ID   NUOCD_CAMFF             Reviewed;         561 AA.
AC   A0RMD1;
DT   16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 96.
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=CFF8240_0159;
OS   Campylobacter fetus subsp. fetus (strain 82-40).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=360106;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=82-40;
RA   Fouts D.E., Nelson K.E.;
RT   "Sequence of Campylobacter fetus subsp. fetus 82-40.";
RL   Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases.
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_01397}.
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; CP000487; ABK82000.1; -; Genomic_DNA.
DR   RefSeq; WP_002848154.1; NC_008599.1.
DR   AlphaFoldDB; A0RMD1; -.
DR   SMR; A0RMD1; -.
DR   STRING; 360106.CFF8240_0159; -.
DR   EnsemblBacteria; ABK82000; ABK82000; CFF8240_0159.
DR   GeneID; 61064004; -.
DR   KEGG; cff:CFF8240_0159; -.
DR   eggNOG; COG0649; Bacteria.
DR   HOGENOM; CLU_015134_3_2_7; -.
DR   OMA; GGRMHYM; -.
DR   OrthoDB; 473681at2; -.
DR   Proteomes; UP000000760; 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; 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; 1.
DR   SUPFAM; SSF143243; SSF143243; 1.
DR   SUPFAM; SSF56762; SSF56762; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Membrane; Multifunctional enzyme; NAD;
KW   Quinone; Translocase; Transport; Ubiquinone.
FT   CHAIN           1..561
FT                   /note="NADH-quinone oxidoreductase subunit C/D"
FT                   /id="PRO_0000358625"
FT   REGION          1..152
FT                   /note="NADH dehydrogenase I subunit C"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01397"
FT   REGION          176..561
FT                   /note="NADH dehydrogenase I subunit D"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01397"
SQ   SEQUENCE   561 AA;  64196 MW;  D0611E957B6257E4 CRC64;
     MLEKFSSKFN VLKHSTTNGL LSVQINPNDI YEAVLFVRDN IGFEILADIV CVDNLYIDKE
     KRFSLYYIFR KISSENLCIY IDIDINQSVK SVESIYKSAN WGERECFDQF GVKFENHPNL
     KRILNHKDFQ GYPLRKDYPI TKYQVLYESD DLVGEMKNEM QRAGLASEEN DEFKTKYTFL
     NIGPSHPATH GTIRNFVALD GEKIISCVTE IGYLHRGFEK ACENHSYAQI IPYTDRLNYC
     SAMLNNVGYA KAVEEALGLN LPDRGIFMRV ILGELARIID HEVCLGAMFV DMGGLTNYWY
     LYNPRERIYN FLSKLTGARF TNSFARIGGM ANDFYDGWKE ELLAHLKDVE KGVDDTMILI
     EKNRIFLDRV QNICKINAND ALSYGFSGPN LRASGVSFDL RKDKPYYYYD SFDFSVPVGS
     EGDIYDRMFV RFFEMRESIS IIRQAIKLIP EGKISVDDKD VFLPSKDQVY SNIESLINHF
     KLIFDGIKLP NGHFYSASEG ANGELGFFIF SNSEPNPYRV KLRPPCFYAL NAFSSMVQGS
     LIADSILNLG SLNIIAGELD R