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P32427 (PCAB_PSEPU) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 79. 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:
3-carboxy-cis,cis-muconate cycloisomerase

EC=5.5.1.2
Alternative name(s):
3-carboxymuconate lactonizing enzyme
Short name=CMLE
Gene names
Name:pcaB
OrganismPseudomonas putida (Arthrobacter siderocapsulatus)
Taxonomic identifier303 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

Protein attributes

Sequence length422 AA.
Sequence statusFragment.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes an anti cycloisomerization.

Catalytic activity

2-carboxy-2,5-dihydro-5-oxofuran-2-acetate = cis,cis-butadiene-1,2,4-tricarboxylate.

Pathway

Aromatic compound metabolism; beta-ketoadipate pathway; 5-oxo-4,5-dihydro-2-furylacetate from 3-carboxy-cis,cis-muconate: step 1/2.

Subunit structure

Homotetramer.

Subcellular location

Cytoplasm.

Sequence similarities

Belongs to the class-II fumarase/aspartase family.

Sequence caution

The sequence AAA25920.1 differs from that shown. Reason: Frameshift at position 379.

Ontologies

Keywords
   Biological processAromatic hydrocarbons catabolism
   Cellular componentCytoplasm
   Molecular functionIsomerase
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological_processbeta-ketoadipate pathway

Inferred from electronic annotation. Source: UniProtKB-UniPathway

protocatechuate catabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_function3-carboxy-cis,cis-muconate cycloisomerase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – ›422›4223-carboxy-cis,cis-muconate cycloisomerase
PRO_0000161349

Experimental info

Non-terminal residue4221

Sequences

Sequence LengthMass (Da)Tools
P32427 [UniParc].

Last modified May 15, 2007. Version 3.
Checksum: DCB0C1E9E90DB03B

FASTA42244,676
        10         20         30         40         50         60 
MTNQLFDAYF TAPAMREIFS DRGRLQGMLD FEAALARAEA AAGLVPHSAV AAIEAACKAE 

        70         80         90        100        110        120 
RYDVGALANA IATAGNSAIP LVKALGKVIA SGVPEAERYV HLGATSQDAM DTGLVLQLRD 

       130        140        150        160        170        180 
ALDLIEADLG KLADTLSQQA LKHADTPMVG RTWLQHATPV TLGMKLAGVL GALTRHRQRL 

       190        200        210        220        230        240 
QELGPPCWCC SSGGASGSLA ALGSKAMPVA EALAEQLKLS LPEQPWHTQR DRLVEFASVL 

       250        260        270        280        290        300 
GLVAGSLGKF GRDVSLLMQT EAGEVFEPSA PGKGGSSTMP HKRNPVGAAV LIGAATRVPG 

       310        320        330        340        350        360 
LVSTLFAAMP QEHERSLGLW HAEWETLPDI CCLVSGALRQ AQVIAEGIEV DAARMRRNLD 

       370        380        390        400        410        420 
LTQGLVLAEA VSIVLARTLG RDRAHHLLEQ CCQRAVAEQR HLRAVLGDDP QVSAELSAEE 


LD 

« Hide

References

[1]"3-carboxy-cis,cis-muconate lactonizing enzyme from Pseudomonas putida is homologous to the class II fumarase family: a new reaction in the evolution of a mechanistic motif."
Williams S.E., Woolridge E.M., Ransom S.C., Landro J.A., Babbitt P.C., Kozarich J.W.
Biochemistry 31:9768-9776(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-15.
Strain: PRS2000.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L17082 Genomic DNA. Translation: AAA25920.1. Frameshift.
PIRA44374.

3D structure databases

ProteinModelPortalP32427.
SMRP32427. Positions 3-422.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-3222.
UniPathwayUPA00157; UER00265.

Family and domain databases

Gene3D1.10.275.10. 1 hit.
InterProIPR019468. AdenyloSucc_lyase_C.
IPR024083. Fumarase/histidase_N.
IPR020557. Fumarate_lyase_CS.
IPR000362. Fumarate_lyase_fam.
IPR022761. Fumarate_lyase_N.
IPR008948. L-Aspartase-like.
IPR012789. Protocat_PcaB.
[Graphical view]
PANTHERPTHR11444. PTHR11444. 1 hit.
PfamPF10397. ADSL_C. 1 hit.
PF00206. Lyase_1. 1 hit.
[Graphical view]
PRINTSPR00149. FUMRATELYASE.
SMARTSM00998. ADSL_C. 1 hit.
[Graphical view]
SUPFAMSSF48557. SSF48557. 1 hit.
TIGRFAMsTIGR02426. protocat_pcaB. 1 hit.
PROSITEPS00163. FUMARATE_LYASES. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePCAB_PSEPU
AccessionPrimary (citable) accession number: P32427
Secondary accession number(s): Q59703
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: May 15, 2007
Last modified: October 16, 2013
This is version 79 of the entry and version 3 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

PATHWAY comments

Index of metabolic and biosynthesis pathways