Identification
NameThreo-3-hydroxyaspartate ammonia-lyase
Synonyms
  • L-threo-3-hydroxyaspartate dehydratase
Gene NameSRY1
Enzyme Class
Biological Properties
General FunctionInvolved in catalytic activity
Specific FunctionExhibits dehydratase activity specific for L-threo-3- hydroxyaspartate
Cellular LocationNot Available
SMPDB Pathways
isoleucine biosynthesisPW002476 ThumbThumb?image type=greyscaleThumb?image type=simple
KEGG PathwaysNot Available
SMPDB Reactions
L-Threoninehydron + water + (2Z)-2-aminobut-2-enoate
KEGG ReactionsNot Available
Metabolites
YMDB IDNameView
YMDB00091AmmoniaShow
YMDB00166(3S)-3-hydroxy-L-aspartic acidShow
YMDB00214L-ThreonineShow
YMDB00235Oxalacetic acidShow
YMDB00862hydronShow
YMDB00890waterShow
YMDB16260(2Z)-2-aminobut-2-enoateShow
GO Classification
Component
Not Available
Function
binding
cofactor binding
pyridoxal phosphate binding
catalytic activity
Process
cellular amino acid and derivative metabolic process
cellular amino acid metabolic process
metabolic process
cellular metabolic process
Gene Properties
Chromosome Locationchromosome 11
LocusYKL218C
Gene Sequence>981 bp ATGATTGTTCCCACTTATGGAGACGTTTTGGATGCCAGCAACAGAATTAAAGAATATGTA AATAAAACACCGGTTCTCACTTCACGAATGCTTAATGATCGACTTGGAGCACAAATATAC TTTAAAGGTGAGAATTTCCAACGAGTGGGAGCGTTCAAGTTTCGTGGAGCAATGAATGCT GTTTCAAAATTAAGTGATGAAAAAAGAAGTAAGGGAGTAATTGCCTTCTCATCAGGAAAC CATGCACAGGCTATTGCTCTTAGTGCAAAACTATTAAATGTACCTGCAACAATTGTTATG CCCGAGGATGCGCCCGCCCTTAAAGTTGCTGCTACAGCCGGTTACGGAGCACATATCATA AGGTATAACAGGTATACTGAAGATCGCGAGCAGATTGGGCGTCAACTAGCAGCCGAACAT GGTTTTGCATTGATTCCGCCCTACGATCATCCTGATGTTATTGCAGGGCAAGGTACGTCG GCAAAAGAGCTATTAGAAGAGGTTGGACAACTTGATGCATTATTTGTTCCTTTGGGCGGT GGTGGGCTCCTTTCAGGATCTGCACTTGCCGCTAGAAGCCTTTCTCCAGGCTGCAAAATT TTTGGGGTTGAACCTGAAGCTGGTAACGATGGACAACAATCCTTCAGATCGGGTTCCATT GTTCATATCAATACGCCAAAAACTATCGCAGATGGCGCTCAAACACAACACCTCGGTGAG TACACATTTGCCATTATTCGCGAAAATGTCGATGATATTTTAACGGTTAGCGACCAAGAG CTAGTAAAATGCATGCACTTTCTTGCGGAACGCATGAAGGTGGTTGTTGAGCCCACAGCT TGTTTGGGATTTGCAGGTGCACTTCTAAAAAAGGAAGAGCTAGTTGGGAAGAAAGTAGGC ATAATACTAAGTGGAGGTAATGTAGACATGAAGAGATATGCTACTTTAATCTCTGGGAAG GAAGATGGCCCAACGATTTAG
Protein Properties
Pfam Domain Function
Protein Residues326
Protein Molecular Weight34898.69922
Protein Theoretical pI7.19
Signalling Regions
  • None
Transmembrane Regions
  • None
Protein Sequence>Threo-3-hydroxyaspartate ammonia-lyase MIVPTYGDVLDASNRIKEYVNKTPVLTSRMLNDRLGAQIYFKGENFQRVGAFKFRGAMNA VSKLSDEKRSKGVIAFSSGNHAQAIALSAKLLNVPATIVMPEDAPALKVAATAGYGAHII RYNRYTEDREQIGRQLAAEHGFALIPPYDHPDVIAGQGTSAKELLEEVGQLDALFVPLGG GGLLSGSALAARSLSPGCKIFGVEPEAGNDGQQSFRSGSIVHINTPKTIADGAQTQHLGE YTFAIIRENVDDILTVSDQELVKCMHFLAERMKVVVEPTACLGFAGALLKKEELVGKKVG IILSGGNVDMKRYATLISGKEDGPTI
References
External Links
ResourceLink
Saccharomyces Genome Database SRY1
Uniprot IDP36007
Uniprot NameSRY1_YEAST
GenBank Gene IDX75951
Genebank Protein ID473132
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