NUOC1_RHIME
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 25-MAY-2022, entry version 115.
DE RecName: Full=NADH-quinone oxidoreductase subunit C 1 {ECO:0000255|HAMAP-Rule:MF_01357};
DE EC=7.1.1.- {ECO:0000255|HAMAP-Rule:MF_01357};
DE AltName: Full=NADH dehydrogenase I subunit C 1 {ECO:0000255|HAMAP-Rule:MF_01357};
DE AltName: Full=NDH-1 subunit C 1 {ECO:0000255|HAMAP-Rule:MF_01357};
GN Name=nuoC1 {ECO:0000255|HAMAP-Rule:MF_01357}; Synonyms=nuoC;
GN OrderedLocusNames=R01266; ORFNames=SMc01914;
OS Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium
OS meliloti).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX NCBI_TaxID=266834;
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 stationary
RT phase survival shows a reduction in the energy charge due to its defect in
RT 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 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., Pohl T.,
RA Portetelle D., Puehler A., Purnelle B., Ramsperger U., Renard C.,
RA Thebault P., Vandenbol M., Weidner S., Galibert F.;
RT "Analysis of the chromosome sequence of the legume symbiont Sinorhizobium
RT meliloti strain 1021.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:9877-9882(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1021;
RX PubMed=11474104; DOI=10.1126/science.1060966;
RA Galibert F., Finan T.M., Long S.R., Puehler A., Abola P., Ampe F.,
RA Barloy-Hubler F., Barnett M.J., Becker A., Boistard P., Bothe G.,
RA Boutry M., Bowser L., Buhrmester J., Cadieu E., Capela D., Chain P.,
RA Cowie A., Davis R.W., Dreano S., Federspiel N.A., Fisher R.F., Gloux S.,
RA Godrie T., Goffeau A., Golding B., Gouzy J., Gurjal M., Hernandez-Lucas I.,
RA Hong A., Huizar L., Hyman R.W., Jones T., Kahn D., Kahn M.L., Kalman S.,
RA Keating D.H., Kiss E., Komp C., Lelaure V., Masuy D., Palm C., Peck M.C.,
RA Pohl T.M., Portetelle D., Purnelle B., Ramsperger U., Surzycki R.,
RA Thebault P., Vandenbol M., Vorhoelter F.J., Weidner S., Wells D.H.,
RA Wong K., Yeh K.-C., Batut J.;
RT "The composite genome of the legume symbiont Sinorhizobium meliloti.";
RL Science 293:668-672(2001).
CC -!- FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur
CC (Fe-S) centers, to quinones in the respiratory chain. The immediate
CC electron acceptor for the enzyme in this species is believed to be
CC ubiquinone. Couples the redox reaction to proton translocation (for
CC every two electrons transferred, four hydrogen ions are translocated
CC across the cytoplasmic membrane), and thus conserves the redox energy
CC in a proton gradient. {ECO:0000255|HAMAP-Rule:MF_01357}.
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, ChEBI:CHEBI:24646,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:132124;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01357};
CC -!- SUBUNIT: NDH-1 is composed of 14 different subunits. Subunits NuoB, C,
CC D, E, F, and G constitute the peripheral sector of the complex.
CC {ECO:0000255|HAMAP-Rule:MF_01357}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_01357}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_01357}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_01357}.
CC -!- SIMILARITY: Belongs to the complex I 30 kDa subunit family.
CC {ECO:0000255|HAMAP-Rule:MF_01357}.
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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; NC_003047.1.
DR RefSeq; WP_010969144.1; NC_003047.1.
DR AlphaFoldDB; O68854; -.
DR SMR; O68854; -.
DR STRING; 266834.SMc01914; -.
DR PRIDE; O68854; -.
DR EnsemblBacteria; CAC45845; CAC45845; SMc01914.
DR GeneID; 61602727; -.
DR KEGG; sme:SMc01914; -.
DR PATRIC; fig|266834.11.peg.2680; -.
DR eggNOG; COG0852; Bacteria.
DR HOGENOM; CLU_042628_2_1_5; -.
DR OMA; MERETYD; -.
DR Proteomes; UP000001976; Chromosome.
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 Gene3D; 3.30.460.80; -; 1.
DR HAMAP; MF_01357; NDH1_NuoC; 1.
DR InterPro; IPR010218; NADH_DH_suC.
DR InterPro; IPR037232; NADH_quin_OxRdtase_su_C/D-like.
DR InterPro; IPR001268; NADH_UbQ_OxRdtase_30kDa_su.
DR InterPro; IPR020396; NADH_UbQ_OxRdtase_CS.
DR Pfam; PF00329; Complex1_30kDa; 1.
DR SUPFAM; SSF143243; SSF143243; 1.
DR TIGRFAMs; TIGR01961; NuoC_fam; 1.
DR PROSITE; PS00542; COMPLEX1_30K; 1.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Membrane; NAD; Quinone;
KW Reference proteome; Translocase; Transport; Ubiquinone.
FT CHAIN 1..201
FT /note="NADH-quinone oxidoreductase subunit C 1"
FT /id="PRO_0000118674"
FT CONFLICT 15
FT /note="A -> G (in Ref. 1; AAC12756)"
FT /evidence="ECO:0000305"
FT CONFLICT 94
FT /note="G -> R (in Ref. 1; AAC12756)"
FT /evidence="ECO:0000305"
FT CONFLICT 97
FT /note="D -> E (in Ref. 2; CAB51622)"
FT /evidence="ECO:0000305"
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
