ID   TODD_PSEP1              Reviewed;         275 AA.
AC   P13859; A5W4E8;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1990, sequence version 1.
DT   03-AUG-2022, entry version 127.
DE   RecName: Full=Cis-toluene dihydrodiol dehydrogenase;
DE            EC=1.3.1.-;
GN   Name=todD; OrderedLocusNames=Pput_2877;
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], AND PROTEIN SEQUENCE OF 1-12.
RX   PubMed=2670929; DOI=10.1016/s0021-9258(18)63793-7;
RA   Zylstra G.J., Gibson D.T.;
RT   "Toluene degradation by Pseudomonas putida F1. Nucleotide sequence of the
RT   todC1C2BADE genes and their expression in Escherichia coli.";
RL   J. Biol. Chem. 264:14940-14946(1989).
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=(1S,2R)-3-methylcyclohexa-3,5-diene-1,2-diol + NAD(+) = 3-
CC         methylcatechol + H(+) + NADH; Xref=Rhea:RHEA:25193,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15565, ChEBI:CHEBI:18404,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC   -!- PATHWAY: Xenobiotic degradation; toluene degradation.
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC       family. {ECO:0000305}.
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DR   EMBL; J04996; AAA26009.1; -; Genomic_DNA.
DR   EMBL; CP000712; ABQ79008.1; -; Genomic_DNA.
DR   PIR; E36516; E36516.
DR   RefSeq; WP_012052597.1; NC_009512.1.
DR   AlphaFoldDB; P13859; -.
DR   SMR; P13859; -.
DR   STRING; 351746.Pput_2877; -.
DR   EnsemblBacteria; ABQ79008; ABQ79008; Pput_2877.
DR   KEGG; ppf:Pput_2877; -.
DR   eggNOG; COG1028; Bacteria.
DR   HOGENOM; CLU_010194_1_0_6; -.
DR   OMA; VFHINVK; -.
DR   OrthoDB; 1356861at2; -.
DR   BioCyc; MetaCyc:MON-11352; -.
DR   UniPathway; UPA00273; -.
DR   GO; GO:0016628; F:oxidoreductase activity, acting on the CH-CH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR   GO; GO:0042203; P:toluene catabolic process; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR017711; BphB_TodD.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR   InterPro; IPR002347; SDR_fam.
DR   Pfam; PF00106; adh_short; 1.
DR   PRINTS; PR00081; GDHRDH.
DR   PRINTS; PR00080; SDRFAMILY.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   TIGRFAMs; TIGR03325; BphB_TodD; 1.
DR   PROSITE; PS00061; ADH_SHORT; 1.
PE   1: Evidence at protein level;
KW   Aromatic hydrocarbons catabolism; Direct protein sequencing; NAD;
KW   Oxidoreductase.
FT   CHAIN           1..275
FT                   /note="Cis-toluene dihydrodiol dehydrogenase"
FT                   /id="PRO_0000054784"
FT   ACT_SITE        155
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT   BINDING         9..33
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         142
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   275 AA;  28782 MW;  D5919208D859234B CRC64;
     MRLEGEVALV TGGGAGLGRA IVDRYVAEGA RVAVLDKSAA GLEALRKLHG DAIVGVEGDV
     RSLDSHREAV ARCVEAFGKL DCLVGNAGVW DYLTQLVDIP DDLISEAFEE MFEVNVKGYI
     LAAKAALPAL YQSKGSAIFT VSNAGFYPGG GGVLYTAGKH AVIGLIKQLA HEWGPRIRVN
     GIAPGGILGS DLRGLKSLDL QDKSISTFPL DDMLKSVLPT GRAATAEEYA GAYVFFATRG
     DTVPLTGSVL NFDGGMGVRG LFEASLGAQL DKHFG