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Reviewed, UniProtKB/Swiss-Prot P0A396 (TFDC_RALEJ)

Last modified March 2, 2010. Version 36. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents
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Names and originHide

Protein namesRecommended name:
Chlorocatechol 1,2-dioxygenase

EC=1.13.11.-
Gene names
Name:tfdC
Synonyms:tfdCI
Ordered Locus Names:Reut_D6466
Encoded onPlasmid pJP4 Ref.1 Ref.2 Ref.3 Ref.4
Plasmid pReut1 Ref.5
OrganismRalstonia eutropha (strain JMP134) (Alcaligenes eutrophus) [Complete proteome] [HAMAP]
Taxonomic identifier264198 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeCupriavidus
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Protein attributesHide

Sequence length255 AA.
Sequence statusComplete.
Protein existenceInferred from homology.
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General annotation (Comments)Hide

Function

Preferentially converts 3,5-dichlorocatechol as opposed to other chlorinated catechols. Retains diminished activity toward non-chlorinated substrates.

Catalytic activity

3,5-dichlorocatechol + O2 = 2,4-dichloro -muconate.

Cofactor

Binds 1 Fe3+ ion per subunit.

Pathway

Aromatic compound metabolism; 3-chlorocatechol degradation.

Sequence similarities

Belongs to the intradiol ring-cleavage dioxygenase family.

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Sequence annotation (Features)Hide

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 255255Chlorocatechol 1,2-dioxygenase
PRO_0000085090

Sites

Metal binding1301Iron By similarity
Metal binding1641Iron By similarity
Metal binding1881Iron By similarity
Metal binding1901Iron By similarity

Experimental info

Sequence conflict115 – 1162ED → DH Ref.2
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SequencesHide

Sequence LengthMass (Da)Tools
P0A396-1 [UniParc].

Last modified March 15, 2005. Version 1.
Checksum: 5BCC1BC6A94B19B4

FASTA25528,283
        10         20         30         40         50         60 
MNKRVKDVVD AIVAAVQRVL DQKEVTEAEY RTAVHYLMQV AEQRETALLC DVFFNSTVAA 

        70         80         90        100        110        120 
TKARISEGST PAIEGPYYRD DAPLVDDRLK TYDTDDHKPL LIQGTVKAVD GSVVEDVTID 

       130        140        150        160        170        180 
VWHSTPDGKY SGFHDDIPTD FYRGKLRVGT DGSFRVRTTM PVPYQIPDQG PTGALLETMG 

       190        200        210        220        230        240 
GHSWRPAHVH FKVKAPGYET LTTQYYFEGG DWITDDCCNG VQSSLITPDI VEEGVRLMNI 

       250 
NFVIEPARAQ AGANP 

« Hide

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ReferencesHide

« Hide 'large scale' references
[1]"Organization and sequence analysis of the 2,4-dichlorophenol hydroxylase and dichlorocatechol oxidative operons of plasmid pJP4."
Perkins E.J., Gordon M.P., Caceres O., Lurquin P.F.
J. Bacteriol. 172:2351-2359(1990) [PubMed: 2185214] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Partial nucleotide sequence of the chlorocatechol degradative operon tfdCDEF of pJP4 and similarity to promoters of the chlorinated aromatic degradative operons tfdA and clcABD."
Perkins E.J., Bolton G., Gordon M.P., Lurquin P.F.
Nucleic Acids Res. 16:7200-7200(1988) [PubMed: 3405772] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Nucleotide homology and organization of chlorocatechol oxidation genes of plasmids pJP4 and pAC27."
Ghosal D., You I.-S.
Mol. Gen. Genet. 211:113-120(1988) [PubMed: 2830460] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"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: 15186344] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]"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].
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Cross-referencesHide

Sequence databases

EMBL
GenBank
DDBJ
M35097 Genomic DNA. Translation: AAA98262.1.
M36280 Genomic DNA. Translation: AAA98261.1.
AY365053 Genomic DNA. Translation: AAR31039.1.
CP000093 Genomic DNA. Translation: AAZ65764.1.
PIRA35255.
RefSeqYP_025387.1.
YP_293621.1.

3D structure databases

SMRP0A396. Positions 2-247.
ModBaseSearch...

Genome annotation databases

GeneID2847422.
3607312.
GenomeReviewsGene locus Reut_D6466 in contig CP000093_GR.
KEGGreu:Reut_D6466.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG429220.
OMAQFAPGIP.
ProtClustDBCLSK926386.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-14417.
REUT264198:REUT_D6466-MONOMER.

Family and domain databases

InterProIPR007535. Catechol_dOase_N.
IPR012817. Chlorcchol_dOase.
IPR000627. Intradiol_dOase_C.
IPR015889. Intradiol_dOase_core.
[Graphical view]
Gene3DG3DSA:2.60.130.10. Intradiol_dOase_core. 1 hit.
PfamPF00775. Dioxygenase_C. 1 hit.
PF04444. Dioxygenase_N. 1 hit.
[Graphical view]
SUPFAMSSF49482. Dioxygenase. 1 hit.
TIGRFAMsTIGR02465. chlorocat_1_2. 1 hit.
PROSITEPS00083. INTRADIOL_DIOXYGENAS. 1 hit.
[Graphical view]
ProtoNetSearch...
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Entry informationHide

Entry nameTFDC_RALEJ
AccessionPrimary (citable) accession number: P0A396
Secondary accession number(s): P05403, P71131, Q46M66
Entry history
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: March 15, 2005
Last modified: March 2, 2010
This is version 36 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)
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Relevant documentsHide

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents