Alpha-ketoglutarate-dependent 2,4-dichlorophenoxyacetate dioxygenase - Cupriavidus pinatubonensis (strain JMP134 / LMG 1197) (Alcaligenes eutrophus)

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P10088 (TFDA_CUPPJ) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 94. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Alpha-ketoglutarate-dependent 2,4-dichlorophenoxyacetate dioxygenase
Short name=2,4-D dioxygenase
EC=1.14.11.-

Gene names

Name:	tfdA
Ordered Locus Names:	Reut_D6479

Encoded on

Plasmid pJP4 Ref.1 Ref.2 Ref.5 Ref.6 Ref.7
Plasmid pReut1 Ref.4

Organism

Cupriavidus pinatubonensis (strain JMP134 / LMG 1197) (Alcaligenes eutrophus) (Ralstonia eutropha) [Complete proteome] [HAMAP]

Taxonomic identifier

264198 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Cupriavidus ›

Protein attributes

Sequence length	287 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Involved in degradation of the herbicide 2,4-dichlorophenoxyacetic acid (2,4-D). Is also able to degrade 2-methyl-4-chlorophenoxyacetic acid and 3-chlorobenzoic acid.
Catalytic activity	2,4-dichlorophenoxyacetate + 2-oxoglutarate + O₂ = 2,4-dichlorophenol + glyoxalate + succinate + CO₂.
Cofactor	Binds 1 Fe²⁺ ion per subunit.
Enzyme regulation	Activated by ascorbate Potential.
Pathway	Xenobiotic degradation; (2,4-dichlorophenoxy)acetate degradation.
Post-translational modification	Hydroxylated on Trp-113; inactivates the enzyme.
Sequence similarities	Belongs to the TfdA dioxygenase family.

Ontologies

Keywords
Biological process	Aromatic hydrocarbons catabolism
Ligand	Iron Metal-binding Vitamin C
Molecular function	Dioxygenase Oxidoreductase
PTM	Hydroxylation
Technical term	3D-structure Complete proteome Plasmid
Gene Ontology (GO)
Biological_process	2,4-dichlorophenoxyacetic acid catabolic process Inferred from electronic annotation. Source: UniProtKB-UniPathway
Molecular_function	L-ascorbic acid binding Inferred from electronic annotation. Source: UniProtKB-KW metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 287

287

Alpha-ketoglutarate-dependent 2,4-dichlorophenoxyacetate dioxygenase

PRO_0000194017

Sites

Metal binding

114

Iron; catalytic Probable

Metal binding

116

Iron; catalytic Probable

Metal binding

263

Iron; catalytic Probable

Binding site

141

2-oxoglutarate By similarity

Binding site

248

2-oxoglutarate By similarity

Binding site

274

2-oxoglutarate By similarity

Binding site

278

2-oxoglutarate By similarity

Amino acid modifications

Modified residue

113

3-hydroxytryptophan; by autocatalysis

Experimental info

Mutagenesis

H → A: No change in activity and substrate affinity. Ref.5

Mutagenesis

114

H → A: Loss of activity. Ref.5

Mutagenesis

116

D → A: Loss of activity. Ref.5

Mutagenesis

168

H → A: Loss of activity. Ref.5

Mutagenesis

201

H → A: Loss of activity. Ref.5

Mutagenesis

214

H → A: 10-fold decrease in affinity for 2,4-D and highly reduced activity. Ref.5

Mutagenesis

217

H → A: 2.5-fold decrease in affinity for 2,4-D but no change in activity. Ref.5

Mutagenesis

236

H → A: No change in activity and substrate affinity. Ref.5

Mutagenesis

246

H → A: Loss of activity. Ref.5

Mutagenesis

263

H → A: Loss of activity. Ref.5

Sequences

Sequence

Length

Mass (Da)

Tools

P10088 [UniParc].

Last modified July 1, 1989. Version 1.
Checksum: 0875BA8BE9119E70
Show »

FASTA

287

32,316

        10         20         30         40         50         60 
MSVVANPLHP LFAAGVEDID LREALGSTEV REIERLMDEK SVLVFRGQPL SQDQQIAFAR 

        70         80         90        100        110        120 
NFGPLEGGFI KVNQRPSRFK YAELADISNV SLDGKVAQRD AREVVGNFAN QLWHSDSSFQ 

       130        140        150        160        170        180 
QPAARYSMLS AVVVPPSGGD TEFCDMRAAY DALPRDLQSE LEGLRAEHYA LNSRFLLGDT 

       190        200        210        220        230        240 
DYSEAQRNAM PPVNWPLVRT HAGSGRKFLF IGAHASHVEG LPVAEGRMLL AELLEHATQR 

