ID   NUOA_SYNC1              Reviewed;         141 AA.
AC   Q3A826;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 1.
DT   25-MAY-2022, entry version 88.
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=Pcar_0205;
OS   Syntrophotalea carbinolica (strain DSM 2380 / NBRC 103641 / GraBd1)
OS   (Pelobacter carbinolicus).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC   Syntrophotaleaceae; Syntrophotalea.
OX   NCBI_TaxID=338963;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 2380 / NBRC 103641 / GraBd1;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Chertkov O., Schmutz J., Larimer F.,
RA   Land M., Kyrpides N., Ivanova N., Richardson P.;
RT   "Complete sequence of Pelobacter carbinolicus DSM 2380.";
RL   Submitted (OCT-2005) 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 14 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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000142; ABA87466.1; -; Genomic_DNA.
DR   RefSeq; WP_011339866.1; NC_007498.2.
DR   AlphaFoldDB; Q3A826; -.
DR   SMR; Q3A826; -.
DR   STRING; 338963.Pcar_0205; -.
DR   EnsemblBacteria; ABA87466; ABA87466; Pcar_0205.
DR   KEGG; pca:Pcar_0205; -.
DR   eggNOG; COG0838; Bacteria.
DR   HOGENOM; CLU_119549_2_0_7; -.
DR   OMA; CGVDPVG; -.
DR   OrthoDB; 1748431at2; -.
DR   Proteomes; UP000002534; 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;
KW   Reference proteome; Translocase; Transmembrane; Transmembrane helix;
KW   Transport; Ubiquinone.
FT   CHAIN           1..141
FT                   /note="NADH-quinone oxidoreductase subunit A"
FT                   /id="PRO_0000362711"
FT   TRANSMEM        24..44
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01394"
FT   TRANSMEM        77..97
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01394"
FT   TRANSMEM        106..126
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01394"
SQ   SEQUENCE   141 AA;  15606 MW;  DF855709210CFBC8 CRC64;
     MVSEHISTQQ VGPDALFSPL GWDLLALALY VALACIIVVS LLLAARFLGH RSRTPLKNLP
     YECGVEPTGP ARPGYPVPFY LTAIFFVVFD VEVAFIASWA VAYDLLGWAG LAQIAFFIIT
     LLVALIYLWR RGALDWGPQR R