ID   NUOE_PSEAE              Reviewed;         166 AA.
AC   Q9I0J8;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 133.
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=PA2640;
OS   Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS   14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208964;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC   PRS 101 / PAO1;
RX   PubMed=10984043; DOI=10.1038/35023079;
RA   Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA   Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA   Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA   Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA   Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA   Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT   "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT   pathogen.";
RL   Nature 406:959-964(2000).
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 (By similarity).
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the complex I 24 kDa subunit family.
CC       {ECO:0000305}.
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DR   EMBL; AE004091; AAG06028.1; -; Genomic_DNA.
DR   PIR; E83316; E83316.
DR   RefSeq; NP_251330.1; NC_002516.2.
DR   RefSeq; WP_003090460.1; NZ_QZGE01000008.1.
DR   AlphaFoldDB; Q9I0J8; -.
DR   SMR; Q9I0J8; -.
DR   STRING; 287.DR97_5322; -.
DR   PaxDb; Q9I0J8; -.
DR   PRIDE; Q9I0J8; -.
DR   DNASU; 882347; -.
DR   EnsemblBacteria; AAG06028; AAG06028; PA2640.
DR   GeneID; 882347; -.
DR   KEGG; pae:PA2640; -.
DR   PATRIC; fig|208964.12.peg.2762; -.
DR   PseudoCAP; PA2640; -.
DR   HOGENOM; CLU_054362_2_0_6; -.
DR   InParanoid; Q9I0J8; -.
DR   OMA; HIIRYCD; -.
DR   PhylomeDB; Q9I0J8; -.
DR   BioCyc; PAER208964:G1FZ6-2680-MON; -.
DR   Proteomes; UP000002438; 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_0000287833"
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;  18089 MW;  1D9E5ED1E13F19AC CRC64;
     MSQSNLIQTD RFVLSETERS SIEHEMHHYE DPRAASIEAL KIVQKQRGWV PDGAIPAIGE
     VLGIPASDVE GVATFYSQIF RQPVGRHIIR VCDSMVCYIG GHESVVGEIQ KQLGIGLGQT
     TADGRFTLLP VCCLGNCDKA PALMIDDDTH GDVRPDGVAK LLEAYV