NUOCD_BACFN
ID NUOCD_BACFN Reviewed; 530 AA.
AC Q5LH50;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-JUN-2005, sequence version 1.
DT 25-MAY-2022, entry version 100.
DE RecName: Full=NADH-quinone oxidoreductase subunit C/D {ECO:0000255|HAMAP-Rule:MF_01397};
DE EC=7.1.1.- {ECO:0000255|HAMAP-Rule:MF_01397};
DE AltName: Full=NADH dehydrogenase I subunit C/D {ECO:0000255|HAMAP-Rule:MF_01397};
DE AltName: Full=NDH-1 subunit C/D {ECO:0000255|HAMAP-Rule:MF_01397};
GN Name=nuoC {ECO:0000255|HAMAP-Rule:MF_01397}; Synonyms=nuoCD, nuoD;
GN OrderedLocusNames=BF0790;
OS Bacteroides fragilis (strain ATCC 25285 / DSM 2151 / CCUG 4856 / JCM 11019
OS / NCTC 9343 / Onslow).
OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=272559;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25285 / DSM 2151 / CCUG 4856 / JCM 11019 / NCTC 9343 / Onslow;
RX PubMed=15746427; DOI=10.1126/science.1107008;
RA Cerdeno-Tarraga A.-M., Patrick S., Crossman L.C., Blakely G., Abratt V.,
RA Lennard N., Poxton I., Duerden B., Harris B., Quail M.A., Barron A.,
RA Clark L., Corton C., Doggett J., Holden M.T.G., Larke N., Line A., Lord A.,
RA Norbertczak H., Ormond D., Price C., Rabbinowitsch E., Woodward J.,
RA Barrell B.G., Parkhill J.;
RT "Extensive DNA inversions in the B. fragilis genome control variable gene
RT expression.";
RL Science 307:1463-1465(2005).
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 (By similarity). {ECO:0000250}.
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_01397};
CC -!- SUBUNIT: NDH-1 is composed of 13 different subunits. Subunits NuoB, CD,
CC E, F, and G constitute the peripheral sector of the complex.
CC {ECO:0000255|HAMAP-Rule:MF_01397}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_01397}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_01397}; Cytoplasmic side {ECO:0000250}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the complex I 30 kDa
CC subunit family. {ECO:0000255|HAMAP-Rule:MF_01397}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the complex I 49 kDa
CC subunit family. {ECO:0000255|HAMAP-Rule:MF_01397}.
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DR EMBL; CR626927; CAH06536.1; -; Genomic_DNA.
DR RefSeq; WP_005785050.1; NC_003228.3.
DR AlphaFoldDB; Q5LH50; -.
DR SMR; Q5LH50; -.
DR STRING; 272559.BF9343_0755; -.
DR EnsemblBacteria; CAH06536; CAH06536; BF9343_0755.
DR KEGG; bfs:BF9343_0755; -.
DR eggNOG; COG0649; Bacteria.
DR eggNOG; COG0852; Bacteria.
DR HOGENOM; CLU_015134_3_2_10; -.
DR OMA; IMGTSME; -.
DR OrthoDB; 473681at2; -.
DR Proteomes; UP000006731; Chromosome.
DR GO; GO:0030964; C:NADH dehydrogenase complex; IEA:InterPro.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:InterPro.
DR GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW.
DR Gene3D; 1.10.645.10; -; 1.
DR Gene3D; 3.30.460.80; -; 1.
DR HAMAP; MF_01397; NDH1_NuoCD_2; 1.
DR HAMAP; MF_01358; NDH1_NuoD; 1.
DR InterPro; IPR001135; NADH_Q_OxRdtase_suD.
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 InterPro; IPR026662; NDH-1_subunit_CD.
DR InterPro; IPR022885; NDH1_su_D/H.
DR InterPro; IPR029014; NiFe-Hase_large.
DR PANTHER; PTHR11993; PTHR11993; 1.
DR Pfam; PF00329; Complex1_30kDa; 1.
DR Pfam; PF00346; Complex1_49kDa; 2.
DR SUPFAM; SSF143243; SSF143243; 1.
DR SUPFAM; SSF56762; SSF56762; 1.
DR PROSITE; PS00542; COMPLEX1_30K; 1.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Membrane; Multifunctional enzyme; NAD;
KW Quinone; Reference proteome; Translocase; Transport.
FT CHAIN 1..530
FT /note="NADH-quinone oxidoreductase subunit C/D"
FT /id="PRO_0000358617"
FT REGION 1..144
FT /note="NADH dehydrogenase I subunit C"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01397"
FT REGION 171..530
FT /note="NADH dehydrogenase I subunit D"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01397"
SQ SEQUENCE 530 AA; 60557 MW; 6EB4B14310664C10 CRC64;
MEEIKYIEPA ALHDEMLRLR NEKQMDFLES LTGMDWGVAD EGDAPNVTRG LGVVYHLEST
VTGERIAIKT STNNRETPEI PSVSDIWKAA DFNEREVFDY YGIVFIGHPD MRRLYLRNDW
VGHPMRKDNN PEKDNPLRMD NEETYDTTRE IELNPDGTYQ TQENVIFDDR EYVVNIGPQH
PATHGVMRFR VSLEGETIKK LDANCGYIHR GIEKMNESLT YPQTLALTDR LDYLGAHQNR
HALCMCIEKA MGIEVSERVK YIRTIMDELQ RIDSHLLFYS CLAMDLGALT AFFYGFRDRE
MILDMFEETC GGRLIMNYNT IGGVQADLHP NFIPRVKKFI PYLRGIIHEY HDVFTGNVIA
RQRLKGVGVL SREDAISFGC TGGTGRASGW ACDVRKRMPY GVYDKVDFKE IVYTEGDSFA
RYMVRMDEIM ESLNIIEQLI DNIPEGPIQE KMKPIIRVPE GSYYTAVEGS RGEFGVFLES
HGDKTPYRLH YRSTGLPLVS AVDTICRGAK IADLIAIGGT LDYVVPDIDR
