ID   NUOD_THET2              Reviewed;         409 AA.
AC   Q72GD1;
DT   16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   02-SEP-2026, entry version 123.
DE   RecName: Full=NADH-quinone oxidoreductase subunit D;
DE            EC=7.1.1.-;
DE   AltName: Full=NADH dehydrogenase I subunit D;
DE   AltName: Full=NDH-1 subunit D;
GN   Name=nuoD; OrderedLocusNames=TT_C1917;
OS   Thermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27).
OC   Bacteria; Thermotogati; Deinococcota; Deinococci; Thermales; Thermaceae;
OC   Thermus.
OX   NCBI_TaxID=262724;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-163 / DSM 7039 / HB27;
RX   PubMed=15064768; DOI=10.1038/nbt956;
RA   Henne A., Brueggemann H., Raasch C., Wiezer A., Hartsch T., Liesegang H.,
RA   Johann A., Lienard T., Gohl O., Martinez-Arias R., Jacobi C.,
RA   Starkuviene V., Schlenczeck S., Dencker S., Huber R., Klenk H.-P.,
RA   Kramer W., Merkl R., Gottschalk G., Fritz H.-J.;
RT   "The genome sequence of the extreme thermophile Thermus thermophilus.";
RL   Nat. Biotechnol. 22:547-553(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
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:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a quinone + NADH + 5 H(+)(in) = a quinol + NAD(+) + 4
CC         H(+)(out); Xref=Rhea:RHEA:57888, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:24646, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC         ChEBI:CHEBI:132124;
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 (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Peripheral
CC       membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the complex I 49 kDa subunit family.
CC       {ECO:0000305}.
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DR   EMBL; AE017221; AAS82259.1; -; Genomic_DNA.
DR   RefSeq; WP_011174269.1; NC_005835.1.
DR   AlphaFoldDB; Q72GD1; -.
DR   SMR; Q72GD1; -.
DR   KEGG; tth:TT_C1917; -.
DR   eggNOG; COG0649; Bacteria.
DR   HOGENOM; CLU_015134_1_2_0; -.
DR   OrthoDB; 9801496at2; -.
DR   Proteomes; UP000000592; 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) (non-electrogenic) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0048038; F:quinone binding; IEA:InterPro.
DR   Gene3D; 1.10.645.10; Cytochrome-c3 Hydrogenase, chain B; 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   NCBIfam; TIGR01962; NuoD; 1.
DR   NCBIfam; NF004739; PRK06075.1; 1.
DR   PANTHER; PTHR11993:SF10; NADH DEHYDROGENASE [UBIQUINONE] IRON-SULFUR PROTEIN 2, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR11993; NADH-UBIQUINONE OXIDOREDUCTASE 49 KDA SUBUNIT; 1.
DR   Pfam; PF00346; Complex1_49kDa; 1.
DR   SUPFAM; SSF56762; HydB/Nqo4-like; 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.
FT   CHAIN           1..409
FT                   /note="NADH-quinone oxidoreductase subunit D"
FT                   /id="PRO_0000357949"
SQ   SEQUENCE   409 AA;  46423 MW;  BC4E058DC6A99E29 CRC64;
     MREEFLEEIP LDAPPEEAKE LRTEVMTLNV GPQHPSTHGV LRLMVTLSGE EVLEVVPHIG
     YLHTGFEKTM EHRTYLQNIT YTPRMDYLHS FAHDLAYALA VEKLLGAVVP PRAETIRVIL
     NELSRLASHL VFLGTGLLDL GALTPFFYAF RERETILDLF EWVTGQRFHH NYIRIGGVKE
     DLPEEFVPEL KKFLEVMPHR IDEYEALFAE SPIFYERARG VGVIPPEVAI DLGLTGGSLR
     ASGVNYDVRK AYPYSGYETY TFDVPLGERG DVFDRMLVRI REMRESVKII KQALERLEPG
     PVRDPNPQIT PPPRHLLETS MEAVIYHFKH YTEGFHPPKG EVYVPTESAR GELGYYIVSD
     GGSMPYRVKV RAPSFVNLQS LPYACKGEQV PDMVAIIASL DPVMGDVDR
//