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Database: UniProt
Entry: Q1RJJ1
LinkDB: Q1RJJ1
Original site: Q1RJJ1 
ID   NUOE_RICBR              Reviewed;         167 AA.
AC   Q1RJJ1;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 1.
DT   26-NOV-2014, entry version 66.
DE   RecName: Full=NADH-quinone oxidoreductase subunit E;
DE            EC=1.6.99.5;
DE   AltName: Full=NADH dehydrogenase I subunit E;
DE   AltName: Full=NDH-1 subunit E;
GN   Name=nuoE; OrderedLocusNames=RBE_0392;
OS   Rickettsia bellii (strain RML369-C).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; belli group.
OX   NCBI_TaxID=336407;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RML369-C;
RX   PubMed=16703114; DOI=10.1371/journal.pgen.0020076;
RA   Ogata H., La Scola B., Audic S., Renesto P., Blanc G., Robert C.,
RA   Fournier P.-E., Claverie J.-M., Raoult D.;
RT   "Genome sequence of Rickettsia bellii illuminates the role of amoebae
RT   in gene exchanges between intracellular pathogens.";
RL   PLoS Genet. 2:733-744(2006).
CC   -!- FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron-
CC       sulfur (Fe-S) centers, to quinones in the respiratory chain.
CC       Couples the redox reaction to proton translocation (for every two
CC       electrons transferred, four hydrogen ions are translocated across
CC       the cytoplasmic membrane), and thus conserves the redox energy in
CC       a proton gradient (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY: NADH + quinone = NAD(+) + 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   -!- SIMILARITY: Belongs to the complex I 24 kDa subunit family.
CC       {ECO:0000305}.
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DR   EMBL; CP000087; ABE04473.1; -; Genomic_DNA.
DR   RefSeq; WP_011477082.1; NC_007940.1.
DR   RefSeq; YP_537562.1; NC_007940.1.
DR   ProteinModelPortal; Q1RJJ1; -.
DR   STRING; 336407.RBE_0392; -.
DR   EnsemblBacteria; ABE04473; ABE04473; RBE_0392.
DR   GeneID; 3995229; -.
DR   KEGG; rbe:RBE_0392; -.
DR   PATRIC; 17882133; VBIRicBel102610_0443.
DR   eggNOG; COG1905; -.
DR   HOGENOM; HOG000257748; -.
DR   KO; K00334; -.
DR   OMA; HIPHIRV; -.
DR   OrthoDB; EOG689HX9; -.
DR   BioCyc; RBEL336407:GJCY-402-MONOMER; -.
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:0050136; F:NADH dehydrogenase (quinone) activity; IEA:UniProtKB-EC.
DR   GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.30.10; -; 1.
DR   InterPro; IPR002023; NuoE-like.
DR   InterPro; IPR012336; Thioredoxin-like_fold.
DR   PANTHER; PTHR10371; PTHR10371; 1.
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; Complete proteome; Iron; Iron-sulfur; Metal-binding; NAD;
KW   Oxidoreductase; Quinone.
FT   CHAIN         1    167       NADH-quinone oxidoreductase subunit E.
FT                                /FTId=PRO_0000287854.
FT   METAL        91     91       Iron-sulfur (2Fe-2S). {ECO:0000255}.
FT   METAL        96     96       Iron-sulfur (2Fe-2S). {ECO:0000255}.
FT   METAL       132    132       Iron-sulfur (2Fe-2S). {ECO:0000255}.
FT   METAL       136    136       Iron-sulfur (2Fe-2S). {ECO:0000255}.
SQ   SEQUENCE   167 AA;  19101 MW;  16179A4204770C38 CRC64;
     MNTKITNFSF DKKNLSLAED IIKKYPPEGK RSAILPLLDL AQRQNGGWLP VPAIEYVANM
     LEMPYMRAYE VATFYTMFNL KPVGKNHIQV CTTTPCWLRG SDDIMKTCKE KLGIKDEEVT
     KDQKFSLIEI ECLGACVNAP VVQINDDYYE DLTPEKMEAI IDKLRND
//
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