ID   NUCD2_AQUAE             Reviewed;         586 AA.
AC   O67335;
DT   16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 120.
DE   RecName: Full=NADH-quinone oxidoreductase subunit C/D 2;
DE            EC=7.1.1.-;
DE   AltName: Full=NADH dehydrogenase I subunit C/D 2;
DE   AltName: Full=NDH-1 subunit C/D 2;
GN   Name=nuoC2; Synonyms=nuoCD, nuoD, nuoD2; OrderedLocusNames=aq_1314;
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; AAC07298.1; -; Genomic_DNA.
DR   PIR; D70413; D70413.
DR   RefSeq; NP_213899.1; NC_000918.1.
DR   RefSeq; WP_010880837.1; NC_000918.1.
DR   AlphaFoldDB; O67335; -.
DR   SMR; O67335; -.
DR   STRING; 224324.aq_1314; -.
DR   EnsemblBacteria; AAC07298; AAC07298; aq_1314.
DR   KEGG; aae:aq_1314; -.
DR   PATRIC; fig|224324.8.peg.1023; -.
DR   eggNOG; COG0649; Bacteria.
DR   eggNOG; COG0852; Bacteria.
DR   HOGENOM; CLU_015134_3_2_0; -.
DR   InParanoid; O67335; -.
DR   OMA; RDSHTIW; -.
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..586
FT                   /note="NADH-quinone oxidoreductase subunit C/D 2"
FT                   /id="PRO_0000358614"
FT   REGION          1..173
FT                   /note="NADH dehydrogenase I subunit C"
FT                   /evidence="ECO:0000250"
FT   REGION          197..586
FT                   /note="NADH dehydrogenase I subunit D"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   586 AA;  67893 MW;  2D25917FA02EEEAE CRC64;
     MKWVNKGTVE RVKQEFKDEV KYYETKHTKG FEVSHDFLKP LLKFLKERER FLHFVDMTCI
     DFPEHPNRFQ GVYILYNPEE NERVIVKSWA KDGKLPTVED LWPGAKWAER EAYDMFGVVF
     EGHENLRRMF MWEGYEHYPL RKDFPLQGIP EVELPSLTEV LHGRTDPPSH DFELVHTKLP
     TLEDLERTEK ARLKKKAELV LNWGPLHPGT HGTIWFLFDL EGEKVVQSDV ILGQLHRGME
     KLAENLHYFQ FIPYTDRMDY ISAICNELAY VETVERLLGV EVPEKARYIR TMFAELQRIN
     SHLLWLGTGA LDLGALTVFL YAFREREKIM DIIEGNAGYR LTSCFLRIGG VHYDLAEGTL
     DVVKHFIKDF PNRLKEYHTL LTRNRIWLRR TKDVGVITRE DVHNYGLSGP VARGSGVPYD
     LRKLQPYAAY DEVEFDIPVG EVGDVYDRYL VRMEEMAQSV RIIEQCVQKL EKLPKDAPYL
     NKEHPAVIPP KEDVFHDLES MVKSFRVVVH GEDAPPGEVY FAGENPRGEL GFFIYSKGGG
     KPYRTRIRSG ALYNLSIFPK LIQGRTIADA IALLGSLDPV VGETDR