ID   Q51976_PSEPU            Unreviewed;       312 AA.
AC   Q51976;
DT   01-NOV-1996, integrated into UniProtKB/TrEMBL.
DT   01-NOV-1996, sequence version 1.
DT   24-NOV-2009, entry version 52.
DE   SubName: Full=2,3-dihydroxy-p-cumate dioxygenase;
DE   SubName: Full=2,3-dihydroxy-p-cumate-3,4-dioxygenase;
GN   Name=cmtC;
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   -!- COFACTOR: Fe(2+) ion (By similarity).
CC   -!- SIMILARITY: Belongs to the extradiol ring-cleavage dioxygenase
CC       family.
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DR   EMBL; U24215; AAB62287.1; -; Genomic_DNA.
DR   EMBL; DQ157469; ABA10796.1; -; Genomic_DNA.
DR   EMBL; AB042508; BAB17773.1; -; Genomic_DNA.
DR   GO; GO:0008198; F:ferrous iron binding; 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:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR004360; Glyas_bleo-R_dOase.
DR   InterPro; IPR000486; Xdiol_ring_cleave_dOase_1/2.
DR   Pfam; PF00903; Glyoxalase; 2.
DR   PROSITE; PS00082; EXTRADIOL_DIOXYGENAS; 1.
PE   3: Inferred from homology;
KW   Aromatic hydrocarbons catabolism; Dioxygenase; Iron; Oxidoreductase.
SQ   SEQUENCE   312 AA;  35366 MW;  0BE88600D9733926 CRC64;
     MDITLPFRYK KLAYAAINVT DLSRSVPFYR DIVGLDLVKQ DGDIAYFRCS RDHHNIVLYQ
     APGHGLKRVG FELEQESDVR AAFEHFDQRG MQPTWVSAEE AKQLRQGLGF RVRERHSGLL
     FELFVGNMHL SNPFVPTVAK IARIGHVVIG SENFEGSRDS LVDDFGFRVS DLIEDRIVFM
     RCHPNPFHHT FAVGPASSSH FHHVNFMVTD IDDIGKALYR IKQHDIKVVF GPGRHPPSDS
     VFFYFLDPDG ITVEYSFGME EFAEHGARPP RYMEPVPESL DAWGAVPDGQ FGRSGPIERE
     RMPTPHAKGV LA
//