       250        260        270        280 
EFVYRHRWNV GDLVMWDNRC VLHRGRRYDI SARRELRRAT TLDDAVV

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Analysis, cloning, and high-level expression of 2,4-dichlorophenoxyacetate monooxygenase gene tfdA of Alcaligenes eutrophus JMP134." Streber W.R., Timmis K.N., Zenk M.H. J. Bacteriol. 169:2950-2955(1987) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Genetic organization of the catabolic plasmid pJP4 from Ralstonia eutropha JMP134 (pJP4) reveals mechanisms of adaptation to chloroaromatic pollutants and evolution of specialized chloroaromatic degradation pathways." Trefault N., De la Iglesia R., Molina A.M., Manzano M., Ledger T., Perez-Pantoja D., Sanchez M.A., Stuardo M., Gonzalez B. Environ. Microbiol. 6:655-668(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Comparison of 16S rRNA gene phylogeny and functional tfdA gene distribution in thirty-one different 2,4-dichlorophenoxyacetic acid and 4-chloro-2-methylphenoxyacetic acid degraders." Baelum J., Jacobsen C.S., Holben W.E. Syst. Appl. Microbiol. 33:67-70(2010) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: JMP134 / LMG 1197.
[4]	"Complete sequence of plasmid 1 of Ralstonia eutropha JMP134." Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Goltsman E., Martinez M., Schmutz J., Larimer F., Land M., Lykidis A., Richardson P. Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: JMP134 / LMG 1197.
[5]	"Site-directed mutagenesis of 2,4-dichlorophenoxyacetic acid/alpha-ketoglutarate dioxygenase. Identification of residues involved in metallocenter formation and substrate binding." Hogan D.A., Smith S.R., Saari E.A., McCracken J., Hausinger R.P. J. Biol. Chem. 275:12400-12409(2000) [PubMed] [Europe PMC] [Abstract] Cited for: MUTAGENESIS OF HIS-9; HIS-114; ASP-116; HIS-168; HIS-201; HIS-214; HIS-217; HIS-236; HIS-246 AND HIS-263.
[6]	"Alternative reactivity of an alpha-ketoglutarate-dependent iron(II) oxygenase: enzyme self-hydroxylation." Liu A., Ho R.Y.N., Que L. Jr., Ryle M.J., Phinney B.S., Hausinger R.P. J. Am. Chem. Soc. 123:5126-5127(2001) [PubMed] [Europe PMC] [Abstract] Cited for: HYDROXYLATION, MASS SPECTROMETRY.
[7]	"X-ray crystal structure of Escherichia coli taurine/alpha-ketoglutarate dioxygenase complexed to ferrous iron and substrates." Elkins J.M., Ryle M.J., Clifton I.J., Dunning Hotopp J.C., Lloyd J.S., Burzlaff N.I., Baldwin J.E., Hausinger R.P., Roach P.L. Biochemistry 41:5185-5192(2002) [PubMed] [Europe PMC] [Abstract] Cited for: 3D-STRUCTURE MODELING.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M16730 Genomic DNA. Translation: AAA21983.1.
AY365053 Genomic DNA. Translation: AAR31052.1.
EU827467 Genomic DNA. Translation: ACF35494.1.
CP000093 Genomic DNA. Translation: AAZ65777.1.

PIR

A27082.

RefSeq

YP_025400.1. NC_005912.1.
YP_293634.1. NC_007337.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1GQX	model	-	A	1-287	[»]

ProteinModelPortal

P10088.

ModBase

Search...

Protein-protein interaction databases

STRING

264198.Reut_D6479.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAZ65777; AAZ65777; Reut_D6479.

GeneID

2847397.
3607903.

KEGG

reu:Reut_D6479.

PATRIC

20225338. VBIRalEut24049_0548.

Organism-specific databases

CMR

Search...

Phylogenomic databases

eggNOG

COG2175.

HOGENOM

HOG000165071.

K06912.

OMA

RYDISAR.

ProtClustDB

CLSK818608.

Enzyme and pathway databases

BioCyc

CPIN264198:GIW3-6565-MONOMER.
MetaCyc:MONOMER-14384.

UniPathway

UPA00685.

Family and domain databases

InterPro

IPR003819. Taurine_dOase.
[Graphical view]

Pfam

PF02668. TauD. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

TFDA_CUPPJ

Accession

Primary (citable) accession number: P10088
Secondary accession number(s): B5A9M3, Q46M53

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	July 1, 1989
Last modified:	May 1, 2013
This is version 94 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents