ID   NQO14_PARDE             Reviewed;         499 AA.
AC   P29926;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   25-NOV-2008, entry version 49.
DE   RecName: Full=NADH-quinone oxidoreductase chain 14;
DE            EC=1.6.99.5;
DE   AltName: Full=NADH dehydrogenase I, chain 14;
DE   AltName: Full=NDH-1, chain 14;
GN   Name=nqo14;
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).
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 2 family.
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DR   EMBL; L02354; AAA25600.1; -; Genomic_DNA.
DR   PIR; A47751; A47751.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
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:0042773; P:ATP synthesis coupled electron transport; IEA:InterPro.
DR   InterPro; IPR003916; NADHub_OxRdtase_5.
DR   InterPro; IPR001750; Oxidored_q1.
DR   InterPro; IPR010096; Prot-transl_NADH-Q_OxRdtase_N.
DR   Pfam; PF00361; Oxidored_q1; 1.
DR   PRINTS; PR01434; NADHDHGNASE5.
DR   TIGRFAMs; TIGR01770; NDH_I_N; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Membrane; NAD; Oxidoreductase;
KW   Quinone; Transmembrane; Ubiquinone.
FT   CHAIN         1    499       NADH-quinone oxidoreductase chain 14.
FT                                /FTId=PRO_0000117686.
FT   TRANSMEM      9     29       Potential.
FT   TRANSMEM     37     57       Potential.
FT   TRANSMEM     76     96       Potential.
FT   TRANSMEM    104    124       Potential.
FT   TRANSMEM    126    146       Potential.
FT   TRANSMEM    161    181       Potential.
FT   TRANSMEM    196    216       Potential.
FT   TRANSMEM    235    255       Potential.
FT   TRANSMEM    269    289       Potential.
FT   TRANSMEM    301    321       Potential.
FT   TRANSMEM    325    345       Potential.
FT   TRANSMEM    369    389       Potential.
FT   TRANSMEM    402    422       Potential.
FT   TRANSMEM    446    466       Potential.
SQ   SEQUENCE   499 AA;  52535 MW;  F116A0CEA09ED72A CRC64;
     MTSLDFSTIL PEVVLAGYAL AALMAGAYLG KDRLARTLLW VTVAAFLVVA AMVGLGNHVD
     GAAFHGMFID DGFSRFAKVV TLVAAAGVLA MSADYMQRRN MLRFEFPIIV ALAVLGMMFM
     VSAGDLLTLY MGLELQSLAL YVVAAMRRDS VRSSEAGLKY FVLGSLSSGL LLYGASLVYG
     FAGTTGFEGI ISTIEAGHLS LGVLFGLVFM LVGLSFKVSA VPFHMWTPDV YEGSPTPVTA
     FFATAPKVAA MALIARLVFD AFGHVIGDWS QIVAALAVMS MFLGSIAGIG QTNIKRLMAY
     SSIAHMGFAL VGLAAGTAIG VQNMLLYMTI YAVMNIGTFA FILSMERDGV PVTDLAALNR
     FAWTDPVKAL AMLVLMFSLA GVPPTLGFFA KFGVLTAAVD AGMGWLAVLG VIASVIGAFY
     YLRIVYYMYF GGESEGMTSR MGAVQYLALM VPALAMLVGA ISMFGVDSAA GRAAETLVGP
     VAAIEQPAEA AQAEPVQGE
//