ID   NUOE_RICCN              Reviewed;         167 AA.
AC   Q92ID9;
DT   23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 122.
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=RC0481;
OS   Rickettsia conorii (strain ATCC VR-613 / Malish 7).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX   NCBI_TaxID=272944;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-613 / Malish 7;
RX   PubMed=11557893; DOI=10.1126/science.1061471;
RA   Ogata H., Audic S., Renesto-Audiffren P., Fournier P.-E., Barbe V.,
RA   Samson D., Roux V., Cossart P., Weissenbach J., Claverie J.-M., Raoult D.;
RT   "Mechanisms of evolution in Rickettsia conorii and R. prowazekii.";
RL   Science 293:2093-2098(2001).
CC   -!- FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur
CC       (Fe-S) centers, to quinones in the respiratory chain. Couples the redox
CC       reaction to proton translocation (for every two electrons transferred,
CC       four hydrogen ions are translocated across the cytoplasmic membrane),
CC       and thus conserves the redox energy in a proton gradient (By
CC       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   -!- SIMILARITY: Belongs to the complex I 24 kDa subunit family.
CC       {ECO:0000305}.
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DR   EMBL; AE006914; AAL03019.1; -; Genomic_DNA.
DR   PIR; A97760; A97760.
DR   RefSeq; WP_010977123.1; NC_003103.1.
DR   AlphaFoldDB; Q92ID9; -.
DR   SMR; Q92ID9; -.
DR   EnsemblBacteria; AAL03019; AAL03019; RC0481.
DR   KEGG; rco:RC0481; -.
DR   PATRIC; fig|272944.4.peg.551; -.
DR   HOGENOM; CLU_054362_2_0_5; -.
DR   OMA; MYDTKPV; -.
DR   Proteomes; UP000000816; 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: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; Translocase.
FT   CHAIN           1..167
FT                   /note="NADH-quinone oxidoreductase subunit E"
FT                   /id="PRO_0000118700"
FT   BINDING         91
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255"
FT   BINDING         96
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255"
FT   BINDING         132
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255"
FT   BINDING         136
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   167 AA;  19156 MW;  DE33CF1F29451EB4 CRC64;
     MNTKITNFTF DKKNLNLAEE IIKKYPPHGK RSAILPLLDL AQRQNGGWLP VPAIEYVANM
     LAMPYIRAYE VATFYTMFNL KRVGKYHIQV CTTTPCWLRG SDDIMKICEK KLGVKLKETT
     EDQKFTLSEI ECLGACVNAP VVQINDDYYE DLTQDKMGKI IDKLQND