHLTKIDKVLEIGPGTGILTSRLLPEVSSVTAIEVDRDLYEQLVKKFHYCKNLLLLQEDILKIDLFTEISNYNLFWPMNKVVANIPYNITNPILEKLLGSVSEPYNLPYEIIVLLVQKEVAKRITALPGNKMYGALSAKIQYLAHCNYICDVPSKAFYPAPKVDSAIITLRPHILDSSVLNRPHLEKLINLGFSSRRKMLHNNLKSIMDIKYITEFLEKNNLDLKVRAENLSINQWIELSNYLYLLKSK | 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: 274
Sequence Mass (Da): 31650
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A0A943CD30 | MYQALYRKYRSQTFGQLVGQQVVARTLRQAVEQDKISHAYLFSGPRGTGKTSVAKIFAKAMNCPNQVNGEPCNDCYICESITNGSLEDVIEIDAASNNGVDEIRDIRDKSTYAPSLAKHKVYIIDEVHMLSTGAFNALLKTLEEPTENVVFILATTELHKIPATILSRVQRFEFKSIKLPDIVHHLESILATEGIAYEADAVQIIARRAEGGMRDALSILDQALSLTAGSELTTAIAEEITGSISLAALDQYVAAILAHDATAALDQLAIIFDNGKNMARFVTDLLQYLRDLLIVQTGGENTHASDLFAANLEVDQARLFALIDQATTSLADIKNSLQPRIYTEMMTIKLAESTGQATNSVAVEVPSNVLAQLEDLKKEVAQLKQQLAQSGSGLPASKPTVTRPTKSSKGYRA | 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: 413
Sequence Mass (Da): 44943
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A0A133UKB0 | MQIDGVDIDDTYSEGFDMVAARVLITAKNRDWALKAATEATGFGTSVIECGVEAGVEQLVDSTITPDGRPGVQVIFTAMSEDGFKDELRKRIGQCIMTSPTSSCFNALEEGNEVSLGGDLRYFGDGYQIPKRVESGFSKASRRVWRIPVMEGEFTIDQDFRIDQNSIGGGNFFILGEDEDSVLKAAEKAVDSIKGVKGSITPFPGGIVRSGSKPTSQYSFLRASTNTKRCPTLKSIVETKVPEGVNSVLEIVINGLTKEHIESAIREGVISACAVDGVLEISAGNYGGDLGRHFFHLYEILEE | Function: Catalyzes the transfer of a formyl group from 5-formyl tetrahydromethanopterin (5-formyl-H(4)MPT) to methanofuran (MFR) to produce formylmethanofuran (formyl-MFR) and tetrahydromethanopterin (H(4)MPT).
Catalytic Activity: 5,6,7,8-tetrahydromethanopterin + H(+) + N-formylmethanofuran = methanofuran + N(5)-formyl-5,6,7,8-tetrahydromethanopterin
EC: 2.3.1.101
Subcellular Location: Cytoplasm
Sequence Length: 303
Sequence Mass (Da): 32782
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A0A238UDJ9 | MAKAFLIAAPWSNSGKTTITLGLARYFSNKNYKVQTFKCGPDYIDTIHHSRAAKRPSINLDSVLMSDTHIQEVFTKYTNEADISIVEGVMGLFDGAVKDQGSSAELAKKLNIPVVLVVNAKAMAYTIAPILYGLKTFDPEVKIAGVLFNFVKTESHYAFLKEACETVGIPSLGYIPPNDDIKIPSRHLGLHIEDKFEELIENAASHIGTHANIKELLNVATSIKNTEIDDVTKEIHLLAKKETAITSVINPIGFHKKIKTKLKIAVAKDEAFTFTYVENLAYLKQLGDVTFFSPIHDTKLPDADIIYLAGGYPELYLEQLSSNAEMKTAIKNAAEDGIKILAECGGMMYLGNQIINADGIAFNMAGVFNFSTTMEQKKLHLGYRKVVFEDETIWGHEFHYSSMIHDQYDSIAKVYTAREKEIATKVFSYKNVMASYIHLYWGAGNFNWLTRLNGINPIGKPLDKEYYFVTFATAKSRISDRMVKYNTSSFIRNLDALIFEEDDLEKMMSLFKKAFKRYDIDVVCFNVLPDHIHILLKVENKEELTTQIKNIKGYTSYKFQRFKEWEKGKQKVWVQKFHRKKISATDGSIERVTNYIKNNHYKHEARWGKEMREFIESLHTQGNQGD | Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route): step 10/10.
Function: Catalyzes the ATP-dependent amidation of the two carboxylate groups at positions a and c of cobyrinate, using either L-glutamine or ammonia as the nitrogen source.
EC: 6.3.5.11
Catalytic Activity: 2 ATP + cob(II)yrinate + 2 H2O + 2 L-glutamine = 2 ADP + cob(II)yrinate a,c diamide + 2 H(+) + 2 L-glutamate + 2 phosphate
Sequence Length: 626
Domain: Comprises of two domains. The C-terminal domain contains the binding site for glutamine and catalyzes the hydrolysis of this substrate to glutamate and ammonia. The N-terminal domain is anticipated to bind ATP and cobyrinate and catalyzes the ultimate synthesis of the diamide product. The ammonia produced via the glutaminase domain is probably translocated to the adjacent domain via a molecular tunnel, where it reacts with an activated intermediate.
Sequence Mass (Da): 71179
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A0A849UY29 | MRNHAAKPIGVFDSGVGGLSVLREIRKQLPNENLIYVADSAHAPYGDKTKQFIEDRSTAIVEFFLSQQVKAVVVACNTATAAAGKELRAMYQLPIVAMEPAIKPATELSKTGVIGVLATHRTINSTNFQVLFSRFADQVKIIPQACPGLVDQIEAGDIDGIKTRDLVCHYVQPLMAQNVDVIVLGCTHYPFLAPLIQEIVGQGIKVIDSGYAIAKRLLFLLESHALLSEHQQQGSVHFYSSSESVKTAEVIFGLWGSDVKTAKMPHIISVLT | 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: 272
Sequence Mass (Da): 29594
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A0A2E6H923 | MPESRPVVAIMASGSGTNAENLLSYAQIKKTYNVACVITDKVDAGVITRCEKYSVDCYVVPYEKSKELSHLEAKTIHESKILNILESNKIEWVFLAGYMRILSADFISKYWDEQKEKSKIINIHPALLPSFPGKDAYEQAWDSGVEQSGVTVHHVDSGIDTGPIIIQESFQRKKEDNLQSFKARGLEVEYKLYKKAIDQLFAT | 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: 203
Sequence Mass (Da): 22910
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A0A1H8FTI4 | MSSLPPSSTTPLPDTYEEALSELEDLVQTLESGQTPLDELLASYQRGAALLAFCKQKLTAVEDQIRVLESGSQGIGTRALEDDNA | Function: Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.
Catalytic Activity: Exonucleolytic cleavage in either 5'- to 3'- or 3'- to 5'-direction to yield nucleoside 5'-phosphates.
EC: 3.1.11.6
Subcellular Location: Cytoplasm
Sequence Length: 85
Sequence Mass (Da): 9125
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A0A1C3PEK0 | MVGDNSDLVALLVSWLPRQRWFAGKGRAWGSLRIVQNVRLSDLLRHFVIEVRYADGGPVDHYQVPLVVRPDAPYGHEGFFVGKYADGLVYDGLHDPDGSAALLAFIRGEAARDGFVPYTLEELEPLPAHVVGAEQSNTSIVYGDAYILKVFRRLWPGTNPDLEMTRALADAGSPRVARPLSWLDGVVDGQTTTFAFMQEFLRSGTEGWRLALASVRDLYAEADLHADEVGGDFAAESERLGAATADVHRIIAETLPTAVGDAEILRAESAQMHSRLDAAIKVVGELQAFEAQLRAAYDELARRARPVVLQRIHGDYHLGQVLRVDSGWVLFDFEGEPARPVTERITLQPVYRDVAGMLRSFDYAAQSMLLERSMLLEREGESALRYRAQEWATRNRDAFCIGYAGVRGHDPREEAALLRAFELDKAVYEVVYEARHRPSWLPIPLGSVERLTSTD | Pathway: Glycan biosynthesis; glycogen biosynthesis.
