Catabolic L-serine/threonine dehydratase (P25379)

Identification
NameCatabolic L-serine/threonine dehydratase
Synonyms
  • L-serine dehydratase
  • L-serine deaminase
  • L-threonine dehydratase
  • L-threonine deaminase
Gene NameCHA1
Enzyme Class
Biological Properties
General FunctionInvolved in catalytic activity
Specific FunctionL-serine = pyruvate + NH(3)
Cellular LocationMitochondrion
SMPDB Pathways
serine metabolismPW002402 ThumbThumb?image type=greyscaleThumb?image type=simple
KEGG Pathways
Glycine, serine and threonine metabolismec00260 Map00260
Valine, leucine and isoleucine biosynthesisec00290 Map00290
SMPDB Reactions
L-Serine → water + hydron + 2-aminoprop-2-enoate
KEGG Reactions
L-Serine → Pyruvic acid + Ammonium
L-Threonine → Ammonium + 2-Ketobutyric acid
Metabolites
YMDB IDNameView
YMDB000712-Ketobutyric acidShow
YMDB00091AmmoniaShow
YMDB00112L-SerineShow
YMDB00175Pyruvic acidShow
YMDB00214L-ThreonineShow
YMDB00423AmmoniumShow
YMDB00862hydronShow
YMDB00890waterShow
YMDB162582-aminoprop-2-enoateShow
GO Classification
Component
Not Available
Function
binding
cofactor binding
pyridoxal phosphate binding
catalytic activity
Process
cellular metabolic process
cellular amino acid and derivative metabolic process
cellular amino acid metabolic process
metabolic process
Gene Properties
Chromosome Locationchromosome 3
LocusYCL064C
Gene Sequence>1083 bp ATGTCGATAGTCTACAATAAAACACCATTATTACGTCAATTCTTCCCCGGAAAGGCTTCT GCACAATTTTTCTTGAAATATGAATGCCTTCAACCAAGTGCCTCCTTCAAAAGTAGAGGA ATCGGTAATCTCATCATGAAAAGTGCCATTCGAATTCAAAAGGACGGTAAAAGATCTCCT CAGGTTTTCGCTAGTTCTGGCGGTAATGCCGGTTTTGCTGCTGCAACAGCATGTCAAAGA CTGTCTCTACCATGTACAGTCGTGGTTCCTACAGCGACAAAGAAGAGAATGGTAGATAAA ATCAGGAACACCGGTGCCCAGGTTATCGTGAGTGGTGCCTACTGGAAAGAAGCAGATACT TTTTTAAAAACAAATGTCATGAATAAAATAGACTCTCAGGTCATTGAGCCCATTTATGTT CATCCCTTCGATAATCCGGATATTTGGGAAGGACATTCATCTATGATAGATGAAATAGTA CAAGATTTGAAATCGCAACATATTTCCGTAAATAAGGTTAAAGGCATAGTATGCAGCGTT GGTGGAGGTGGTTTATACAATGGTATTATTCAAGGTTTGGAAAGGTATGGTTTAGCTGAT AGGATCCCTATTGTGGGGGTGGAAACGAATGGATGTCATGTTTTCAATACTTCTTTGAAA ATAGGCCAACCAGTTCAATTCAAGAAGATAACAAGTATTGCTACTTCTCTAGGAACGGCC GTGATCTCTAATCAAACTTTCGAATACGCTCGCAAATACAACACCAGATCCGTTGTAATA GAGGACAAAGATGTGATTGAACCCTGTCTTAAATATACACATCAATTCAATATGGTGATT GAACCGGCATGTGGCGCCGCATTGCATTTGGGTTACAACACTAAGATCCTAGAAAATGCA CTGGGCTCAAAATTAGCTGCGGATGACATTGTGATAATTATTGCTTGTGCGAGCTCCTCT AATACTATAAAGGACTTGGAAGAAGCGTTGGATAGCATGAGAAAAAAAGACACTCCTGTA ATAGAAGTCGCTGACAATTTCATATTTCCAGAAAAAAATATTGTGAATTTAAAAAGTGCT TGA
Protein Properties
Pfam Domain Function
Protein Residues360
Protein Molecular Weight39301.0
Protein Theoretical pI9.01
Signalling Regions
  • None
Transmembrane Regions
  • None
Protein Sequence>Catabolic L-serine/threonine dehydratase MSIVYNKTPLLRQFFPGKASAQFFLKYECLQPSGSFKSRGIGNLIMKSAIRIQKDGKRSP QVFASSGGNAGFAAATACQRLSLPCTVVVPTATKKRMVDKIRNTGAQVIVSGAYWKEADT FLKTNVMNKIDSQVIEPIYVHPFDNPDIWEGHSSMIDEIVQDLKSQHISVNKVKGIVCSV GGGGLYNGIIQGLERYGLADRIPIVGVETNGCHVFNTSLKIGQPVQFKKITSIATSLGTA VISNQTFEYARKYNTRSVVIEDKDVIETCLKYTHQFNMVIEPACGAALHLGYNTKILENA LGSKLAADDIVIIIACGGSSNTIKDLEEALDSMRKKDTPVIEVADNFIFPEKNIVNLKSA
References
External Links
ResourceLink
Saccharomyces Genome Database CHA1
Uniprot IDP25379
Uniprot NameSTDH_YEAST
GenBank Gene IDM85194
Genebank Protein ID172589
General Reference
  • Bornaes, C., Petersen, J. G., Holmberg, S. (1992). "Serine and threonine catabolism in Saccharomyces cerevisiae: the CHA1 polypeptide is homologous with other serine and threonine dehydratases." Genetics 131:531-539.1628804
  • Oliver, S. G., van der Aart, Q. J., Agostoni-Carbone, M. L., Aigle, M., Alberghina, L., Alexandraki, D., Antoine, G., Anwar, R., Ballesta, J. P., Benit, P., et, a. l. .. (1992). "The complete DNA sequence of yeast chromosome III." Nature 357:38-46.1574125
  • Huh, W. K., Falvo, J. V., Gerke, L. C., Carroll, A. S., Howson, R. W., Weissman, J. S., O'Shea, E. K. (2003). "Global analysis of protein localization in budding yeast." Nature 425:686-691.14562095
  • Ghaemmaghami, S., Huh, W. K., Bower, K., Howson, R. W., Belle, A., Dephoure, N., O'Shea, E. K., Weissman, J. S. (2003). "Global analysis of protein expression in yeast." Nature 425:737-741.14562106