ID Q206Z1_9BACT Unreviewed; 307 AA.
AC Q206Z1;
DT 18-APR-2006, integrated into UniProtKB/TrEMBL.
DT 18-APR-2006, sequence version 1.
DT 13-SEP-2023, entry version 47.
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};
OS uncultured bacterium.
OC Bacteria; environmental samples.
OX NCBI_TaxID=77133 {ECO:0000313|EMBL:ABD72922.1};
RN [1] {ECO:0000313|EMBL:ABD72922.1}
RP NUCLEOTIDE SEQUENCE.
RA Wu Y.C., Luo Y.M., Teng Y., Li Z.G.;
RT "Catechol 2,3-dioxygenase gene diversity of soil bacteria in a petroleum
RT contaminated site.";
RL Submitted (FEB-2006) 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 Evidence={ECO:0000256|ARBA:ARBA00000163};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000256|ARBA:ARBA00001954,
CC ECO:0000256|RuleBase:RU000683};
CC -!- SIMILARITY: Belongs to the extradiol ring-cleavage dioxygenase family.
CC {ECO:0000256|ARBA:ARBA00008784, ECO:0000256|RuleBase:RU000683}.
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DR EMBL; DQ408374; ABD72922.1; -; Genomic_DNA.
DR AlphaFoldDB; Q206Z1; -.
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 CDD; cd07265; 2_3_CTD_N; 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 PANTHER; PTHR36113; LYASE, PUTATIVE-RELATED-RELATED; 1.
DR PANTHER; PTHR36113:SF3; SLL5075 PROTEIN; 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 {ECO:0000256|ARBA:ARBA00022797,
KW ECO:0000256|RuleBase:RU000683};
KW Dioxygenase {ECO:0000256|ARBA:ARBA00022964, ECO:0000256|RuleBase:RU000683};
KW Iron {ECO:0000256|RuleBase:RU000683};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU000683}.
FT DOMAIN 7..122
FT /note="VOC"
FT /evidence="ECO:0000259|PROSITE:PS51819"
FT DOMAIN 150..269
FT /note="VOC"
FT /evidence="ECO:0000259|PROSITE:PS51819"
SQ SEQUENCE 307 AA; 35110 MW; 9DC2E9525A9D547B CRC64;
MNKGVMRPGH VQLRVLDMVK ALEHYVELLG LIEMDRDDQG RVYLKAWTEV DKFSVVLREA
DEPGMDFMGF KVIDEECLSR LSQDLIDYGC PVETIPAGEL TGCGRRVRFQ APSGHHFELY
ADKEYTGKWG VSEVNPEAWP RDLKGMAAVR FDHCLLYGDE LQATYELFTK VLGFYLAEQV
LDEDGTRVAQ FLSLSTKAHD VAFIHHPEKG RFHHASFYLE TWEDILRAAD LISMTDTSID
IGPTRHGLTH GKTIYFFDPS GNRCEVFCGG NYNYPDHKPV TWLAKDVGKA IFYHDRVLNE
RFMTVMT
//
