ID   NUOCD_BACTN             Reviewed;         530 AA.
AC   Q8A0F6;
DT   16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 2.
DT   03-AUG-2022, entry version 122.
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=BT_4065;
OS   Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / JCM 5827 /
OS   CCUG 10774 / NCTC 10582 / VPI-5482 / E50).
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=226186;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 /
RC   VPI-5482 / E50;
RX   PubMed=12663928; DOI=10.1126/science.1080029;
RA   Xu J., Bjursell M.K., Himrod J., Deng S., Carmichael L.K., Chiang H.C.,
RA   Hooper L.V., Gordon J.I.;
RT   "A genomic view of the human-Bacteroides thetaiotaomicron symbiosis.";
RL   Science 299:2074-2076(2003).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAO79170.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE015928; AAO79170.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; NP_812976.1; NC_004663.1.
DR   RefSeq; WP_008760950.1; NC_004663.1.
DR   AlphaFoldDB; Q8A0F6; -.
DR   SMR; Q8A0F6; -.
DR   STRING; 226186.BT_4065; -.
DR   PaxDb; Q8A0F6; -.
DR   PRIDE; Q8A0F6; -.
DR   EnsemblBacteria; AAO79170; AAO79170; BT_4065.
DR   GeneID; 60925240; -.
DR   KEGG; bth:BT_4065; -.
DR   PATRIC; fig|226186.12.peg.4130; -.
DR   eggNOG; COG0649; Bacteria.
DR   eggNOG; COG0852; Bacteria.
DR   HOGENOM; CLU_015134_3_2_10; -.
DR   InParanoid; Q8A0F6; -.
DR   OMA; IMGTSME; -.
DR   Proteomes; UP000001414; 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; IBA:GO_Central.
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_0000358618"
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;  60594 MW;  B13341475F17B845 CRC64;
     MQEIQFIVPA ALHDEMLRLR NEKQMDFLES LTGMDWGVAD EKDAPEKLRG LGVVYHLEST
     VTGERIALKT AVTDRERPEI PSVSDIWKIA DFYEREVFDY YGIVFVGHPD MRRLYLRNDW
     VGYPMRKDND PEKDNPLCMA NEETFDTTQE IELNPDGTIK NREMKLFGEE EYVVNIGPQH
     PATHGVMRFR VSLEGEIIRK IDANCGYIHR GIEKMNESLT YPQTLALTDR LDYLGAHQNR
     HALCMCIEKA MGIEVSDRVK YIRTIMDELQ RIDSHLLFYS ALAMDLGALT AFFYGFRDRE
     KILDIFEETC GGRLIMNYNT IGGVQADLHP NFVKRVKEFI PYMRGIIHEY HDIFTGNIIA
     QSRMKGVGVL SREDAISFGC TGGTGRASGW ACDVRKRIPY GVYDKVDFQE IVYTEGDCFA
     RYLVRMDEIM ESLKIIEQLI DNIPEGPYQE KMKPIIRVPE GSYYAAVEGS RGEFGVFLES
     QGDKMPYRLH YRATGLPLVA AIDTICRGAK IADLIAIGGT LDYVVPDIDR