ID O68311_GEOTH Unreviewed; 308 AA.
AC O68311;
DT 01-AUG-1998, integrated into UniProtKB/TrEMBL.
DT 01-AUG-1998, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE SubName: Full=Catechol 2,3-dioxygenase {ECO:0000313|EMBL:AAC38323.1};
GN Name=pheB {ECO:0000313|EMBL:AAC38323.1};
OS Geobacillus thermoleovorans (Bacillus thermoleovorans).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Geobacillus;
OC Geobacillus thermoleovorans group.
OX NCBI_TaxID=33941 {ECO:0000313|EMBL:AAC38323.1};
RN [1] {ECO:0000313|EMBL:AAC38323.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=A2 {ECO:0000313|EMBL:AAC38323.1};
RA Duffner F.D., Mueller R.;
RL Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AAC38323.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=A2 {ECO:0000313|EMBL:AAC38323.1};
RX PubMed=9561730; DOI=10.1111/j.1574-6968.1998.tb12926.x;
RA Duffner F.M., Muller R.;
RT "A novel phenol hydroxylase and catechol 2,3-dioxygenase from the
RT thermophilic Bacillus thermoleovorans strain A2: nucleotide sequence and
RT analysis of the genes.";
RL FEMS Microbiol. Lett. 161:37-45(1998).
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DR EMBL; AF031325; AAC38323.1; -; Genomic_DNA.
DR AlphaFoldDB; O68311; -.
DR GO; GO:0018577; F:catechol 2,3-dioxygenase activity; IEA:InterPro.
DR GO; GO:0008198; F:ferrous iron binding; IEA:InterPro.
DR GO; GO:0019439; P:aromatic compound catabolic process; IEA:InterPro.
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 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; PS51819; VOC; 2.
PE 4: Predicted;
KW Dioxygenase {ECO:0000313|EMBL:AAC38323.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000313|EMBL:AAC38323.1}.
FT DOMAIN 7..121
FT /note="VOC"
FT /evidence="ECO:0000259|PROSITE:PS51819"
FT DOMAIN 148..268
FT /note="VOC"
FT /evidence="ECO:0000259|PROSITE:PS51819"
SQ SEQUENCE 308 AA; 35510 MW; 1ADC509634EC96BB CRC64;
MGEGIMRLGF VSVNVTDLEA ARKHYVEVMG MQMTDRTENE IYLKGWDEYD HHSIVLRQSN
RAGLDKMAFK VHTYEDMEQL EKQLQQYGAS VQRVSKGENH KVGEGLRFRL PSGHTMELFV
EMEYKGKALP QVNPAPWPEG LIGVGAPRID HLLITAERPH ETVDFLMKAL NFYMSEKVVE
NERSETPIAA WLFRSYTPHD IAIIPGKDEK LHHFAFWLDE FNELRKAGDV FSKHDVPIDV
GIERHGITRG QTIYYFDPSG NRNEVFTGGY IAYPDMPVVK WTVDQLARGI FYFNHRQEWI
EGFTGVTT
//
