ID NUOA_ECOLI Reviewed; 147 AA. AC P0AFC3; P33597; P77159; DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot. DT 20-DEC-2005, sequence version 1. DT 16-JUN-2009, entry version 35. DE RecName: Full=NADH-quinone oxidoreductase subunit A; DE EC=1.6.99.5; DE AltName: Full=NADH dehydrogenase I subunit A; DE AltName: Full=NDH-1 subunit A; DE AltName: Full=NUO1; GN Name=nuoA; OrderedLocusNames=b2288, JW2283; OS Escherichia coli (strain K12). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=83333; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=K12 / AN387; RX MEDLINE=93389724; PubMed=7690854; DOI=10.1006/jmbi.1993.1488; RA Weidner U., Geier S., Ptock A., Friedrich T., Leif H., Weiss H.; RT "The gene locus of the proton-translocating NADH: ubiquinone RT oxidoreductase in Escherichia coli. Organization of the 14 genes and RT relationship between the derived proteins and subunits of RT mitochondrial complex I."; RL J. Mol. Biol. 233:109-122(1993). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RX MEDLINE=97349980; PubMed=9205837; DOI=10.1093/dnares/4.2.91; RA Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., RA Itoh T., Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., RA Mizobuchi K., Mori H., Nakade S., Nakamura Y., Nashimoto H., RA Oshima T., Oyama S., Saito N., Sampei G., Satoh Y., Sivasundaram S., RA Tagami H., Takahashi H., Takeda J., Takemoto K., Uehara K., Wada C., RA Yamagata S., Horiuchi T.; RT "Construction of a contiguous 874-kb sequence of the Escherichia coli- RT K12 genome corresponding to 50.0-68.8 min on the linkage map and RT analysis of its sequence features."; RL DNA Res. 4:91-113(1997). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / MG1655 / ATCC 47076; RX MEDLINE=97426617; PubMed=9278503; DOI=10.1126/science.277.5331.1453; RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., RA Mau B., Shao Y.; RT "The complete genome sequence of Escherichia coli K-12."; RL Science 277:1453-1474(1997). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RX PubMed=16738553; DOI=10.1038/msb4100049; RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.; RT "Highly accurate genome sequences of Escherichia coli K-12 strains RT MG1655 and W3110."; RL Mol. Syst. Biol. 2:E1-E5(2006). RN [5] RP SUBCELLULAR LOCATION. RC STRAIN=K12 / MG1655 / ATCC 47076; RX PubMed=15919996; DOI=10.1126/science.1109730; RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.; RT "Global topology analysis of the Escherichia coli inner membrane RT proteome."; RL Science 308:1321-1323(2005). CC -!- FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron- CC sulfur (Fe-S) centers, to quinones in the respiratory chain. The CC immediate electron acceptor for the enzyme in this species is CC believed to be ubiquinone. Couples the redox reaction to proton CC translocation (for every two electrons transferred, four hydrogen CC ions are translocated across the cytoplasmic membrane), and thus CC conserves the redox energy in a proton gradient. CC -!- CATALYTIC ACTIVITY: NADH + quinone = NAD(+) + quinol. CC -!- SUBUNIT: NDH-1 is composed of 13 different subunits. Subunits CC nuoA, H, J, K, L, M, N constitute the membrane sector of the CC complex. CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane CC protein. CC -!- SIMILARITY: Belongs to the complex I subunit 3 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X68301; CAA48360.1; -; Genomic_DNA. DR EMBL; U00096; AAC75348.1; -; Genomic_DNA. DR EMBL; AP009048; BAA16123.1; -; Genomic_DNA. DR PIR; F65000; F65000. DR RefSeq; AP_002886.1; -. DR RefSeq; NP_416791.3; -. DR TCDB; 3.D.1.1.1; proton-translocating NADH dehydrogenase (NDH) family. DR GeneID; 946764; -. DR GenomeReviews; AP009048_GR; JW2283. DR GenomeReviews; U00096_GR; b2288. DR KEGG; ecj:JW2283; -. DR KEGG; eco:b2288; -. DR EchoBASE; EB2007; -. DR EcoGene; EG12082; nuoA. DR HOGENOM; P0AFC3; -. DR OMA; P0AFC3; FIEATIF. DR BioCyc; EcoCyc:NUOA-MON; -. DR BioCyc; MetaCyc:NUOA-MON; -. DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:InterPro. DR GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW. DR GO; GO:0055114; P:oxidation reduction; IEA:HAMAP. DR GO; GO:0019684; P:photosynthesis, light reaction; IEA:HAMAP. DR GO; GO:0006810; P:transport; IEA:UniProtKB-KW. DR HAMAP; MF_01394; -; 1. DR InterPro; IPR000440; NADH_UbQ/plastoQ_OxRdtase_su3. DR PANTHER; PTHR11058; Oxidored_q4; 1. DR Pfam; PF00507; Oxidored_q4; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; Membrane; NAD; KW Oxidoreductase; Quinone; Transmembrane; Transport; Ubiquinone. FT CHAIN 1 147 NADH-quinone oxidoreductase subunit A. FT /FTId=PRO_0000117862. FT TRANSMEM 16 36 Potential. FT TRANSMEM 68 88 Potential. FT TRANSMEM 98 118 Potential. FT CONFLICT 60 60 A -> G (in Ref. 1; CAA48360). FT CONFLICT 82 91 ALYLFAWSTS -> GAVSVRMVLL (in Ref. 1; FT CAA48360). SQ SEQUENCE 147 AA; 16457 MW; 1F9E0804B2B0D1B5 CRC64; MSMSTSTEVI AHHWAFAIFL IVAIGLCCLM LVGGWFLGGR ARARSKNVPF ESGIDSVGSA RLRLSAKFYL VAMFFVIFDV EALYLFAWST SIRESGWVGF VEAAIFIFVL LAGLVYLVRI GALDWTPARS RRERMNPETN SIANRQR //