Skip Header

Contribute Send feedback
Read comments (?) or add your own

P27100 (TCBE_PSESQ) Reviewed, UniProtKB/Swiss-Prot

Last modified June 28, 2011. Version 44. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:
Carboxymethylenebutenolidase

EC=3.1.1.45
Alternative name(s):
Dienelactone hydrolase
Short name=DLH
Gene names
Name:tcbE
Encoded onPlasmid pP51
OrganismPseudomonas sp. (strain P51)
Taxonomic identifier65067 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesComamonadaceae

Protein attributes

Sequence length238 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Ring cleavage of cyclic ester dienelactone to produce maleylacetate.

Catalytic activity

4-carboxymethylenebut-2-en-4-olide + H2O = 4-oxohex-2-enedioate.

Pathway

Aromatic compound metabolism; 3-chlorocatechol degradation.

Subunit structure

Monomer.

Miscellaneous

Carboxymethylenebutenolidase is specific for dienelactone and has no activity toward enol-lactones.

Sequence similarities

Belongs to the dienelactone hydrolase family.

Ontologies

Keywords
   Biological processAromatic hydrocarbons catabolism
   Molecular functionHydrolase
Serine esterase
   Technical termPlasmid
Gene Ontology (GO)
   Biological processaromatic compound catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functioncarboxylesterase activity

Inferred from electronic annotation. Source: UniProtKB-KW

carboxymethylenebutenolidase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 238238Carboxymethylenebutenolidase
PRO_0000161573

Sites

Active site1231 By similarity
Active site1711 By similarity
Active site2011 By similarity

Sequences

Sequence LengthMass (Da)Tools
P27100 [UniParc].

Last modified August 1, 1992. Version 1.
Checksum: DB57EAD5229C03C8

FASTA23825,812
        10         20         30         40         50         60 
MLTEGLSIDA KGGGRFGAHL QLPARGRGPV VMVAQEIFGV NPFMTEVLAW LASEGFVGLC 

        70         80         90        100        110        120 
PDLYWRHGPG IEFDPNDEVQ RARALGMFRD YKLEDGVADL RATVAYAASQ PFCDGGVAVI 

       130        140        150        160        170        180 
GYCLGGALAY EVAAEGFAQC CVGYYGVGFE KRLERARLVK TPSMFHMGTN DHFVTAEARQ 

       190        200        210        220        230 
LITNAFEANP AIALHWYDAG HSFARASSPN FSPEATRTAN ARTLEMLKRM KPIGTIGQ 

« Hide

References

[1]"Sequence analysis of the Pseudomonas sp. strain P51 tcb gene cluster, which encodes metabolism of chlorinated catechols: evidence for specialization of catechol 1,2-dioxygenases for chlorinated substrates."
van der Meer J.R., Eggen R.I., Zehnder A.J., de Vos W.M.
J. Bacteriol. 173:2425-2434(1991) [PubMed: 2013566] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M57629 Genomic DNA. Translation: AAD13628.1.
PIRD43673.

3D structure databases

ProteinModelPortalP27100.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-14406.

Family and domain databases

InterProIPR002925. Dienelactn_hydro.
[Graphical view]
PfamPF01738. DLH. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameTCBE_PSESQ
AccessionPrimary (citable) accession number: P27100
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: August 1, 1992
Last modified: June 28, 2011
This is version 44 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families