ID   NUOA_PECCC              Reviewed;         146 AA.
AC   O85273;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   16-JUN-2009, entry version 49.
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;
OS   Pectobacterium carotovorum subsp. carotovorum (Erwinia carotovora
OS   subsp. carotovora).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Pectobacterium.
OX   NCBI_TaxID=555;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=SCRI 193;
RX   MEDLINE=98305692; PubMed=9643539;
RX   DOI=10.1046/j.1365-2958.1998.00825.x;
RA   Harris S.J., Shih Y.L., Bentley S.D., Salmond G.P.C.;
RT   "The hexA gene of Erwinia carotovora encodes a LysR homologue and
RT   regulates motility and the expression of multiple virulence
RT   determinants.";
RL   Mol. Microbiol. 28:705-717(1998).
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 (By similarity).
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 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane
CC       protein (By similarity).
CC   -!- SIMILARITY: Belongs to the complex I subunit 3 family.
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DR   EMBL; AF057063; AAC38640.1; -; Genomic_DNA.
DR   BRENDA; 1.6.99.5; 290410.
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; Membrane; NAD; Oxidoreductase;
KW   Quinone; Transmembrane; Transport; Ubiquinone.
FT   CHAIN         1    146       NADH-quinone oxidoreductase subunit A.
FT                                /FTId=PRO_0000117869.
FT   TRANSMEM     14     34       Potential.
FT   TRANSMEM     68     88       Potential.
FT   TRANSMEM     96    116       Potential.
SQ   SEQUENCE   146 AA;  16156 MW;  D6B016B39D292AA6 CRC64;
     MSTTTEILAH HWAFGLFLII AVGLCVFMLT GGFLLGGRAK GRAKNVPYES GIDSVGSARL
     RLSAKFYLVA MFFVIFDVEA LYLYAWAVSI KESGWIGFIE ATIFILVLLA GLIYLVRVGA
     LDWTPVRSKR QVVKSDIINT TNNHPQ
//