ID   PHEB_GEOSE              Reviewed;         327 AA.
AC   P31003;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   02-SEP-2026, entry version 90.
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=pheB;
OS   Geobacillus stearothermophilus (Bacillus stearothermophilus).
OC   Bacteria; Bacillati; Bacillota; Bacilli; Caryophanales; Anoxybacillaceae;
OC   Geobacillus.
OX   NCBI_TaxID=1422;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=FDTP-3;
RA   He Z.-Q., Mao Y.-M., Sheng Z.-J., Shen R.-Q.;
RL   Submitted (JUL-1992) to the EMBL/GenBank/DDBJ databases.
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   -!- SIMILARITY: Belongs to the extradiol ring-cleavage dioxygenase family.
CC       {ECO:0000305}.
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DR   EMBL; X67860; CAA48044.1; -; Genomic_DNA.
DR   PIR; JC1324; JC1324.
DR   AlphaFoldDB; P31003; -.
DR   SMR; P31003; -.
DR   GO; GO:0018577; F:catechol 2,3-dioxygenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008198; F:ferrous iron binding; IEA:InterPro.
DR   CDD; cd09014; BphC-JF8_C_like; 1.
DR   CDD; cd09013; BphC-JF8_N_like; 1.
DR   Gene3D; 3.10.180.10; 2,3-Dihydroxybiphenyl 1,2-Dioxygenase, domain 1; 2.
DR   InterPro; IPR017624; Catechol_2-3_dOase.
DR   InterPro; IPR051332; Fosfomycin_Res_Enzymes.
DR   InterPro; IPR029068; Glyas_Bleomycin-R_OHBP_Dase.
DR   InterPro; IPR004360; Glyas_Fos-R_dOase_dom.
DR   InterPro; IPR037523; VOC_core.
DR   InterPro; IPR000486; Xdiol_ring_cleave_dOase_1/2.
DR   NCBIfam; TIGR03211; catechol_2_3; 1.
DR   PANTHER; PTHR36113:SF6; FOSFOMYCIN RESISTANCE PROTEIN FOSX; 1.
DR   PANTHER; PTHR36113; LYASE, PUTATIVE-RELATED-RELATED; 1.
DR   Pfam; PF00903; Glyoxalase; 2.
DR   SUPFAM; SSF54593; Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase; 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..327
FT                   /note="Metapyrocatechase"
FT                   /id="PRO_0000085025"
FT   DOMAIN          14..126
FT                   /note="VOC 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01163"
FT   DOMAIN          156..276
FT                   /note="VOC 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01163"
FT   BINDING         159
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   BINDING         221
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   BINDING         272
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   327 AA;  37419 MW;  F8E7550697798EA7 CRC64;
     MSKNFQEPIF DVAQLAHVEL LSPKLEESIV FFTKYLGMEV TARAGNSVYL RAYEDFYHNT
     LKITESAEAG LGHVGWRASS PQALERRVLE LEKSGLGRGW IDGDIGHGKA YQFTTPDGHQ
     MEIFFEVEYY KPQPEQKTKL LNRPSKRPAQ GVPVRRLDHI NLMTSNPGVD TQFMIDTLGF
     RLREQIRDKG KILGSWISVS NLVHEIAFMQ EPNQEKGKLH HLCYWYGIPQ NLYDLADLLK
     DHEYFIEVPP NKHGISQAFC MYVYEPGGNR IELFGDAGYL ITDPTWEPVI WEMEDVPGNG
     DTWIGTAFPD SWWLRGTPVT TKEVVKP
//