TFDA_CUPPJ
ID TFDA_CUPPJ Reviewed; 287 AA.
AC P10088; B5A9M3; Q46M53;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Alpha-ketoglutarate-dependent 2,4-dichlorophenoxyacetate dioxygenase;
DE Short=2,4-D dioxygenase;
DE EC=1.14.11.-;
GN Name=tfdA; OrderedLocusNames=Reut_D6479;
OS Cupriavidus pinatubonensis (strain JMP 134 / LMG 1197) (Cupriavidus necator
OS (strain JMP 134)).
OG Plasmid pJP4, and Plasmid pPJ4.
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=264198;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC PLASMID=pJP4;
RX PubMed=3036764; DOI=10.1128/jb.169.7.2950-2955.1987;
RA Streber W.R., Timmis K.N., Zenk M.H.;
RT "Analysis, cloning, and high-level expression of 2,4-dichlorophenoxyacetate
RT monooxygenase gene tfdA of Alcaligenes eutrophus JMP134.";
RL J. Bacteriol. 169:2950-2955(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC PLASMID=pJP4;
RX PubMed=15186344; DOI=10.1111/j.1462-2920.2004.00596.x;
RA Trefault N., De la Iglesia R., Molina A.M., Manzano M., Ledger T.,
RA Perez-Pantoja D., Sanchez M.A., Stuardo M., Gonzalez B.;
RT "Genetic organization of the catabolic plasmid pJP4 from Ralstonia eutropha
RT JMP134 (pJP4) reveals mechanisms of adaptation to chloroaromatic pollutants
RT and evolution of specialized chloroaromatic degradation pathways.";
RL Environ. Microbiol. 6:655-668(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=JMP134 / LMG 1197;
RX PubMed=20206455; DOI=10.1016/j.syapm.2010.01.001;
RA Baelum J., Jacobsen C.S., Holben W.E.;
RT "Comparison of 16S rRNA gene phylogeny and functional tfdA gene
RT distribution in thirty-one different 2,4-dichlorophenoxyacetic acid and 4-
RT chloro-2-methylphenoxyacetic acid degraders.";
RL Syst. Appl. Microbiol. 33:67-70(2010).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JMP134 / LMG 1197; PLASMID=pPJ4;
RX PubMed=20339589; DOI=10.1371/journal.pone.0009729;
RA Lykidis A., Perez-Pantoja D., Ledger T., Mavromatis K., Anderson I.J.,
RA Ivanova N.N., Hooper S.D., Lapidus A., Lucas S., Gonzalez B.,
RA Kyrpides N.C.;
RT "The complete multipartite genome sequence of Cupriavidus necator JMP134, a
RT versatile pollutant degrader.";
RL PLoS ONE 5:E9729-E9729(2010).
RN [5]
RP MUTAGENESIS OF HIS-9; HIS-114; ASP-116; HIS-168; HIS-201; HIS-214; HIS-217;
RP HIS-236; HIS-246 AND HIS-263.
RC PLASMID=pJP4;
RX PubMed=10777523; DOI=10.1074/jbc.275.17.12400;
RA Hogan D.A., Smith S.R., Saari E.A., McCracken J., Hausinger R.P.;
RT "Site-directed mutagenesis of 2,4-dichlorophenoxyacetic acid/alpha-
RT ketoglutarate dioxygenase. Identification of residues involved in
RT metallocenter formation and substrate binding.";
RL J. Biol. Chem. 275:12400-12409(2000).
RN [6]
RP HYDROXYLATION AT TRP-113, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC PLASMID=pJP4;
RX PubMed=11457355; DOI=10.1021/ja005879x;
RA Liu A., Ho R.Y.N., Que L. Jr., Ryle M.J., Phinney B.S., Hausinger R.P.;
RT "Alternative reactivity of an alpha-ketoglutarate-dependent iron(II)
RT oxygenase: enzyme self-hydroxylation.";
RL J. Am. Chem. Soc. 123:5126-5127(2001).
RN [7]
RP 3D-STRUCTURE MODELING.
