Tag | Content |
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CPLM ID | CPLM-002750 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Respiratory nitrate reductase 1 alpha chain |
Protein Synonyms/Alias | Nitrate reductase A subunit alpha; Quinol-nitrate oxidoreductase subunit alpha |
Gene Name | narG |
Gene Synonyms/Alias | bisD; narC; b1224; JW1215 |
Created Date | July 27, 2013 |
Organism | Escherichia coli (strain K12) |
NCBI Taxa ID | 83333 |
Lysine Modification | Position | Peptide | Type | References |
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455 | LENVLLHKLPVKRLQ | acetylation | [1] | 686 | NPVDYTVKSLKEGSI | acetylation | [1] | 730 | KGHEFMLKYLLGTEH | acetylation | [1] | 742 | TEHGIQGKDLGQQGG | acetylation | [1] | 909 | SIGPLMEKIGNGGKG | acetylation | [1] | 1229 | FVVVRKMKNIDWLDG | acetylation | [1] |
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Reference | [1] Acetyl-Phosphate Is a Critical Determinant of Lysine Acetylation in E. coli. Weinert BT, Iesmantavicius V, Wagner SA, Schölz C, Gummesson B, Beli P, Nyström T, Choudhary C. Mol Cell. 2013 Jul 25;51(2):265-72. [ PMID: 23830618] |
Functional Description | The nitrate reductase enzyme complex allows E.coli to use nitrate as an electron acceptor during anaerobic growth. The alpha chain is the actual site of nitrate reduction. |
Sequence Annotation | DOMAIN 43 107 4Fe-4S Mo/W bis-MGD-type. METAL 50 50 Iron-sulfur (4Fe-4S); via pros nitrogen. METAL 54 54 Iron-sulfur (4Fe-4S). METAL 58 58 Iron-sulfur (4Fe-4S). METAL 93 93 Iron-sulfur (4Fe-4S). METAL 223 223 Molybdenum. |
Keyword | 3D-structure; 4Fe-4S; Cell membrane; Complete proteome; Direct protein sequencing; Electron transport; Iron; Iron-sulfur; Membrane; Metal-binding; Molybdenum; Nitrate assimilation; Oxidoreductase; Reference proteome; Transport. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 1247 AA |
Protein Sequence | MSKFLDRFRY FKQKGETFAD GHGQLLNTNR DWEDGYRQRW QHDKIVRSTH GVNCTGSCSW 60 KIYVKNGLVT WETQQTDYPR TRPDLPNHEP RGCPRGASYS WYLYSANRLK YPMMRKRLMK 120 MWREAKALHS DPVEAWASII EDADKAKSFK QARGRGGFVR SSWQEVNELI AASNVYTIKN 180 YGPDRVAGFS PIPAMSMVSY ASGARYLSLI GGTCLSFYDW YCDLPPASPQ TWGEQTDVPE 240 SADWYNSSYI IAWGSNVPQT RTPDAHFFTE VRYKGTKTVA VTPDYAEIAK LCDLWLAPKQ 300 GTDAAMALAM GHVMLREFHL DNPSQYFTDY VRRYTDMPML VMLEERDGYY AAGRMLRAAD 360 LVDALGQENN PEWKTVAFNT NGEMVAPNGS IGFRWGEKGK WNLEQRDGKT GEETELQLSL 420 LGSQDEIAEV GFPYFGGDGT EHFNKVELEN VLLHKLPVKR LQLADGSTAL VTTVYDLTLA 480 NYGLERGLND VNCATSYDDV KAYTPAWAEQ ITGVSRSQII RIAREFADNA DKTHGRSMII 540 VGAGLNHWYH LDMNYRGLIN MLIFCGCVGQ SGGGWAHYVG QEKLRPQTGW QPLAFALDWQ 600 RPARHMNSTS YFYNHSSQWR YETVTAEELL SPMADKSRYT GHLIDFNVRA ERMGWLPSAP 660 QLGTNPLTIA GEAEKAGMNP VDYTVKSLKE GSIRFAAEQP ENGKNHPRNL FIWRSNLLGS 720 SGKGHEFMLK YLLGTEHGIQ GKDLGQQGGV KPEEVDWQDN GLEGKLDLVV TLDFRLSSTC 780 LYSDIILPTA TWYEKDDMNT SDMHPFIHPL SAAVDPAWEA KSDWEIYKAI AKKFSEVCVG 840 HLGKETDIVT LPIQHDSAAE LAQPLDVKDW KKGECDLIPG KTAPHIMVVE RDYPATYERF 900 TSIGPLMEKI GNGGKGIAWN TQSEMDLLRK LNYTKAEGPA KGQPMLNTAI DAAEMILTLA 960 PETNGQVAVK AWAALSEFTG RDHTHLALNK EDEKIRFRDI QAQPRKIISS PTWSGLEDEH 1020 VSYNAGYTNV HELIPWRTLS GRQQLYQDHQ WMRDFGESLL VYRPPIDTRS VKEVIGQKSN 1080 GNQEKALNFL TPHQKWGIHS TYSDNLLMLT LGRGGPVVWL SEADAKDLGI ADNDWIEVFN 1140 SNGALTARAV VSQRVPAGMT MMYHAQERIV NLPGSEITQQ RGGIHNSVTR ITPKPTHMIG 1200 GYAHLAYGFN YYGTVGSNRD EFVVVRKMKN IDWLDGEGND QVQESVK 1247 |
Gene Ontology | GO:0031224; C:intrinsic to membrane; IDA:EcoCyc. GO:0009325; C:nitrate reductase complex; IEA:InterPro. GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. GO:0051539; F:4 iron, 4 sulfur cluster binding; IDA:EcoCyc. GO:0009055; F:electron carrier activity; IPI:EcoCyc. GO:0030151; F:molybdenum ion binding; IDA:EcoCyc. GO:0008940; F:nitrate reductase activity; IEA:EC. GO:0016651; F:oxidoreductase activity, acting on NAD(P)H; IBA:RefGenome. GO:0009061; P:anaerobic respiration; IEP:EcoCyc. GO:0017004; P:cytochrome complex assembly; IDA:EcoCyc. GO:0022900; P:electron transport chain; IEA:UniProtKB-KW. GO:0042128; P:nitrate assimilation; IEA:UniProtKB-KW. |
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PRINTS | |