ID   NQO11_PARDE             Reviewed;         101 AA.
AC   P29923;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   04-NOV-2008, entry version 57.
DE   RecName: Full=NADH-quinone oxidoreductase chain 11;
DE            EC=1.6.99.5;
DE   AltName: Full=NADH dehydrogenase I, chain 11;
DE   AltName: Full=NDH-1, chain 11;
GN   Name=nqo11;
OS   Paracoccus denitrificans.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Paracoccus.
OX   NCBI_TaxID=266;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 13543 / NRRL B-3784;
RX   MEDLINE=93136200; PubMed=8422400; DOI=10.1021/bi00054a030;
RA   Xu X., Matsuno-Yagi A., Yagi T.;
RT   "DNA sequencing of the seven remaining structural genes of the gene
RT   cluster encoding the energy-transducing NADH-quinone oxidoreductase of
RT   Paracoccus denitrificans.";
RL   Biochemistry 32:968-981(1993).
RN   [2]
RP   SUBCELLULAR LOCATION, AND TOPOLOGY.
RX   PubMed=11914084; DOI=10.1021/bi025525d;
RA   Kao M.-C., Di Bernardo S., Matsuno-Yagi A., Yagi T.;
RT   "Characterization of the membrane domain Nqo11 subunit of the proton-
RT   translocating NADH-quinone oxidoreductase of Paracoccus
RT   denitrificans.";
RL   Biochemistry 41:4377-4384(2002).
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.
CC   -!- CATALYTIC ACTIVITY: NADH + quinone = NAD(+) + quinol.
CC   -!- SUBUNIT: NDH-1 is composed of at least 14 different subunits, nqo1
CC       to nqo14. The complex has a L-shaped structure, with the
CC       hydrophobic arm (subunits nqo7, nqo8, nqo10 to nqo14) embedded in
CC       the inner membrane and the hydrophilic peripheral arm (subunits
CC       nqo1 to nqo6, nqo9) protruding into the bacterial cytoplasm. The
CC       hydrophilic domain contains all the redox centers.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane
CC       protein.
CC   -!- SIMILARITY: Belongs to the complex I subunit 4L family.
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DR   EMBL; L02354; AAA25597.1; -; Genomic_DNA.
DR   PIR; G45456; G45456.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0050136; F:NADH dehydrogenase (quinone) activity; IEA:EC.
DR   GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW.
DR   InterPro; IPR001133; NADH_ubQ_OxRdtase_4L.
DR   PANTHER; PTHR11434; Oxidored_4L; 1.
DR   Pfam; PF00420; Oxidored_q2; 1.
DR   ProDom; PD002107; NADH_dh_ubiq1; 1.
DR   ProDom; PD000359; Oxidred4L; 1.
PE   1: Evidence at protein level;
KW   Cell inner membrane; Cell membrane; Membrane; NAD; Oxidoreductase;
KW   Quinone; Transmembrane; Ubiquinone.
FT   CHAIN         1    101       NADH-quinone oxidoreductase chain 11.
FT                                /FTId=PRO_0000118522.
FT   TOPO_DOM      1      3       Periplasmic (Probable).
FT   TRANSMEM      4     24       Potential.
FT   TOPO_DOM     25     29       Cytoplasmic (Probable).
FT   TRANSMEM     30     50       Potential.
FT   TOPO_DOM     51     64       Periplasmic (Probable).
FT   TRANSMEM     65     85       Potential.
FT   TOPO_DOM     86    101       Cytoplasmic.
SQ   SEQUENCE   101 AA;  10856 MW;  A8061FD86A8B9AB8 CRC64;
     MIGLTHYLVV GAILFVTGIF GIFVNRKNVI VILMSIELML LAVNINFVAF STHLGDLAGQ
     VFTMFVLTVA AAEAAIGLAI LVVFFRNRGT IAVEDVNVMK G
//