ID NUOE_ECOLI Reviewed; 166 AA.
AC P0AFD1; P33601;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 02-NOV-2016, entry version 99.
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=b2285, JW2280;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12 / AN387;
RX PubMed=7690854; DOI=10.1006/jmbi.1993.1488;
RA Weidner U., Geier S., Ptock A., Friedrich T., Leif H., Weiss H.;
RT "The gene locus of the proton-translocating NADH: ubiquinone
RT oxidoreductase in Escherichia coli. Organization of the 14 genes and
RT relationship between the derived proteins and subunits of
RT mitochondrial complex I.";
RL J. Mol. Biol. 233:109-122(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8157582;
RA Pruss B.M., Nelms J.M., Park C., Wolfe A.J.;
RT "Mutations in NADH:ubiquinone oxidoreductase of Escherichia coli
RT affect growth on mixed amino acids.";
RL J. Bacteriol. 176:2143-2150(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9205837; DOI=10.1093/dnares/4.2.91;
RA Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K.,
RA Itoh T., Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N.,
RA Mizobuchi K., Mori H., Nakade S., Nakamura Y., Nashimoto H.,
RA Oshima T., Oyama S., Saito N., Sampei G., Satoh Y., Sivasundaram S.,
RA Tagami H., Takahashi H., Takeda J., Takemoto K., Uehara K., Wada C.,
RA Yamagata S., Horiuchi T.;
RT "Construction of a contiguous 874-kb sequence of the Escherichia coli-
RT K12 genome corresponding to 50.0-68.8 min on the linkage map and
RT analysis of its sequence features.";
RL DNA Res. 4:91-113(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
RA Mau B., Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains
RT MG1655 and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [6]
RP PROTEIN SEQUENCE OF 1-5.
RX PubMed=7607227; DOI=10.1111/j.1432-1033.1995.tb20594.x;
RA Leif H., Sled V.D., Ohnishi T., Weiss H., Friedrich T.;
RT "Isolation and characterization of the proton-translocating NADH:
RT ubiquinone oxidoreductase from Escherichia coli.";
RL Eur. J. Biochem. 230:538-548(1995).
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.
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.
CC -!- INTERACTION:
CC P33602:nuoG; NbExp=4; IntAct=EBI-1117136, EBI-559737;
CC -!- SIMILARITY: Belongs to the complex I 24 kDa subunit family.
CC {ECO:0000305}.
DR EMBL; X68301; CAA48364.1; -; Genomic_DNA.
DR EMBL; L25055; AAA03536.1; -; Unassigned_DNA.
DR EMBL; U00096; AAC75345.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA16114.1; -; Genomic_DNA.
DR PIR; C65000; C65000.
DR RefSeq; NP_416788.1; NC_000913.3.
DR RefSeq; WP_000545042.1; NZ_LN832404.1.
DR ProteinModelPortal; P0AFD1; -.
DR SMR; P0AFD1; -.
DR BioGrid; 4262977; 15.
DR DIP; DIP-35917N; -.
DR IntAct; P0AFD1; 31.
DR STRING; 511145.b2285; -.
DR TCDB; 3.D.1.1.1; the h(+) or na(+)-translocating nadh dehydrogenase (ndh) family.
DR PaxDb; P0AFD1; -.
DR PRIDE; P0AFD1; -.
DR EnsemblBacteria; AAC75345; AAC75345; b2285.
DR EnsemblBacteria; BAA16114; BAA16114; BAA16114.
DR GeneID; 946746; -.
DR KEGG; ecj:JW2280; -.
DR KEGG; eco:b2285; -.
DR PATRIC; 32119937; VBIEscCol129921_2378.
DR EchoBASE; EB2010; -.
DR EcoGene; EG12086; nuoE.
DR eggNOG; ENOG4105GKE; Bacteria.
DR eggNOG; COG1905; LUCA.
DR HOGENOM; HOG000257749; -.
DR InParanoid; P0AFD1; -.
DR KO; K00334; -.
DR OMA; CDKGPSM; -.
DR PhylomeDB; P0AFD1; -.
DR BioCyc; EcoCyc:NUOE-MONOMER; -.
DR BioCyc; ECOL316407:JW2280-MONOMER; -.
DR BioCyc; MetaCyc:NUOE-MONOMER; -.
DR PRO; PR:P0AFD1; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0030964; C:NADH dehydrogenase complex; IDA:EcoliWiki.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoliWiki.
DR GO; GO:0045272; C:plasma membrane respiratory chain complex I; IDA:EcoCyc.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; ISS:EcoCyc.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IBA:GO_Central.
DR GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW.
DR GO; GO:0022904; P:respiratory electron transport chain; IBA:GO_Central.
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 1: Evidence at protein level;
KW 2Fe-2S; Complete proteome; Direct protein sequencing; Iron;
KW Iron-sulfur; Metal-binding; NAD; Oxidoreductase; Quinone;
KW Reference proteome; Ubiquinone.
FT CHAIN 1 166 NADH-quinone oxidoreductase subunit E.
FT /FTId=PRO_0000118691.
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}.
FT CONFLICT 22 22 I -> V (in Ref. 1; CAA48364).
FT {ECO:0000305}.
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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