P32427 (PCAB_PSEPU) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 78.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: 3-carboxy-cis,cis-muconate cycloisomerase EC=5.5.1.2 Alternative name(s): 3-carboxymuconate lactonizing enzyme Short name=CMLE | ||
| Gene names |
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| Organism | Pseudomonas putida (Arthrobacter siderocapsulatus) | ||
| Taxonomic identifier | 303 [NCBI] | ||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Pseudomonas › ![]() |
Protein attributes
| Sequence length | 422 AA. |
| Sequence status | Fragment. |
| Protein existence | Evidence 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 | |
| Subunit structure | Homotetramer. |
| Subcellular location | |
| 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 process | Aromatic hydrocarbons catabolism |
| Cellular component | Cytoplasm |
| Molecular function | Isomerase |
| Technical term | Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological_process | beta-ketoadipate pathway Inferred from electronic annotation. Source: UniProtKB-UniPathway protocatechuate catabolic processInferred from electronic annotation. Source: InterPro |
| Cellular_component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular_function | 3-carboxy-cis,cis-muconate cycloisomerase activity Inferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
Sequences
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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. |
| PIR | A44374. |
3D structure databases | |
| ProteinModelPortal | P32427. |
| SMR | P32427. Positions 3-422. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Enzyme and pathway databases | |
| BioCyc | MetaCyc:MONOMER-3222. |
| UniPathway | UPA00157; UER00265. |
Family and domain databases | |
| Gene3D | 1.10.275.10. 1 hit. |
| InterPro | IPR019468. AdenyloSucc_lyase_C. IPR003031. D_crystallin. IPR024083. Fumarase/histidase_N. IPR000362. Fumarate_lyase. IPR020557. Fumarate_lyase_CS. IPR022761. Fumarate_lyase_N. IPR008948. L-Aspartase-like. IPR012789. Protocat_PcaB. [Graphical view] |
| Pfam | PF10397. ADSL_C. 1 hit. PF00206. Lyase_1. 1 hit. [Graphical view] |
| PRINTS | PR00145. ARGSUCLYASE. PR00149. FUMRATELYASE. |
| SMART | SM00998. ADSL_C. 1 hit. [Graphical view] |
| SUPFAM | SSF48557. L-Aspartase-like. 1 hit. |
| TIGRFAMs | TIGR02426. protocat_pcaB. 1 hit. |
| PROSITE | PS00163. FUMARATE_LYASES. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | PCAB_PSEPU | ||||||||
| Accession | Primary (citable) accession number: P32427 Secondary accession number(s): Q59703 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with
