ID   NQO1_PARDE              Reviewed;         431 AA.
AC   P29913;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   25-NOV-2008, entry version 55.
DE   RecName: Full=NADH-quinone oxidoreductase chain 1;
DE            EC=1.6.99.5;
DE   AltName: Full=NADH dehydrogenase I, chain 1;
DE   AltName: Full=NDH-1, chain 1;
GN   Name=nqo1;
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 1-37.
RC   STRAIN=ATCC 13543 / NRRL B-3784;
RX   MEDLINE=91274292; PubMed=1905152; DOI=10.1021/bi00240a012;
RA   Xu X., Matsuno-Yagi A., Yagi T.;
RT   "The NADH-binding subunit of the energy-transducing NADH-ubiquinone
RT   oxidoreductase of Paracoccus denitrificans: gene cloning and deduced
RT   primary structure.";
RL   Biochemistry 30:6422-6428(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-8, AND PROTEIN SEQUENCE OF 1-37
RP   AND 194-203.
RC   STRAIN=ATCC 13543 / NRRL B-3784;
RX   MEDLINE=91363357; PubMed=1909571; DOI=10.1021/bi00099a027;
RA   Xu X., Matsuno-Yagi A., Yagi T.;
RT   "Characterization of the 25-kilodalton subunit of the energy-
RT   transducing NADH-ubiquinone oxidoreductase of Paracoccus
RT   denitrificans: sequence similarity to the 24-kilodalton subunit of the
RT   flavoprotein fraction of mammalian complex I.";
RL   Biochemistry 30:8678-8684(1991).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 416-431.
RX   MEDLINE=92296779; PubMed=1605643; DOI=10.1016/0003-9861(92)90542-5;
RA   Xu X., Matsuno-Yagi A., Yagi T.;
RT   "Structural features of the 66-kDa subunit of the energy-transducing
RT   NADH-ubiquinone oxidoreductase (NDH-1) of Paracoccus denitrificans.";
RL   Arch. Biochem. Biophys. 296:40-48(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   -!- COFACTOR: Binds 1 FMN (Potential).
CC   -!- COFACTOR: Binds 1 4Fe-4S cluster (Potential).
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 51 kDa subunit family.
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DR   EMBL; M64432; AAA25585.1; -; Genomic_DNA.
DR   PIR; A39588; A39588.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:InterPro.
DR   GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
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; IPR001949; NADH-ubq_OxRdtase_51KDa_CS.
DR   InterPro; IPR011538; NADH-UbQ_OxRdtase_51KDa_su.
DR   InterPro; IPR011537; NADH-UbQ_OxRdtase_F_su.
DR   Pfam; PF01512; Complex1_51K; 1.
DR   TIGRFAMs; TIGR01959; nuoF_fam; 1.
DR   PROSITE; PS00644; COMPLEX1_51K_1; 1.
DR   PROSITE; PS00645; COMPLEX1_51K_2; 1.
PE   1: Evidence at protein level;
KW   4Fe-4S; Cell inner membrane; Cell membrane; Direct protein sequencing;
KW   Flavoprotein; FMN; Iron; Iron-sulfur; Membrane; Metal-binding; NAD;
KW   Oxidoreductase; Quinone; Ubiquinone.
FT   CHAIN         1    431       NADH-quinone oxidoreductase chain 1.
FT                                /FTId=PRO_0000118566.
FT   NP_BIND      54     63       NAD (By similarity).
FT   NP_BIND     167    214       FMN (By similarity).
FT   METAL       346    346       Iron-sulfur (4Fe-4S) (Potential).
FT   METAL       349    349       Iron-sulfur (4Fe-4S) (Potential).
FT   METAL       352    352       Iron-sulfur (4Fe-4S) (Potential).
FT   METAL       392    392       Iron-sulfur (4Fe-4S) (Potential).
SQ   SEQUENCE   431 AA;  47191 MW;  AA25C5A0A7570048 CRC64;
     MLNDQDRIFT NLYGMGDRSL AGAKKRGHWD GTAAIIQRGR DKIIDEMKAS GLRGRGGAGF
     PTGMKWSFMP KESDGRPSYL VINADESEPA TCKDREIMRH DPHTLIEGAL IASFAMGAHA
     AYIYIRGEFI REREALQAAI DECYDAGLLG RNAAGSGWDF DLYLHHGAGA YICGEETALL
     ESLEGKKGMP RMKPPFPAGA GLYGCPTTVN NVESIAVVPT ILRRGAEWFA SFGRPNNAGV
     KLFGLTGHVN TPCVVEEAMS IPMRELIEKH GGGIRGGWKN LKAVIPGGAS CPVLTAEQCE
     NAIMDYDGMR DVRSSFGTAC MIVMDQSTDV VKAIWRLSKF FKHESCGQCT PCREGTGWMM
     RVMERLVRGD AEVEEIDMLF DVTKQVEGHT ICALGDAAAW PIQGLIRNFR EEIEDRIKAK
     RTGRMGAMAA E
//