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   03-AUG-2022, entry version 51.
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 (Arthrobacter siderocapsulatus).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=303;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=CE2010;
RX   PubMed=11160798; DOI=10.1099/00221287-147-1-31;
RA   Ohta Y., Maeda M., Kudo T.;
RT   "Pseudomonas putida CE2010 can degrade biphenyl by a mosaic pathway encoded
RT   by the tod operon and cmtE, which are identical to those of P. putida F1
RT   except for a single base difference in the operator-promoter region of the
RT   cmt operon.";
RL   Microbiology 147:31-41(2001).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2R,3S)-2,3-dihydroxy-2,3-dihydro-p-cumate + NAD(+) = 2,3-
CC         dihydroxy-p-cumate + H(+) + NADH; Xref=Rhea:RHEA:23772,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:36647, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945, ChEBI:CHEBI:58420; EC=1.3.1.58;
CC   -!- PATHWAY: Aromatic compound metabolism; p-cumate degradation;
CC       acetaldehyde and pyruvate from p-cumate: step 2/7.
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC       family. {ECO:0000305}.
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DR   EMBL; AB042508; BAB17774.1; -; Genomic_DNA.
DR   RefSeq; WP_012052614.1; NZ_NHBC01000013.1.
DR   AlphaFoldDB; P0C622; -.
DR   SMR; P0C622; -.
DR   UniPathway; UPA00937; UER00902.
DR   GO; GO:0018511; F:2,3-dihydroxy-2,3-dihydro-p-cumate dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-KW.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR   InterPro; IPR002347; SDR_fam.
DR   PRINTS; PR00081; GDHRDH.
DR   PRINTS; PR00080; SDRFAMILY.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   PROSITE; PS00061; ADH_SHORT; 1.
PE   3: Inferred from homology;
KW   Aromatic hydrocarbons catabolism; NAD; Oxidoreductase.
FT   CHAIN           1..259
FT                   /note="2,3-dihydroxy-2,3-dihydro-p-cumate dehydrogenase"
FT                   /id="PRO_0000054550"
FT   ACT_SITE        163
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT   BINDING         18..42
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
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