ID   NUOD_CHLPM              Reviewed;         400 AA.
AC   A4SF45;
DT   16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 87.
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=Cvib_1090;
OS   Chlorobium phaeovibrioides (strain DSM 265 / 1930) (Prosthecochloris
OS   vibrioformis (strain DSM 265)).
OC   Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae;
OC   Chlorobium/Pelodictyon group; Chlorobium.
OX   NCBI_TaxID=290318;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 265 / 1930;
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., Pitluck S., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Mikhailova N., Li T., Overmann J.,
RA   Schuster S.C., Bryant D.A., Richardson P.;
RT   "Complete sequence of Prosthecochloris vibrioformis DSM 265.";
RL   Submitted (MAR-2007) 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 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 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; CP000607; ABP37104.1; -; Genomic_DNA.
DR   RefSeq; WP_011890327.1; NC_009337.1.
DR   AlphaFoldDB; A4SF45; -.
DR   SMR; A4SF45; -.
DR   STRING; 290318.Cvib_1090; -.
DR   PRIDE; A4SF45; -.
DR   EnsemblBacteria; ABP37104; ABP37104; Cvib_1090.
DR   KEGG; pvi:Cvib_1090; -.
DR   eggNOG; COG0649; Bacteria.
DR   HOGENOM; CLU_015134_1_2_10; -.
DR   OMA; IMGTSME; -.
DR   OrthoDB; 473681at2; -.
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; 1.
DR   SUPFAM; SSF56762; SSF56762; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Membrane; NAD; Quinone; Translocase;
KW   Transport.
FT   CHAIN           1..400
FT                   /note="NADH-quinone oxidoreductase subunit D"
FT                   /id="PRO_0000357890"
SQ   SEQUENCE   400 AA;  44966 MW;  49A52A6B5204D14B CRC64;
     MQELEMAGQG SLRLSRKSDT IVVLEKDLST EQMVLSMGPQ HPSTHGVLRL ECLTDGEVVT
     EAEPYLGYLH RCFEKHCEHV DYPAIVPYTD RMDYLAGINS EMAYCVAVEK LLDLEIPRRV
     EFIRVIVSEL NRIASHLVAI GTYAIDLGAF TPFLFCFRDR EHILNMLEWA TGARMLYNYI
     WVGGLAYDVP AGFNERVLEF VNYFRPKALE LQQLLTENEI FVKRTKGIGI MPADVAINYG
     WSGPMLRGSG VQWDIRRNDP YSIYPELDFA VPVPDGKLSV VGDCLSRHLV RALEIEESLK
     IIEQCIDKMP GTQGFDPRSA VPKRVRPKAG EVYGRAENPR GELGFYIQSD GKSTSPLRCK
     ARSSCFVNLS AMKDLSRGQL IPDLVAIIGS LDIVLGEVDR