ID   NUOD_PARDP              Reviewed;         412 AA.
AC   A1B495;
DT   16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   25-MAY-2022, entry version 94.
DE   RecName: Full=NADH-quinone oxidoreductase subunit D;
DE            EC=7.1.1.-;
DE   AltName: Full=NADH dehydrogenase I, subunit 4;
DE   AltName: Full=NADH dehydrogenase I, subunit D;
DE   AltName: Full=NADH-quinone oxidoreductase subunit 4;
DE            Short=NQO4;
DE   AltName: Full=NDH-1, subunit 4;
DE   AltName: Full=NDH-1, subunit D;
GN   Name=nuoD; Synonyms=nqo4 {ECO:0000303|PubMed:14610094};
GN   OrderedLocusNames=Pden_2247;
OS   Paracoccus denitrificans (strain Pd 1222).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Paracoccus.
OX   NCBI_TaxID=318586;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pd 1222;
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   Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Spiro S.,
RA   Richardson D.J., Moir J.W.B., Ferguson S.J., van Spanning R.J.M.,
RA   Richardson P.;
RT   "Complete sequence of chromosome 1 of Paracoccus denitrificans PD1222.";
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   IDENTIFICATION IN NADH OXIDASE SUPERCOMPLEX, FUNCTION, SUBUNIT, AND
RP   SUBCELLULAR LOCATION.
RX   PubMed=14610094; DOI=10.1074/jbc.m309505200;
RA   Stroh A., Anderka O., Pfeiffer K., Yagi T., Finel M., Ludwig B.,
RA   Schagger H.;
RT   "Assembly of respiratory complexes I, III, and IV into NADH oxidase
RT   supercomplex stabilizes complex I in Paracoccus denitrificans.";
RL   J. Biol. Chem. 279:5000-5007(2004).
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:0000305|PubMed:14610094}.
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 at least 14 different subunits, Nqo1 to
CC       Nqo14. The complex has a L-shaped structure, with the hydrophobic arm
CC       (subunits Nqo7, Nqo8, Nqo10 to Nqo14) embedded in the inner membrane
CC       and the hydrophilic peripheral arm (subunits Nqo1 to Nqo6, Nqo9)
CC       protruding into the bacterial cytoplasm. The hydrophilic domain
CC       contains all the redox centers (By similarity). NADH-quinone
CC       oxidoreductase forms a supercomplex with ubiquinol-cytochrome c
CC       reductase complex (complex III or cytochrome b-c1 complex) and
CC       cytochrome c oxidase (complex IV), which stabilizes the NADH-quinone
CC       oxidoreductase complex (PubMed:14610094). {ECO:0000250,
CC       ECO:0000269|PubMed:14610094}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane
CC       {ECO:0000305|PubMed:14610094}; Peripheral membrane protein
CC       {ECO:0000305|PubMed:14610094}.
CC   -!- SIMILARITY: Belongs to the complex I 49 kDa subunit family.
CC       {ECO:0000305}.
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DR   EMBL; CP000489; ABL70339.1; -; Genomic_DNA.
DR   RefSeq; WP_011748533.1; NC_008686.1.
DR   AlphaFoldDB; A1B495; -.
DR   SMR; A1B495; -.
DR   STRING; 318586.Pden_2247; -.
DR   PRIDE; A1B495; -.
DR   EnsemblBacteria; ABL70339; ABL70339; Pden_2247.
DR   KEGG; pde:Pden_2247; -.
DR   eggNOG; COG0649; Bacteria.
DR   HOGENOM; CLU_015134_1_1_5; -.
DR   OMA; IMGTSME; -.
DR   Proteomes; UP000000361; Chromosome 1.
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   1: Evidence at protein level;
KW   Cell inner membrane; Cell membrane; Membrane; NAD; Quinone;
KW   Reference proteome; Translocase; Transport; Ubiquinone.
FT   CHAIN           1..412
FT                   /note="NADH-quinone oxidoreductase subunit D"
FT                   /id="PRO_0000357882"
SQ   SEQUENCE   412 AA;  46724 MW;  9D22F7ABA02151FE CRC64;
     MDGDIRKNSY DDGSMDALTG EQSIRNFNIN FGPQHPAAHG VLRMVLELDG EIVERADPHI
     GLLHRGTEKL MESRTYLQNL PYLDRLDYVA PMNQEHAWCL AIERLTGTVI PRRASLIRVL
     YSEIGRILNH LMGVTTGAMD VGALTPPLWG FEAREELMIF YERACGARLH AAYFRPGGVH
     QDLPPDLLDD IEEWCERFPK LVDDLDTLLT ENRIFKQRLV DIGIVTEADA LDWGYTGVMV
     RGSGLAWDLR RSQPYECYDE FDFQIPVGRN GDCYDRYLCR MAEMRESCKI MQQAVQKLRA
     EPAGDVLARG KLTPPRRAEM KRDMESLIHH FKLYTEGFKV PAGEVYAAVE APKGEFGVYL
     VADGTNKPWR AKLRAPGFAH LQSIDWMSRG HMLADVPAII ATLDIVFGEV DR