ID   DMPB_PSEUF              Reviewed;         307 AA.
AC   P17262;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1990, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Metapyrocatechase;
DE            Short=MPC;
DE            EC=1.13.11.2;
DE   AltName: Full=CatO2ase;
DE   AltName: Full=Catechol 2,3-dioxygenase;
DE            Short=C23O;
GN   Name=dmpB;
OS   Pseudomonas sp. (strain CF600).
OG   Plasmid pVI150.
OC   Bacteria; Proteobacteria.
OX   NCBI_TaxID=79676;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2620833; DOI=10.1016/0378-1119(89)90487-3;
RA   Bartilson M., Shingler V.;
RT   "Nucleotide sequence and expression of the catechol 2,3-dioxygenase-
RT   encoding gene of phenol-catabolizing Pseudomonas CF600.";
RL   Gene 85:233-238(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 287-307.
RX   PubMed=2194577; DOI=10.1016/0167-4781(90)90046-5;
RA   Nordlund I., Shingler V.;
RT   "Nucleotide sequences of the meta-cleavage pathway enzymes 2-hydroxymuconic
RT   semialdehyde dehydrogenase and 2-hydroxymuconic semialdehyde hydrolase from
RT   Pseudomonas CF600.";
RL   Biochim. Biophys. Acta 1049:227-230(1990).
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: Aromatic compound metabolism; benzoate degradation via
CC       hydroxylation.
CC   -!- SUBUNIT: Homotetramer.
CC   -!- SIMILARITY: Belongs to the extradiol ring-cleavage dioxygenase family.
CC       {ECO:0000305}.
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DR   EMBL; M33263; AAA27512.1; -; Genomic_DNA.
DR   EMBL; X52805; CAA36991.1; -; Genomic_DNA.
DR   PIR; JQ0182; JQ0182.
DR   AlphaFoldDB; P17262; -.
DR   SMR; P17262; -.
DR   UniPathway; UPA00156; -.
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:0043640; P:benzoate catabolic process via hydroxylation; 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_0000085029"
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;  35255 MW;  96439652C23800BF CRC64;
     MKKGVMRPGH VQLRVLNLES ALAHYRDLLG LIEMDRDEQG RVYLKAWTEV DKFSVVLREA
     DQPGMDFMGF KVIDEDCLNR LTQDLLNYGC LIETIPAGEL KGCGRRVRFQ TPSGHFFELY
     ADKEYTGKWG LEEINPEAWP RNLKGMRAVR FDHCLLYGDE LQATYALFTE VLGFYLAEQV
     IDDDGTRVAQ FLSLSTKAHD VAFIHCPEKG KFHHVSFFLE TWEDVLRAAD LISMTDTSID
     IGPTRHGLTH GKTIYFFDPS GNRNEVFCGG DYNYQDHKPV TWLAKDLGKA IFYHDRVLNE
     RFLTVLT