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Q93PS7 (PDCH_COMTE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 29. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
2-pyrone-4,6-dicarbaxylate hydrolase
Alternative name(s):
2-pyrone-4,6-dicarboxylate lactonohydrolase
PDC hydrolase
EC=3.1.1.57
OrganismComamonas testosteroni (Pseudomonas testosteroni)
Taxonomic identifier285 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesComamonadaceaeComamonas

Protein attributes

Sequence length305 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Involved in the meta fission degradative pathway of protocatechuate. Catalyzes the reversible hydrolysis of 2-pyrone-4,6-dicarboxylate (PDC) to a mixture of 4-carboxy-2-hydroxymuconate (CHM) and 4-oxalomesaconate (OMA). Ref.2

Catalytic activity

2-oxo-2H-pyran-4,6-dicarboxylate + H2O = (1E)-4-oxobut-1-ene-1,2,4-tricarboxylate.

Subunit structure

Homodimer By similarity.

Disruption phenotype

Cells lacking this gene completely lose the ability to grow on protocatechuate (PCA) and accumulated PDC. Ref.2

Sequence similarities

Belongs to the PDC hydrolase family.

Ontologies

Keywords
   Molecular functionHydrolase
Gene Ontology (GO)
   Biological_processprotocatechuate catabolic process

Inferred from direct assay Ref.2. Source: UniProtKB

   Molecular_function2-pyrone-4,6-dicarboxylate lactonase activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 3053052-pyrone-4,6-dicarbaxylate hydrolase
PRO_0000422784

Regions

Region341Substrate binding By similarity

Sites

Active site2581 By similarity
Binding site501Substrate By similarity
Binding site781Substrate By similarity
Binding site1251Substrate By similarity
Binding site1311Substrate By similarity
Binding site1581Substrate By similarity
Binding site1821Substrate By similarity
Binding site2631Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q93PS7 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: 2167B504424FDDDF

FASTA30534,451
        10         20         30         40         50         60 
MSQFEKTPGW LDWYANPSKP QFKLPAGAVD AHCHVFGPGN EFPFAPERKY TPCDASKAQL 

        70         80         90        100        110        120 
YALRDHLGFA RNVVVQATCH GADNRAMVDA CKSSGGKARG VATVKRSISD AELQQLHDAG 

       130        140        150        160        170        180 
VRGVRFNFVK RLVDFTPKDE LMEIAGRIAK LGWHVVIYFE AVDLPELWDF FTALPTTVVV 

       190        200        210        220        230        240 
DHMGRPDVTK GVDSEEFALF LKFMREHQNV WSKVSCPERL SVTGPKALNG EQNAYRDVVP 

       250        260        270        280        290        300 
FARRVVEEFP DRVLWGTDWP HPNLKDHMPD DGLLVDFIPH IAPTAELQQK LLVDNPMRLY 


WPEEV 

« Hide

References

[1]"Comamonas testosteroni BR6020 possesses a single genetic locus for extradiol cleavage of protocatechuate."
Providenti M.A., Mampel J., MacSween S., Cook A.M., Wyndham R.C.
Microbiology 147:2157-2167(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: BR6020.
[2]"Characterization of the protocatechuate 4,5-cleavage pathway operon in Comamonas sp. strain E6 and discovery of a novel pathway gene."
Kamimura N., Aoyama T., Yoshida R., Takahashi K., Kasai D., Abe T., Mase K., Katayama Y., Fukuda M., Masai E.
Appl. Environ. Microbiol. 76:8093-8101(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF305325 Genomic DNA. Translation: AAK73571.1.

3D structure databases

ProteinModelPortalQ93PS7.
SMRQ93PS7. Positions 8-305.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-3463.

Family and domain databases

InterProIPR006992. Amidohydro_2.
[Graphical view]
PfamPF04909. Amidohydro_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePDCH_COMTE
AccessionPrimary (citable) accession number: Q93PS7
Entry history
Integrated into UniProtKB/Swiss-Prot: June 26, 2013
Last sequence update: December 1, 2001
Last modified: April 16, 2014
This is version 29 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families