ID W9TT56_9PSED Unreviewed; 307 AA.
AC W9TT56;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 37.
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};
GN ORFNames=BAY1663_01643 {ECO:0000313|EMBL:EXF45979.1};
OS Pseudomonas sp. BAY1663.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1439940 {ECO:0000313|EMBL:EXF45979.1, ECO:0000313|Proteomes:UP000019475};
RN [1] {ECO:0000313|EMBL:EXF45979.1, ECO:0000313|Proteomes:UP000019475}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BAY1663 {ECO:0000313|EMBL:EXF45979.1,
RC ECO:0000313|Proteomes:UP000019475};
RA Gyula P., Szabo Z., Robotka H., Bihari Z.;
RT "Genome sequencing of Pseudomonas sp. BAY1663.";
RL Submitted (DEC-2013) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EXF45979.1}.
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DR EMBL; AZSV01000016; EXF45979.1; -; Genomic_DNA.
DR RefSeq; WP_009397178.1; NZ_AZSV01000016.1.
DR AlphaFoldDB; W9TT56; -.
DR STRING; 1439940.BAY1663_01643; -.
DR GeneID; 77261146; -.
DR PATRIC; fig|1439940.3.peg.1635; -.
DR eggNOG; COG0346; Bacteria.
DR OrthoDB; 9804944at2; -.
DR Proteomes; UP000019475; Unassembled WGS sequence.
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; PTHR21366; GLYOXALASE FAMILY 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000019475}.
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; 35065 MW; 6E68E4E846401ACA CRC64;
MNKGIMRPGH VQLRVLDMSK ALEHYVELLG LIEMDRDDQG RVYLKAWTEV DKFSVVLREA
DEPGMDFMGF KVVDEDALRQ LERDLTAYGC AVEQLPAGEL NSCGRRVRFQ APSGHHFELY
ADKEYTGKWG VNEVNPEAWP RDLKGMAAVR FDHCLLYGDE LPATYDLFTK VLGFYLAEQV
LDENGTRVAQ FLSLSTKAHD VAFIHHPEKG RLHHVSFYLE TWEDVLRAAD LISMTDTSID
IGPTRHGLTH GKTIYFFDPS GNRSEVFCGG NYSYPDHKPV TWLAKDLGKA IFYHDRVLNE
RFMTVLT
//