ID   Q5TL02_9BACT            Unreviewed;       127 AA.
AC   Q5TL02;
DT   21-DEC-2004, integrated into UniProtKB/TrEMBL.
DT   21-DEC-2004, sequence version 1.
DT   22-FEB-2023, entry version 47.
DE   SubName: Full=Catechol 2,3-dioxygenase {ECO:0000313|EMBL:BAD72704.1};
DE            EC=1.13.11.2 {ECO:0000313|EMBL:BAD72704.1};
DE   Flags: Fragment;
GN   Name=C23O {ECO:0000313|EMBL:BAD72704.1};
OS   uncultured bacterium.
OC   Bacteria; environmental samples.
OX   NCBI_TaxID=77133 {ECO:0000313|EMBL:BAD72704.1};
RN   [1] {ECO:0000313|EMBL:BAD72704.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=17645532; DOI=10.1111/j.1574-6941.2007.00347.x;
RA   Kasuga I., Nakajima F., Furumai H.;
RT   "Diversity of catechol 2,3-dioxygenase genes of bacteria responding to
RT   dissolved organic matter derived from different sources in a eutrophic
RT   lake.";
RL   FEMS Microbiol. Ecol. 61:449-458(2007).
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; AB195074; BAD72704.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q5TL02; -.
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   Gene3D; 3.10.180.10; 2,3-Dihydroxybiphenyl 1,2-Dioxygenase, domain 1; 1.
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; Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase; 1.
DR   PROSITE; PS00082; EXTRADIOL_DIOXYGENAS; 1.
DR   PROSITE; PS51819; VOC; 1.
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   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU000683}.
FT   DOMAIN          7..127
FT                   /note="VOC"
FT                   /evidence="ECO:0000259|PROSITE:PS51819"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:BAD72704.1"
FT   NON_TER         127
FT                   /evidence="ECO:0000313|EMBL:BAD72704.1"
SQ   SEQUENCE   127 AA;  13846 MW;  2764AEBB92F5373A CRC64;
     RGMGAHRFDH CALNGVDISA SAKIFVDALD FAVTEELVDE GSGTRLGIFL SCSNKAHDVA
     FLGYPEDGKI HHTSFNLESW HDVGHAADII SHYDISLDIG PTRHGITRGQ TIYFFDPSGN
     RNEVFAG
//