ID   NQO5_PARDE              Reviewed;         207 AA.
AC   P29917;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   25-NOV-2008, entry version 53.
DE   RecName: Full=NADH-quinone oxidoreductase chain 5;
DE            EC=1.6.99.5;
DE   AltName: Full=NADH dehydrogenase I, chain 5;
DE   AltName: Full=NDH-1, chain 5;
GN   Name=nqo5;
OS   Paracoccus denitrificans.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Paracoccus.
OX   NCBI_TaxID=266;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-15.
RC   STRAIN=ATCC 13543 / NRRL B-3784;
RX   MEDLINE=92345253; PubMed=1637825; DOI=10.1021/bi00145a009;
RA   Xu X., Matsuno-Yagi A., Yagi T.;
RT   "Gene cluster of the energy-transducing NADH-quinone oxidoreductase of
RT   Paracoccus denitrificans: characterization of four structural gene
RT   products.";
RL   Biochemistry 31:6925-6932(1992).
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; Peripheral membrane
CC       protein.
CC   -!- SIMILARITY: Belongs to the complex I 30 kDa subunit family.
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DR   EMBL; M93015; AAA03037.1; ALT_SEQ; Unassigned_DNA.
DR   PIR; D42573; D42573.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:InterPro.
DR   GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW.
DR   GO; GO:0006120; P:mitochondrial electron transport, NADH to u...; IEA:InterPro.
DR   InterPro; IPR010218; NADH_DH_csu.
DR   InterPro; IPR001268; NADH_DHase_Ub_30kDa_su.
DR   Pfam; PF00329; Complex1_30kDa; 1.
DR   ProDom; PD001581; Complex1_30K; 1.
DR   TIGRFAMs; TIGR01961; NuoC_fam; 1.
DR   PROSITE; PS00542; COMPLEX1_30K; 1.
PE   1: Evidence at protein level;
KW   Cell inner membrane; Cell membrane; Direct protein sequencing;
KW   Membrane; NAD; Oxidoreductase; Quinone; Ubiquinone.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    207       NADH-quinone oxidoreductase chain 5.
FT                                /FTId=PRO_0000118668.
SQ   SEQUENCE   207 AA;  23731 MW;  070DFDEBE70FEC6D CRC64;
     MSEALSDEAL LELAEHIAVR RENDVISTQA VGELTVNATL SGVIGLIEFL RNDPNCRFST
     LIDITAVDNP ARPARFDVVY HLLSMYQNQR IRVKVQVRED ELVPSLIGVF PGANWYEREV
     FDLFGILFSG HSDLRRILTD YGFRGHPLRK DFPTTGYVEV RWSDIEKRVV YEPVNLVQEY
     RQFDFLSPWE GAKYVLPGDE KAPEAKK
//