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Protein

2-pyrone-4,6-dicarbaxylate hydrolase

Gene
N/A
Organism
Comamonas testosteroni (Pseudomonas testosteroni)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

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).1 Publication

Catalytic activityi

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei50SubstrateBy similarity1
Binding sitei78SubstrateBy similarity1
Binding sitei125SubstrateBy similarity1
Binding sitei131SubstrateBy similarity1
Binding sitei158SubstrateBy similarity1
Binding sitei182SubstrateBy similarity1
Active sitei258By similarity1
Binding sitei263SubstrateBy similarity1

GO - Molecular functioni

GO - Biological processi

  • 3,4-dihydroxybenzoate catabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-3463.

Names & Taxonomyi

Protein namesi
Recommended name:
2-pyrone-4,6-dicarbaxylate hydrolase
Alternative name(s):
2-pyrone-4,6-dicarboxylate lactonohydrolase
PDC hydrolase (EC:3.1.1.57)
OrganismiComamonas testosteroni (Pseudomonas testosteroni)
Taxonomic identifieri285 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesComamonadaceaeComamonas

Pathology & Biotechi

Disruption phenotypei

Cells lacking this gene completely lose the ability to grow on protocatechuate (PCA) and accumulated PDC.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004227841 – 3052-pyrone-4,6-dicarbaxylate hydrolaseAdd BLAST305

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

STRINGi399795.CtesDRAFT_PD1896.

Structurei

3D structure databases

ProteinModelPortaliQ93PS7.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni34Substrate bindingBy similarity1

Sequence similaritiesi

Belongs to the PDC hydrolase family.Curated

Phylogenomic databases

eggNOGiENOG4105GAK. Bacteria.
COG3618. LUCA.

Family and domain databases

InterProiIPR006680. Amidohydro-rel.
IPR032466. Metal_Hydrolase.
[Graphical view]
PfamiPF04909. Amidohydro_2. 1 hit.
[Graphical view]
SUPFAMiSSF51556. SSF51556. 1 hit.

Sequencei

Sequence statusi: Complete.

Q93PS7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSQFEKTPGW LDWYANPSKP QFKLPAGAVD AHCHVFGPGN EFPFAPERKY
60 70 80 90 100
TPCDASKAQL YALRDHLGFA RNVVVQATCH GADNRAMVDA CKSSGGKARG
110 120 130 140 150
VATVKRSISD AELQQLHDAG VRGVRFNFVK RLVDFTPKDE LMEIAGRIAK
160 170 180 190 200
LGWHVVIYFE AVDLPELWDF FTALPTTVVV DHMGRPDVTK GVDSEEFALF
210 220 230 240 250
LKFMREHQNV WSKVSCPERL SVTGPKALNG EQNAYRDVVP FARRVVEEFP
260 270 280 290 300
DRVLWGTDWP HPNLKDHMPD DGLLVDFIPH IAPTAELQQK LLVDNPMRLY

WPEEV
Length:305
Mass (Da):34,451
Last modified:December 1, 2001 - v1
Checksum:i2167B504424FDDDF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF305325 Genomic DNA. Translation: AAK73571.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF305325 Genomic DNA. Translation: AAK73571.1.

3D structure databases

ProteinModelPortaliQ93PS7.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi399795.CtesDRAFT_PD1896.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG4105GAK. Bacteria.
COG3618. LUCA.

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-3463.

Family and domain databases

InterProiIPR006680. Amidohydro-rel.
IPR032466. Metal_Hydrolase.
[Graphical view]
PfamiPF04909. Amidohydro_2. 1 hit.
[Graphical view]
SUPFAMiSSF51556. SSF51556. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiPDCH_COMTE
AccessioniPrimary (citable) accession number: Q93PS7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 26, 2013
Last sequence update: December 1, 2001
Last modified: October 5, 2016
This is version 36 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.