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Identification |
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Name | Threo-3-hydroxyaspartate ammonia-lyase |
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Synonyms | - L-threo-3-hydroxyaspartate dehydratase
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Gene Name | SRY1 |
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Enzyme Class | |
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Biological Properties |
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General Function | Involved in catalytic activity |
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Specific Function | Exhibits dehydratase activity specific for L-threo-3- hydroxyaspartate |
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Cellular Location | Not Available |
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SMPDB Pathways | |
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KEGG Pathways | Not Available |
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SMPDB Reactions | |
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KEGG Reactions | Not Available |
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Metabolites | YMDB ID | Name | View |
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YMDB00091 | Ammonia | Show | YMDB00166 | (3S)-3-hydroxy-L-aspartic acid | Show | YMDB00214 | L-Threonine | Show | YMDB00235 | Oxalacetic acid | Show | YMDB00862 | hydron | Show | YMDB00890 | water | Show | YMDB16260 | (2Z)-2-aminobut-2-enoate | Show |
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GO Classification | Component |
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Not Available | Function |
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catalytic activity | binding | cofactor binding | pyridoxal phosphate binding | Process |
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metabolic process | cellular metabolic process | cellular amino acid and derivative metabolic process | cellular amino acid metabolic process |
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Gene Properties |
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Chromosome Location | chromosome 11 |
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Locus | YKL218C |
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Gene Sequence | >981 bp
ATGATTGTTCCCACTTATGGAGACGTTTTGGATGCCAGCAACAGAATTAAAGAATATGTA
AATAAAACACCGGTTCTCACTTCACGAATGCTTAATGATCGACTTGGAGCACAAATATAC
TTTAAAGGTGAGAATTTCCAACGAGTGGGAGCGTTCAAGTTTCGTGGAGCAATGAATGCT
GTTTCAAAATTAAGTGATGAAAAAAGAAGTAAGGGAGTAATTGCCTTCTCATCAGGAAAC
CATGCACAGGCTATTGCTCTTAGTGCAAAACTATTAAATGTACCTGCAACAATTGTTATG
CCCGAGGATGCGCCCGCCCTTAAAGTTGCTGCTACAGCCGGTTACGGAGCACATATCATA
AGGTATAACAGGTATACTGAAGATCGCGAGCAGATTGGGCGTCAACTAGCAGCCGAACAT
GGTTTTGCATTGATTCCGCCCTACGATCATCCTGATGTTATTGCAGGGCAAGGTACGTCG
GCAAAAGAGCTATTAGAAGAGGTTGGACAACTTGATGCATTATTTGTTCCTTTGGGCGGT
GGTGGGCTCCTTTCAGGATCTGCACTTGCCGCTAGAAGCCTTTCTCCAGGCTGCAAAATT
TTTGGGGTTGAACCTGAAGCTGGTAACGATGGACAACAATCCTTCAGATCGGGTTCCATT
GTTCATATCAATACGCCAAAAACTATCGCAGATGGCGCTCAAACACAACACCTCGGTGAG
TACACATTTGCCATTATTCGCGAAAATGTCGATGATATTTTAACGGTTAGCGACCAAGAG
CTAGTAAAATGCATGCACTTTCTTGCGGAACGCATGAAGGTGGTTGTTGAGCCCACAGCT
TGTTTGGGATTTGCAGGTGCACTTCTAAAAAAGGAAGAGCTAGTTGGGAAGAAAGTAGGC
ATAATACTAAGTGGAGGTAATGTAGACATGAAGAGATATGCTACTTTAATCTCTGGGAAG
GAAGATGGCCCAACGATTTAG |
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Protein Properties |
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Pfam Domain Function | |
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Protein Residues | 326 |
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Protein Molecular Weight | 34898.69922 |
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Protein Theoretical pI | 7.19 |
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Signalling Regions | |
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Transmembrane Regions | |
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Protein Sequence | >Threo-3-hydroxyaspartate ammonia-lyase
MIVPTYGDVLDASNRIKEYVNKTPVLTSRMLNDRLGAQIYFKGENFQRVGAFKFRGAMNA
VSKLSDEKRSKGVIAFSSGNHAQAIALSAKLLNVPATIVMPEDAPALKVAATAGYGAHII
RYNRYTEDREQIGRQLAAEHGFALIPPYDHPDVIAGQGTSAKELLEEVGQLDALFVPLGG
GGLLSGSALAARSLSPGCKIFGVEPEAGNDGQQSFRSGSIVHINTPKTIADGAQTQHLGE
YTFAIIRENVDDILTVSDQELVKCMHFLAERMKVVVEPTACLGFAGALLKKEELVGKKVG
IILSGGNVDMKRYATLISGKEDGPTI |
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References |
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External Links | |
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General Reference | - Tzermia, M., Horaitis, O., Alexandraki, D. (1994). "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." Yeast 10:663-679.7941750
- Dujon, B., Alexandraki, D., Andre, B., Ansorge, W., Baladron, V., Ballesta, J. P., Banrevi, A., Bolle, P. A., Bolotin-Fukuhara, M., Bossier, P., et, a. l. .. (1994). "Complete DNA sequence of yeast chromosome XI." Nature 369:371-378.8196765
- Wada, M., Nakamori, S., Takagi, H. (2003). "Serine racemase homologue of Saccharomyces cerevisiae has L-threo-3-hydroxyaspartate dehydratase activity." FEMS Microbiol Lett 225:189-193.12951240
- Albuquerque, C. P., Smolka, M. B., Payne, S. H., Bafna, V., Eng, J., Zhou, H. (2008). "A multidimensional chromatography technology for in-depth phosphoproteome analysis." Mol Cell Proteomics 7:1389-1396.18407956
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