Reviewed,
UniProtKB/Swiss-Prot Q05911 (PUR8_YEAST)
Last modified
November 24, 2009.
Version 91.
History...
Clusters with 100%,
90%,
50% identity |
Documents (3) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Adenylosuccinate lyase Short name=ASL EC=4.3.2.2 Alternative name(s): Adenylosuccinase Short name=ASase | ||||||
| Gene names |
| ||||||
| Organism | Saccharomyces cerevisiae (Baker's yeast) [Complete proteome] | ||||||
| Taxonomic identifier | 4932 [NCBI] | ||||||
| Taxonomic lineage | Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces |
Protein attributes
| Sequence length | 482 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Catalytic activity | N(6)-(1,2-dicarboxyethyl)AMP = fumarate + AMP. (S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido)succinate = fumarate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide. |
| Pathway | Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 2/2. |
| Sequence similarities | Belongs to the lyase 1 family. Adenylosuccinate lyase subfamily. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Purine biosynthesis |
| Molecular function | Lyase |
| PTM | Isopeptide bond Phosphoprotein Ubl conjugation |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | 'de novo' IMP biosynthetic process Inferred from mutant phenotype. Source: SGD |
| Molecular function | (S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido)succinate AMP-lyase (fumarate-forming) activity Inferred from electronic annotation. Source: EC N6-(1,2-dicarboxyethyl)AMP AMP-lyase (fumarate-forming) activityInferred from mutant phenotype. Source: SGD protein bindingInferred from physical interaction. Source: IntAct |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 482 | 482 | Adenylosuccinate lyase | PRO_0000137899 | |||||
Sites | |||||||||
| Active site | 83 | 1 | Proton donor By similarity | ||||||
| Active site | 156 | 1 | Proton acceptor By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 4 | 1 | Phosphotyrosine Ref.3 | ||||||
| Modified residue | 9 | 1 | Phosphothreonine Ref.3 | ||||||
| Cross-link | 196 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.2 | |||||||
Sequences
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References
| [1] | "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII." Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W., Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K., Heuss-Neitzel D., Hilbert H. Hoheisel J.D.Nature 387:87-90(1997) [PubMed: 9169871] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972. |
| [2] | "A proteomics approach to understanding protein ubiquitination." Peng J., Schwartz D., Elias J.E., Thoreen C.C., Cheng D., Marsischky G., Roelofs J., Finley D., Gygi S.P. Nat. Biotechnol. 21:921-926(2003) [PubMed: 12872131] [Abstract] Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-196, MASS SPECTROMETRY. |
| [3] | "A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-4 AND THR-9, MASS SPECTROMETRY. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| U19103 Genomic DNA. Translation: AAB67573.1. U19102 Genomic DNA. Translation: AAB67755.2. | |
| PIR | S51377. |
| RefSeq | NP_013463.1. |
3D structure databases | |
| ModBase | Search... |
Protein-protein interaction databases | |
| DIP | DIP:2787N. |
| IntAct | Q05911. 7 interactions. |
| STRING | Q05911. |
Proteomic databases | |
| PeptideAtlas | Q05911. |
Genome annotation databases | |
| Ensembl | YLR359W; YLR359W; YLR359W; Saccharomyces cerevisiae. [Genome view] |
| GeneID | 851073. |
| KEGG | sce:YLR359W. |
| NMPDR | fig|4932.3.peg.4485. |
Organism-specific databases | |
| CYGD | YLR359w. |
| SGD | S000004351. ADE13. |
Phylogenomic databases | |
| HOGENOM | Q05911. |
| OMA | DDSAIRR |
| OrthoDB | EOG9DBVXF |
Enzyme and pathway databases | |
| BioCyc | MetaCyc:MONOMER-489. |
| BRENDA | 4.3.2.2. 250. |
Gene expression databases | |
| ArrayExpress | Q05911. |
| Genevestigator | Q05911. |
| GermOnline | YLR359W. Saccharomyces cerevisiae. |
Family and domain databases | |
| InterPro | IPR019468. Adenylosuccinate_lyase_C. IPR000362. Fumarate_lyase. IPR020557. Fumarate_lyase_CS. IPR008948. L-Aspartase-like. IPR004769. Pur_lyase. [Graphical view] |
| Pfam | PF10397. ADSL_C. 1 hit. PF00206. Lyase_1. 1 hit. [Graphical view] |
| PRINTS | PR00149. FUMRATELYASE. |
| TIGRFAMs | TIGR00928. purB. 1 hit. |
| PROSITE | PS00163. FUMARATE_LYASES. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other Resources | |
| NextBio | 967720. |
Entry information
| Entry name | PUR8_YEAST | ||||||||
| Accession | Primary (citable) accession number: Q05911 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | FPAP (Fungal Proteome Annotation Project) | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |
| Yeast Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD |

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