NUOA_ECOL6
ID NUOA_ECOL6 Reviewed; 147 AA.
AC P0AFC4; P33597; P77159;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 90.
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}; OrderedLocusNames=c2829;
OS Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=199310;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFT073 / ATCC 700928 / UPEC;
RX PubMed=12471157; DOI=10.1073/pnas.252529799;
RA Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA Donnenberg M.S., Blattner F.R.;
RT "Extensive mosaic structure revealed by the complete genome sequence of
RT uropathogenic Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
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. {ECO:0000255|HAMAP-Rule:MF_01394}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a quinone + 5 H(+)(in) + NADH = a quinol + 4 H(+)(out) +
CC NAD(+); Xref=Rhea:RHEA:57888, ChEBI:CHEBI:15378, ChEBI:CHEBI:24646,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:132124;
CC 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 {ECO:0000255|HAMAP-Rule:MF_01394}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_01394}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_01394}.
CC -!- SIMILARITY: Belongs to the complex I subunit 3 family.
CC {ECO:0000255|HAMAP-Rule:MF_01394}.
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DR EMBL; AE014075; AAN81283.1; -; Genomic_DNA.
DR RefSeq; WP_000062997.1; NC_004431.1.
DR AlphaFoldDB; P0AFC4; -.
DR SMR; P0AFC4; -.
DR STRING; 199310.c2829; -.
DR EnsemblBacteria; AAN81283; AAN81283; c2829.
DR GeneID; 66673829; -.
DR KEGG; ecc:c2829; -.
DR eggNOG; COG0838; Bacteria.
DR HOGENOM; CLU_119549_2_0_6; -.
DR OMA; CGVDPVG; -.
DR BioCyc; ECOL199310:C2829-MON; -.
DR Proteomes; UP000001410; Chromosome.
DR GO; GO:0016021; C:integral component of 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 Gene3D; 1.20.58.1610; -; 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; PTHR11058; 1.
DR Pfam; PF00507; Oxidored_q4; 1.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Membrane; NAD; Quinone; Translocase;
KW Transmembrane; Transmembrane helix; Transport; Ubiquinone.
FT CHAIN 1..147
FT /note="NADH-quinone oxidoreductase subunit A"
FT /id="PRO_0000117864"
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"
SQ SEQUENCE 147 AA; 16457 MW; 1F9E0804B2B0D1B5 CRC64;
MSMSTSTEVI AHHWAFAIFL IVAIGLCCLM LVGGWFLGGR ARARSKNVPF ESGIDSVGSA
RLRLSAKFYL VAMFFVIFDV EALYLFAWST SIRESGWVGF VEAAIFIFVL LAGLVYLVRI
GALDWTPARS RRERMNPETN SIANRQR