EC: 2.7.1.175
Catalytic Activity: ATP + D-maltose = ADP + alpha-maltose 1-phosphate + H(+)
Sequence Length: 455
Sequence Mass (Da): 50671
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A0A923UIA2 | VITGEGKIVGVSIAPGLKTAVKALFSNTAQLPEVPLVMPDSAIGKNTVHAIQAGILWGYVGMVREMIYQIKKEIGQDCMVLATGGLSSILTPLQDDFDEVDKALTLNGLKIISELIN | Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 1/5.
EC: 2.7.1.33
Catalytic Activity: (R)-pantothenate + ATP = (R)-4'-phosphopantothenate + ADP + H(+)
Sequence Length: 117
Sequence Mass (Da): 12407
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A0A191HVM2 | MDNEKIEIGEIIGVFGIKGEAKIYPLTNEKEMFLTFKEFQYQDKHQEGILLVERIRLHKNIIVCKFKDKGTIESVLPLKGLKLWVPTSVLPNLDNDEHYVYELVGASVWTDDGMELGQLCDVMNTGAYDVYVVKDYENKEYLLPGIPEVILEKNMEEKKLVVHLLPGLVD | Function: An accessory protein needed during the final step in the assembly of 30S ribosomal subunit, possibly for assembly of the head region. Essential for efficient processing of 16S rRNA. May be needed both before and after RbfA during the maturation of 16S rRNA. It has affinity for free ribosomal 30S subunits but not for 70S ribosomes.
Subcellular Location: Cytoplasm
Sequence Length: 170
Domain: The PRC barrel domain binds ribosomal protein uS19.
Sequence Mass (Da): 19514
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A0A191HWN3 | MNLMNTYKPFPEKMVKGEGNYLIDENGKIYLDFLSGIAVNALGYGYKPLVEAMIDQVEQLIHCSNYFQTEPQLKLAELLVENTCFDKVFFSNSGAEANEGAIKLARKYSEGKYGKEKNKIITFKESFHGRTLATVSATGQDSFHTNFSPLPTGFEYAILNDIESVKALVNEDVCAILVEPIQGEGGLNSCTVGFMKDLNQLCKEQNLLLIFDEIQTGLGRTGSLFAYEWLGVEPDILTSAKALGGGLPLGAILAKAEVAETFVPGDHGSTFGGNPVACRGGIVVLETLLSDGFMDTIKKRSVYLSSGLFALQQKHESILELKGRGLMVGFSLVDDGSDLVAKAYEKGIIINQAKGNTMRFLPPLTIEEEEIDKLIFLLDDLLEERGN | Cofactor: Binds 1 pyridoxal phosphate per subunit.
Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 4/4.
Catalytic Activity: 2-oxoglutarate + N(2)-acetyl-L-ornithine = L-glutamate + N-acetyl-L-glutamate 5-semialdehyde
EC: 2.6.1.11
Subcellular Location: Cytoplasm
Sequence Length: 387
Sequence Mass (Da): 42339
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E6SHF2 | MRRLTPSELVAELDRRQPFSPEIRAAAEAIVDDVRRRGDEALLEYTRRWDAPHLTRDELALPPEAPAQALAALPASLREALETAAARIAAYHRRFVPESTAWTDAAGNRLGRLVQPLDRVGIYVPGGRAAYPSTVLMTAIPARLAGVGEIVLATPPRPDGSIPPVVLAAAALAGVHRVIRAGGAQAVAALAYGTATVPAVDKIVGPGNAYVTAAKAAVAHRVGIDSLAGPSEIVVVADDSAHPAWVAADLLAQAEHDPLAVVGCLSPVPELLDAVAAELDRRLEAAPRAAIAAAALERGFLVATASLAEAIDLASRLAPEHLSLQVRDPEAWLRRVRAAGAVFLGPFAPVAAGDYAAGTNHVLPTGGAARFQGALSPEAFVRCIPFFAGSREGVAAWAPAARVLAEAEGLPAHAASIRLREGDEPGAREAPAGTASRPQGAPGPAAVRLPEPQDAAVAPPAEPGTPKGARAGGAAIRPQEGAAPAGAPGYTVADSPAPVKLDANEAEPWPAELREALVAEMGRILAGDGPAPHRYPARALRQAVTAQLAAYARVPEEAVVLGNGSDELVQAVLGTLGRHCTAAVAPSPTFGYYATAAAAAGVPYRPVPVPPERAVTLDDLVPVLDGLPGEKLVFLCRPNNPTGLSCDADVVWGLLQRGDTWLVVDEAYAEFAGESVLDAWTVAPGPDGPATAGSAPRSCRDDGGQARGHGVHGDSSHGEPRLERLVILRTLSKAFALAGARVGYAVAAPAVASRLRRWLQPYNVNTFSLVAARVALEHREVFRRRAEATRRRRDRLFAALGRVPGITPLPSRGNFLLFRVEPAGAARRLQQELAQRGIAVRAFPWEPSLDGYLRVTVGTEEENQAFLTALAELQGGGQGTPAPRAAQPGGTGAGARDAGPGREPVPGAAVDHPGPAGPGPAPAGSPGQLRGRDGA | Cofactor: Binds 1 zinc ion per subunit.
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 9/9.
Function: Catalyzes the sequential NAD-dependent oxidations of L-histidinol to L-histidinaldehyde and then to L-histidine.
EC: 1.1.1.23
Catalytic Activity: H2O + L-histidinol + 2 NAD(+) = 3 H(+) + L-histidine + 2 NADH
Sequence Length: 935
Sequence Mass (Da): 96651
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F6G209 | MTSIRAVVFDAYGTLFDVYSVAARAEQLFPGRGEALSVLWRDRQIDYTRIRSLAGPSGEHYKPFWDITVDALRYACARLGLALSAHNEATLMREYACLSAFPENVPVLRQLREMRLPLGILSNGNPQMLDIAVKSAGMSGLFDHVLSVDAVRQYKTAPAAYALAPQAFGVPAAQILFVSSNGWDACGATWYGFTTFWINRLGHPPEALDVAPAAAGHDMRDLLQFVQARQSMR | Function: Catalyzes the hydrolytic dehalogenation of small (S)-2-haloalkanoic acids to yield the corresponding (R)-2-hydroxyalkanoic acids.
EC: 3.8.1.2
Catalytic Activity: an (S)-2-haloacid + H2O = a (2R)-2-hydroxycarboxylate + a halide anion + H(+)
Sequence Length: 233
Sequence Mass (Da): 25682
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A0A4W4GNS3 | MEKVDVLRALGAEIVRTPTSACFDSPESHVGVAWSLKNEIPNSHDQDQYRNPSNPLAHYDTTAEEILEQCDGKVDMLVAGAGTGGTITGIACKLKEKCPNVKIIGVDPEGSILAEPKELNHKKTQYEVEGIGHDFIPTVLDRSVVDRWYKASDDETFAMAHMLIREEGLLCGGSSGSAMAAAVKEAKELKEGQRCVVILPDSIRNYMSKFLNDKWMFQKGFLTVEEFMVNKPWWWNLKLQSLNLSAPLTVLPTVTCQKMIKILKEKGYDQAPVVDEAGLILGMVTLGNMLASVLAGKVKPSDPVSKVLYKQFKQVHLTDNLGKLSRILETDHFALVVHEQIQYLTDGSTSLKQMVFGVVTAIDLLNFVTGHEKRERSVSECTDEL | Pathway: Amino-acid biosynthesis; L-cysteine biosynthesis.
