ID   NUCD1_AQUAE             Reviewed;         593 AA.
AC   O66826;
DT   16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 126.
DE   RecName: Full=NADH-quinone oxidoreductase subunit C/D 1;
DE            EC=7.1.1.-;
DE   AltName: Full=NADH dehydrogenase I subunit C/D 1;
DE   AltName: Full=NDH-1 subunit C/D 1;
GN   Name=nuoC1; Synonyms=nuoCD, nuoD, nuoD1; OrderedLocusNames=aq_551;
OS   Aquifex aeolicus (strain VF5).
OC   Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX   NCBI_TaxID=224324;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VF5;
RX   PubMed=9537320; DOI=10.1038/32831;
RA   Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA   Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA   Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT   "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL   Nature 392:353-358(1998).
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; AE000657; AAC06787.1; -; Genomic_DNA.
DR   PIR; F70349; F70349.
DR   RefSeq; NP_213386.1; NC_000918.1.
DR   RefSeq; WP_010880324.1; NC_000918.1.
DR   AlphaFoldDB; O66826; -.
DR   SMR; O66826; -.
DR   STRING; 224324.aq_551; -.
DR   EnsemblBacteria; AAC06787; AAC06787; aq_551.
DR   KEGG; aae:aq_551; -.
DR   PATRIC; fig|224324.8.peg.452; -.
DR   eggNOG; COG0649; Bacteria.
DR   eggNOG; COG0852; Bacteria.
DR   HOGENOM; CLU_015134_3_2_0; -.
DR   InParanoid; O66826; -.
DR   OMA; IMGTSME; -.
DR   OrthoDB; 473681at2; -.
DR   Proteomes; UP000000798; 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; 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; TIGR01962; NuoD; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Membrane; Multifunctional enzyme; NAD;
KW   Quinone; Reference proteome; Translocase; Transport; Ubiquinone.
FT   CHAIN           1..593
FT                   /note="NADH-quinone oxidoreductase subunit C/D 1"
FT                   /id="PRO_0000358613"
FT   REGION          1..193
FT                   /note="NADH dehydrogenase I subunit C"
FT                   /evidence="ECO:0000250"
FT   REGION          217..593
FT                   /note="NADH dehydrogenase I subunit D"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   593 AA;  68691 MW;  0068D87942A1E86F CRC64;
     MPWAKEGDLQ ELLKAFPQAS VVELQNSTSV IVPKDILIDV LKYLKEKLGY KLFLDHSVVD
     LKDLLENEKE FNKVVKQNLI AFPEDRESRF QAFYILYNVD ERKRVIVKTR TNGKLPTIEK
     LWFAGKWAER ECYDMFGIEY EGHENLVRAF MWDTYPYFPL RKDFPLEGIP EQELPSLNEV
     VFGDNLEGLM NYDRMHTRVP TLEDLEVTEK KRLKKKAQIV LNWGPLHPGT HGTMWFLFDL
     EGERIVQTDV ILGQLHRGVE KLAEHEMYNQ FLVYTDRMDY LSALCSNQAW VVAIERLMGI
     HDKVPPKAKY IRTMMSELQR INSHLLWLGT YALDLGALTI FLYAFKEREK IMDIIEGITG
     ARLTISYPRI GGVRMDLPEG ALEVIKAFIK KFPEELKDWE TILTRNRIWL RRNKEVGIIS
     KEDAYFHGVT GPVIRGSGIP YDIRKFEPYD AYDEVEFDIP VGEIGDCYDR YLVRIEEMKQ
     SIRIIEQCVA KLEKMSKNEP FFYEGEGKKL KLSLDGIGVK APVGEIYSSG ENPRGELGFY
     VVSTGGTSPY RVKIRPPSYY NLCIYPHLMK DRYVADAVTI LASIDPVVGE TDR