ID   NUOCD_BACFR             Reviewed;         530 AA.
AC   Q64Y08;
DT   16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, 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=BF0867;
OS   Bacteroides fragilis (strain YCH46).
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=295405;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YCH46;
RX   PubMed=15466707; DOI=10.1073/pnas.0404172101;
RA   Kuwahara T., Yamashita A., Hirakawa H., Nakayama H., Toh H., Okada N.,
RA   Kuhara S., Hattori M., Hayashi T., Ohnishi Y.;
RT   "Genomic analysis of Bacteroides fragilis reveals extensive DNA inversions
RT   regulating cell surface adaptation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:14919-14924(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 (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; AP006841; BAD47618.1; -; Genomic_DNA.
DR   RefSeq; WP_005785050.1; NZ_UYXF01000001.1.
DR   RefSeq; YP_098152.1; NC_006347.1.
DR   AlphaFoldDB; Q64Y08; -.
DR   SMR; Q64Y08; -.
DR   STRING; 295405.BF0867; -.
DR   EnsemblBacteria; BAD47618; BAD47618; BF0867.
DR   KEGG; bfr:BF0867; -.
DR   PATRIC; fig|295405.11.peg.873; -.
DR   HOGENOM; CLU_015134_3_2_10; -.
DR   OMA; IMGTSME; -.
DR   Proteomes; UP000002197; 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; Translocase; Transport.
FT   CHAIN           1..530
FT                   /note="NADH-quinone oxidoreductase subunit C/D"
FT                   /id="PRO_0000358616"
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