ID   XYLE2_PSEPU             Reviewed;         307 AA.
AC   Q04285;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 102.
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=xylE;
OS   Pseudomonas putida (Arthrobacter siderocapsulatus).
OG   Plasmid TOL pDK1.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=303;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1672868; DOI=10.1128/jb.173.8.2724-2728.1991;
RA   Benjamin R.C., Voss J.A., Kunz D.A.;
RT   "Nucleotide sequence of xylE from the TOL pDK1 plasmid and structural
RT   comparison with isofunctional catechol-2,3-dioxygenase genes from TOL, pWW0
RT   and NAH7.";
RL   J. Bacteriol. 173:2724-2728(1991).
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; M65205; AAA23353.1; -; Genomic_DNA.
DR   PIR; A42733; A42733.
DR   RefSeq; WP_004576014.1; NZ_MING01000087.1.
DR   RefSeq; YP_003617184.1; NC_014124.1.
DR   RefSeq; YP_709347.1; NC_008275.1.
DR   AlphaFoldDB; Q04285; -.
DR   SMR; Q04285; -.
DR   KEGG; ag:AAA23353; -.
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; Plasmid; Repeat.
FT   CHAIN           1..307
FT                   /note="Metapyrocatechase"
FT                   /id="PRO_0000085028"
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;  35234 MW;  E91D95B331ECFEB8 CRC64;
     MKKGVMRPGH VQLRVLNLEA ALTHYRDLLG LIEMDRDEQG RVYLKAWSEV DKFSVVLREA
     DQPGMDFMGF KVTDDACLTR LAGELLEFGC QVEEIPAGEL KDCGRRVRFL APSGHFFELY
     AEKEYTGKWG IEEVNPEAWP RDLKGMRAVR FDHCLMYGDE LQATYELFTE VLGFYLAEQV
     IEDNGTRISQ FLSLSTKAHD VAFIQHAEKG KFHHVSFFLE TWEDVLRAAD LISMTDTSID
     IGPTRHGLTH GKTIYFFDPS GNRNEVFCGG DYNYPDHKPV TWTADQLGKA IFYHDRILNE
     RFMTVLT