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   02-SEP-2026, entry version 134.
DE   RecName: Full=NADH-quinone oxidoreductase subunit A {ECO:0000255|HAMAP-Rule:MF_01394};
DE            EC=7.1.1.- {ECO:0000255|HAMAP-Rule:MF_01394};
DE   AltName: Full=NADH dehydrogenase I subunit A {ECO:0000255|HAMAP-Rule:MF_01394};
DE   AltName: Full=NDH-1 subunit A {ECO:0000255|HAMAP-Rule:MF_01394};
DE   AltName: Full=NUO1 {ECO:0000255|HAMAP-Rule:MF_01394};
GN   Name=nuoA {ECO:0000255|HAMAP-Rule:MF_01394};
GN   OrderedLocusNames=b2288, JW2283;
OS   Escherichia coli (strain K12).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Enterobacterales; Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=K12 / AN387;
RX   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 oxidoreductase
RT   in Escherichia coli. Organization of the 14 genes and relationship between
RT   the derived proteins and subunits of 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   PubMed=9205837; DOI=10.1093/dnares/4.2.91;
RA   Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T.,
RA   Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K.,
RA   Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T., Oyama S.,
RA   Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H.,
RA   Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.;
RT   "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12
RT   genome corresponding to 50.0-68.8 min on the linkage map and analysis of
RT   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   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., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(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 MG1655
RT   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-sulfur
CC       (Fe-S) centers, to quinones in the respiratory chain. The immediate
CC       electron acceptor for the enzyme in this species is believed to be
CC       ubiquinone. Couples the redox reaction to proton translocation (for
CC       every two electrons transferred, four hydrogen ions are translocated
CC       across the cytoplasmic membrane), and thus conserves the redox energy
CC       in a proton gradient.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a quinone + NADH + 5 H(+)(in) = a quinol + NAD(+) + 4
CC         H(+)(out); Xref=Rhea:RHEA:57888, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:24646, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC         ChEBI:CHEBI:132124; Evidence={ECO:0000255|HAMAP-Rule:MF_01394};
CC   -!- SUBUNIT: NDH-1 is composed of 13 different subunits. Subunits NuoA, H,
CC       J, K, L, M, N constitute the membrane sector of the complex.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_01394, ECO:0000269|PubMed:15919996}; Multi-pass membrane
CC       protein {ECO:0000255|HAMAP-Rule:MF_01394, ECO:0000269|PubMed:15919996}.
CC   -!- SIMILARITY: Belongs to the complex I subunit 3 family.
CC       {ECO:0000255|HAMAP-Rule:MF_01394}.
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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; NP_416791.3; NC_000913.3.
DR   RefSeq; WP_000062997.1; NZ_CP009789.1.
DR   PDB; 7NYH; EM; 3.60 A; A=1-147.
DR   PDB; 7NYR; EM; 3.30 A; A=1-147.
DR   PDB; 7NYU; EM; 3.80 A; A=1-147.
DR   PDB; 7NYV; EM; 3.70 A; A=1-147.
DR   PDB; 7P61; EM; 3.20 A; A=1-147.
DR   PDB; 7P62; EM; 3.60 A; A=1-147.
DR   PDB; 7P63; EM; 3.40 A; A=1-147.
DR   PDB; 7P64; EM; 2.50 A; A=1-147.
DR   PDB; 7P69; EM; 3.00 A; A=1-147.
DR   PDB; 7P7C; EM; 2.40 A; A=1-147.
DR   PDB; 7P7E; EM; 2.70 A; A=1-147.
DR   PDB; 7P7J; EM; 2.70 A; A=1-147.
DR   PDB; 7P7K; EM; 3.10 A; A=1-147.
DR   PDB; 7P7L; EM; 3.00 A; A=1-147.
DR   PDB; 7P7M; EM; 3.20 A; A=1-147.
DR   PDB; 7Z7R; EM; 3.36 A; A=1-147.
