NUOD_GEOTN
ID NUOD_GEOTN Reviewed; 366 AA.
AC A4ITI4;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 1.
DT 25-MAY-2022, entry version 90.
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=GTNG_3299;
OS Geobacillus thermodenitrificans (strain NG80-2).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX NCBI_TaxID=420246;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NG80-2;
RX PubMed=17372208; DOI=10.1073/pnas.0609650104;
RA Feng L., Wang W., Cheng J., Ren Y., Zhao G., Gao C., Tang Y., Liu X.,
RA Han W., Peng X., Liu R., Wang L.;
RT "Genome and proteome of long-chain alkane degrading Geobacillus
RT thermodenitrificans NG80-2 isolated from a deep-subsurface oil reservoir.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:5602-5607(2007).
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; CP000557; ABO68638.1; -; Genomic_DNA.
DR RefSeq; WP_011888393.1; NC_009328.1.
DR AlphaFoldDB; A4ITI4; -.
DR SMR; A4ITI4; -.
DR STRING; 420246.GTNG_3299; -.
DR EnsemblBacteria; ABO68638; ABO68638; GTNG_3299.
DR KEGG; gtn:GTNG_3299; -.
DR eggNOG; COG0649; Bacteria.
DR HOGENOM; CLU_015134_1_2_9; -.
DR OMA; IMGTSME; -.
DR OrthoDB; 473681at2; -.
DR Proteomes; UP000001578; 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; 2.
DR SUPFAM; SSF56762; SSF56762; 1.
PE 3: Inferred from homology;
KW Cell membrane; Membrane; NAD; Quinone; Translocase; Transport.
FT CHAIN 1..366
FT /note="NADH-quinone oxidoreductase subunit D"
FT /id="PRO_0000357820"
SQ SEQUENCE 366 AA; 41697 MW; 4DE8F0400AFC8872 CRC64;
MLRTEEMILN VGPQHPSTHG VFRLILKIDG EIIQEATPVI GYLHRGTEKI AEGLQYTQII
PYTDRMDYLS AMTNNYVLCH AVETMMGIEV PERAEYLRVL AMELGRIASH LVWWGTYLLD
LGATSPFLYA FREREMIINL LNELSGARLT FNYMRIGGVK WDAPDGWIDK VKQFVPYMRE
KLAGYHDLVT GNEIFRERVT GVGRYTKEEA ISYSLSGVNL RSTGVKWDLR KDEPYSVYDR
FDFDVPVREG GDCLARYECR MAEIEQSLRI IEQACEQFPA DGPIMGKLPR IIKAPPGETF
VRIEAPRGEI GCYIASDGKK EPYRLKFRRP SFYNLQILPK LLKGENLANV IAILGSIDIV
LGEVDG