ID   NUOCD_SALTI             Reviewed;         596 AA.
AC   P0A1Y7; P33902;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   22-JUL-2008, sequence version 2.
DT   16-JUN-2009, entry version 30.
DE   RecName: Full=NADH-quinone oxidoreductase subunit C/D;
DE            EC=1.6.99.5;
DE   AltName: Full=NADH dehydrogenase I subunit C/D;
DE   AltName: Full=NDH-1 subunit C/D;
GN   Name=nuoC; Synonyms=nuoCD, nuoD; OrderedLocusNames=STY2556, t0538;
OS   Salmonella typhi.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=90370;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CT18;
RX   MEDLINE=21534947; PubMed=11677608; DOI=10.1038/35101607;
RA   Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J.,
RA   Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M.,
RA   Baker S., Basham D., Brooks K., Chillingworth T., Connerton P.,
RA   Cronin A., Davis P., Davies R.M., Dowd L., White N., Farrar J.,
RA   Feltwell T., Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K.,
RA   Krogh A., Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C.,
RA   Quail M.A., Rutherford K.M., Simmonds M., Skelton J., Stevens K.,
RA   Whitehead S., Barrell B.G.;
RT   "Complete genome sequence of a multiple drug resistant Salmonella
RT   enterica serovar Typhi CT18.";
RL   Nature 413:848-852(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700931 / Ty2;
RX   MEDLINE=22531367; PubMed=12644504;
RX   DOI=10.1128/JB.185.7.2330-2337.2003;
RA   Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J.,
RA   Burland V., Kodoyianni V., Schwartz D.C., Blattner F.R.;
RT   "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2
RT   and CT18.";
RL   J. Bacteriol. 185:2330-2337(2003).
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 (By similarity).
CC   -!- CATALYTIC ACTIVITY: NADH + quinone = NAD(+) + quinol.
CC   -!- SUBUNIT: NDH-1 is composed of 13 different subunits. Subunits
CC       nuoB, CD, E, F, and G constitute the peripheral sector of the
CC       complex (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane
CC       protein; Cytoplasmic side (By similarity).
CC   -!- SIMILARITY: In the N-terminal section; belongs to the complex I 30
CC       kDa subunit family.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the complex I 49
CC       kDa subunit family.
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DR   EMBL; AL627274; CAD07558.1; -; Genomic_DNA.
DR   EMBL; AE014613; AAO68244.1; -; Genomic_DNA.
DR   RefSeq; NP_456868.1; -.
DR   RefSeq; NP_804395.1; -.
DR   GeneID; 1069525; -.
DR   GeneID; 1248881; -.
DR   GenomeReviews; AE014613_GR; t0538.
DR   GenomeReviews; AL513382_GR; STY2556.
DR   KEGG; stt:t0538; -.
DR   KEGG; sty:STY2556; -.
DR   HOGENOM; P0A1Y7; -.
DR   BioCyc; SENT209261:T0538-MON; -.
DR   BioCyc; SENT220341:STY2556-MON; -.
DR   BRENDA; 1.6.99.5; 3716.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0051287; F:NAD or NADH 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:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
DR   HAMAP; MF_01359; -; 1.
DR   InterPro; IPR010219; NADH_DH_1_dsu.
DR   InterPro; IPR010218; NADH_DH_csu.
DR   InterPro; IPR001135; NADH_Q_OxRdtase_suD.
DR   InterPro; IPR001268; NADH_UbQ_OxRdtase_30kDa_su.
DR   InterPro; IPR014029; NADH_UbQ_OxRdtase_su-49kDa_CS.
DR   Pfam; PF00329; Complex1_30kDa; 1.
DR   Pfam; PF00346; Complex1_49kDa; 1.
DR   ProDom; PD001581; Complex1_30K; 1.
DR   TIGRFAMs; TIGR01961; NuoC_fam; 1.
DR   TIGRFAMs; TIGR01962; NuoD; 1.
DR   PROSITE; PS00542; COMPLEX1_30K; FALSE_NEG.
DR   PROSITE; PS00535; COMPLEX1_49K; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Complete proteome; Membrane;
KW   Multifunctional enzyme; NAD; Oxidoreductase; Quinone; Transport;
KW   Ubiquinone.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    596       NADH-quinone oxidoreductase subunit C/D.
FT                                /FTId=PRO_0000118679.
FT   REGION        2    186       NADH dehydrogenase I subunit C (By
FT                                similarity).
FT   REGION      210    596       NADH dehydrogenase I subunit D (By
FT                                similarity).
SQ   SEQUENCE   596 AA;  68402 MW;  362B1FBD9A864F46 CRC64;
     MTDLTAQDAA WSTRDHLDDP VIGELRNRFG PDAFTVQATR TGIPVVWVKR EQLLEVGDFL
     KKLPKPYVML FDLHGMDERL RTHRDGLPAA DFSVFYHLIS IERNRDIMLK VALSENDLRV
     PTFTKLFPNA NWYERETWEM FGIDIEGHPH LTRIMMPQTW EGHPLRKDYP ARATEFDPFE
     LTKAKQDLEM EALTFKPEDW GMKRGTDNED FMFLNLGPNH PSAHGAFRII LQLDGEEIVD
     CVPDIGYHHR GAEKMGERQS WHSYIPYTDR IEYLGGCVNE MPYVLAVEKL AGITVPDRVN
     VIRVMLSELF RINSHLLYIS TFIQDVGAMT PVFFAFTDRQ KIYDLVEAIT GFRMHPAWFR
     IGGVAHDLPR GWDRLLREFL EWMPKRLDSY EKAALRNTIL KGRSQGVAAY GAKEALEWGT
     TGAGLRATGI DFDVRKWRPY SGYENFDFEV PVGGGVSDCY TRVMLKVEEL RQSLRILQQC
     LDNMPEGPFK ADHPLTTPPP KERTLQHIET LITHFLQVSW GPVMPAQESF QMVEATKGIN
     SYYLTSDGST MSYRTRVRTP SFAHLQQIPS AIRGSLVSDL IVYLGSIDFV MSDVDR
//