DR   PDB; 7Z7S; EM; 2.40 A; A=1-147.
DR   PDB; 7Z7T; EM; 3.10 A; A=1-147.
DR   PDB; 7Z7V; EM; 2.29 A; A=1-147.
DR   PDB; 7Z80; EM; 2.93 A; A=1-147.
DR   PDB; 7Z83; EM; 2.88 A; A=1-147.
DR   PDB; 7Z84; EM; 2.87 A; A=1-147.
DR   PDB; 7ZC5; EM; 3.00 A; A=1-147.
DR   PDB; 7ZCI; EM; 2.69 A; A=1-147.
DR   PDB; 9Q8I; EM; 2.35 A; A=1-147.
DR   PDB; 9TAJ; EM; 3.00 A; A=1-147.
DR   PDB; 9TAK; EM; 2.80 A; A=1-147.
DR   PDB; 9TAL; EM; 2.66 A; A=1-147.
DR   PDB; 9TAM; EM; 2.96 A; A=1-147.
DR   PDB; 9TAO; EM; 2.61 A; A=1-147.
DR   AlphaFoldDB; P0AFC3; -.
DR   EMDB; EMD-12652; -.
DR   EMDB; EMD-12653; -.
DR   EMDB; EMD-12654; -.
DR   EMDB; EMD-12655; -.
DR   EMDB; EMD-52895; -.
DR   SMR; P0AFC3; -.
DR   BioGRID; 4262974; 132.
DR   ComplexPortal; CPX-243; Respiratory chain complex I.
DR   DIP; DIP-59257N; -.
DR   FunCoup; P0AFC3; 265.
DR   IntAct; P0AFC3; 5.
DR   STRING; 511145.b2288; -.
DR   TCDB; 3.D.1.1.1; the h+ or na+-translocating nadh dehydrogenase (ndh) family.
DR   jPOST; P0AFC3; -.
DR   PaxDb; 511145-b2288; -.
DR   EnsemblBacteria; AAC75348; AAC75348; b2288.
DR   GeneID; 89517123; -.
DR   GeneID; 93774886; -.
DR   GeneID; 946764; -.
DR   KEGG; ecj:JW2283; -.
DR   KEGG; eco:b2288; -.
DR   KEGG; ecoc:C3026_12765; -.
DR   PATRIC; fig|1411691.4.peg.4448; -.
DR   EchoBASE; EB2007; -.
DR   eggNOG; COG0838; Bacteria.
DR   HOGENOM; CLU_119549_2_0_6; -.
DR   InParanoid; P0AFC3; -.
DR   OMA; YVYAFLY; -.
DR   OrthoDB; 9791970at2; -.
DR   PhylomeDB; P0AFC3; -.
DR   BioCyc; EcoCyc:NUOA-MONOMER; -.
DR   BioCyc; MetaCyc:NUOA-MONOMER; -.
DR   PRO; PR:P0AFC3; -.
DR   Proteomes; UP000000625; Chromosome.
DR   AbasyAtlas; P0AFC3; -.
DR   GO; GO:0016020; C:membrane; IDA:ComplexPortal.
DR   GO; GO:0030964; C:NADH dehydrogenase complex; IDA:EcoliWiki.
DR   GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR   GO; GO:0045271; C:respiratory chain complex I; IDA:EcoCyc.
DR   GO; GO:0050136; F:NADH dehydrogenase (quinone) (non-electrogenic) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IMP:EcoCyc.
DR   GO; GO:0022904; P:respiratory electron transport chain; IDA:ComplexPortal.
DR   DisProt; DP03504; -.
DR   FunFam; 1.20.58.1610:FF:000003; NADH-quinone oxidoreductase subunit A; 1.
DR   Gene3D; 1.20.58.1610; NADH:ubiquinone/plastoquinone oxidoreductase, chain 3; 1.
DR   HAMAP; MF_01394; NDH1_NuoA; 1.
DR   InterPro; IPR023043; NAD(P)H_OxRDtase_bac/plastid.
