ID   NUOD_VESOH              Reviewed;         417 AA.
AC   A5CXG0;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   03-AUG-2022, entry version 88.
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=COSY_0232;
OS   Vesicomyosocius okutanii subsp. Calyptogena okutanii (strain HA).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; sulfur-oxidizing symbionts;
OC   Candidatus Vesicomyosocius.
OX   NCBI_TaxID=412965;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HA;
RX   PubMed=17493812; DOI=10.1016/j.cub.2007.04.039;
RA   Kuwahara H., Yoshida T., Takaki Y., Shimamura S., Nishi S., Harada M.,
RA   Matsuyama K., Takishita K., Kawato M., Uematsu K., Fujiwara Y., Sato T.,
RA   Kato C., Kitagawa M., Kato I., Maruyama T.;
RT   "Reduced genome of the thioautotrophic intracellular symbiont in a deep-sea
RT   clam, Calyptogena okutanii.";
RL   Curr. Biol. 17:881-886(2007).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AP009247; BAF61362.1; -; Genomic_DNA.
DR   RefSeq; WP_011929632.1; NC_009465.1.
DR   AlphaFoldDB; A5CXG0; -.
DR   SMR; A5CXG0; -.
DR   STRING; 412965.COSY_0232; -.
DR   EnsemblBacteria; BAF61362; BAF61362; COSY_0232.
DR   KEGG; vok:COSY_0232; -.
DR   eggNOG; COG0649; Bacteria.
DR   HOGENOM; CLU_015134_1_1_6; -.
DR   OMA; IMGTSME; -.
DR   OrthoDB; 473681at2; -.
DR   Proteomes; UP000000247; 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   GO; GO:0022904; P:respiratory electron transport chain; IEA:UniProt.
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_0000371946"
SQ   SEQUENCE   417 AA;  48129 MW;  7DB47CEEADE003CA CRC64;
     MSEIRNYTLN FGPQHPAAHG VLRLILEIDG EVIERADPHI GLLHRGTEKL VESKPYNQSI
     GYMDRLDYVS MMCNEHAYVM AIEAMLNLKV PKRAQYIRVM FDEITRILNH LMWLGTHGLD
     VGAMSIFLYA FREREKLIDC YEAVSGSRMH ATYYRPGGVY RDLPDKMPQY LASDFRTSKE
     LETMNENRQG SLLDFIADFV KEFPKSIKQY DDLLTDNRIW KQRLVNIGVV SANRAKQLGF
     TGPMLRGSGV EWDLRKNQPY AVYDQLKFDI PVGMTGDSYD RYLVRMEEMR QSNYIIKQCV
     KWLRENPGAV MSDDHKVSQP KRTNMKNDME SLIHHFKLFT EGYCLPEGEV YRAVEHPKGE
     FGVYLISDGA NKPYRVKIRA PGFSHLAAMN EMTRGHMLSD VVTIIGTQDV VFGEIDR