EC: 4.2.1.22
Catalytic Activity: L-homocysteine + L-serine = H2O + L,L-cystathionine
Sequence Length: 385
Sequence Mass (Da): 42636
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A0A4W4HJ71 | MEGTEKQDLIFLELRQRLQSGLLIIRSDAFEDKAEVNVTSRDSAIEIHVPDGGYLVKLKPGVSLVEGSWHKSQQLNADGLHVRMHLRVDQPSEALDSATVCLKALEKYHFLCQSCGAILVKEKVFRRVLPLPNGNWNALVDDWCCHPDPFANKKLLPQEEDCLVGDTYFLLTRDSSCDNSLTQQIDSSCVNLDTSQYSVKQTAGCKNVVVFCKMCSAVLGEAVTSEVLKFYITEVVIKQSEEREFTVPQHRQQFLERALTSRLLELSSAQSIFRFSIQTPDCKSVIMLWLLNTDTLIASFSEKVTSSNGLISSDRHLDEHQSCQAASAVKVLYLACNRAEHQEAVDAWEKDISVHPLALPWSTCDELLQLLSSCTSTLPPSLSSMNSYQVAYLKR | Function: E3 ubiquitin-protein ligase which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes, and transfers it to substrates, generally promoting their degradation by the proteasome.
EC: 2.3.2.26
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
Sequence Length: 395
Sequence Mass (Da): 44249
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A0A4W4H1B5 | MTCVCHELVSNLHELVSNLLCKQFLQEFYNEDSAGKKVFKYGAQLVCLAHREQVALVVDLDDVAEEDPQLVESVCENTKRYTGLFADAVHELLSEYREREVLAKDALDVYIEHRLMMEMRGRDPADTRDPRNQYPVDLMRRFEVYFRPPSTSKPEVIRDVKADHIGKLVTVRGIVTRATEVKPMMAVATYTCDQCGAETYQPIASPSFMPLIMCPSQECVTNRSGGRLYLQTRGSKFIKFQELRIQEHSDQVPVGNIPRSMTLYARGENTRVAQPGDHVAVSGVFLPLLRSGFRQAVQGLLSETYLEIHCIALMNKTEDDELGTEELSEEELRQITEEDFYEKLAGSIAPEIYGHEDVKKALLLLLMGGVEQAPRGMKIRGNINICLMGDPGVAKSQLLSYIDRLAPRSQYTTGRGSSGVGLTAAVMRDPVTGEMTLEGGALVLADLGVCCIDEFDKMADADRTAIHEVMEQQTISIAKAGIMTSLNARCSILAAANPAYGRYNPRKSIEQNIQLPAALLSRFDLLWLIQDKPDTDNDLRLPGGRECVRQRDHCVIKCLQCR | Function: Acts as component of the MCM2-7 complex (MCM complex) which is the replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. The active ATPase sites in the MCM2-7 ring are formed through the interaction surfaces of two neighboring subunits such that a critical structure of a conserved arginine finger motif is provided in trans relative to the ATP-binding site of the Walker A box of the adjacent subunit. The six ATPase active sites, however, are likely to contribute differentially to the complex helicase activity.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
EC: 3.6.4.12
Subcellular Location: Chromosome
Sequence Length: 562
Sequence Mass (Da): 62842
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A0A8K0DW54 | MKKSLAMMLMYRFGIAVLVAAVLLEGVGAQQNQQNWCVNQLRPCLNYLNGNREPPDSCCDPLKSIIKNKPQCLCSLISNQGTRQAEQAGINVTEAQTLPGRCGQHVNPLPCLRAGGSPSGGGSNSEKKENDNYQNSAAASSRVFVFGCCWMNIAVAALSYLIVCVLRFL | Function: Plant non-specific lipid-transfer proteins transfer phospholipids as well as galactolipids across membranes. May play a role in wax or cutin deposition in the cell walls of expanding epidermal cells and certain secretory tissues.
Subcellular Location: Cell membrane
Sequence Length: 169
Sequence Mass (Da): 18268
Location Topology: Lipid-anchor
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A0A3A1Y9H4 | MTKKDKLVTLGKLGSTYGYKGWIRVNSFTEEPTNIFNYDNWYINLNNNLTPVKVESWKVHANHLVCKLDCLDSLEAAKAFNNLFVYVKSDELPELDGEYYWKDLMGCKVFTPAGYELGTVSQIMETGANDVLVLQAPLNDAYNRKDRMVPFIDKYLVEVDVRNKKIIIDWDPEF | Function: An accessory protein needed during the final step in the assembly of 30S ribosomal subunit, possibly for assembly of the head region. Essential for efficient processing of 16S rRNA. May be needed both before and after RbfA during the maturation of 16S rRNA. It has affinity for free ribosomal 30S subunits but not for 70S ribosomes.
Subcellular Location: Cytoplasm
Sequence Length: 174
Domain: The PRC barrel domain binds ribosomal protein uS19.
Sequence Mass (Da): 20117
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A0A0E3ZBI9 | MAKKVTFEEKLKKLEENLKKLEDTEIGLDEAIKIYEESKKIISDANKILDDASGKVKKIIDKNNEYELEDFEDK | Function: Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.
Catalytic Activity: Exonucleolytic cleavage in either 5'- to 3'- or 3'- to 5'-direction to yield nucleoside 5'-phosphates.
EC: 3.1.11.6
Subcellular Location: Cytoplasm
Sequence Length: 74
Sequence Mass (Da): 8634
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A0A2C6KP55 | MRRPFYFPAIRSSVFPASAVRGVFSSSLTVFFLTRGGSSKDAFAENTADGPVRRSLEEILQAAACSRSSYLSSHPHSLFTSRQLSGDCSPWSLSSTHPALLLKNSGHPSFLPRRSLRVSSRGIMTAGGGDADPEKNPREGANALLIKTAKDFFIPRLEFNRHKGQNGRVCVIGGSLEFTGAPYFSAISALRMGMDLAYIITTSDAAVPIKSYSPELIVYPLLPGGDQKVGIEESLHHLKDKSRAILKKSDVIVMGPGLGAPKPYVANAGAAAEENACPIQKAALLLLDLAMEEKKFVIIDADMIRVLCQPHNEPSLHRLKHYRRCLLTPNKREFDLIHGAFQSLPEGRRHPSPGDMAYLTELARALRLEQSKDGSDGCKDHPSPGSESGKGEGTGEEGGGQEEGKSAPPSPSSSSSLPRCCSLYCDSNNKLNPLLQSLYPSSLKPFFPSLTGMTQHLYGPSLFLKGTADIVVVPGCVRTRQQTSDGKAADDDGEGGSCPAAVLAACGLSLSSRGSPKRSGGQGDVLGGVLATFIAWWHVYSRHRAEKLAGPDQKRGGKGGEVVAGHGDSTHHLHTDKDKDKKEKVRSGHSSEPEKRSSSSGEKQENSHTTGEGNESQRGDRDGEGEIGRALGMEDEDSAGLLCAAFNASLVVRRAAAKAFELKGRSMLAGDVIELLGETFREMYDEK | Function: Catalyzes the dehydration of the S-form of NAD(P)HX at the expense of ATP, which is converted to ADP. Together with NAD(P)HX epimerase, which catalyzes the epimerization of the S- and R-forms, the enzyme allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration.
