ID   NUOD_BACHK              Reviewed;         366 AA.
AC   Q6HAY8;
DT   16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 104.
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=BT9727_4979;
OS   Bacillus thuringiensis subsp. konkukian (strain 97-27).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=281309;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=97-27;
RX   PubMed=16621833; DOI=10.1128/jb.188.9.3382-3390.2006;
RA   Han C.S., Xie G., Challacombe J.F., Altherr M.R., Bhotika S.S., Bruce D.,
RA   Campbell C.S., Campbell M.L., Chen J., Chertkov O., Cleland C.,
RA   Dimitrijevic M., Doggett N.A., Fawcett J.J., Glavina T., Goodwin L.A.,
RA   Hill K.K., Hitchcock P., Jackson P.J., Keim P., Kewalramani A.R.,
RA   Longmire J., Lucas S., Malfatti S., McMurry K., Meincke L.J., Misra M.,
RA   Moseman B.L., Mundt M., Munk A.C., Okinaka R.T., Parson-Quintana B.,
RA   Reilly L.P., Richardson P., Robinson D.L., Rubin E., Saunders E., Tapia R.,
RA   Tesmer J.G., Thayer N., Thompson L.S., Tice H., Ticknor L.O., Wills P.L.,
RA   Brettin T.S., Gilna P.;
RT   "Pathogenomic sequence analysis of Bacillus cereus and Bacillus
RT   thuringiensis isolates closely related to Bacillus anthracis.";
RL   J. Bacteriol. 188:3382-3390(2006).
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 a
CC       menaquinone. 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 membrane {ECO:0000255|HAMAP-Rule:MF_01358};
CC       Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_01358};
CC       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; AE017355; AAT63577.1; -; Genomic_DNA.
DR   RefSeq; WP_000621441.1; NC_005957.1.
DR   RefSeq; YP_039288.1; NC_005957.1.
DR   AlphaFoldDB; Q6HAY8; -.
DR   SMR; Q6HAY8; -.
DR   EnsemblBacteria; AAT63577; AAT63577; BT9727_4979.
DR   KEGG; btk:BT9727_4979; -.
DR   PATRIC; fig|281309.8.peg.5296; -.
DR   HOGENOM; CLU_015134_1_2_9; -.
DR   OMA; IMGTSME; -.
DR   Proteomes; UP000001301; Chromosome.
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; IPR022885; NDH1_su_D/H.
DR   InterPro; IPR029014; NiFe-Hase_large.
DR   PANTHER; PTHR11993; PTHR11993; 1.
DR   Pfam; PF00346; Complex1_49kDa; 2.
DR   SUPFAM; SSF56762; SSF56762; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Membrane; NAD; Quinone; Translocase; Transport.
FT   CHAIN           1..366
FT                   /note="NADH-quinone oxidoreductase subunit D"
FT                   /id="PRO_0000357769"
SQ   SEQUENCE   366 AA;  41528 MW;  CC295D20FE088E3E CRC64;
     MIRTEEMLLN VGPQHPSTHG VFRLVIKIDG EIIKEATPVI GYLHRGTEKI AESLQYTQII
     PYTDRMDYLS AMTNNYVICH AVETMMGLEI PERAEYLRVL AMELGRIASH LVWWGTNLLD
     IGAVSPFLYA FREREMIINL LNELCGARLT FNYMRVGGVK WDAPDGWIEK VEEFVPYMRE
     QLAGYHDLVS GNEIFLNRVK GVGIYSAEEA ISYSLSGANL RCTGVNWDLR KDEPYSIYDR
     FDFHIPVGSV GDAWDRYVCR MQEIEESLKI VEQAVQQFPK EGAVLAKVPK IIKAPKGEAF
     VRIESPRGEI GCYIASDGKK EPYRLKFRRP SFYNLQILPK LLKGENIANL ITILGGVDIV
     LGEVDG