ID   Q51974_PSEPU            Unreviewed;       434 AA.
AC   Q51974;
DT   01-NOV-1996, integrated into UniProtKB/TrEMBL.
DT   01-NOV-1996, sequence version 1.
DT   19-JAN-2010, entry version 53.
DE   SubName: Full=Large terminal subunit of p-cumate dioxygenase;
DE   SubName: Full=P-cumate dioxygenase large subunit;
GN   Name=cmtAb;
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; AAB62285.1; -; Genomic_DNA.
DR   EMBL; DQ157469; ABA10794.1; -; Genomic_DNA.
DR   EMBL; AB042508; BAB17771.1; -; Genomic_DNA.
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:0016708; F:oxidoreductase activity, acting on paired d...; IEA:InterPro.
DR   GO; GO:0016702; F:oxidoreductase activity, acting on single d...; IEA:UniProtKB-KW.
DR   GO; GO:0019439; P:aromatic compound catabolic process; IEA:InterPro.
DR   GO; GO:0055114; P:oxidation reduction; IEA:InterPro.
DR   InterPro; IPR017941; Rieske_2Fe-2S.
DR   InterPro; IPR015881; Ring-hydroxy_dOase_2Fe2S_BS.
DR   InterPro; IPR015879; Ring_hydroxy_dOase_asu_C.
DR   InterPro; IPR001663; Rng_hydr_dOase-A.
DR   Gene3D; G3DSA:2.102.10.10; Rieske_reg; 1.
DR   PANTHER; PTHR21266:SF2; Rng_hydr_dOase-A; 1.
DR   Pfam; PF00355; Rieske; 1.
DR   Pfam; PF00848; Ring_hydroxyl_A; 1.
DR   PRINTS; PR00090; RNGDIOXGNASE.
DR   PROSITE; PS51296; RIESKE; 1.
DR   PROSITE; PS00570; RING_HYDROXYL_ALPHA; 1.
PE   4: Predicted;
KW   2Fe-2S; Dioxygenase; Iron; Iron-sulfur; Metal-binding.
SQ   SEQUENCE   434 AA;  48968 MW;  820ABF7E578F4BCC CRC64;
     MNNDKNLVEI DDENLLFRVA RESFVSEEVL AEEYEKIFDR CWLYVGHTSE FKKPGDFVTR
     TVARRNLLVT MGTDRTINAF FNTCPHRGAT VCRERSGNSK NFQCFYHGWV FGCDGNLKSQ
     PGKERYCADF ITGGAGNLVP VPRFDIYAGF CFVSFNAEVE PLPDYLAGAK EYLELVSKYS
     ESGMGITTGT QEYAIRANWK LLVENSIDGY HAVSTHASYL DYLKNINDGF SGAKLEGKST
     DLGNGHAVIE FSAPWGRPIA SWVPIWGEEG KQEIDQIYAR LVELHGAEMA DRMAYKNRNL
     LIFPNLIIND IMAITVRTFY PQAPNYMHVN GWSLAPNEES DWARKYRLSN FLEFLGPGGF
     ATPDDVEALE SCQNGFSNYR LVPWSDISKG MGKETANYDD ELQMRAFWTR WNQFIGGAPT
     PDSGVQYIPT IALA
//