GenomeNet

Database: UniProt
Entry: G3G9W9_9BACT
LinkDB: G3G9W9_9BACT
Original site: G3G9W9_9BACT 
ID   G3G9W9_9BACT            Unreviewed;       148 AA.
AC   G3G9W9;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   22-FEB-2023, entry version 18.
DE   SubName: Full=Catechol 2, 3-dioxygenase {ECO:0000313|EMBL:AEO86803.1};
DE   Flags: Fragment;
OS   uncultured bacterium.
OC   Bacteria; environmental samples.
OX   NCBI_TaxID=77133 {ECO:0000313|EMBL:AEO86803.1};
RN   [1] {ECO:0000313|EMBL:AEO86803.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Malik S., Beer M., Megharaj M., Naidu R.;
RT   "Evidence of monitored natural attenuation at BTEX contaminated aquifers:
RT   Analysis of catechol 2, 3-dioxygenase and toluene/biphenyl dioxygenase
RT   genes.";
RL   Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; JF800794; AEO86803.1; -; Genomic_DNA.
DR   AlphaFoldDB; G3G9W9; -.
DR   GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
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          4..128
FT                   /note="VOC"
FT                   /evidence="ECO:0000259|PROSITE:PS51819"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AEO86803.1"
FT   NON_TER         148
FT                   /evidence="ECO:0000313|EMBL:AEO86803.1"
SQ   SEQUENCE   148 AA;  16372 MW;  9ED5741C9508B7F4 CRC64;
     LDHALLMCEL NPEAGVNTVA DNTRFMQEVL GFFLTEQVVV GPDGCVQAAA WLARSTTPHD
     IAFVGGPRSG LHHIAFFLDS WHDMLKAADV MAKNQTKIDV APTRHGITRG ETIYFFDPSG
     NRNETFAGLG YLAQPDRPVT TWSEDKLW
//
DBGET integrated database retrieval system