ID   TODE_PSEP1              Reviewed;         291 AA.
AC   P13453; A5W4E7;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 115.
DE   RecName: Full=3-methylcatechol 2,3-dioxygenase;
DE            EC=1.13.11.-;
GN   Name=todE; OrderedLocusNames=Pput_2876;
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 2-13.
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=3-methylcatechol + O2 = 2-hydroxy-6-oxo-2,4-heptadienoate +
CC         H(+); Xref=Rhea:RHEA:48996, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:18404, ChEBI:CHEBI:90887;
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC   -!- PATHWAY: Xenobiotic degradation; toluene degradation.
CC   -!- SUBUNIT: Homooctamer.
CC   -!- SIMILARITY: Belongs to the extradiol ring-cleavage dioxygenase family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; J04996; AAA26010.1; -; Genomic_DNA.
DR   EMBL; CP000712; ABQ79007.1; -; Genomic_DNA.
DR   PIR; F36516; F36516.
DR   RefSeq; WP_012052596.1; NC_009512.1.
DR   AlphaFoldDB; P13453; -.
DR   SMR; P13453; -.
DR   STRING; 351746.Pput_2876; -.
DR   PRIDE; P13453; -.
DR   EnsemblBacteria; ABQ79007; ABQ79007; Pput_2876.
DR   KEGG; ppf:Pput_2876; -.
DR   eggNOG; COG0346; Bacteria.
DR   HOGENOM; CLU_052361_2_0_6; -.
DR   OMA; KMSATLG; -.
DR   OrthoDB; 1335734at2; -.
DR   BioCyc; MetaCyc:MON-11354; -.
DR   UniPathway; UPA00273; -.
DR   GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008198; F:ferrous iron binding; IEA:InterPro.
DR   GO; GO:0042203; P:toluene catabolic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.10.180.10; -; 2.
DR   InterPro; IPR017626; DiOHbiphenyl_dOase.
DR   InterPro; IPR029068; Glyas_Bleomycin-R_OHBP_Dase.
DR   InterPro; IPR004360; Glyas_Fos-R_dOase_dom.
DR   InterPro; IPR037523; VOC.
DR   InterPro; IPR000486; Xdiol_ring_cleave_dOase_1/2.
DR   Pfam; PF00903; Glyoxalase; 1.
DR   SUPFAM; SSF54593; SSF54593; 2.
DR   TIGRFAMs; TIGR03213; 23dbph12diox; 1.
DR   PROSITE; PS00082; EXTRADIOL_DIOXYGENAS; 1.
DR   PROSITE; PS51819; VOC; 2.
PE   1: Evidence at protein level;
KW   Aromatic hydrocarbons catabolism; Dioxygenase; Direct protein sequencing;
KW   Iron; Metal-binding; Oxidoreductase; Repeat.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:2670929"
FT   CHAIN           2..291
FT                   /note="3-methylcatechol 2,3-dioxygenase"
FT                   /id="PRO_0000085032"
FT   DOMAIN          5..119
FT                   /note="VOC 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01163"
FT   DOMAIN          143..264
FT                   /note="VOC 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01163"
FT   BINDING         146
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   BINDING         210
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   BINDING         260
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   291 AA;  32209 MW;  6D5911CB1A9043FF CRC64;
     MSIQRLGYLG FEVADVRSWR TFATTRLGMM EASASETEAT FRIDSRAWRL SVSRGPADDY
     LFAGFEVDSE QGLQEVKESL QAHGVTVKVE GGELIAKRGV LGLISCTDPF GNRVEIYYGA
     TELFERPFAS PTGVSGFQTG DQGLGHYVLS VADVDAALAF YTKALGFQLA DVIDWTIGDG
     LSVTLYFLYC NGRHHSFAFA KLPGSKRLHH FMLQANGMDD VGLAYDKFDA ERAVVMSLGR
     HTNDHMISFY GATPSGFAVE YGWGAREVTR HWSVVRYDRI SIWGHKFQAP A