ID   NUOD_CHLTE              Reviewed;         400 AA.
AC   Q8KEC0;
DT   16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 2.
DT   25-MAY-2022, entry version 113.
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=CT0769;
OS   Chlorobaculum tepidum (strain ATCC 49652 / DSM 12025 / NBRC 103806 / TLS)
OS   (Chlorobium tepidum).
OC   Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae; Chlorobaculum.
OX   NCBI_TaxID=194439;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49652 / DSM 12025 / NBRC 103806 / TLS;
RX   PubMed=12093901; DOI=10.1073/pnas.132181499;
RA   Eisen J.A., Nelson K.E., Paulsen I.T., Heidelberg J.F., Wu M., Dodson R.J.,
RA   DeBoy R.T., Gwinn M.L., Nelson W.C., Haft D.H., Hickey E.K., Peterson J.D.,
RA   Durkin A.S., Kolonay J.F., Yang F., Holt I.E., Umayam L.A., Mason T.M.,
RA   Brenner M., Shea T.P., Parksey D.S., Nierman W.C., Feldblyum T.V.,
RA   Hansen C.L., Craven M.B., Radune D., Vamathevan J.J., Khouri H.M.,
RA   White O., Gruber T.M., Ketchum K.A., Venter J.C., Tettelin H., Bryant D.A.,
RA   Fraser C.M.;
RT   "The complete genome sequence of Chlorobium tepidum TLS, a photosynthetic,
RT   anaerobic, green-sulfur bacterium.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:9509-9514(2002).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAM72006.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE006470; AAM72006.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; NP_661664.1; NC_002932.3.
DR   AlphaFoldDB; Q8KEC0; -.
DR   SMR; Q8KEC0; -.
DR   STRING; 194439.CT0769; -.
DR   EnsemblBacteria; AAM72006; AAM72006; CT0769.
DR   KEGG; cte:CT0769; -.
DR   PATRIC; fig|194439.7.peg.700; -.
DR   eggNOG; COG0649; Bacteria.
DR   HOGENOM; CLU_015134_1_2_10; -.
DR   OMA; IMGTSME; -.
DR   OrthoDB; 473681at2; -.
DR   Proteomes; UP000001007; 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.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Membrane; NAD; Quinone;
KW   Reference proteome; Translocase; Transport.
FT   CHAIN           1..400
FT                   /note="NADH-quinone oxidoreductase subunit D"
FT                   /id="PRO_0000357798"
SQ   SEQUENCE   400 AA;  45518 MW;  50264C4D647922E8 CRC64;
     MQELGKAETN STRIIRQDDK RVTIEKDLDT EHMVLSMGPQ HPSTHGVLRL ECITDGEVVV
     EAEPYLGYLH RCFEKHCEKI DYPAIVPYTD RMDYLAGMNN ELAYCITVEK LLDIEIPRRV
     EFIRVIVAEL NRIASHLVAI GTYAIDLGAF TPFLFCFRDR EHIMSLLEWI SGARMLYNYI
     WIGGLAYDVP ADFKTRVAEF VTYFRPKAKE LYQLLTENEI FVKRTYDIGI MPADVAINYG
     WSGPMLRGSG VKWDLRRNDP YSVYPELDFD VPVPDGKFSV VGDCLSRHLV RALEMEESLK
     IIEQCLDKMP EEPNFNSRAL IPKKIRPKAG EVYGRAENPR GELGYYIVSD GKSTSPVRCK
     ARSSCFVNLS AMKDLSKGQL IPDLVAIIGS IDIVLGEVDR