EC: 4.2.1.93
Catalytic Activity: (6S)-NADHX + ATP = ADP + H(+) + NADH + phosphate
Sequence Length: 687
Sequence Mass (Da): 73623
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A0A5J6MCZ6 | MNAIVKPRRPWLAVLLSLITPGLGQLYCRRPMRAAAWYLVGAGGGFTVYYLMSQGILAPTLAVQWVFYVTVAVFFVAMLADAWLLAKRMGAVTLAWYNRWYVYLLIPLSLNLASLALPPKPTFEHFSMPSASMNPTLVVGDMFTVATSVYKNSPPRPGDVVVVRKEEGGRSFVKRVVAVAGDRVQMKDGRLYINGAMVEREKLGDYNDPGNGTGSAVLTLYRETLPNGRSYQIAELSDKEFFDNTPEFQVPPDHIFVLGDNRDSSMDSRAPGEFGFIALAHVEGRVAKITGSLDSSRIGIEVQ | 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: 303
Sequence Mass (Da): 33404
Location Topology: Single-pass type II membrane protein
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A0A1H0ABN1 | MQPMRTTRTTNNDDPDRTMTGKTLAEKLLSEKSGTDARAGDYVEAEIDVAMAHDITGPLAFQTFHEVAGEDADLFAPDRTVFTIDHHAPADGVQAANNHNAVRDFAAKHGAHQFDVGDGICHAVLVEEGFVRPGDLVIGADSHSTTYGGIGAFGTGVGSTDLGTALATGELWFRVPETLKFEVEGDLADGVYAKDLILRFIGDVGFDGCTYKAAEYTGSTIESLPIHERLVLSNMAIEMGGKAGFVAPDERTVDYLERQTGNDIELDGSLRSDDDAEFDEVYTYRAADLAPQVSKPSNPENAVDVTEVEGTEIDQLFVGTCTNGRYEDIKVVADILAGEELAPNVRMVVVPASKSVYQHMLHTGVFQTLTDAGAVIQSAGCGPCAGYHQGVLGDDDVCLATANRNFPGREGSMDSKVYLSSPATVGASALYGEITDPRSIETTRHDDTVFAEVSP | Cofactor: Binds 1 [4Fe-4S] cluster per subunit.
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
Sequence Length: 455
Sequence Mass (Da): 48552
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E6SKT4 | MSQAGWQVDPESGWLVESQTIGFQVRWRLLRLLHHERSPYQDIVVAELDRFGRALFLDRILQVAEMDEFIYHEMLVHVPLAALPAARRVLIIGGGDGGTLREVTRWPDVEEIHLVELDEAVVRVCRQWLPQVGDGAWDDPRLKIHYADGYAFLQEAPAGTYDAILVDCSDPGTPADTLYSETFYRLADRALAPGGFLVQQALSPFIHRDVLAAILRRLAGVFSQSGVYFCPSIAYLIGLQAFVWGSKGTNPAAGPARPAPGGTRWYTPEVHRAAFIVPPALENLQSATSG | Pathway: Amine and polyamine biosynthesis; spermidine biosynthesis; spermidine from putrescine: step 1/1.
Function: Catalyzes the irreversible transfer of a propylamine group from the amino donor S-adenosylmethioninamine (decarboxy-AdoMet) to putrescine (1,4-diaminobutane) to yield spermidine.
Catalytic Activity: putrescine + S-adenosyl 3-(methylsulfanyl)propylamine = H(+) + S-methyl-5'-thioadenosine + spermidine
Sequence Length: 290
Sequence Mass (Da): 32101
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D7G3W0 | MLQGRGQEKHAKRAKLYEMSSPGPPRLCDRAGTSGMLLAALQQCGQQQGGSKSAASREKSEPTPPASTAAARGADELGSIDNDWMSLTSRPRELDAGALSGKDRMVDAFDLVLIVDLGEQRDKVRAPIRDKLERFLSQLSPRRAGLAAASPTGVVGLEMQVARLQTGDFAWAWRRRRSGSRGTDLLTGPSEELLLLDCLVERKKEDDIINSVEGLAGRYRAQKRRMSLCGLSRLIYLLEGKLEGHVAYKSSVDKTKTMRTMETDTLAEGFAIKRVDNVEETAAFLLSLSLQLMASQGAETIQEYCSNPSRPKVSFGEWSTAMKPKRLEPRTVTMEFARCLLMVNGVSAEGARVIAREFPTPMRFIEALRQCSSPEEQKSLVQKLKLADGGKKGSCRTVNEPTARKLVALFADKPQA | Function: Interacts with EME1 to form a DNA structure-specific endonuclease with substrate preference for branched DNA structures with a 5'-end at the branch nick. Typical substrates include 3'-flap structures, D-loops, replication forks and nicked Holliday junctions. May be required in mitosis for the processing of stalled or collapsed replication fork intermediates. May be required in meiosis for the repair of meiosis-specific double strand breaks subsequent to single-end invasion (SEI).
EC: 3.1.22.-
Subcellular Location: Nucleus
Sequence Length: 416
Sequence Mass (Da): 45646
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A0A8K0E1F5 | MRRHPFWLHLYAFVFSCMGATYRTAKSGVGVASMGVMRSELAIKSIMPVVMAGVLACGLAGLAAGMAIEIIGDASVRFIERNMYERGHDFELLPFGCGRRMCPGVVLSQLVHCFNWELPSGLKPNDLDMTEVFGLTVPRANHLLLKPKNRLLVRTT | Function: Proton-conducting pore forming subunit of the membrane integral V0 complex of vacuolar ATPase. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells.
Subcellular Location: Vacuole membrane
Sequence Length: 156
Sequence Mass (Da): 17225
Location Topology: Multi-pass membrane protein
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B3M1I0 | MTGKLRSLGLKLFQKAKGGFNWTSVRPKASLPGRTFFAGRPKLLGALGVLAGGAGLLIYALEASVDASSDCVHPPHQDWNHTGLLAALDKESVRRGYFVYKEVCSSCHSLQYIAYRNLVGVCMTESEAKSEAEGITVKDGPNEEGNYFDRPGKLSDHFPSPYPNEDAARSANNGAYPPDLSYIVSARKGGEDYVFALLTGYCEPPAGFTLRDGQYFNPYFSGGAISMGKVIDNEVVSYADENVAASAAQIAKDVVTFLKWTSEPESDERRLLLIKVVLMSAFLIAMSYYIKRHKWSALKSRKIFYIPELERQAAQAAREAELAAKKAESDQCNRCENKNTDKD | Cofactor: Binds 1 heme c group covalently per subunit.
Function: Electron carrier protein. The oxidized form of the cytochrome c heme group can accept an electron from the heme group of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c then transfers this electron to the cytochrome oxidase complex, the final protein carrier in the mitochondrial electron-transport chain.
Subcellular Location: Membrane
Sequence Length: 343
Sequence Mass (Da): 37712
Location Topology: Single-pass membrane protein
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A0A1F3SN93 | MDKILAGKRALILGVANERSIAWGITKAFKAYGASVALTYLNDQLKKRVEPLSKEVGADFIHETDVTIDEHYGKLADRVKSEWGDFDILVHSLAFANKDDLQGRFVATSREGFKLACDVSAFSLIGLSNCLKGMIRPDGSVMAMTYHGSTKVLEGYNVMGVAKAALEASTRYLANDLGPDKIRVNCISAGPIRTLASSAVKSAKTTSEFIEQRAPLRRNVSIDDVAGTAVYLASSLSSAVTGQVIYVDSGVSIMAM | Pathway: Lipid metabolism.
