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 01-MAY-2013, entry version 58.
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).
CC -!- CATALYTIC ACTIVITY: NADH + quinone = NAD(+) + quinol.
CC -!- COFACTOR: Binds 1 2Fe-2S cluster (Potential).
CC -!- SIMILARITY: Belongs to the complex I 24 kDa subunit family.
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DR EMBL; CP000087; ABE04473.1; -; Genomic_DNA.
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; AMNYIAD; -.
DR ProtClustDB; PRK07539; -.
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:EC.
DR GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW.
DR Gene3D; 3.40.30.10; -; 1.
DR InterPro; IPR002023; 2Fe-2S_Ferredox.
DR InterPro; IPR012336; Thioredoxin-like_fold.
DR PANTHER; PTHR10371; PTHR10371; 1.
DR Pfam; PF01257; Complex1_24kDa; 1.
DR PIRSF; PIRSF000216; NADH_DH_24kDa; 1.
DR SUPFAM; SSF52833; Thiordxn-like_fd; 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) (Potential).
FT METAL 96 96 Iron-sulfur (2Fe-2S) (Potential).
FT METAL 132 132 Iron-sulfur (2Fe-2S) (Potential).
FT METAL 136 136 Iron-sulfur (2Fe-2S) (Potential).
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
//
