ID   NUOD_RUEST              Reviewed;         403 AA.
AC   Q1GIN9;
DT   16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT   27-JUN-2006, sequence version 1.
DT   25-MAY-2022, entry version 111.
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=TM1040_0744;
OS   Ruegeria sp. (strain TM1040) (Silicibacter sp.).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Ruegeria; unclassified Ruegeria.
OX   NCBI_TaxID=292414;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TM1040;
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   Brettin T., Bruce D., Han C., Tapia R., Goodwin L., Thompson L.S.,
RA   Gilna P., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA   Belas R., Moran M.A., Buchan A., Gonzalez J.M., Schell M.A., Sun F.,
RA   Richardson P.;
RT   "Complete sequence of chromosome of Silicibacter sp. TM1040.";
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; CP000377; ABF63477.1; -; Genomic_DNA.
DR   RefSeq; WP_011538089.1; NC_008044.1.
DR   AlphaFoldDB; Q1GIN9; -.
DR   SMR; Q1GIN9; -.
DR   STRING; 292414.TM1040_0744; -.
DR   EnsemblBacteria; ABF63477; ABF63477; TM1040_0744.
DR   KEGG; sit:TM1040_0744; -.
DR   eggNOG; COG0649; Bacteria.
DR   HOGENOM; CLU_015134_1_1_5; -.
DR   OMA; IMGTSME; -.
DR   OrthoDB; 473681at2; -.
DR   Proteomes; UP000000636; 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; 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;
KW   Reference proteome; Translocase; Transport; Ubiquinone.
FT   CHAIN           1..403
FT                   /note="NADH-quinone oxidoreductase subunit D"
FT                   /id="PRO_0000357928"
SQ   SEQUENCE   403 AA;  45805 MW;  470A283B1BE00596 CRC64;
     MDGSKFDDAQ TGEQKIRNFN INFGPQHPAA HGVLRLVLEL DGEIVERCDP HIGLLHRGTE
     KLMESRTYLQ NLPYFDRLDY VAPMNQEHAW CLAIEKLTGV EVPRRAQLIR VLYSEIGRIL
     NHLLNITTQA MDVGALTPPL WGFEEREKLM IFYERACGAR LHAAYFRPGG VHQDLPDELL
     DDIDLWAMEF PKVMDDIDGL LTENRIFKQR NCDIGVVTED DIQKYGFSGV MVRGSGLAWD
     LRRAQPYECY DEFDFQIPVG KNGDCYDRYL VRMEEMRQSL SIIRQAIAKL REATGDVLAR
     GKLTPPKRGD MKTSMESLIH HFKLYTEGFH VPEGEVYAAV EAPKGEFGVY LVADGSNKPY
     RAKLRAPGFL HLQAMDYVAK GHQLADVAAI IGTMDIVFGE IDR