CMTB_PSEP1
ID CMTB_PSEP1 Reviewed; 259 AA.
AC A5W4G5; Q51977;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 79.
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; OrderedLocusNames=Pput_2895;
OS Pseudomonas putida (strain ATCC 700007 / DSM 6899 / BCRC 17059 / F1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=351746;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8631713; DOI=10.1128/jb.178.5.1351-1362.1996;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700007 / DSM 6899 / BCRC 17059 / F1;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Lykidis A., Parales R., Richardson P.;
RT "Complete sequence of Pseudomonas putida F1.";
RL Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases.
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; U24215; AAB62288.1; -; Genomic_DNA.
DR EMBL; CP000712; ABQ79025.1; -; Genomic_DNA.
DR RefSeq; WP_012052614.1; NC_009512.1.
DR AlphaFoldDB; A5W4G5; -.
DR SMR; A5W4G5; -.
DR STRING; 351746.Pput_2895; -.
DR EnsemblBacteria; ABQ79025; ABQ79025; Pput_2895.
DR KEGG; ppf:Pput_2895; -.
DR eggNOG; COG1028; Bacteria.
DR HOGENOM; CLU_010194_1_3_6; -.
DR OMA; SIMLLHP; -.
DR OrthoDB; 1356861at2; -.
DR BioCyc; MetaCyc:MON-348; -.
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_0000314469"
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
