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O67988 (CLCD_RHOOP) Reviewed, UniProtKB/Swiss-Prot

Last modified June 28, 2011. Version 43. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Carboxymethylenebutenolidase

EC=3.1.1.45
Alternative name(s):
Dienelactone hydrolase
Short name=DLH
Gene names
Name:clcD
OrganismRhodococcus opacus (Nocardia opaca)
Taxonomic identifier37919 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeNocardiaceaeRhodococcus

Protein attributes

Sequence length252 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.

Sequence similarities

Belongs to the dienelactone hydrolase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 252252Carboxymethylenebutenolidase
PRO_0000161572

Sites

Active site1261 By similarity
Active site1831 By similarity
Active site2141 By similarity

Sequences

Sequence LengthMass (Da)Tools
O67988 [UniParc].

Last modified August 1, 1998. Version 1.
Checksum: E7E73E7743CE7E9C

FASTA25227,304
        10         20         30         40         50         60 
MCHNKSSAPP TPAHISIQQN RTPGTDPVPY LHASSDTGSG DTIVLLTDIF GVTPFYRHLA 

        70         80         90        100        110        120 
AMLAEKGHDV VIPDVFHRVG HATDPGRDAA LARRRQLDDR LAIEDIERTV AHTVDDQQTF 

       130        140        150        160        170        180 
GVLGFCLGGS FALLTAAAHP NQVTATYYAF PKGAPGAKVP VKPPLEAADA IDGPVLCHWG 

       190        200        210        220        230        240 
RDDYIDHEEI DQLEQILASA PGPSEIRWYD NAGHSFLAGL TEPNHPSTAA AHDSWQRTVE 

       250 
FFERYLTVGS AN 

« Hide

References

[1]"Evolutionary relationship between chlorocatechol catabolic enzymes from Rhodococcus opacus 1CP and their counterparts in proteobacteria: sequence divergence and functional convergence."
Eulberg D., Kourbatova E.M., Golovleva L.A., Schloemann M.
J. Bacteriol. 180:1082-1094(1998) [PubMed: 9495745] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 1CP.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF003948 Genomic DNA. Translation: AAC38252.1.

3D structure databases

ProteinModelPortalO67988.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

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

Entry information

Entry nameCLCD_RHOOP
AccessionPrimary (citable) accession number: O67988
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: August 1, 1998
Last modified: June 28, 2011
This is version 43 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