EC: 1.3.1.9
Catalytic Activity: a 2,3-saturated acyl-[ACP] + NAD(+) = a (2E)-enoyl-[ACP] + H(+) + NADH
Sequence Length: 256
Sequence Mass (Da): 27490
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A0A3A1Y0P1 | MPRLPLSNYVKNLLRLQVDAKILLSIALGAVLGAWARAYLSLWLNPSLAFINLGTLVANVVGCFIIGLMVCAVKDLQISARVQQLIVTGFLGSLTTFSSYSSEVVQRFYQGAWGQALGIALIHLLLGFLSTGVAIALWRLFKG | Function: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Subcellular Location: Cell membrane
Sequence Length: 143
Sequence Mass (Da): 15480
Location Topology: Multi-pass membrane protein
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A0A7S8F7F5 | MPKIRPANGPGGLQDSFGRRFSYLRVSLTDRCNFRCTYCLPNGYQKPADAPSELSREEFRRAVEAFARLGVWKVRLTGGEPTVRRDFSEIARDMANIAGVRRVAMTTNGYRLAREALDWRAAGVDAVNVSVDTLDPKAFAAITGHDRLAEILRGVDAAIEAQFDAVKINSVLMDGTEPGDLADILDFIRERDVSWRFIELMRTNDNAAFHLQNSRTSERLRAALVATGWTVQPKAPGAGPSIDLAHPDYRGAIGIIAPYASGFCDSCNRLRLSSRGKLHLCLFGEAGIDLRYLLQHDGQIDELVERIRSAMPHKTLGHRLHDQDSGQTPHLASIGG | Pathway: Cofactor biosynthesis; molybdopterin biosynthesis.
EC: 4.1.99.22
Catalytic Activity: AH2 + GTP + S-adenosyl-L-methionine = (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate + 5'-deoxyadenosine + A + H(+) + L-methionine
Sequence Length: 336
Sequence Mass (Da): 37096
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A0A2D4KCR4 | MSDKLPYKVADISLAEWGRKALNIAENEMPGLMKMREMYSPTKPLKGARIAGCLHMTVQTAVLIETLTALGAEVQWSSCNIFSTQDHAAAAIAKTGIPVYAWKGETDEEYIWCIEQTLYFKDGEPLNMILDDGGDLTSLVHTKYPQLLKGIKGISEETTTGVHNLYKMHANGTLKLPAINVNDSVTKSKFDNLYGCRESLIDGIKRATDVMIAGKVAVVAGYGDVGKGCAQALRNFGARVIITEIDPINALQAAMEGYEVTTMEEACKEGNIFVTTTGCSDIVQGRHFEHMKDDSIVCNIGHFDVEIDVKWLNQNAMEIVNIKPQVDRYTLKNGHHIILLA | Cofactor: Binds 1 NAD(+) per subunit.
Pathway: Amino-acid biosynthesis; L-homocysteine biosynthesis; L-homocysteine from S-adenosyl-L-homocysteine: step 1/1.
EC: 3.13.2.1
Catalytic Activity: H2O + S-adenosyl-L-homocysteine = adenosine + L-homocysteine
Sequence Length: 341
Sequence Mass (Da): 37527
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A0A6H5IJH4 | MFYPTVSIVSALCYVLGICCAYVTFATYINIEGIEGMGFLTFLMHIINSLVGFWVVLFIVVFGQMVSSGAFATWYWHQNKSDIPKYTVFRCIKIISRYHLGTVAYSTSMFGAMSILYLLGMRLLNHEGNKAGKIWLVLYHMVDAVVGRFMAAGAVLNCITNGQDFAESASRTLDNFEANIKKTLLATKIIEYVLVLAYVLVSGLVGLAIYPYALNFTYPLPLAVIIYIGTNMFLFSLLATLHASFNAILISCYEDRTINDGTTLRPYVMHDDLRMAFIRRGSPRWYACCATRKSYYENS | Function: Choline transporter.
Subcellular Location: Cell membrane
Sequence Length: 299
Sequence Mass (Da): 33648
Location Topology: Multi-pass membrane protein
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A0A963PXU9 | GSLDRVFISRGLANAFYSHRTTDYLNDVSEEFDPAHRQGIAWNDPHLAVAWPHAAPVLSAVDARHPTLKQLFPTHPGLA | 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 Length: 79
Sequence Mass (Da): 8742
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A0PHQ6 | MWAFKSVLLLSIAMVLSINLSIQQINSSSVYQYVWSWIITNDFSLELGYLIDPLTCIMLILITTVGIMVLIYSDNYMSHDQGYLRFFAYMSFFSTSMLGLVTSSNLIQIYIFWELVGMCSYLLIGFWFMRPVAANACQKAFVTNRVGDFGLLLGILGFYWITGSFEFRDMFEILKNLIYNNEVNVLFVIFCAVLLFSGAVAKSAQFPLHVWLPDAMEGPTPISALIHAATMVAAGIFLVARLLPLFTVIPYILNLISFIGIITVFLGATLALAQKDIKRGLAYSTMSQLGYMMLALGMGSYRTALFHLITHAYSKALLFLGSGSVIHAMETAGGYSPEK | Catalytic Activity: a plastoquinone + (n+1) H(+)(in) + NADH = a plastoquinol + n H(+)(out) + NAD(+)
Subcellular Location: Membrane
Sequence Length: 339
Sequence Mass (Da): 37773
Location Topology: Multi-pass membrane protein
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A0A2T1A0M0 | MAGQESVERRGGRDDGDDAADAQTTARREDATEDVDSILDEIDGVLEENAEEFVKQFVQKGGQ | PTM: Is modified by deamidation of its C-terminal glutamine to glutamate by the deamidase Dop, a prerequisite to the subsequent pupylation process.
Pathway: Protein degradation; proteasomal Pup-dependent pathway.
Function: Protein modifier that is covalently attached to lysine residues of substrate proteins, thereby targeting them for proteasomal degradation. The tagging system is termed pupylation.
Sequence Length: 63
Domain: The N-terminal unstructured half of Pup provides a signal required to initiate unfolding and degradation by the proteasome but is not needed for pupylation, while the C-terminal helical half of Pup interacts with ARC to target proteins to the proteasome.
Sequence Mass (Da): 6871
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A0A3Q9G217 | MDTDAQLASLPERDRSPEPAQGEEQGSRSARFPRVAAGWRWLTGGGPLRRAGVLIFTCLITLLLVSSYLVQPFLIPSGSMRGTLQVGDRVLVNKLAYRFGDEPRRGDVIVFDGTDSFVQDDGPSENAVTTIIRKGAAAVGLMRPSETDYVKRVVGVGGDRVRCCDKWGRLEINGRPVLEEYLYPGDVPSQVPFDVVVPEGKLWVMGDHRSDSRDSRDHLGEPGGGMVPVNRVVGRADWIGWPLGRTTSLGRTGAFADVPDPGPGHGGGGPHG | 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: 272
Sequence Mass (Da): 29296
Location Topology: Single-pass type II membrane protein
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A0A7T1L7Q6 | MVPGAALVTLACLLSRACSVVLRGSSVSLTTNRPFDVGVASDSEMTVPGDLTVPGKLFFMGRQMPSAKYYDGTLELIHKPDDGSCAKLVYVGEFTACPRRSTEAFVLCRELRFAQSPSYPGLSLDPAHGTLLRVRNADPLYSGTYTLKVWLEGAANASVFPMTLRVDGEERAHPATPPVSRAAGEEDCVEAGAPTRGNGPSEPRHVYVSNGPSETTTATTASTPDTTTYEARPMPSPSSPPNPLLVETNQRSGLLGMPVPMLIAAGLAAVVIMGTIGACCAIRCCGNRSPPRAPVYRRNVDPAFVEANEAALSRLGDEVKAEGFPRRPSYTIMPSLSAIAEEPPSYRSE | Function: In epithelial cells, the heterodimer gE/gI is required for the cell-to-cell spread of the virus, by sorting nascent virions to cell junctions. Once the virus reaches the cell junctions, virus particles can spread to adjacent cells extremely rapidly through interactions with cellular receptors that accumulate at these junctions. Implicated in basolateral spread in polarized cells. In neuronal cells, gE/gI is essential for the anterograde spread of the infection throughout the host nervous system. Together with US9, the heterodimer gE/gI is involved in the sorting and transport of viral structural components toward axon tips.