DR   InterPro; IPR000440; NADH_UbQ/plastoQ_OxRdtase_su3.
DR   InterPro; IPR038430; NDAH_ubi_oxred_su3_sf.
DR   PANTHER; PTHR11058:SF21; NADH-QUINONE OXIDOREDUCTASE SUBUNIT A; 1.
DR   PANTHER; PTHR11058; NADH-UBIQUINONE OXIDOREDUCTASE CHAIN 3; 1.
DR   Pfam; PF00507; Oxidored_q4; 1.
DR   PDBsum; 7NYH; -.
DR   PDBsum; 7NYR; -.
DR   PDBsum; 7NYU; -.
DR   PDBsum; 7NYV; -.
DR   PDBsum; 7P61; -.
DR   PDBsum; 7P62; -.
DR   PDBsum; 7P63; -.
DR   PDBsum; 7P64; -.
DR   PDBsum; 7P69; -.
DR   PDBsum; 7P7C; -.
DR   PDBsum; 7P7E; -.
DR   PDBsum; 7P7J; -.
DR   PDBsum; 7P7K; -.
DR   PDBsum; 7P7L; -.
DR   PDBsum; 7P7M; -.
DR   PDBsum; 7Z7R; -.
DR   PDBsum; 7Z7S; -.
DR   PDBsum; 7Z7T; -.
DR   PDBsum; 7Z7V; -.
DR   PDBsum; 7Z80; -.
DR   PDBsum; 7Z83; -.
DR   PDBsum; 7Z84; -.
DR   PDBsum; 7ZC5; -.
DR   PDBsum; 7ZCI; -.
DR   PDBsum; 9Q8I; -.
DR   PDBsum; 9TAJ; -.
DR   PDBsum; 9TAK; -.
DR   PDBsum; 9TAL; -.
DR   PDBsum; 9TAM; -.
DR   PDBsum; 9TAO; -.
PE   1: Evidence at protein level;
KW   3D-structure; Cell inner membrane; Cell membrane; Membrane; NAD; Quinone;
KW   Reference proteome; Translocase; Transmembrane; Transmembrane helix;
KW   Transport; Ubiquinone.
FT   CHAIN           1..147
FT                   /note="NADH-quinone oxidoreductase subunit A"
FT                   /id="PRO_0000117862"
FT   TRANSMEM        16..36
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01394"
FT   TRANSMEM        68..88
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01394"
FT   TRANSMEM        98..118
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01394"
FT   CONFLICT        60
FT                   /note="A -> G (in Ref. 1; CAA48360)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        82..91
FT                   /note="ALYLFAWSTS -> GAVSVRMVLL (in Ref. 1; CAA48360)"
FT                   /evidence="ECO:0000305"
FT   HELIX           7..36
FT                   /evidence="ECO:0007829|PDB:7Z7V"
FT   STRAND          44..48
FT                   /evidence="ECO:0007829|PDB:7Z7V"
FT   HELIX           63..65
FT                   /evidence="ECO:0007829|PDB:7P7J"
FT   HELIX           67..89
FT                   /evidence="ECO:0007829|PDB:7Z7V"
FT   HELIX           92..119
FT                   /evidence="ECO:0007829|PDB:7Z7V"
FT   TURN            120..123
FT                   /evidence="ECO:0007829|PDB:7Z7V"
FT   HELIX           128..130
FT                   /evidence="ECO:0007829|PDB:7Z7S"
SQ   SEQUENCE   147 AA;  16457 MW;  1F9E0804B2B0D1B5 CRC64;
     MSMSTSTEVI AHHWAFAIFL IVAIGLCCLM LVGGWFLGGR ARARSKNVPF ESGIDSVGSA
     RLRLSAKFYL VAMFFVIFDV EALYLFAWST SIRESGWVGF VEAAIFIFVL LAGLVYLVRI
     GALDWTPARS RRERMNPETN SIANRQR
//