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NUOC2_RHIE6
ID   NUOC2_RHIE6             Reviewed;         187 AA.
AC   B3PY58;
DT   16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 1.
DT   25-MAY-2022, entry version 67.
DE   RecName: Full=NADH-quinone oxidoreductase subunit C 2 {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 2 {ECO:0000255|HAMAP-Rule:MF_01357};
DE   AltName: Full=NDH-1 subunit C 2 {ECO:0000255|HAMAP-Rule:MF_01357};
GN   Name=nuoC2 {ECO:0000255|HAMAP-Rule:MF_01357};
GN   OrderedLocusNames=RHECIAT_CH0003634;
OS   Rhizobium etli (strain CIAT 652).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX   NCBI_TaxID=491916;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CIAT 652;
RA   Gonzalez V., Acosta J.L., Santamaria R.I., Bustos P.,
RA   Hernandez-Gonzalez I.L., Fernandez J.L., Diaz R., Flores M., Mora J.,
RA   Palacios R., Davila G.;
RT   "Genome diversity and DNA divergence of Rhizobium etli.";
RL   Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
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; CP001074; ACE92579.1; -; Genomic_DNA.
DR   RefSeq; WP_012485039.1; NC_010994.1.
DR   AlphaFoldDB; B3PY58; -.
DR   SMR; B3PY58; -.
DR   EnsemblBacteria; ACE92579; ACE92579; RHECIAT_CH0003634.
DR   KEGG; rec:RHECIAT_CH0003634; -.
DR   eggNOG; COG0852; Bacteria.
DR   HOGENOM; CLU_042628_6_2_5; -.
DR   OMA; KDIFRGP; -.
DR   Proteomes; UP000008817; 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; Translocase;
KW   Transport; Ubiquinone.
FT   CHAIN           1..187
FT                   /note="NADH-quinone oxidoreductase subunit C 2"
FT                   /id="PRO_0000358180"
FT   REGION          153..187
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   187 AA;  21655 MW;  41E241A76FF66976 CRC64;
     MSVEPSLNRA PIMERFGDTI EDLGTAHGID VFAVPPERIV EFCRFLKEHP AMQFNFLSDI
     CGVDHYPETP RFEAVYHLYS LPNRWRVRIK CRLGDPPEVP SVTGVWRTAN WHEREAWDMY
     GIRFAGHPDL RRIYMWEGFE GFPQRKDFPL RGYKDKLNPF GAEGPPPTQP DLATRDIPQG
     RPSTPES
 
 
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