ID   NUOD1_SYMTH             Reviewed;         404 AA.
AC   Q67P19;
DT   16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   25-MAY-2022, entry version 104.
DE   RecName: Full=NADH-quinone oxidoreductase subunit D 1 {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 1 {ECO:0000255|HAMAP-Rule:MF_01358};
DE   AltName: Full=NDH-1 subunit D 1 {ECO:0000255|HAMAP-Rule:MF_01358};
GN   Name=nuoD1 {ECO:0000255|HAMAP-Rule:MF_01358}; OrderedLocusNames=STH1589;
OS   Symbiobacterium thermophilum (strain T / IAM 14863).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Symbiobacteriaceae;
OC   Symbiobacterium.
OX   NCBI_TaxID=292459;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=T / IAM 14863;
RX   PubMed=15383646; DOI=10.1093/nar/gkh830;
RA   Ueda K., Yamashita A., Ishikawa J., Shimada M., Watsuji T., Morimura K.,
RA   Ikeda H., Hattori M., Beppu T.;
RT   "Genome sequence of Symbiobacterium thermophilum, an uncultivable bacterium
RT   that depends on microbial commensalism.";
RL   Nucleic Acids Res. 32:4937-4944(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 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 membrane {ECO:0000255|HAMAP-Rule:MF_01358};
CC       Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_01358};
CC       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; AP006840; BAD40574.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q67P19; -.
DR   SMR; Q67P19; -.
DR   STRING; 292459.STH1589; -.
DR   EnsemblBacteria; BAD40574; BAD40574; STH1589.
DR   KEGG; sth:STH1589; -.
DR   eggNOG; COG0649; Bacteria.
DR   HOGENOM; CLU_015134_1_2_9; -.
DR   Proteomes; UP000000417; 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 membrane; Membrane; NAD; Quinone; Reference proteome; Translocase;
KW   Transport.
FT   CHAIN           1..404
FT                   /note="NADH-quinone oxidoreductase subunit D 1"
FT                   /id="PRO_0000357943"
SQ   SEQUENCE   404 AA;  45942 MW;  15CAE7C39A248B93 CRC64;
     MSMAEDLHLE EQRPERMTLS IGPHHPATHG VLRVKLELEG ETVVKAEPET GFLHTGIEKT
     AEHLTWNQAT TVMDRMDYLS PISNNTGYVM AVEKLLGIED RIPEKARVTR VILLELNRVA
     SHLVGLGTGG LDYGNIGTPI FWAFELRDRI LDIFEHTTGQ RMNPSYMRVG GLAYDLPHNF
     KEMVEDFLKV APGRIQELKD VMLHNPIFVD RAKGVSVITY EQALRYGLTG RNLRVTGSDY
     DVRKYYPYLG YENYDFKVPV YTDGDSWSRV AITFDEMFES LKIIRQALDN LPWDDRYIID
     DRKLVLPPKQ EVKHSMEALI HHFKLVHHGF DVPAGEVYVS IESPRGEIGF YVVSDGGNKP
     MRVRVRPPSF YAVYSLPVLL EGHLLSDMVG AIATIDPVFG EVDR