ID   NUOD_BURCA              Reviewed;         417 AA.
AC   Q1BV16;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, sequence version 1.
DT   03-AUG-2022, entry version 102.
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}; OrderedLocusNames=Bcen_1634;
OS   Burkholderia cenocepacia (strain AU 1054).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX   NCBI_TaxID=331271;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AU 1054;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Lykidis A., LiPuma J.J., Konstantinidis K.,
RA   Tiedje J.M., Richardson P.;
RT   "Complete sequence of chromosome 1 of Burkholderia cenocepacia AU 1054.";
RL   Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
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:0000255|HAMAP-Rule:MF_01358}.
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; CP000378; ABF76539.1; -; Genomic_DNA.
DR   RefSeq; WP_006478265.1; NC_008060.1.
DR   AlphaFoldDB; Q1BV16; -.
DR   SMR; Q1BV16; -.
DR   EnsemblBacteria; ABF76539; ABF76539; Bcen_1634.
DR   GeneID; 56558838; -.
DR   KEGG; bcn:Bcen_1634; -.
DR   HOGENOM; CLU_015134_1_1_4; -.
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..417
FT                   /note="NADH-quinone oxidoreductase subunit D"
FT                   /id="PRO_0000371824"
SQ   SEQUENCE   417 AA;  47444 MW;  C5E591F78A03C5E3 CRC64;
     MAEIKNYTLN FGPQHPAAHG VLRLVLELDG EVIQRADPHI GLLHRATEKL AESKTFIQSV
     PYMDRLDYVS MMVNEHGYVL AIEKLLGIEV PERAQYIRVL FDEITRVLNH LMWIGAHALD
     VGAMAVFLYA FREREDLMDV YEAVSGARMH AAYYRPGGVY RDLPDAMPQY KASKIRNEKA
     LAKMNEARSG SVLDFIDDFF TRFPKCVDEY ETLLTDNRIW KQRLVGIGVV SPERALQMGL
     TGPMLRGSGI AWDLRKKQPY EVYDRMDFDV PVGVNGDCYD RYLVRVEEMR QSIRIAKQCI
     EWLRKNPGPV MTDNHKVAPP SRVGMKTNME DLIHHFKLFT EGFHVPEGEA YAAVEHPKGE
     FGIYLVSDGA NKPYRLKIRA PGFAHLASLD EMARGHMIAD AVTIIGTQDI VFGEIDR