RC PLASMID=pJP4;
RX PubMed=11955067; DOI=10.1021/bi016014e;
RA Elkins J.M., Ryle M.J., Clifton I.J., Dunning Hotopp J.C., Lloyd J.S.,
RA Burzlaff N.I., Baldwin J.E., Hausinger R.P., Roach P.L.;
RT "X-ray crystal structure of Escherichia coli taurine/alpha-ketoglutarate
RT dioxygenase complexed to ferrous iron and substrates.";
RL Biochemistry 41:5185-5192(2002).
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;
CC Note=Binds 1 Fe(2+) ion per subunit.;
CC -!- ACTIVITY REGULATION: Activated by ascorbate. {ECO:0000305}.
CC -!- PATHWAY: Xenobiotic degradation; (2,4-dichlorophenoxy)acetate
CC degradation.
CC -!- PTM: Hydroxylated on Trp-113; inactivates the enzyme.
CC {ECO:0000269|PubMed:11457355}.
CC -!- SIMILARITY: Belongs to the TfdA dioxygenase family. {ECO:0000305}.
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DR EMBL; M16730; AAA21983.1; -; Genomic_DNA.
DR EMBL; AY365053; AAR31052.1; -; Genomic_DNA.
DR EMBL; EU827467; ACF35494.1; -; Genomic_DNA.
DR EMBL; CP000093; AAZ65777.1; -; Genomic_DNA.
DR PIR; A27082; A27082.
DR RefSeq; WP_011178399.1; NZ_AY365053.1.
DR AlphaFoldDB; P10088; -.
DR SMR; P10088; -.
DR EnsemblBacteria; AAZ65777; AAZ65777; Reut_D6479.
DR GeneID; 55536829; -.
DR KEGG; reu:Reut_D6479; -.
DR HOGENOM; CLU_036005_2_0_4; -.
DR OMA; TEFANSY; -.
DR OrthoDB; 1742732at2; -.
DR BioCyc; MetaCyc:MON-14384; -.
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 1: Evidence at protein level;
KW Aromatic hydrocarbons catabolism; Dioxygenase; Hydroxylation; Iron;
KW Metal-binding; Oxidoreductase; Plasmid; Vitamin C.
FT CHAIN 1..287
FT /note="Alpha-ketoglutarate-dependent 2,4-
FT dichlorophenoxyacetate dioxygenase"
FT /id="PRO_0000194017"
FT BINDING 114
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000305"
FT BINDING 116
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000305"
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:0000305"
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"
FT MOD_RES 113
FT /note="3-hydroxytryptophan; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:11457355"
FT MUTAGEN 9
FT /note="H->A: No change in activity and substrate affinity."
FT /evidence="ECO:0000269|PubMed:10777523"
FT MUTAGEN 114
FT /note="H->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:10777523"
FT MUTAGEN 116
FT /note="D->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:10777523"
FT MUTAGEN 168
FT /note="H->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:10777523"
FT MUTAGEN 201
FT /note="H->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:10777523"
FT MUTAGEN 214
FT /note="H->A: 10-fold decrease in affinity for 2,4-D and
FT highly reduced activity."
FT /evidence="ECO:0000269|PubMed:10777523"
FT MUTAGEN 217
FT /note="H->A: 2.5-fold decrease in affinity for 2,4-D but no
FT change in activity."
FT /evidence="ECO:0000269|PubMed:10777523"
FT MUTAGEN 236
FT /note="H->A: No change in activity and substrate affinity."
FT /evidence="ECO:0000269|PubMed:10777523"
FT MUTAGEN 246
FT /note="H->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:10777523"
FT MUTAGEN 263
FT /note="H->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:10777523"
SQ SEQUENCE 287 AA; 32316 MW; 0875BA8BE9119E70 CRC64;
MSVVANPLHP LFAAGVEDID LREALGSTEV REIERLMDEK SVLVFRGQPL SQDQQIAFAR
NFGPLEGGFI KVNQRPSRFK YAELADISNV SLDGKVAQRD AREVVGNFAN QLWHSDSSFQ
QPAARYSMLS AVVVPPSGGD TEFCDMRAAY DALPRDLQSE LEGLRAEHYA LNSRFLLGDT
DYSEAQRNAM PPVNWPLVRT HAGSGRKFLF IGAHASHVEG LPVAEGRMLL AELLEHATQR
EFVYRHRWNV GDLVMWDNRC VLHRGRRYDI SARRELRRAT TLDDAVV
