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 27-MAR-2024, entry version 123.
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; Pseudomonadota; 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}.
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DR EMBL; J04996; AAA26010.1; -; Genomic_DNA.
DR EMBL; CP000712; ABQ79007.1; -; Genomic_DNA.
DR PIR; F36516; F36516.
DR AlphaFoldDB; P13453; -.
DR SMR; P13453; -.
DR KEGG; ppf:Pput_2876; -.
DR eggNOG; COG0346; Bacteria.
DR HOGENOM; CLU_052361_2_0_6; -.
DR BioCyc; MetaCyc:MONOMER-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 CDD; cd07237; BphC1-RGP6_C_like; 1.
DR CDD; cd07252; BphC1-RGP6_N_like; 1.
DR Gene3D; 3.10.180.10; 2,3-Dihydroxybiphenyl 1,2-Dioxygenase, domain 1; 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 NCBIfam; TIGR03213; 23dbph12diox; 1.
DR PANTHER; PTHR21366; GLYOXALASE FAMILY PROTEIN; 1.
DR PANTHER; PTHR21366:SF34; IRON-DEPENDENT EXTRADIOL DIOXYGENASE; 1.
DR Pfam; PF00903; Glyoxalase; 1.
DR SUPFAM; SSF54593; Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase; 2.
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
//
