Reviewed,
UniProtKB/Swiss-Prot P36007 (SRY1_YEAST)
Last modified
January 19, 2010.
Version 74.
History...
Clusters with 100%,
90%,
50% identity |
Documents (3) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Threo-3-hydroxyaspartate ammonia-lyase EC=4.3.1.16 Alternative name(s): L-threo-3-hydroxyaspartate dehydratase | ||||
| 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 | 326 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Exhibits dehydratase activity specific for L-threo-3-hydroxyaspartate. Ref.3 |
| Catalytic activity | Threo-3-hydroxy-L-aspartate = oxaloacetate + NH3. |
| Cofactor | Pyridoxal phosphate By similarity. Ref.3 |
| Sequence similarities | Belongs to the serine/threonine dehydratase family. |
| Biophysicochemical properties | Kinetic parameters: KM=3.9 mM for L-threo-3-hydroxyaspartate Vmax=110 µmol/min/mg enzyme toward L-threo-3-hydroxyaspartate |
Ontologies
| Keywords | |
|---|---|
| Ligand | Pyridoxal phosphate |
| Molecular function | Lyase |
| PTM | Phosphoprotein |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | cellular amino acid derivative catabolic process Ref.3 Inferred from direct assay. Source: SGD cellular amino acid metabolic processInferred from electronic annotation. Source: InterPro |
| Molecular function | pyridoxal phosphate binding Inferred from electronic annotation. Source: InterPro threo-3-hydroxyaspartate ammonia-lyase activity Ref.3Inferred from direct assay. Source: SGD |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 326 | 326 | Threo-3-hydroxyaspartate ammonia-lyase | PRO_0000185589 | |||||
Amino acid modifications | |||||||||
| Modified residue | 53 | 1 | N6-(pyridoxal phosphate)lysine By similarity | ||||||
| Modified residue | 217 | 1 | Phosphoserine Ref.4 | ||||||
| Modified residue | 219 | 1 | Phosphoserine Ref.4 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "The complete sequencing of a 24.6 kb segment of yeast chromosome XI identified the known loci URA1, SAC1 and TRP3, and revealed 6 new open reading frames including homologues to the threonine dehydratases, membrane transporters, hydantoinases and the phospholipase A2-activating protein." Tzermia M., Horaitis O., Alexandraki D. Yeast 10:663-679(1994) [PubMed: 7941750] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c. |
| [2] | "Complete DNA sequence of yeast chromosome XI." Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V., Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P., Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L., Daignan-Fornier B., del Rey F., Dion C. Mewes H.-W.Nature 369:371-378(1994) [PubMed: 8196765] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204508 / S288c. |
| [3] | "Serine racemase homologue of Saccharomyces cerevisiae has L-threo-3-hydroxyaspartate dehydratase activity." Wada M., Nakamori S., Takagi H. FEMS Microbiol. Lett. 225:189-193(2003) [PubMed: 12951240] [Abstract] Cited for: FUNCTION, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES. |
| [4] | "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 SER-217 AND SER-219, MASS SPECTROMETRY. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | X75951 Genomic DNA. Translation: CAA53555.1. Z28218 Genomic DNA. Translation: CAA82063.1. |
| PIR | S38061. |
| RefSeq | NP_012704.1. |
3D structure databases | |
| SMR | P36007. Positions 2-318. |
| ModBase | Search... |
Protein-protein interaction databases | |
| DIP | DIP-6523N. |
| STRING | P36007. |
Proteomic databases | |
| PeptideAtlas | P36007. |
| PRIDE | P36007. |
Genome annotation databases | |
| Ensembl | YKL218C; YKL218C; YKL218C; Saccharomyces cerevisiae. [Genome view] |
| GeneID | 853662. |
| KEGG | sce:YKL218C. |
| NMPDR | fig|4932.3.peg.3682. |
Organism-specific databases | |
| CYGD | YKL218c. |
| SGD | S000001701. SRY1. |
Phylogenomic databases | |
| eggNOG | fuNOG07508. |
| HOGENOM | HBG714501. |
| OMA | MTLIPPY. |
| OrthoDB | EOG9KWM9M. |
| PhylomeDB | P36007. |
Enzyme and pathway databases | |
| BRENDA | 4.3.1.16. 250. |
Gene expression databases | |
| ArrayExpress | P36007. |
| Genevestigator | P36007. |
| GermOnline | YKL218C. Saccharomyces cerevisiae. |
Family and domain databases | |
| InterPro | IPR001926. PyrdxlP-dep_enz_bsu. IPR000634. Ser/Thr_deHydtase_PyrdxlP-BS. [Graphical view] |
| Pfam | PF00291. PALP. 1 hit. [Graphical view] |
| PROSITE | PS00165. DEHYDRATASE_SER_THR. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other Resources | |
| NextBio | 974590. |
Entry information
| Entry name | SRY1_YEAST | ||||||||
| Accession | Primary (citable) accession number: P36007 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | FPAP (Fungal Proteome Annotation Project) | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |
| Yeast Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD |
| Yeast chromosome XI Yeast (Saccharomyces cerevisiae) chromosome XI: entries and gene names |

Clusters with


