ID   NQO9_RHOMR              Reviewed;         230 AA.
AC   Q4QSC5;
DT   11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   16-JUN-2009, entry version 31.
DE   RecName: Full=NADH-quinone oxidoreductase subunit 9;
DE            EC=1.6.99.5;
DE   AltName: Full=NADH dehydrogenase I subunit 9;
DE   AltName: Full=NDH-1 subunit 9;
GN   Name=nqo9;
OS   Rhodothermus marinus (Rhodothermus obamensis).
OC   Bacteria; Bacteroidetes; Sphingobacteria; Sphingobacteriales;
OC   Rhodothermaceae; Rhodothermus.
OX   NCBI_TaxID=29549;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=PRQ 62B;
RX   PubMed=16023073; DOI=10.1016/j.bbabio.2005.06.003;
RA   Melo A.M.P., Lobo S.A.L., Sousa F.L., Fernandes A.S., Pereira M.M.,
RA   Hreggvidsson G.O., Kristjansson J.K., Saraiva L.M., Teixeira M.;
RT   "A nhaD Na+/H+ antiporter and a pcd homologues are among the
RT   Rhodothermus marinus complex I genes.";
RL   Biochim. Biophys. Acta 1709:95-103(2005).
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 menaquinone. 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 (By similarity).
CC   -!- CATALYTIC ACTIVITY: NADH + quinone = NAD(+) + quinol.
CC   -!- COFACTOR: Binds 2 4Fe-4S clusters per subunit (By similarity).
CC   -!- SUBUNIT: NDH-1 is composed of 14 different subunits. Subunits
CC       NQO7-14 constitute the membrane sector of the complex (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane
CC       protein (Potential).
CC   -!- SIMILARITY: Belongs to the complex I 23 kDa subunit family.
CC   -!- SIMILARITY: Contains 2 4Fe-4S ferredoxin-type domains.
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DR   EMBL; AY972099; AAY42993.1; -; Genomic_DNA.
DR   BRENDA; 1.6.99.5; 1132.
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:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:HAMAP.
DR   GO; GO:0050136; F:NADH dehydrogenase (quinone) activity; IEA:EC.
DR   GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:HAMAP.
DR   GO; GO:0019684; P:photosynthesis, light reaction; IEA:HAMAP.
DR   HAMAP; MF_01351; -; 1.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR001450; 4Fe4S_Fe_S_bd_subgr.
DR   InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR   InterPro; IPR010226; NADH_quinone_OxRdtase_chainI.
DR   Pfam; PF00037; Fer4; 2.
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; Oxidoreductase; Quinone; Repeat.
FT   CHAIN         1    230       NADH-quinone oxidoreductase subunit 9.
FT                                /FTId=PRO_0000245739.
FT   DOMAIN       60     93       4Fe-4S ferredoxin-type 1.
FT   DOMAIN      104    133       4Fe-4S ferredoxin-type 2.
FT   METAL        73     73       Iron-sulfur 1 (4Fe-4S) (By similarity).
FT   METAL        76     76       Iron-sulfur 1 (4Fe-4S) (By similarity).
FT   METAL        79     79       Iron-sulfur 1 (4Fe-4S) (By similarity).
FT   METAL        83     83       Iron-sulfur 2 (4Fe-4S) (By similarity).
FT   METAL       113    113       Iron-sulfur 2 (4Fe-4S) (By similarity).
FT   METAL       116    116       Iron-sulfur 2 (4Fe-4S) (By similarity).
FT   METAL       119    119       Iron-sulfur 2 (4Fe-4S) (By similarity).
FT   METAL       123    123       Iron-sulfur 1 (4Fe-4S) (By similarity).
SQ   SEQUENCE   230 AA;  27120 MW;  E951770E49179E57 CRC64;
     MPGKPVNLAS PNERKLNFWE RLYLPAVVQG LAYTWRKMRS PRYTFQYPDE LWYPPDSYRG
     RPVLVEENGR PRCVACGLCA RACPPLAISM QAKEVDDVKE REPAWFEINM LRCIYCGYCE
     EVCPEEAIVM SKEYDLTFQS RDEAIFGLEK LLVPAERLKD RLEWLDRYKD PQYGQHWEFR
     KENNLHSLKD RPFLKWLLEE EGMEELKSTH LRPEEPVAAE RSWGGVRAEG
//