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Database: UniProt
Entry: P29921
LinkDB: P29921
Original site: P29921 
ID   NQO9_PARDE              Reviewed;         163 AA.
AC   P29921;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   16-JAN-2019, entry version 107.
DE   RecName: Full=NADH-quinone oxidoreductase subunit 9;
DE            EC=7.1.1.-;
DE   AltName: Full=NADH dehydrogenase I subunit 9;
DE   AltName: Full=NDH-1 subunit 9;
GN   Name=nqo9 {ECO:0000303|PubMed:8422400};
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 / NRC 449;
RX   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:
CC       Reaction=a quinone + 5 H(+)(in) + NADH = a quinol + 4 H(+)(out) +
CC         NAD(+); Xref=Rhea:RHEA:57888, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:24646, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC         ChEBI:CHEBI:132124;
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000250};
CC       Note=Binds 2 [4Fe-4S] clusters per subunit. {ECO:0000250};
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 23 kDa subunit family.
CC       {ECO:0000305}.
DR   EMBL; L02354; AAA25593.1; -; Genomic_DNA.
DR   PIR; D45456; D45456.
DR   ProteinModelPortal; P29921; -.
DR   TCDB; 3.D.1.2.1; the h(+) or na(+)-translocating nadh dehydrogenase (ndh) family.
DR   eggNOG; ENOG4105P3U; Bacteria.
DR   eggNOG; COG1143; LUCA.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0050136; F:NADH dehydrogenase (quinone) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW.
DR   HAMAP; MF_01351; NDH1_NuoI; 1.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR   InterPro; IPR010226; NADH_quinone_OxRdtase_chainI.
DR   PANTHER; PTHR10849; PTHR10849; 1.
DR   Pfam; PF12838; Fer4_7; 1.
DR   TIGRFAMs; TIGR01971; NuoI; 1.
DR   PROSITE; PS00198; 4FE4S_FER_1; 2.
DR   PROSITE; PS51379; 4FE4S_FER_2; 2.
PE   3: Inferred from homology;
KW   4Fe-4S; Cell inner membrane; Cell membrane; Iron; Iron-sulfur;
KW   Membrane; Metal-binding; NAD; Quinone; Repeat; Translocase;
KW   Ubiquinone.
FT   CHAIN         1    163       NADH-quinone oxidoreductase subunit 9.
FT                                /FTId=PRO_0000118720.
FT   DOMAIN       54     84       4Fe-4S ferredoxin-type 1.
FT   DOMAIN       94    123       4Fe-4S ferredoxin-type 2.
FT   METAL        64     64       Iron-sulfur 1 (4Fe-4S). {ECO:0000250}.
FT   METAL        67     67       Iron-sulfur 1 (4Fe-4S). {ECO:0000250}.
FT   METAL        70     70       Iron-sulfur 1 (4Fe-4S). {ECO:0000250}.
FT   METAL        74     74       Iron-sulfur 2 (4Fe-4S). {ECO:0000250}.
FT   METAL       103    103       Iron-sulfur 2 (4Fe-4S). {ECO:0000250}.
FT   METAL       106    106       Iron-sulfur 2 (4Fe-4S). {ECO:0000250}.
FT   METAL       109    109       Iron-sulfur 2 (4Fe-4S). {ECO:0000250}.
FT   METAL       113    113       Iron-sulfur 1 (4Fe-4S). {ECO:0000250}.
SQ   SEQUENCE   163 AA;  18960 MW;  71163CEA824B2475 CRC64;
     MAFDFARATK YFLMWDFIKG FGLGMRYFVS PKPTLNYPHE KGPLSPRFRG EHALRRYPNG
     EERCIACKLC EAVCPAQAIT IDAERREDGS RRTTRYDIDM TKCIYCGFCQ EACPVDAIVE
     GPNFEYATET REELFYDKQK LLANGERWEA EIARNLQLDA PYR
//
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