Subcellular Location: Cell junction
Sequence Length: 349
Sequence Mass (Da): 37033
Location Topology: Single-pass type I membrane protein
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A0A2T2UTB5 | MTPYELLRRYDEEQYNSDNRMVNGQFFPSSTLEVKEGETVGVVLLNLGGPDSEEAVKPFLYNLFMDPAIIDFSQVVYFQARGRVRQAFSKIISYFRSKSVAEDYKEISDDGGSPINPLTREQSENLEQTLNEQYAAEMGVAFKTYMAMRYWKPFSEDAVAQMQDDGVDKVVLLPLYPQYSKTTTGASLVEWYEMEKAGEMPEWPTSFVFEYATYPKYLKALSERIDEGLERFPEEVRDDVHFLFSAHGTPLNEMQDRRDPYCCLVHSTVKHLMEHRGHDHEFSTAFQSKVGPSKWLEPPTDETVAELAEEGEDVLVIPVAFVTDHIETSYELAIEIPEDLEEEGEPIPEHYEVMPGLNSHPKFIEALADVTAAQLELPDAHTMRPWSARPCYDSRERDIRCQQCQRIAEATDWSEKESEEPERTPAAA | 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: 428
Sequence Mass (Da): 49083
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A0A2D5YMR2 | MKDLALVFVGGGSGAILRFLTSKGVRFFMPHKMWLSTLIVNVVGSLIMVYLYKNFNDQPEAFKKMVQVGILGGLTTYSSFSLDIFSLVSKGSYSEALLVFLLNIMFGIVVGIFIFR | Function: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Subcellular Location: Cell membrane
Sequence Length: 116
Sequence Mass (Da): 12872
Location Topology: Multi-pass membrane protein
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A0A8J6MS74 | MTLASSMKEFGWLTSHPLVPNDLPNLLNTDSRSLQAGQWFLPIRGQHYDGHDYIRLAMTKGAAGFFYQASHAKHLDDHDRKFGIEVADTTLALQQLARWWRQKMGCTVIGITGSSGKTTVKEMTGVMLRHFAPVLLTEGNYNNEIGVALTLCRLKSEHKYAVIEMGARHKGNIAFLSAMVEQDIGVLLNVGSAHVAEFGGPLKVLETKMEIAAAPTLVFGSDDERISAAMDKLSNKTVIRFAERAESEVNLTRVRLDGRGSVQLTFKIGEQNLSLESNFYHSRFAINIGACLAIGLALKLDLRECIRGLETFHGVKGRFKVHRLDERLLIDDSYNANPESMKSGLSTLHQAYGQRQICLVLGDMLELGESSEDFHRKIGAYSALEVKPMRLITVGHMARWIADEALSCGMEKASIQEFENVDTLMDEMSDLWNDCDLIYVKGSNGMKLAKFVDAFFTGSLASNDPTSNSKTEHPKKYSTTINDG | 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: 484
Sequence Mass (Da): 53685
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A0A8K0DRH6 | MSVMVANRDKRLKDNCNGILKISMDDNLVLSDAKGQFLWSSSDSTTSSETTMAINNSSTSVQLLFRYWKLGVERFQGTMRCSFQVFPEFSIATATDTITFNHSIKGSETIISNSSVFELGFFSPVNSTNRYLGIWYSFSPNVVVWVANRDKPLRDNSNGILKISMDGNLVLSDAKGQVLWSSSNSTASSRTTMVSNNPSAQLLDTGNLVLKDYQGTTIWESFLHPCDTILPKMRVPANSNARSKIQLTSWKSISDPSIGSFSGSLDSRDVPEAFIWKGDRPYWRSGPWNGQKFLGTYESTFGYLDGLLVVENKEGTMYVTFDFGRSFTFSRLVLHRQGYLALSYLSSEKEDWELHQSDPVPSSTSCAVYGTCGVFGSCSNMYSTDCRCLRGFEPRNKQEWNRGNWTSGCVRRTPLKCERLNNSTTASTGDKESGKDDAFMKLKAMKVPDFMIVSSAPRDNCQDQCLKNCSCTAYGFDSGIGCMLWSGNLIDLQQYPEGTATDLYIRLAYSELSETKKLGEIITIAVIVGTFIIATGVYFLYMWNYKQRVRKRKSKEMHSLGLEGRNSPKFPGEVLKQQELRVFNFEKLAMATNNFHSDTILGQGGFGQVYRGKLEDGEEIAIKRLSRASGQGLVEFTNEVVVISELQHRNLVKLLGYCVDGEEKMLIYEYLPNKSLDAFVFDPLKKESLNWRNRFKIIEGIGRGLLYLHRDSRLKIIHRDLKPSNILLDEELNPKISDFGMAKIFQGNEDHANTRRVVGTYGYMSPEYAFKGLFSEKSDVFSYGVLLLEIISGRRNSSFHQEEEPSSLLNFAWKLWNENNIIALTDPALSSCNRDDENEIMRCLQVGLLCVQESASSRPSMPSVVSMLNSEIVDLPTPNKPAFSERHIGSDTDSSSQLNRGKCSINNASITAIDGR | Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
EC: 2.7.11.1
Subcellular Location: Membrane
Sequence Length: 916
Sequence Mass (Da): 102818
Location Topology: Single-pass type I membrane protein
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A0A6M8EET1 | MRFINRNFKNSILLSLLLSLLFFTGCSQKSGDVDYSFYKDTKNSKINNSKEMHKYTMRPYSVFGITYYPFVAKIGDDFDGIASWYGPDFHSKKTSNGEIYDMYDMTAAHKTLPMNTVVKVENLENGKTIIVRINDRGPFVKGRIIDLSNKAAHEIDMVRRGTAKVKVSVLGYNGEIDNRNAPTIEIPSTQVASNNIGKEIEPGIDTLEPLEIKEDNIKTTSVPVSASRSDISTTSSAKITRPSNTSSSASFSSGNYNLQVGAFSLESGAIKVKSDYQKKFRKNKVEVQKVFVNGKTLNKVFVRGFSSYENAQEFKNANGLDNAVISND | Function: Lytic transglycosylase with a strong preference for naked glycan strands that lack stem peptides.
