NUOA1_PSEA7
ID NUOA1_PSEA7 Reviewed; 137 AA.
AC A6V4E9;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 25-MAY-2022, entry version 73.
DE RecName: Full=NADH-quinone oxidoreductase subunit A 1 {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 1 {ECO:0000255|HAMAP-Rule:MF_01394};
DE AltName: Full=NDH-1 subunit A 1 {ECO:0000255|HAMAP-Rule:MF_01394};
DE AltName: Full=NUO1 1 {ECO:0000255|HAMAP-Rule:MF_01394};
GN Name=nuoA1 {ECO:0000255|HAMAP-Rule:MF_01394}; OrderedLocusNames=PSPA7_2570;
OS Pseudomonas aeruginosa (strain PA7).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=381754;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PA7;
RA Dodson R.J., Harkins D., Paulsen I.T.;
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000744; ABR82089.1; -; Genomic_DNA.
DR RefSeq; WP_012075444.1; NC_009656.1.
DR AlphaFoldDB; A6V4E9; -.
DR SMR; A6V4E9; -.
DR EnsemblBacteria; ABR82089; ABR82089; PSPA7_2570.
DR KEGG; pap:PSPA7_2570; -.
DR HOGENOM; CLU_119549_2_1_6; -.
DR OMA; CGVDPVG; -.
DR OrthoDB; 1748431at2; -.
DR Proteomes; UP000001582; 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..137
FT /note="NADH-quinone oxidoreductase subunit A 1"
FT /id="PRO_0000362734"
FT TRANSMEM 14..34
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01394"
FT TRANSMEM 66..86
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01394"
FT TRANSMEM 95..115
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01394"
SQ SEQUENCE 137 AA; 14994 MW; BD6F6195E5280BF9 CRC64;
MPNPAELAAH HWGFAAFLLG VVGLLAFMLG VSALLGSKAF GRSKNEPFES GIVPTGGARL
RLSAKFYLVA MLFVIFDVEA LFLFAWSVSV RESGWAGLIE ATIFIAILLA GLVYLWRIGA
LDWAPESRRK RQAKLKQ
