ID   NUOE_RICFE              Reviewed;         167 AA.
AC   Q4UM09;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 102.
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=RF_0563;
OS   Rickettsia felis (strain ATCC VR-1525 / URRWXCal2) (Rickettsia azadi).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX   NCBI_TaxID=315456;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-1525 / URRWXCal2;
RX   PubMed=15984913; DOI=10.1371/journal.pbio.0030248;
RA   Ogata H., Renesto P., Audic S., Robert C., Blanc G., Fournier P.-E.,
RA   Parinello H., Claverie J.-M., Raoult D.;
RT   "The genome sequence of Rickettsia felis identifies the first putative
RT   conjugative plasmid in an obligate intracellular parasite.";
RL   PLoS Biol. 3:1-12(2005).
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; CP000053; AAY61414.1; -; Genomic_DNA.
DR   RefSeq; WP_011270895.1; NC_007109.1.
DR   AlphaFoldDB; Q4UM09; -.
DR   SMR; Q4UM09; -.
DR   STRING; 315456.RF_0563; -.
DR   EnsemblBacteria; AAY61414; AAY61414; RF_0563.
DR   KEGG; rfe:RF_0563; -.
DR   eggNOG; COG1905; Bacteria.
DR   HOGENOM; CLU_054362_2_0_5; -.
DR   OMA; MYDTKPV; -.
DR   OrthoDB; 1206880at2; -.
DR   Proteomes; UP000008548; 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_0000287855"
FT   BINDING         88
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255"
FT   BINDING         93
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255"
FT   BINDING         129
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"
SQ   SEQUENCE   167 AA;  19316 MW;  212E48C1B1945973 CRC64;
     MSTNFTFDKK NLNLAEDIIK KYPPHGKRSA ILPLLDLAQR QNGGWLPVPA IEYVANMLEM
     PYMRAYEVAT FYSMFNLKRV GKYHIQVCTT TPCWLHGSDD IMKICEKKLG IKLKETTEDQ
     KFTLSEIECL GACVNAPVVQ INDDYYEDLT EEKMEKLIDE YSNDFKN