EC: 4.2.2.-
Subcellular Location: Cell membrane
Sequence Length: 328
Sequence Mass (Da): 36495
Location Topology: Lipid-anchor
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D2YVG5 | MFWMMLLVMLMMIFVLQFTGNSFLYWVFMEMVSLIIVVYLLVVSKNVGNLYGVLNYFLVQGLGGLIVLLGLVWGILEDGGIYGFFNNSHNNVMLILILGLFIKMGFFPFFYMVIMVMLKLGYKECFIIIILPKIIPLYLFLNMNLSMFEGLLYLVILMSLFTAGVNGLKAADIRELMGWSSINQTGWMMLLVMCDVMLFLLFYVFYLVLMFMFWYYVKGVSSSSFFGVSHLMGKGDMGVIMTLLLGMIGGFSPFALFLFKMFGLLMVVNSFGAWGVGFLFLMLTGSFLFYMRIFQFLLCVTSSYGSLGFSYKDSNSGAVSFFLMLVLTVTGFIVFYI | Catalytic Activity: a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) + NAD(+)
EC: 7.1.1.2
Subcellular Location: Membrane
Sequence Length: 337
Sequence Mass (Da): 38393
Location Topology: Multi-pass membrane protein
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A0A930F0S6 | MNYLLTYALYVLILSVLMGVSTWKLFKKLGYSPLAAFVPFYNYFIVLKETKHPKWWVVLAYFPIVGTIMMTIFHLFLMKKFGRDSIGQKLLTIVFPFIYMAVVNYSSDVRVIKDYDEDDRKETVLGSLTYAVVFATLVHTFSFQPFGIPTGSMERTLLVGDFLFVNKLSYGYRLPMRPLALPFLQGTIWDTGEKGNPKDDPKSYVEAVKLPYWRLPGWDSVQKNDIVVFNYPDDSVHVSIDRKDSYVKRAVAVAGDVLEIKGGKLFINGKPE | 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: 272
Sequence Mass (Da): 31166
Location Topology: Single-pass type II membrane protein
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A0A221KG05 | MGHMHTASFLDLALSEQNLLQAWDHVRTNAGAPGSDGETIQNFSRHILHHLQQLKTELLSGQYRPQPLRYVPIPKKNGGTRTLAIPTVRDRILQTSVAHVMSQFLDPQLDAASYAYRPGRSVSQAIACVLSCRDAGLQWVLDADIEQFFDHIDHEILNTQLESYFPNDPVCQMVAAWIANGSPEPHAGVPQGSPLSPLLANVYLHPLDRQLRQEHQTLIRYADDFVVLCADENQARQAWATVQQILADLKLRLQLEKTHLTTFDQGFNFLGVHFHRHTAQPLHPHAAPWVLPSDTPPDDPASGPPDVPRWLESIDPALSCDDTPASDEPPATPPAALEPRAPLLQSLYVTEPGCWLTQEHDRVVVSHQHTVRASVPLGQVDQVAILSNAMVSTALLRRCAQRRVSVVMGGWGTELLTLDRGALADHALWQAQWDLQAEPERGLMLARCLVAGKLHNSCTILRRFSRREGREAVEPLVQSMLQDERKLAAAERLEVIRGLEGAAARAYFAALRGLLPPGVDFPGRQRHPPPDPVNACLSLGYGVLAHNLHTLIRLEGLNAHLGHLHVATPGSLALVSDLMEEFRAPVVDAVVLTLWREGRLQASDFECRLGDDAEGWPCRMVSAARKRLVDALEEKLESHMVHPRLERLLDLRRIMQAQVRHYRSVVMGEVGVYHPFKLR | Function: CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain spacers, sequences complementary to antecedent mobile elements, and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). Acts as a dsDNA endonuclease. Involved in the integration of spacer DNA into the CRISPR cassette.
EC: 3.1.-.-
Catalytic Activity: a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)
Sequence Length: 679
Sequence Mass (Da): 75641
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A0A7X9YLS4 | MVIEVPRSLLQKTQNNFPMELLYLGIVMIIIFMIFIIMSILFFARIRKRLIRLQTAMMTPGKEGIPLPVDIRRSDEIGQLEESFNQMVHQLSDSRYREREEEQLRKRLIAGLSHDLRTPLTVIRGHMHALHKEALSEQGDRSLHRMEAKMEDLGGLIDNMLSYNLLTSGKYTLKLEEKDMLRIVRETAAAWYPVWEKDQFDIDIDLPEEPLIWYIDEQGMRRILDNLFQNVNRHAAGGKYIGITTQEIHGETAVVIQDRGPGMQPNSDTKGTGLGLSIVDLLIREMGLRKRVDSSDTGVRTYIYSGKGNREIPNR | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Membrane
Sequence Length: 315
Sequence Mass (Da): 36317
Location Topology: Multi-pass membrane protein
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A0A9D1LNX4 | MRLLFASLAILSDSGVDSTPFDKDDFIAKIFPNGMIDFVIQLLGFVVLLLIVFFIAYKPVHNLIKRRRDYIEGNLRESEASLAKAREAESHKEETILQGKKEAARIVAEAREQANREAIASKQATAEAIEKAKKDADAEIEASKRQAEKEVGKKAIDLAIAASSAILGREVTDVDQQKLLDEMIDKLGDNNG | 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: 192
Sequence Mass (Da): 21198
Location Topology: Single-pass membrane protein
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A0A191HT42 | MGKRNLYLSNIPVAEALGYMVAYLEKEKIELGIETVPVADAVGRVTGIPIYAKKSNPLFLSSAMDGIATIHTYLKEAKETNPIILETNQFEEIDTGDKVRPPFNCVVPAEEVTYLENGKVELIKSVTPWSHVRPVGEDIGDNELIVPIYHTLTPYDTGVVLNGGWTEIEVLKKPHIVLIPTGDEMISPYKLYKEGKLIDCNSTVFKGILEEIGGKVTTFPIVADDKFLLKKAIMDAVNIGDIVVINAGSSAGRDDYTVHIIRELGEVFCHGIAMCPGKPTVLGGIAKTPVLGIPGFPVSAAFSLETFVKPLIARLLKRQLPDVEILEGTLATQVPSQFGALELVRVLVGKIEEQYKVLPLPRGSSSLSSLSKADGLIKIPPLSQGYEKGESVKVELLSKRSQLAKRLVFQGSHDFTLDVLKNTVKIMNPQYELITTNVGSLTGILAVKNKEAHGAGIHLLNEETHTYNFSYIDKYLGKEGHLIHIAKRQQGLILPKGNPQNIHSLKDVIDKEGVYVNRQLGAGTRVLLDYLLKKEALDKKRIEGYNQIVYTHLEVGARIASGQADVGMGIYSAAALYDLDFIPITEESYDLCCLDSFMESYLYELFIKCLKESSFREKIEQYGGYDLRESGKVLR | 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: 635
Sequence Mass (Da): 70034
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A0A0S7BPU5 | MLKVGLTGSIGSGKSTIAGLFRVFGIPVYIADVEAKKFLGDPEVIRMVVEMAGDGVLSPDGSIDRRMLASLVFNDPARLTTLNNIIHPRVRRHFFDWIETQSGVPYIIQEAAIIFESGFYKMFDKIITVAAPVEERISRVMLRDGLKREDVMARIENQWPEESKIAMSDFVIRNSDTDLAIPQVLEIHRNLMGISEAFKNQ | 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: 201
Sequence Mass (Da): 22597
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A0A2N4Y2C4 | MSKPSIQPHGHHEQGHGHDTSGHDHGSYRSYLTGFVLAAILTIIPFAIVMSGGFDSRVLTAVTVIGFAVVQILVHMVYFLHMNTRSDEGWTMLSMIFTIIVVVIMIAGSVWVMYNLNTNMMPSMDHESFQGFGS | Function: Cytochrome bo(3) ubiquinol terminal oxidase is the component of the aerobic respiratory chain of E.coli that predominates when cells are grown at high aeration. Has proton pump activity across the membrane in addition to electron transfer, pumping 2 protons/electron.
