NUOC_PARP8
ID NUOC_PARP8 Reviewed; 200 AA.
AC B2JDM6;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 25-MAY-2022, entry version 72.
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=Bphy_2007;
OS Paraburkholderia phymatum (strain DSM 17167 / CIP 108236 / LMG 21445 /
OS STM815) (Burkholderia phymatum).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=391038;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17167 / CIP 108236 / LMG 21445 / STM815;
RX PubMed=25197461; DOI=10.4056/sigs.4861021;
RA Moulin L., Klonowska A., Caroline B., Booth K., Vriezen J.A., Melkonian R.,
RA James E.K., Young J.P., Bena G., Hauser L., Land M., Kyrpides N., Bruce D.,
RA Chain P., Copeland A., Pitluck S., Woyke T., Lizotte-Waniewski M.,
RA Bristow J., Riley M.;
RT "Complete genome sequence of Burkholderia phymatum STM815(T), a broad host
RT range and efficient nitrogen-fixing symbiont of Mimosa species.";
RL Stand. Genomic Sci. 9:763-774(2014).
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; CP001043; ACC71186.1; -; Genomic_DNA.
DR RefSeq; WP_012401395.1; NZ_CADFGH010000002.1.
DR AlphaFoldDB; B2JDM6; -.
DR SMR; B2JDM6; -.
DR STRING; 391038.Bphy_2007; -.
DR EnsemblBacteria; ACC71186; ACC71186; Bphy_2007.
DR KEGG; bph:Bphy_2007; -.
DR eggNOG; COG0852; Bacteria.
DR HOGENOM; CLU_042628_2_1_4; -.
DR OMA; MERETYD; -.
DR OrthoDB; 1735902at2; -.
DR Proteomes; UP000001192; Chromosome 1.
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..200
FT /note="NADH-quinone oxidoreductase subunit C"
FT /id="PRO_0000358069"
SQ SEQUENCE 200 AA; 23007 MW; 893749FD387E9CF7 CRC64;
MASKLETLKA NLEAAFGGRL TSITESIGEL TIVVKADDFL EVATRLRDDA KLHFEQLIDL
CGIDYQTYGE GAYDGPRFAA VLHLLSITNN WRLRVRVFAP DDDVPLIPSV VEIWNSANWY
EREAFDLYGI VFEGHPDLRR ILTDYGFIGH PFRKDFPVSG YVEMRYDPEE KRVVYQPVTI
EPREITPRVI REDRYGGLKH