ID   CATA_RHORH              Reviewed;         318 AA.
AC   Q53034;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 71.
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=catA;
OS   Rhodococcus rhodochrous.
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Rhodococcus.
OX   NCBI_TaxID=1829;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=NCIMB 13064 / Isolate P200;
RX   PubMed=9579069; DOI=10.1099/00221287-144-4-955;
RA   Kulakov L.A., Delcroix V.A., Larkin M.J., Ksenzenko V.N., Kulakova A.N.;
RT   "Cloning of new Rhodococcus extradiol dioxygenase genes and study of their
RT   distribution in different Rhodococcus strains.";
RL   Microbiology 144:955-963(1998).
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; Evidence={ECO:0000250};
CC   -!- SIMILARITY: Belongs to the extradiol ring-cleavage dioxygenase family.
CC       {ECO:0000305}.
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DR   EMBL; L77225; AAC18907.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q53034; -.
DR   SMR; Q53034; -.
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:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0042178; P:xenobiotic catabolic process; IEA:InterPro.
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; 1.
DR   TIGRFAMs; TIGR03213; 23dbph12diox; 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..318
FT                   /note="Metapyrocatechase"
FT                   /id="PRO_0000085031"
FT   DOMAIN          6..120
FT                   /note="VOC 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01163"
FT   DOMAIN          143..263
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         209
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   BINDING         259
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   318 AA;  35438 MW;  ED9EB5EAA9659058 CRC64;
     MALVTGIGYI GIGVSDLPAW EEFAETIGFQ IRERGEDGTL YLRMDKAHHR VAVHPTGEDD
     LTYVGWQVAD ENGFDELERT LRAAGVPVEM AGEDDAELRG VARLMRFEDP SGIKSEAYYG
     LVSEPEVPYV SPYAVDFVTE DQGFGHIVVM VDDYDETMRF YREVLGLQTS DLVKVGAGGV
     QTRMAFMRCN PRQHSLAFWA GDSTTRLNHF MLQTQTLDQT GMTLDRCFHG GIPATNLGRH
     VNDYAVSFYI TTPSGFMIEY GWGVREVVSD YPVDKYRSVS IWGHRNLDGI HYTQALPPEA
     AESPAEQHLV EEPVAAAV