ID   NUOCD_BUCAP             Reviewed;         597 AA.
AC   Q8K9Y5;
DT   08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   16-JUN-2009, entry version 47.
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=BUsg_149;
OS   Buchnera aphidicola subsp. Schizaphis graminum.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Buchnera.
OX   NCBI_TaxID=98794;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   MEDLINE=22084549; PubMed=12089438; DOI=10.1126/science.1071278;
RA   Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S.,
RA   Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.;
RT   "50 million years of genomic stasis in endosymbiotic bacteria.";
RL   Science 296:2376-2379(2002).
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; AE013218; AAM67717.1; -; Genomic_DNA.
DR   RefSeq; NP_660506.1; -.
DR   GeneID; 1005966; -.
DR   GenomeReviews; AE013218_GR; BUsg_149.
DR   KEGG; bas:BUsg149; -.
DR   HOGENOM; Q8K9Y5; -.
DR   OMA; Q8K9Y5; PPTWEGH.
DR   BioCyc; BAPH198804:BUSG149-MON; -.
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   CHAIN         1    597       NADH-quinone oxidoreductase subunit C/D.
FT                                /FTId=PRO_0000118682.
FT   REGION        1    187       NADH dehydrogenase I subunit C (By
FT                                similarity).
FT   REGION      211    597       NADH dehydrogenase I subunit D (By
FT                                similarity).
SQ   SEQUENCE   597 AA;  69343 MW;  CC39F0373D2F387A CRC64;
     MIDENKKKNT NLNKNEYEEK SILKDLFHFF GKDFCVVQDT CIDFPVIWIN KSLLLKVGKF
     LSSSPKPYNM LFDLHGVDER FRLNRLNLPE ADFSIFYHLI SIERNSDILI KVPLLKDDLN
     VSTFISLFPN ANWYERETWE MFGIIFDQHP NLTHIIMPNE WKGFPLRKDY PARATEHESF
     FLDEQKEDLE MENLRFKPEL WGMKRKNDNV DFMFLNLGPN HPSAHGAFRI VLQLDGENIV
     DCVPDIGYHH RGAEKMAERQ SWHSYIPYTD RIEYLGGCVN EMPYVLAVEK LANISVPEKV
     EVIRVMLSEL FRINSHLLYI STFIQDVGCM TPVFLAFTDR QKIYDLIEAI TGARMHPAWF
     RIGGVAHDLP KGWNVLLKEF LEWMPKRLKY YVQLALENPI LIRRSKGIAQ YNQKEALQWG
     VTGSGLRSTG LDLDVRKWRP YSGYQNYTFE IPIGQGISDC YSRVIIKVEE IYQSLSILKQ
     CLKNMPEGPF KSDHPLTTPP PKERVLKDID TMITHFLQVS WGPVIPANES FQMIEATKGI
     NSYYLISDGG TMSYRTRIRT PSFPHLQQIP SVIRGSLISD LIVYLGSIDF VMSDVDR
//