Subcellular Location: Membrane
Sequence Length: 134
Sequence Mass (Da): 14813
Location Topology: Multi-pass membrane protein
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A0A4W4E7X3 | MAVLLETTLGDIVVDLYTEERPKACLNFLKLCKIKYYNYCLIHNVQRDFIIQMGDPTGTGRGGESVFCKLYGDQARFFDGEKVPRIKHRKKGTVSMVNNGSDQHGSQFLITTGENLDYLDGVHTVFGEVTEGMDILTKINECFVDKDFVPYQDIRINHTVILDDPFDDPVDLPVPDRSPEPTREQLDSGRIGADEEINDAEGKDAEELDELIKEKEAKTQAILLEMVGDLPDADVKPPENVLFVCKLNPVTTDEDLEIIFSRFGPIQCCEIIRDWKTGESLCYAFIEFEKVEDCEKAYFKMDNVLIDDRRIHVDFSQSVSKIKWKGKGGKYTKDDFKAYEKDLDSRSKLTLKDKVKPKQEYPSQKKKNLKIQMKSIMLLFFPPFLLVLCFCAYKQSEKLQSPKYTPEEVSHTNHSNQPPETPRQNFIPFLCYRVTRCCNPVTQSLLPAN | Function: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
EC: 5.2.1.8
Subcellular Location: Nucleus
Sequence Length: 449
Sequence Mass (Da): 51452
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A0A4R6TXL9 | MFSDLRENHPNVPGKLITFCGVDGSGKSTMIEKLAAYLRAKGHDVVVTMQPTPEMRELAIFKTFIYEPEKRDQIDYRALQLYMLADRLQHSKEVIEPALAKGAYVVCDRYIFTMLSTLLTRGHRPEPWMNEIISYILRPDAAFIMDVDLKSSIQRIKQRRSFEDSYVERDHLKKSLHAYRDVGKMFKAHMLNSSSLPIEEASHQVFSIVDEL | 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: 212
Sequence Mass (Da): 24525
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A0A4W4DN10 | MIAAMCLTLVGLIGAAASTGMPMWRVTAFIQENIIVMETRWEGLWMNCFRQANIRMQCKVYDSLLYLPPELQASRGLMCCSVALAFIGLIISIAGMKCTDQNRLKALLIVIAGVMQIMAAICVFIPVSWTAHVIIQDFYNPLLLDAQRRELGEALYIGWVTGAFLFLSGVVFLCCRSTLNSDPLGPGIQVDVTLTSTTYLNIVSNQRVTKSSRC | 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: 214
Sequence Mass (Da): 23610
Location Topology: Multi-pass membrane protein
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A0A0J1FS96 | MLHTLAVLVENHPGVLIKVAGLFARRAYNIESLTVCQTEDPEVSRMTIVVAGDDQVIEQVRNQLSKLVVVHSVVDLTEKSVVDRELALVRIPINSETRSEVFQTVDVFRGRVVDMGRSNITVELTGDIDKIDAFVHALRPYGLLELVRTGKIAIMRSEA | Pathway: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 1/4.
Function: Catalyzes the conversion of 2 pyruvate molecules into acetolactate in the first common step of the biosynthetic pathway of the branched-amino acids such as leucine, isoleucine, and valine.
EC: 2.2.1.6
Catalytic Activity: H(+) + 2 pyruvate = (2S)-2-acetolactate + CO2
Sequence Length: 159
Sequence Mass (Da): 17675
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A0A496P1H6 | MIKFYKYQGTGNDFIMIDNRNQSFPKNDVDLVKKMCDRRFGIGADGLILLENHESLDFQMVYYNSDGNESTMCGNGGRCIVAFAHFLNVFENKAKFNAIDGLHEAEINGNVVKLKMIDVPEIVKISTDYQLNTGSPHFVRYVEDVQNLDVYKNGYEIRNSEPYK | Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; DL-2,6-diaminopimelate from LL-2,6-diaminopimelate: step 1/1.
EC: 5.1.1.7
Catalytic Activity: (2S,6S)-2,6-diaminoheptanedioate = meso-2,6-diaminoheptanedioate
Sequence Length: 164
Sequence Mass (Da): 18795
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A0A5C7VDV3 | MTTTALHTPKQAARWLREHVRGQLQADSRRVGPGDGFIAWPGAATDGRRYVGAALAQGASACLVEQAGVEAFGFDQPEVATHAHLKAATGPIAAAYYEAPSEALNVVAITGTNGKTSTAWWLAWALSKAELPALAPCALVGTLGMGLPSALQATGMTTPDPVLLQQRFRAFVDAGVKSCAIEASSIGIVERRLDGTAIRVAVFTNFTQDHLDYHGSMQAYWQAKAELFDWPGLQAAVINIDDPRGAELVQRAEARGLDVWTVSCQGPARLRATDFGYGAHGLDWVLREGERAESLRTALVGEYNVANLMCVLGALRALGLDLAQAVAACTDLPPVPGRMERIDLARAPLAVIDYAHTPDAVDKALQALRPLSQKRAGRLWCVLGCGGNRDAAKRPLMAAAAERGADRVVLTSDNPRDEDPLAIIAAMRAGLQHEGAVAVQPDRAEAIALALAQAAPEDVVLIAGKGHEDYQEVRGQRRAFSDQAEARRALARRGPAAGPAA | PTM: Carboxylation is probably crucial for Mg(2+) binding and, consequently, for the gamma-phosphate positioning of ATP.
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Catalyzes the addition of meso-diaminopimelic acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan.
EC: 6.3.2.13
Subcellular Location: Cytoplasm
Catalytic Activity: ATP + meso-2,6-diaminoheptanedioate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-2,6-diaminoheptanedioate
Sequence Length: 501
Sequence Mass (Da): 53062
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A0A069D210 | MQKFEARTTRQDSAKKQRPGGKKPKQSKRMRIIIAVIGLLLVIGIGYAVYYHAEVTNYSALDSSSKREQQIEIKSGTSTKAIATDLKNKGVIRSDKAFLHYIDVKNVAELKAGYYLLSPAMSLSTITTKLSAGGSPYPLNGKGAVTVREGENAEAIAKEVAVETNFSAKEFLAALNDTSFLNRLKAAYPGLLDDAVNAQNVRYKLEGYLYPATYEVKNAANVRQIINQMVAADYEKMSPYFDQIKQSGMTVQQVMTLASLVEREGTSQDNRGIIAGVFLNRIKVNMPLASDVAVKYALDTDKANLSDADVKVNSPYNLYANTGFGPGPFDSPTVSSVEAVLNPKDQDKGYLFFVANLKTGEIYYSKTYDDQLKNTSKVQSANNAAGAASKSSK | 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: 393
Sequence Mass (Da): 42864
Location Topology: Single-pass membrane protein
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A0A484BL28 | MTFKKLLFVCMGNSCSSPMAETIMQTLMVKTSLYWEVDSAALRTWNIGRRPHKLCLKVLREHGLRSDHFCRLLTVQDFYYFDYIIAMNEHIFKELLLWADANRILDTSHVIMLGAYGKNGKSPTIIDLSPARKLKAFRNAYYQIKDCCKELILGEQVSIVRYNVPSTDDDDEENAYQVKNMSHGDSTEGPDSPYSLVAPCHKSSSKNSVSPCSVCSQLLSMERSLLPQTLDAAWSASGLGPRFEAQASGNGSVLDNVLPDMAHLVNPYWSRFAPMDATMSKILGLFTLAIMIISCCGNGVVVYIFGGTKSLRTPANLLVLNLAFSDFCMMASQSPVMLVNFYYETWVLGPLWCDIYAVCGSMFGCVSIWSMCMIAFDRYNVIVKGINGTPMTIKLSIMKILFIWLMATFWTIMPLIGWSSYVPEGNLTACSIDYMTRQWNPRSYLITYSIFVYYVPLFLICYSYWFIIAAVAAHEKAMREQAKKMNVKSLRSSEDCDKSAEGKLAKVALTTISLWFMAWTPYLVICYFGLFKIEGLTPLTTIWGATFAKTSAVYNPIVYGISHPKYRLVLKEKCPFCVCGNTDEPKPDAPAGDTETTSEAESKA | Function: Visual pigments are the light-absorbing molecules that mediate vision. They consist of an apoprotein, opsin, covalently linked to cis-retinal.
Subcellular Location: Membrane
Sequence Length: 604
Sequence Mass (Da): 67826
Location Topology: Multi-pass membrane protein
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Subsets and Splits