P82678 (ALLC_CHLRE) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 31, 2011.
Version 31.
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: Allantoicase EC=3.5.3.4 Alternative name(s): Allantoate amidinohydrolase |
| Organism | Chlamydomonas reinhardtii (Chlamydomonas smithii) |
| Taxonomic identifier | 3055 [NCBI] |
| Taxonomic lineage | Eukaryota › Viridiplantae › Chlorophyta › Chlorophyceae › Chlamydomonadales › Chlamydomonadaceae › Chlamydomonas |
Protein attributes
| Sequence length | 9 AA. |
| Sequence status | Fragment. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Catalyzes the degradation of allantoate to (-)-ureidoglycolate and (+)-ureidoglycolate to glyoxylate. |
| Catalytic activity | Allantoate + H2O = (S)-ureidoglycolate + urea. |
| Pathway | |
| Subunit structure | Homohexamer. |
| Sequence similarities | Belongs to the allantoicase family. |
| Biophysicochemical properties | Kinetic parameters: Vmax of the reaction with allantoate as substrate is nine times higher than that with ureidoglycolate. KM=2.0 mM for allantoate KM=0.7 mM for ureidoglycolate pH dependence: Optimum pH is 6.5 with allantoate as substrate, and 8 with ureidoglycolate as substrate. Temperature dependence: Optimum temperature is 60 degrees Celsius. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Purine metabolism |
| Molecular function | Hydrolase |
| Technical term | Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological process | purine base metabolic process Inferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | allantoicase activity Inferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
Sequences
References
| [1] | "Allantoate amidinohydrolase (Allantoicase) from Chlamydomonas reinhardtii: its purification and catalytic and molecular characterization." Piedras P., Munoz A., Aguilar M., Pineda M. Arch. Biochem. Biophys. 378:340-348(2000) [PubMed: 10860551] [Abstract] Cited for: PROTEIN SEQUENCE. Strain: 6145C. |
Cross-references
3D structure databases | |
|---|---|
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Enzyme and pathway databases | |
| BioCyc | MetaCyc:MONOMER-13513. |
Family and domain databases | |
| ProtoNet | Search... |
Entry information
| Entry name | ALLC_CHLRE | ||||||||
| Accession | Primary (citable) accession number: P82678 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Plant Protein Annotation Program | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with