NUOC_NOCFA
ID NUOC_NOCFA Reviewed; 253 AA.
AC Q5YWC9;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=NADH-quinone oxidoreductase subunit C {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 {ECO:0000255|HAMAP-Rule:MF_01357};
DE AltName: Full=NDH-1 subunit C {ECO:0000255|HAMAP-Rule:MF_01357};
GN Name=nuoC {ECO:0000255|HAMAP-Rule:MF_01357}; OrderedLocusNames=NFA_26650;
OS Nocardia farcinica (strain IFM 10152).
OC Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Nocardia.
OX NCBI_TaxID=247156;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IFM 10152;
RX PubMed=15466710; DOI=10.1073/pnas.0406410101;
RA Ishikawa J., Yamashita A., Mikami Y., Hoshino Y., Kurita H., Hotta K.,
RA Shiba T., Hattori M.;
RT "The complete genomic sequence of Nocardia farcinica IFM 10152.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:14925-14930(2004).
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 a
CC menaquinone. 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 membrane {ECO:0000255|HAMAP-Rule:MF_01357};
CC Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_01357};
CC 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; AP006618; BAD57512.1; -; Genomic_DNA.
DR RefSeq; WP_011209197.1; NC_006361.1.
DR AlphaFoldDB; Q5YWC9; -.
DR SMR; Q5YWC9; -.
DR STRING; 247156.NFA_26650; -.
DR EnsemblBacteria; BAD57512; BAD57512; NFA_26650.
DR GeneID; 61133406; -.
DR KEGG; nfa:NFA_26650; -.
DR eggNOG; COG0852; Bacteria.
DR HOGENOM; CLU_042628_4_0_11; -.
DR OMA; RFELCTG; -.
DR BioCyc; NFAR247156:NFA_RS13335-MON; -.
DR Proteomes; UP000006820; 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 Pfam; PF00329; Complex1_30kDa; 1.
DR SUPFAM; SSF143243; SSF143243; 1.
DR TIGRFAMs; TIGR01961; NuoC_fam; 1.
PE 3: Inferred from homology;
KW Cell membrane; Membrane; NAD; Quinone; Reference proteome; Translocase;
KW Transport.
FT CHAIN 1..253
FT /note="NADH-quinone oxidoreductase subunit C"
FT /id="PRO_0000358153"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 234..253
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 253 AA; 27984 MW; C4B61EDC4157AD7C CRC64;
MSPDTPRGGD LHPPEPDAAA TAGPEGTPPD TEPAAEVIGV RHGMFGIRGT GDTSGYGRLV
RPVTLPGGTA PPYGGWFDEV VDRLRTALEN SGTPFGSALE KIVVFRGELT LHVRREHLVT
VARLLRDDPA LRFELCLGVN GVHYPDDAGR ELHAVYPLRS ITHNRLLRVE TCAPDTDPHI
PSLFEVYPTT DWHERETYDF FGILFDGHPS LTRITMPDDW RGHPQRKDYP LGGIPVEYKG
ARIPPPDERR AYS