ID   NUOC1_RHIME             Reviewed;         201 AA.
AC   O68854;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2000, sequence version 2.
DT   16-JUN-2009, entry version 57.
DE   RecName: Full=NADH-quinone oxidoreductase subunit C 1;
DE            EC=1.6.99.5;
DE   AltName: Full=NADH dehydrogenase I subunit C 1;
DE   AltName: Full=NDH-1 subunit C 1;
GN   Name=nuoC1; Synonyms=nuoC; OrderedLocusNames=R01266;
GN   ORFNames=SMc01914;
OS   Rhizobium meliloti (Sinorhizobium meliloti).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=382;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=RCR2011 / SU47;
RA   Schmidt R., Uhde C., Nagel A., Puehler A., Selbitschka W.;
RT   "Sinorhizobium meliloti mutant strain SP10 which is impaired in
RT   stationary phase survival shows a reduction in the energy charge due
RT   to its defect in the energy-conserving NADH dehydrogenase.";
RL   Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=41;
RA   Putnoky P., Jady B., Chellapilla K.P., Barta F., Kiss E.;
RT   "Rhizobium meliloti carries two sets of nuo genes.";
RL   Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1021;
RX   MEDLINE=21396507; PubMed=11481430; DOI=10.1073/pnas.161294398;
RA   Capela D., Barloy-Hubler F., Gouzy J., Bothe G., Ampe F., Batut J.,
RA   Boistard P., Becker A., Boutry M., Cadieu E., Dreano S., Gloux S.,
RA   Godrie T., Goffeau A., Kahn D., Kiss E., Lelaure V., Masuy D.,
RA   Pohl T., Portetelle D., Puehler A., Purnelle B., Ramsperger U.,
RA   Renard C., Thebault P., Vandenbol M., Weidner S., Galibert F.;
RT   "Analysis of the chromosome sequence of the legume symbiont
RT   Sinorhizobium meliloti strain 1021.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:9877-9882(2001).
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 14 different subunits. Subunits
CC       nuoB, C, D, 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: Belongs to the complex I 30 kDa subunit family.
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DR   EMBL; AF055637; AAC12756.1; -; Genomic_DNA.
DR   EMBL; AJ245398; CAB51622.1; -; Genomic_DNA.
DR   EMBL; AL591688; CAC45845.1; -; Genomic_DNA.
DR   RefSeq; NP_385372.1; -.
DR   GeneID; 1232914; -.
DR   GenomeReviews; AL591688_GR; R01266.
DR   KEGG; sme:SMc01914; -.
DR   NMPDR; fig|266834.1.peg.2560; -.
DR   HOGENOM; O68854; -.
DR   OMA; O68854; KQEFRNF.
DR   BioCyc; SMEL266834:SMC01914-MON; -.
DR   BRENDA; 1.6.99.5; 142.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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:HAMAP.
DR   GO; GO:0019684; P:photosynthesis, light reaction; IEA:HAMAP.
DR   GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
DR   HAMAP; MF_01357; -; 1.
DR   InterPro; IPR010218; NADH_DH_csu.
DR   InterPro; IPR001268; NADH_UbQ_OxRdtase_30kDa_su.
DR   Pfam; PF00329; Complex1_30kDa; 1.
DR   ProDom; PD001581; Complex1_30K; 1.
DR   TIGRFAMs; TIGR01961; NuoC_fam; 1.
DR   PROSITE; PS00542; COMPLEX1_30K; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Complete proteome; Membrane; NAD;
KW   Oxidoreductase; Quinone; Transport; Ubiquinone.
FT   CHAIN         1    201       NADH-quinone oxidoreductase subunit C 1.
FT                                /FTId=PRO_0000118674.
FT   CONFLICT     15     15       A -> G (in Ref. 1; AAC12756).
FT   CONFLICT     94     94       G -> R (in Ref. 1; AAC12756).
FT   CONFLICT     97     97       D -> E (in Ref. 2; CAB51622).
SQ   SEQUENCE   201 AA;  23074 MW;  CAC177C10EB57E09 CRC64;
     MSEALNELAS YLREARGALI ADAEVKYGEL TVTAKAENLI ALLTFLRDDV QCGFVSFIDV
     CGVDYPQRPD RFDVVYHLLS PRQNQRVRVK VATGENDPVP SATSVFPGAD WFEREAYDMY
     GILFTGHPDL RRILTDYGFE GYPLRKDFPL TGFVEVRYDN EAKRVVYEPV ELKQEFRNFD
     FLSPWEGTEY VLPGDEKARP R
//