ID   NUOD_PELPD              Reviewed;         403 AA.
AC   A1ALP2;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   25-MAY-2022, entry version 84.
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=nuoD1 {ECO:0000255|HAMAP-Rule:MF_01358}; OrderedLocusNames=Ppro_0631;
GN   and
GN   Name=nuoD2 {ECO:0000255|HAMAP-Rule:MF_01358}; OrderedLocusNames=Ppro_1626;
GN   and
GN   Name=nuoD3 {ECO:0000255|HAMAP-Rule:MF_01358}; OrderedLocusNames=Ppro_3190;
OS   Pelobacter propionicus (strain DSM 2379 / NBRC 103807 / OttBd1).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC   Desulfuromonadaceae; Pelobacter.
OX   NCBI_TaxID=338966;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 2379 / NBRC 103807 / OttBd1;
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   Saunders E., Brettin T., Bruce D., Han C., Tapia R., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Lovley D.,
RA   Richardson P.;
RT   "Complete sequence of chromosome of Pelobacter propionicus DSM 2379.";
RL   Submitted (OCT-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; CP000482; ABK98262.1; -; Genomic_DNA.
DR   EMBL; CP000482; ABK99241.1; -; Genomic_DNA.
DR   EMBL; CP000482; ABL00784.1; -; Genomic_DNA.
DR   RefSeq; WP_011734575.1; NC_008609.1.
DR   AlphaFoldDB; A1ALP2; -.
DR   SMR; A1ALP2; -.
DR   STRING; 338966.Ppro_0631; -.
DR   EnsemblBacteria; ABK98262; ABK98262; Ppro_0631.
DR   EnsemblBacteria; ABK99241; ABK99241; Ppro_1626.
DR   EnsemblBacteria; ABL00784; ABL00784; Ppro_3190.
DR   KEGG; ppd:Ppro_0631; -.
DR   KEGG; ppd:Ppro_1626; -.
DR   KEGG; ppd:Ppro_3190; -.
DR   eggNOG; COG0649; Bacteria.
DR   HOGENOM; CLU_015134_1_2_7; -.
DR   OMA; GGRMHYM; -.
DR   OrthoDB; 473681at2; -.
DR   Proteomes; UP000006732; 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; 1.
DR   SUPFAM; SSF56762; SSF56762; 1.
DR   TIGRFAMs; TIGR01962; NuoD; 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_0000371900"
SQ   SEQUENCE   403 AA;  45753 MW;  6BBA18CB3925ECE4 CRC64;
     MEYKSPVRSN LEQTADPNHV LVNMGPSHPA THGTIQIIAA LDGERVAKAD IHCGYLHRGF
     EKESEHHTYH KIIPFTDRLN YCSALNNNFA YVEGVEKLLG IELTPRCIYL RTLLAEYNRV
     ADHVTCVAAT VMEMGAMTAF LYLMTIRDYI FEHLNQLTGA RLTYSFARVG GLKNDLPDGW
     LERLEEILQF TEKYCGRIHG LLDRNRIFID RTRDVGAMSP EHALNWGYTG PILRSTGAKI
     DIRKDNPYLA YADLDFEVPV GIKGDNYDRY YVRMREIDES ISMVRQCMKK LPDGPVNIDD
     RRIMYPTKDK VYTKIEYLIS HFKLVIDGIQ VPAGEIYVSH EAPNGELGFY LISDGSGRPY
     KLHVRSPSFA HMGGMHTLLE GYQVADVIAT FGSMNMIGGE CDR