ID   NUOD_RHOCA              Reviewed;         413 AA.
AC   O07310;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 2.
DT   25-MAY-2022, entry version 98.
DE   RecName: Full=NADH-quinone oxidoreductase subunit D {ECO:0000255|HAMAP-Rule:MF_01358};
DE            EC=7.1.1.- {ECO:0000255|HAMAP-Rule:MF_01358};
DE   AltName: Full=NADH dehydrogenase I subunit D {ECO:0000255|HAMAP-Rule:MF_01358};
DE   AltName: Full=NDH-1 subunit D {ECO:0000255|HAMAP-Rule:MF_01358};
GN   Name=nuoD {ECO:0000255|HAMAP-Rule:MF_01358};
OS   Rhodobacter capsulatus (Rhodopseudomonas capsulata).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Rhodobacter.
OX   NCBI_TaxID=1061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 33303 / B10;
RA   Dupuis A., Issartel J.P.;
RL   Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 356-413.
RX   PubMed=9219542; DOI=10.1111/j.1432-1033.1997.t01-1-00800.x;
RA   Herter S.M., Schiltz E., Drews G.;
RT   "Protein and gene structure of the NADH-binding fragment of Rhodobacter
RT   capsulatus NADH:ubiquinone oxidoreductase.";
RL   Eur. J. Biochem. 246:800-808(1997).
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_01358};
CC   -!- SUBUNIT: NDH-1 is composed of 14 different subunits. Subunits NuoB, C,
CC       D, E, F, and G constitute the peripheral sector of the complex.
CC       {ECO:0000255|HAMAP-Rule:MF_01358}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_01358}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_01358}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_01358}.
CC   -!- SIMILARITY: Belongs to the complex I 49 kDa subunit family.
CC       {ECO:0000255|HAMAP-Rule:MF_01358}.
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DR   EMBL; AF029365; AAC24988.1; -; Genomic_DNA.
DR   EMBL; Y09884; CAA71010.1; -; Genomic_DNA.
DR   RefSeq; WP_013067244.1; NZ_VIBE01000008.1.
DR   AlphaFoldDB; O07310; -.
DR   SMR; O07310; -.
DR   PRIDE; O07310; -.
DR   GeneID; 31490400; -.
DR   OMA; IMGTSME; -.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0050136; F:NADH dehydrogenase (quinone) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.645.10; -; 1.
DR   HAMAP; MF_01358; NDH1_NuoD; 1.
DR   InterPro; IPR001135; NADH_Q_OxRdtase_suD.
DR   InterPro; IPR014029; NADH_UbQ_OxRdtase_49kDa_CS.
DR   InterPro; IPR022885; NDH1_su_D/H.
DR   InterPro; IPR029014; NiFe-Hase_large.
DR   PANTHER; PTHR11993; PTHR11993; 1.
DR   Pfam; PF00346; Complex1_49kDa; 1.
DR   SUPFAM; SSF56762; SSF56762; 1.
DR   TIGRFAMs; TIGR01962; NuoD; 1.
DR   PROSITE; PS00535; COMPLEX1_49K; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Membrane; NAD; Quinone; Translocase;
KW   Transport; Ubiquinone.
FT   CHAIN           1..413
FT                   /note="NADH-quinone oxidoreductase subunit D"
FT                   /id="PRO_0000118624"
SQ   SEQUENCE   413 AA;  46449 MW;  D69E3BD61E534CCB CRC64;
     MDGDIRHNSY DDGSEDVLTG EQSIRNFNIN FGPQHPAAHG VLRMVLELDG EIVERADPHI
     GLLHRGTEKL MESRTYLQNT PYFDRLDYVA PMNQEHAWCL AIEKLTGTAV PRRASIIRVL
     FSEIGRILNH LLNVTTQAMD VGALTPPLWG FEEREKLMIF YERACGARLH ANYFRPGGVH
     QDLPPDLIDD IEIWAKAFPQ VLDDIEGLLT ENRIFKQRNA DICIITEAEI EKWGYSGVMV
     RGSGLAWDLR RAQPYECYDE FDFKVAVGKN GDCYDRYLVR MAEMRESTKI ILQACAKLRA
     PDGQGDILAR GKLTPPKRAE MKTSMEALIH HFKLYTEGFK VPAGEVYAAV EAPKGEFGVY
     LVADGTNKPY RAKIRAPGYA HLQSIDAVAK GHQLADVSAI IGTMDVVFGE IDR