ID   Q5EGN6_9ZZZZ            Unreviewed;       240 AA.
AC   Q5EGN6;
DT   15-MAR-2005, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2005, sequence version 1.
DT   13-SEP-2023, entry version 38.
DE   RecName: Full=Metapyrocatechase {ECO:0000256|ARBA:ARBA00022190};
DE            EC=1.13.11.2 {ECO:0000256|ARBA:ARBA00013117};
DE   AltName: Full=CatO2ase {ECO:0000256|ARBA:ARBA00031146};
DE   AltName: Full=Catechol 2,3-dioxygenase {ECO:0000256|ARBA:ARBA00030369};
DE   Flags: Fragment;
GN   Name=C23O {ECO:0000313|EMBL:AAW82369.1};
OS   uncultured organism.
OC   unclassified sequences; environmental samples.
OX   NCBI_TaxID=155900 {ECO:0000313|EMBL:AAW82369.1};
RN   [1] {ECO:0000313|EMBL:AAW82369.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Khomenkov V.G., Shevelev A.B., Zhukov V.G., Zagustina N.A., Popov V.O.;
RT   "Molecular genetic characterization of aromatic hydrocarbons utilization
RT   metabolic pathways in microbial consortia.";
RL   Appl. Biochem. Microbiol. 41:0-0(2005).
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         Evidence={ECO:0000256|ARBA:ARBA00000163};
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC         Evidence={ECO:0000256|ARBA:ARBA00001954};
CC   -!- SIMILARITY: Belongs to the extradiol ring-cleavage dioxygenase family.
CC       {ECO:0000256|ARBA:ARBA00008784}.
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DR   EMBL; AY882599; AAW82369.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q5EGN6; -.
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   CDD; cd07243; 2_3_CTD_C; 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; 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   NCBIfam; TIGR03211; catechol_2_3; 1.
DR   Pfam; PF00903; Glyoxalase; 1.
DR   SUPFAM; SSF54593; Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase; 2.
DR   PROSITE; PS00082; EXTRADIOL_DIOXYGENAS; 1.
DR   PROSITE; PS51819; VOC; 2.
PE   3: Inferred from homology;
KW   Aromatic hydrocarbons catabolism {ECO:0000256|ARBA:ARBA00022797};
KW   Dioxygenase {ECO:0000256|ARBA:ARBA00022964, ECO:0000313|EMBL:AAW82369.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT   DOMAIN          1..58
FT                   /note="VOC"
FT                   /evidence="ECO:0000259|PROSITE:PS51819"
FT   DOMAIN          86..205
FT                   /note="VOC"
FT                   /evidence="ECO:0000259|PROSITE:PS51819"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AAW82369.1"
FT   NON_TER         240
FT                   /evidence="ECO:0000313|EMBL:AAW82369.1"
SQ   SEQUENCE   240 AA;  27447 MW;  8803438C167B7640 CRC64;
     MDFMGFKVVD EDALRQLERD LMAYGCAVEQ LPAGELNSCG RRVRFQAPSG HHFELYADKE
     YTGKWGLNDV NPEAWPRDLK GMAAVRFDHA LMYGDELPAT YDLFTKVLGF YLAEQVLDEN
     GTRVAQFLSL STKAHDVAFI HHPEKGRLHH VSFHLETWED LLRAADLISM TDTSIDIGPT
     RHGLTHGKTI YFFDPSGNRN EVFCGGDYNY PDHKPVTWTT DQLGKAIFYH DRILNDRFMT
//