ID NUOE_ECOL6 Reviewed; 166 AA.
AC P0AFD2; P33601;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 02-NOV-2016, entry version 78.
DE RecName: Full=NADH-quinone oxidoreductase subunit E;
DE EC=1.6.5.11;
DE AltName: Full=NADH dehydrogenase I subunit E;
DE AltName: Full=NDH-1 subunit E;
DE AltName: Full=NUO5;
GN Name=nuoE; OrderedLocusNames=c2826;
OS Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=199310;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFT073 / ATCC 700928 / UPEC;
RX PubMed=12471157; DOI=10.1073/pnas.252529799;
RA Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P.,
RA Rasko D., Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D.,
RA Mayhew G.F., Rose D.J., Zhou S., Schwartz D.C., Perna N.T.,
RA Mobley H.L.T., Donnenberg M.S., Blattner F.R.;
RT "Extensive mosaic structure revealed by the complete genome sequence
RT of uropathogenic Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
CC -!- FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron-
CC sulfur (Fe-S) centers, to quinones in the respiratory chain. The
CC immediate electron acceptor for the enzyme in this species is
CC believed to be ubiquinone. Couples the redox reaction to proton
CC translocation (for every two electrons transferred, four hydrogen
CC ions are translocated across the cytoplasmic membrane), and thus
CC conserves the redox energy in a proton gradient (By similarity).
CC {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY: NADH + a quinone = NAD(+) + a quinol.
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:49601;
CC Evidence={ECO:0000305};
CC Note=Binds 1 [2Fe-2S] cluster. {ECO:0000305};
CC -!- SUBUNIT: Composed of 13 different subunits. Subunits NuoCD, E, F,
CC and G constitute the peripheral sector of the complex (By
CC similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the complex I 24 kDa subunit family.
CC {ECO:0000305}.
DR EMBL; AE014075; AAN81280.1; -; Genomic_DNA.
DR RefSeq; WP_000545042.1; NC_004431.1.
DR ProteinModelPortal; P0AFD2; -.
DR SMR; P0AFD2; -.
DR STRING; 199310.c2826; -.
DR EnsemblBacteria; AAN81280; AAN81280; c2826.
DR KEGG; ecc:c2826; -.
DR PATRIC; 18283514; VBIEscCol75197_2664.
DR eggNOG; ENOG4105GKE; Bacteria.
DR eggNOG; COG1905; LUCA.
DR HOGENOM; HOG000257749; -.
DR KO; K00334; -.
DR OMA; CDKGPSM; -.
DR BioCyc; ECOL199310:C2826-MONOMER; -.
DR Proteomes; UP000001410; Chromosome.
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:UniProtKB-KW.
DR GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW.
DR Gene3D; 3.40.30.10; -; 1.
DR InterPro; IPR002023; NuoE-like.
DR InterPro; IPR012336; Thioredoxin-like_fold.
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; Complete proteome; Iron; Iron-sulfur; Metal-binding; NAD;
KW Oxidoreductase; Quinone; Ubiquinone.
FT CHAIN 1 166 NADH-quinone oxidoreductase subunit E.
FT /FTId=PRO_0000118692.
FT METAL 92 92 Iron-sulfur (2Fe-2S). {ECO:0000255}.
FT METAL 97 97 Iron-sulfur (2Fe-2S). {ECO:0000255}.
FT METAL 133 133 Iron-sulfur (2Fe-2S). {ECO:0000255}.
FT METAL 137 137 Iron-sulfur (2Fe-2S). {ECO:0000255}.
CC --------------------------------------------------------------------------
CC The following FT lines are automated annotations from the MyHits database.
CC --------------------------------------------------------------------------
FT MYHIT 123 141 ipat:COMPLEX1_24K [T]
SQ SEQUENCE 166 AA; 18590 MW; A1EA95085B9B9107 CRC64;
MHENQQPQTE AFELSAAERE AIEHEMHHYE DPRAASIEAL KIVQKQRGWV PDGAIHAIAD
VLGIPASDVE GVATFYSQIF RQPVGRHVIR YCDSVVCHIN GYQGIQAALE KKLNIKPGQT
TFDGRFTLLP TCCLGNCDKG PNMMIDEDTH AHLTPEAIPE LLERYK
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