ID   NUOCD_HYDS0             Reviewed;         571 AA.
AC   B4U8I3;
DT   16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   25-MAY-2022, entry version 78.
DE   RecName: Full=NADH-quinone oxidoreductase subunit C/D;
DE            EC=7.1.1.-;
DE   AltName: Full=NADH dehydrogenase I subunit C/D;
DE   AltName: Full=NDH-1 subunit C/D;
GN   Name=nuoC; Synonyms=nuoCD, nuoD; OrderedLocusNames=HY04AAS1_0757;
OS   Hydrogenobaculum sp. (strain Y04AAS1).
OC   Bacteria; Aquificae; Aquificales; Aquificaceae; Hydrogenobaculum;
OC   unclassified Hydrogenobaculum.
OX   NCBI_TaxID=380749;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Y04AAS1;
RX   PubMed=19136599; DOI=10.1128/jb.01645-08;
RA   Reysenbach A.-L., Hamamura N., Podar M., Griffiths E., Ferreira S.,
RA   Hochstein R., Heidelberg J., Johnson J., Mead D., Pohorille A.,
RA   Sarmiento M., Schweighofer K., Seshadri R., Voytek M.A.;
RT   "Complete and draft genome sequences of six members of the Aquificales.";
RL   J. Bacteriol. 191:1992-1993(2009).
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: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   -!- SUBUNIT: NDH-1 is composed of 13 different subunits. Subunits NuoB, CD,
CC       E, F, and G constitute the peripheral sector of the complex (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Peripheral
CC       membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the complex I 30 kDa
CC       subunit family. {ECO:0000305}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the complex I 49 kDa
CC       subunit family. {ECO:0000305}.
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DR   EMBL; CP001130; ACG57444.1; -; Genomic_DNA.
DR   RefSeq; WP_012513800.1; NC_011126.1.
DR   AlphaFoldDB; B4U8I3; -.
DR   SMR; B4U8I3; -.
DR   STRING; 380749.HY04AAS1_0757; -.
DR   EnsemblBacteria; ACG57444; ACG57444; HY04AAS1_0757.
DR   KEGG; hya:HY04AAS1_0757; -.
DR   eggNOG; COG0649; Bacteria.
DR   eggNOG; COG0852; Bacteria.
DR   HOGENOM; CLU_015134_3_2_0; -.
DR   OMA; GGRMHYM; -.
DR   OrthoDB; 473681at2; -.
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..571
FT                   /note="NADH-quinone oxidoreductase subunit C/D"
FT                   /id="PRO_0000358647"
FT   REGION          1..171
FT                   /note="NADH dehydrogenase I subunit C"
FT                   /evidence="ECO:0000250"
FT   REGION          194..571
FT                   /note="NADH dehydrogenase I subunit D"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   571 AA;  66149 MW;  8D4061249857728F CRC64;
     MQASEKTLNE IKAKLPYVEV KKDKLLSIVY VQKELLINTL KAIKEDFGFK LFLDHSVVDT
     LEAQNRFEAF YILYNVDTKE RIAVKTRTEH SLPSAEKLWF AAKWAERECY DMFGINYEGH
     EHLVRAFMWD TYNYHPLRKD FPLQGYETVE LPSLNETVFG DNLSNTMNYR RTHTYVPTLK
     DLEYTEKNRI KKKAQVVLNW GPLHPGTHGT MWFLFDLEGE RIVQTDVILG QLHRGVEKLA
     EHEPYQQFLV YTDRMDYISA LCSNQAWTVA VERLLGIEDI VPIKAKYIRT MMSELQRINS
     HLLWLGTYAL DLGALTIFLY AFKEREKIMD IIEGITGARL TISYTRIGGV RMDLPEGALE
     VIESFIKFFP KELKDWEKIL SRNRIWVKRN KNVGVLTKED IYFYGLTGAV ARGSGVFYDI
     RKLEPYDAYG MVEFDVPLGE NGDCYDRYLV RIEEMKQSIR IIEQCVQKLK TMSPNEPFMA
     ESQDPKKLRL TLDGIGLKVP VGEIYSSGEN PRGELGFYIN SKGGLKPYRV KIRPGSFYNL
     CVYPHLMENR YVADAVTILA SLDPVVGEVD R