NUOE_ECOLI
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 03-AUG-2022, entry version 132.
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;
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 oxidoreductase
RT in Escherichia coli. Organization of the 14 genes and relationship between
RT the derived proteins and subunits of mitochondrial complex I.";
RL J. Mol. Biol. 233:109-122(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8157582; DOI=10.1128/jb.176.8.2143-2150.1994;
RA Pruss B.M., Nelms J.M., Park C., Wolfe A.J.;
RT "Mutations in NADH:ubiquinone oxidoreductase of Escherichia coli affect
RT 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., Itoh T.,
RA Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K.,
RA Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T., Oyama S.,
RA Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H.,
RA Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.;
RT "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12
RT genome corresponding to 50.0-68.8 min on the linkage map and analysis of
RT 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., Mau B.,
RA 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 MG1655
RT 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-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.
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 -!- INTERACTION:
CC P0AFD1; P33602: nuoG; NbExp=4; IntAct=EBI-1117136, EBI-559737;
CC -!- SIMILARITY: Belongs to the complex I 24 kDa subunit family.
CC {ECO:0000305}.
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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_STEB01000008.1.
DR PDB; 7AWT; EM; 2.73 A; E=1-166.
DR PDB; 7NYR; EM; 3.30 A; E=1-166.
DR PDB; 7NYU; EM; 3.80 A; E=1-166.
DR PDB; 7NYV; EM; 3.70 A; E=1-166.
DR PDB; 7NZ1; EM; 2.10 A; E=1-166.
DR PDBsum; 7AWT; -.
DR PDBsum; 7NYR; -.
DR PDBsum; 7NYU; -.
DR PDBsum; 7NYV; -.
DR PDBsum; 7NZ1; -.
DR AlphaFoldDB; P0AFD1; -.
DR SMR; P0AFD1; -.
DR BioGRID; 4262977; 41.
DR BioGRID; 851087; 6.
DR ComplexPortal; CPX-243; Respiratory chain complex I.
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 jPOST; P0AFD1; -.
DR PaxDb; P0AFD1; -.
DR PRIDE; P0AFD1; -.
DR EnsemblBacteria; AAC75345; AAC75345; b2285.
DR EnsemblBacteria; BAA16114; BAA16114; BAA16114.
DR GeneID; 67416715; -.
DR GeneID; 946746; -.
DR KEGG; ecj:JW2280; -.
DR KEGG; eco:b2285; -.
DR PATRIC; fig|1411691.4.peg.4451; -.
DR EchoBASE; EB2010; -.
DR eggNOG; COG1905; Bacteria.
DR HOGENOM; CLU_054362_2_0_6; -.
DR InParanoid; P0AFD1; -.
DR OMA; HIIRYCD; -.
DR PhylomeDB; P0AFD1; -.
DR BioCyc; EcoCyc:NUOE-MON; -.
DR BioCyc; MetaCyc:NUOE-MON; -.
DR PRO; PR:P0AFD1; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0016020; C:membrane; IDA:ComplexPortal.
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:0045271; C:respiratory chain complex I; IC:ComplexPortal.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IMP:EcoCyc.
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 GO; GO:0022904; P:respiratory electron transport chain; IDA:ComplexPortal.
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 1: Evidence at protein level;
KW 2Fe-2S; 3D-structure; Direct protein sequencing; Iron; Iron-sulfur;
KW Metal-binding; NAD; Quinone; Reference proteome; Translocase; Ubiquinone.
FT CHAIN 1..166
FT /note="NADH-quinone oxidoreductase subunit E"
FT /id="PRO_0000118691"
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"
FT CONFLICT 22
FT /note="I -> V (in Ref. 1; CAA48364)"
FT /evidence="ECO:0000305"
FT HELIX 16..25
FT /evidence="ECO:0007829|PDB:7NZ1"
FT HELIX 26..28
FT /evidence="ECO:0007829|PDB:7NZ1"
FT STRAND 29..31
FT /evidence="ECO:0007829|PDB:7NZ1"
FT HELIX 32..35
FT /evidence="ECO:0007829|PDB:7NZ1"
FT HELIX 36..47
FT /evidence="ECO:0007829|PDB:7NZ1"
FT HELIX 53..62
FT /evidence="ECO:0007829|PDB:7NZ1"
FT HELIX 66..75
FT /evidence="ECO:0007829|PDB:7NZ1"
FT STRAND 76..79
FT /evidence="ECO:0007829|PDB:7NZ1"
FT STRAND 86..92
FT /evidence="ECO:0007829|PDB:7NZ1"
FT HELIX 95..99
FT /evidence="ECO:0007829|PDB:7NZ1"
FT HELIX 102..112
FT /evidence="ECO:0007829|PDB:7NZ1"
FT STRAND 122..131
FT /evidence="ECO:0007829|PDB:7NZ1"
FT HELIX 137..139
FT /evidence="ECO:0007829|PDB:7NZ1"
FT STRAND 143..145
FT /evidence="ECO:0007829|PDB:7NZ1"
FT STRAND 148..150
FT /evidence="ECO:0007829|PDB:7NZ1"
FT HELIX 155..157
FT /evidence="ECO:0007829|PDB:7NYR"
FT HELIX 158..163
FT /evidence="ECO:0007829|PDB:7NZ1"
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
