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Database: UniProt
Entry: Q51978
LinkDB: Q51978
Original site: Q51978 
ID   Q51978_PSEPU            Unreviewed;       118 AA.
AC   Q51978;
DT   01-NOV-1996, integrated into UniProtKB/TrEMBL.
DT   01-NOV-1996, sequence version 1.
DT   19-JAN-2010, entry version 46.
DE   SubName: Full=Ferredoxin subunit of p-cumate dioxygenase;
DE   SubName: Full=P-cumate dioxygenase ferredoxin component;
DE   SubName: Full=P-cumate dioxygenase ferredoxin subunit;
GN   Name=cmtAd;
OS   Pseudomonas putida.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=303;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=F1;
RX   MEDLINE=96200106; PubMed=8631713;
RA   Eaton R.W.;
RT   "p-cumate catabolic pathway in Pseudomonas putida F1: cloning and
RT   characterization of DNA carrying the cmt operon.";
RL   J. Bacteriol. 178:1351-1362(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=F1;
RX   MEDLINE=97294455; PubMed=9150211;
RA   Eaton R.W.;
RT   "p-Cymene catabolic pathway in Pseudomonas putida F1: cloning and
RT   characterization of DNA encoding conversion of p-cymene to p-cumate.";
RL   J. Bacteriol. 179:3171-3180(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=KL47;
RX   PubMed=16728956;
RA   Lee K., Ryu E.K., Choi K.S., Cho M.C., Jeong J.J., Choi E.N.,
RA   Lee S.O., Yoon D.Y., Hwang I., Kim C.K.;
RT   "Identification and expression of the cym, cmt, and tod catabolic
RT   genes from Pseudomonas putida KL47: expression of the regulatory todST
RT   genes as a factor for catabolic adaptation.";
RL   J. Microbiol. 44:192-199(2006).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RX   MEDLINE=21097241; PubMed=11160798;
RA   Ohta Y., Maeda M., Kudo T.;
RT   "Pseudomonas putida CE2010 can degrade biphenyl by a mosaic pathway
RT   encoded by the tod operon and cmtE, which are identical to those of P.
RT   putida F1 except for a single base difference in the operator-promoter
RT   region of the cmt operon.";
RL   Microbiology 147:31-41(2001).
CC   -!- SIMILARITY: Contains 1 Rieske domain.
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DR   EMBL; U24215; AAB62289.1; -; Genomic_DNA.
DR   EMBL; DQ157469; ABA10798.1; -; Genomic_DNA.
DR   EMBL; AB042508; BAB17775.1; -; Genomic_DNA.
DR   HSSP; P37332; 1FQT.
DR   SMR; Q51978; 13-113.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016702; F:oxidoreductase activity, acting on single d...; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:InterPro.
DR   InterPro; IPR017941; Rieske_2Fe-2S.
DR   Gene3D; G3DSA:2.102.10.10; Rieske_reg; 1.
DR   Pfam; PF00355; Rieske; 1.
DR   PROSITE; PS51296; RIESKE; 1.
PE   4: Predicted;
KW   2Fe-2S; Dioxygenase; Iron; Iron-sulfur; Metal-binding.
SQ   SEQUENCE   118 AA;  12736 MW;  045B2031DCE756D6 CRC64;
     MTNIIETVDL TDLVGLCATD DVAEGEILRV KLPSGHALAI YCVNGEFFAT DDICSHGEAS
     LSEDGSLDGY EVECSWHFGR FDIRTGHACA MPCEHPLRSW PVTVEGGQIF VDVGAHPV
//
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Ontology (4)   
   GO (4)   
DNA sequence (3)   
   EMBL (3)   
Protein domain (5)   
   InterPro (1)   
   Pfam (1)   
   PROSITE (1)   
   Blocks (2)   
Literature (4)   
   PubMed (4)   
All databases (16)   
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