ID   CMTB_PSEPU              Reviewed;         259 AA.
AC   P0C622; Q51977;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   16-JUN-2009, entry version 10.
DE   RecName: Full=2,3-dihydroxy-2,3-dihydro-p-cumate dehydrogenase;
DE            EC=1.3.1.58;
DE   AltName: Full=Biphenyl-2,3-dihydro-2,3-diol dehydrogenase;
GN   Name=cmtB;
OS   Pseudomonas putida.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=303;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=CE2010;
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   -!- CATALYTIC ACTIVITY: Cis-5,6-dihydroxy-4-isopropylcyclohexa-1,3-
CC       dienecarboxylate + NAD(+) = 2,3-dihydroxy-p-cumate + NADH.
CC   -!- PATHWAY: Aromatic compound metabolism; p-cumic acid degradation;
CC       acetaldehyde and pyruvate from p-cumic acid: step 2/7.
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases
CC       (SDR) family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AB042508; BAB17774.1; -; Genomic_DNA.
DR   HSSP; P50163; 2AE1.
DR   BRENDA; 1.3.1.58; 403.
DR   GO; GO:0018511; F:2,3-dihydroxy-2,3-dihydro-p-cumate dehydrog...; IEA:EC.
DR   GO; GO:0005488; F:binding; IEA:InterPro.
DR   GO; GO:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR002198; DH_sc/Rdtase_SDR.
DR   InterPro; IPR002347; Glc/ribitol_DH.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1.
DR   PANTHER; PTHR19410; ADH_short_C2; 1.
DR   Pfam; PF00106; adh_short; 1.
DR   PRINTS; PR00081; GDHRDH.
DR   PRINTS; PR00080; SDRFAMILY.
DR   PROSITE; PS00061; ADH_SHORT; 1.
PE   3: Inferred from homology;
KW   Aromatic hydrocarbons catabolism; NAD; Oxidoreductase.
FT   CHAIN         1    259       2,3-dihydroxy-2,3-dihydro-p-cumate
FT                                dehydrogenase.
FT                                /FTId=PRO_0000054550.
FT   NP_BIND      18     42       NAD (By similarity).
FT   ACT_SITE    163    163       Proton acceptor (By similarity).
SQ   SEQUENCE   259 AA;  27310 MW;  B4CD9C3DDC833A8B CRC64;
     MSTLSRNALP LEGQVAVVTG GAHGIGLGIV ERLLGLGARV TASDIDESGL SLLCERLAAK
     HADAIAVHAA DLSEEQGAQG LHRAAVERFG SVQILVNCAG GGVIRPFLEH TPETLKATID
     RNLWTALWCS RVFLPDMLAR QYGRIINIGA DSVRNGLPDH AAYNAAKGGM HGLTTGLARE
     FARQGVTVNT VAPCAVNTEV WVRIKNANPE LAQRFLDVIP MGRVGEIEEV ASMVGYLAQP
     EAAFVTGQVI SVNGGSTML
//