NUOE_SALTY
ID NUOE_SALTY Reviewed; 166 AA.
AC P0A1Y8; P33903;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=NADH-quinone oxidoreductase subunit E;
DE EC=7.1.1.-;
DE AltName: Full=NADH dehydrogenase I subunit E;
DE AltName: Full=NDH-1 subunit E;
GN Name=nuoE; OrderedLocusNames=STM2325;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8234329; DOI=10.1073/pnas.90.21.9877;
RA Archer C.D., Wang X., Elliott T.;
RT "Mutants defective in the energy-conserving NADH dehydrogenase of
RT Salmonella typhimurium identified by a decrease in energy-dependent
RT proteolysis after carbon starvation.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:9877-9881(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
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 (By similarity). {ECO:0000250}.
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 -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; Evidence={ECO:0000305};
CC Note=Binds 1 [2Fe-2S] cluster. {ECO:0000305};
CC -!- SUBUNIT: Composed of 13 different subunits. Subunits NuoCD, E, F, and G
CC constitute the peripheral sector of the complex.
CC -!- SIMILARITY: Belongs to the complex I 24 kDa subunit family.
CC {ECO:0000305}.
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DR EMBL; L22504; AAA16061.1; -; Unassigned_DNA.
DR EMBL; AE006468; AAL21226.1; -; Genomic_DNA.
DR RefSeq; NP_461267.1; NC_003197.2.
DR RefSeq; WP_000545038.1; NC_003197.2.
DR AlphaFoldDB; P0A1Y8; -.
DR SMR; P0A1Y8; -.
DR STRING; 99287.STM2325; -.
DR PaxDb; P0A1Y8; -.
DR EnsemblBacteria; AAL21226; AAL21226; STM2325.
DR GeneID; 1253847; -.
DR KEGG; stm:STM2325; -.
DR PATRIC; fig|99287.12.peg.2462; -.
DR HOGENOM; CLU_054362_2_0_6; -.
DR OMA; HIIRYCD; -.
DR PhylomeDB; P0A1Y8; -.
DR BioCyc; SENT99287:STM2325-MON; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0045272; C:plasma membrane respiratory chain complex I; IBA:GO_Central.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW.
DR CDD; cd03064; TRX_Fd_NuoE; 1.
DR Gene3D; 1.10.10.1590; -; 1.
DR InterPro; IPR002023; NuoE-like.
DR InterPro; IPR042128; NuoE_dom.
DR InterPro; IPR041921; NuoE_N.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR PIRSF; PIRSF000216; NADH_DH_24kDa; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR TIGRFAMs; TIGR01958; nuoE_fam; 1.
DR PROSITE; PS01099; COMPLEX1_24K; 1.
PE 3: Inferred from homology;
KW 2Fe-2S; Iron; Iron-sulfur; Metal-binding; NAD; Quinone; Reference proteome;
KW Translocase; Ubiquinone.
FT CHAIN 1..166
FT /note="NADH-quinone oxidoreductase subunit E"
FT /id="PRO_0000118694"
FT BINDING 92
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255"
FT BINDING 97
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255"
FT BINDING 133
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255"
FT BINDING 137
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255"
SQ SEQUENCE 166 AA; 18602 MW; 86D4EC905E1021E3 CRC64;
MHENQQPQTE AFELSAAERE AIEHEKHHYE DPRAASIEAL KIVQKQRGWV PDGAIYAIAD
VLGIPASDVE GVATFYSQIF RQPVGRHVIR YCDSVVCHIT GYQGIQAALE KNLNIKPGQT
TFDGRFTLLP TCCLGNCDKG PNMMIDEDTH SHLTPEAIPE LLERYK
