ID   XYLE_PSEAI              Reviewed;         307 AA.
AC   P27887;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Metapyrocatechase;
DE            Short=MPC;
DE            EC=1.13.11.2;
DE   AltName: Full=CatO2ase;
DE   AltName: Full=Catechol 2,3-dioxygenase;
GN   Name=bztE;
OS   Pseudomonas aeruginosa.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=JI104;
RA   Kitayama A., Achioku T., Yanagawa T., Kanou K., Kikuchi M., Ueda H.,
RA   Suzuki E., Nishimura H., Nagamune T., Kawakami Y.;
RT   "Cloning and characterization of extradiol aromatic ring-cleavage
RT   dioxygenases of Pseudomonas aeruginosa JI104.";
RL   J. Ferment. Bioeng. 82:217-223(1996).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=catechol + O2 = (2Z,4E)-2-hydroxy-6-oxohexa-2,4-dienoate +
CC         H(+); Xref=Rhea:RHEA:17337, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:18135, ChEBI:CHEBI:71198; EC=1.13.11.2;
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC   -!- PATHWAY: Xenobiotic degradation; toluene degradation.
CC   -!- SUBUNIT: Homotetramer.
CC   -!- SIMILARITY: Belongs to the extradiol ring-cleavage dioxygenase family.
CC       {ECO:0000305}.
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DR   EMBL; X60740; CAA43145.1; -; Genomic_DNA.
DR   PIR; S15522; JC2503.
DR   AlphaFoldDB; P27887; -.
DR   SMR; P27887; -.
DR   UniPathway; UPA00273; -.
DR   GO; GO:0018577; F:catechol 2,3-dioxygenase activity; IEA:UniProtKB-EC.
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; IPR017624; Catechol_2-3_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; 1.
DR   TIGRFAMs; TIGR03211; catechol_2_3; 1.
DR   PROSITE; PS00082; EXTRADIOL_DIOXYGENAS; 1.
DR   PROSITE; PS51819; VOC; 2.
PE   3: Inferred from homology;
KW   Aromatic hydrocarbons catabolism; Dioxygenase; Iron; Metal-binding;
KW   Oxidoreductase; Repeat.
FT   CHAIN           1..307
FT                   /note="Metapyrocatechase"
FT                   /id="PRO_0000085026"
FT   DOMAIN          7..122
FT                   /note="VOC 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01163"
FT   DOMAIN          150..269
FT                   /note="VOC 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01163"
FT   BINDING         153
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   BINDING         214
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   BINDING         265
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   307 AA;  35124 MW;  E178E5F287410ACC CRC64;
     MNKGIMRPGH VQLRVLDMSK ALEHYVELLG LIEMDRDDQG RVYLKAWTEV DKFSVVLRER
     DEPGMDFMGF KVVDEDALRQ LERDLTAYGC AVEQLPAGEL NSCGRRVRFQ APSGHHFELY
     ADKEYTGKWG VNEVNPEAWP RDLKGMAAVR FDHCLLYGDE LPATYDLFTK VLGFYLAEQV
     LDENGTRVAQ FLSLSTKAHD VAFIHHPEKG RLHHVSFHLE TWEDVLRAAD LISMTDTSID
     IGPTRHGLTH GKTIYFFDPS GNRSEVFCGG NYSYPDHKPV TWLAKDLGKA IFYHDRVLNE
     RFMTVLT