TFDA_BURSR
ID TFDA_BURSR Reviewed; 297 AA.
AC Q45423;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 62.
DE RecName: Full=Alpha-ketoglutarate-dependent 2,4-dichlorophenoxyacetate dioxygenase;
DE Short=2,4-D dioxygenase;
DE EC=1.14.11.-;
GN Name=tfdA;
OS Burkholderia sp. (strain RASC).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia.
OX NCBI_TaxID=69003;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8779585; DOI=10.1128/aem.62.7.2464-2469.1996;
RA Suwa Y., Wright A.D., Fukimori F., Nummy K.A., Hausinger R.P., Holben W.E.,
RA Forney L.J.;
RT "Characterization of a chromosomally encoded 2,4-dichlorophenoxyacetic
RT acid/alpha-ketoglutarate dioxygenase from Burkholderia sp. strain RASC.";
RL Appl. Environ. Microbiol. 62:2464-2469(1996).
CC -!- FUNCTION: Involved in degradation of the herbicide 2,4-
CC dichlorophenoxyacetic acid (2,4-D). Is also able to degrade 2-methyl-4-
CC chlorophenoxyacetic acid and 3-chlorobenzoic acid.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2,4-dichlorophenoxy)acetate + 2-oxoglutarate + O2 = 2,4-
CC dichlorophenol + CO2 + glyoxylate + succinate; Xref=Rhea:RHEA:48984,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16738,
CC ChEBI:CHEBI:16810, ChEBI:CHEBI:19351, ChEBI:CHEBI:30031,
CC ChEBI:CHEBI:36655;
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000250};
CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000250};
CC -!- ACTIVITY REGULATION: Activated by ascorbate. {ECO:0000305}.
CC -!- PATHWAY: Xenobiotic degradation; (2,4-dichlorophenoxy)acetate
CC degradation.
CC -!- SIMILARITY: Belongs to the TfdA dioxygenase family. {ECO:0000305}.
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DR EMBL; U25717; AAB17363.1; -; Genomic_DNA.
DR AlphaFoldDB; Q45423; -.
DR SMR; Q45423; -.
DR KEGG; ag:AAB17363; -.
DR UniPathway; UPA00685; -.
DR GO; GO:0018602; F:2,4-dichlorophenoxyacetate alpha-ketoglutarate dioxygenase activity; IEA:RHEA.
DR GO; GO:0031418; F:L-ascorbic acid binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0046300; P:2,4-dichlorophenoxyacetic acid catabolic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.60.130.10; -; 1.
DR InterPro; IPR042098; TauD-like_sf.
DR InterPro; IPR003819; TauD/TfdA-like.
DR Pfam; PF02668; TauD; 1.
PE 3: Inferred from homology;
KW Aromatic hydrocarbons catabolism; Dioxygenase; Iron; Metal-binding;
KW Oxidoreductase; Vitamin C.
FT CHAIN 1..297
FT /note="Alpha-ketoglutarate-dependent 2,4-
FT dichlorophenoxyacetate dioxygenase"
FT /id="PRO_0000194018"
FT BINDING 114
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 116
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 141
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250"
FT BINDING 248
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250"
FT BINDING 263
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 274
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250"
FT BINDING 278
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250"
SQ SEQUENCE 297 AA; 33638 MW; 17BF90A067C511FD CRC64;
MSINSEYLHP LFVGQVDNLA LQGALSPAEV RDVENEMDQK AVLVFRGQPL DQDQQIAFAR
NFGQLEGGFI KVNQRPSRFK YAELADISNV SVDGKVAEAD AREVVGNFAN QLWHSDSSFQ
QPAARYSMLS AIVLPPSGGD TEFCDMRAAY DDLPEDFKKE LQGLRAEHYA LHSRFILGDT
EYSESQRNAM PPVSWPLIRT HAGSGRKFLF IGAHASHIEG RPVAEGRMLL AELLEHATQP
KFVYRHSWKV GDLVMWDNRC VLHRGRRYDV TARRELRRAT TLGRRCRLSP RGQSWVQ
