ID   NUOCD_BDEBA             Reviewed;         560 AA.
AC   Q6MIR5;
DT   16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 106.
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};
DE   AltName: Full=NUO3/NUO4 {ECO:0000255|HAMAP-Rule:MF_01397};
GN   Name=nuoC {ECO:0000255|HAMAP-Rule:MF_01397}; Synonyms=nuoCD, nuoD;
GN   OrderedLocusNames=Bd3085;
OS   Bdellovibrio bacteriovorus (strain ATCC 15356 / DSM 50701 / NCIMB 9529 /
OS   HD100).
OC   Bacteria; Proteobacteria; Oligoflexia; Bdellovibrionales;
OC   Bdellovibrionaceae; Bdellovibrio.
OX   NCBI_TaxID=264462;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15356 / DSM 50701 / NCIMB 9529 / HD100;
RX   PubMed=14752164; DOI=10.1126/science.1093027;
RA   Rendulic S., Jagtap P., Rosinus A., Eppinger M., Baar C., Lanz C.,
RA   Keller H., Lambert C., Evans K.J., Goesmann A., Meyer F., Sockett R.E.,
RA   Schuster S.C.;
RT   "A predator unmasked: life cycle of Bdellovibrio bacteriovorus from a
RT   genomic perspective.";
RL   Science 303:689-692(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
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.
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   -!- SUBCELLULAR LOCATION: Cytoplasm. Cell inner membrane; Peripheral
CC       membrane protein.
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; BX842654; CAE80848.1; -; Genomic_DNA.
DR   RefSeq; WP_011165452.1; NC_005363.1.
DR   AlphaFoldDB; Q6MIR5; -.
DR   SMR; Q6MIR5; -.
DR   STRING; 264462.Bd3085; -.
DR   EnsemblBacteria; CAE80848; CAE80848; Bd3085.
DR   KEGG; bba:Bd3085; -.
DR   eggNOG; COG0649; Bacteria.
DR   eggNOG; COG0852; Bacteria.
DR   HOGENOM; CLU_015134_3_2_7; -.
DR   OMA; GGRMHYM; -.
DR   OrthoDB; 473681at2; -.
DR   Proteomes; UP000008080; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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_01357; NDH1_NuoC; 1.
DR   HAMAP; MF_01397; NDH1_NuoCD_2; 1.
DR   HAMAP; MF_01358; NDH1_NuoD; 1.
DR   InterPro; IPR010218; NADH_DH_suC.
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; 1.
DR   SUPFAM; SSF143243; SSF143243; 1.
DR   SUPFAM; SSF56762; SSF56762; 1.
DR   TIGRFAMs; TIGR01961; NuoC_fam; 1.
DR   TIGRFAMs; TIGR01962; NuoD; 1.
DR   PROSITE; PS00542; COMPLEX1_30K; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Cytoplasm; Membrane;
KW   Multifunctional enzyme; NAD; Quinone; Reference proteome; Translocase;
KW   Transport; Ubiquinone.
FT   CHAIN           1..560
FT                   /note="NADH-quinone oxidoreductase subunit C/D"
FT                   /id="PRO_0000358621"
FT   REGION          2..157
FT                   /note="NADH dehydrogenase I subunit C"
FT   REGION          175..560
FT                   /note="NADH dehydrogenase I subunit D"
SQ   SEQUENCE   560 AA;  62705 MW;  B0B315476C7AFAE0 CRC64;
     MNKLENLKQL LAGKFKIENF KFTHAVGDDV IEVPKEDAPA LLLFLRESGQ FDFLMDVCGA
     DYPSREKRFD VVYNLFNSKD SSRLRVKAQV GEGESIGTAI PAYRGADWFE REAYDMFGII
     FEGHPNLRKI LTHHQFVGHP LRKDYDANNQ QACTNSLPIH FNNEPGSPGD VLNDKYLPLN
     IGPSHTAMHG TLRVMAEMDG ETIVRCNNEI GYLHRCFEKM AETHPYNQVI PYTDRLNYCS
     APMNNIGYCK AVERLLGVEI PPKAQAMRVI LAELSRIIDH TIAIGTGAMD LGALTSFFYM
     FGMREKVYGL FEKLCGARLT VSMTRIGGMA QDAPEGWFDE VLALVKEIRK GTDEMANMVI
     DNKIFIQRTK NVCPVSAADA IQWGYTGPML RACGVNLDLR KAQPYYGYDA LDFDVPVGTN
     GDIYDRYLVR FEEMRQSVRI IEQVCKNVPG GDYTIRDKGI VLPEKKDVYG NIEGLMNHFM
     LIIKGLRPPV GEVYDATEAA NGELGFYLVS DGSANPYRLK VRPPCFAIYQ SFPTVVKGAM
     LADAIATVAS MNLIAGELDR