Low specificity L-threonine aldolase (P37303)

Identification
NameLow specificity L-threonine aldolase
Synonyms
  • Low specificity L-TA
  • TA
Gene NameGLY1
Enzyme Class
Biological Properties
General FunctionInvolved in lyase activity
Specific FunctionCatalyzes the cleavage of L-allo-threonine and L- threonine to glycine and acetaldehyde
Cellular LocationNot Available
SMPDB Pathways
glycine metabolismPW002398 ThumbThumb?image type=greyscaleThumb?image type=simple
threonine metabolismPW002401 ThumbThumb?image type=greyscaleThumb?image type=simple
KEGG Pathways
Glycine, serine and threonine metabolismec00260 Map00260
SMPDB Reactions
L-Threonine → Acetaldehyde + Glycine
KEGG Reactions
L-Allothreonine → Glycine + Acetaldehyde
L-Threonine → Glycine + Acetaldehyde
Metabolites
YMDB IDNameView
YMDB00016GlycineShow
YMDB00022AcetaldehydeShow
YMDB00214L-ThreonineShow
YMDB00295L-AllothreonineShow
GO Classification
Component
Not Available
Function
binding
cofactor binding
pyridoxal phosphate binding
catalytic activity
lyase activity
Process
metabolic process
cellular metabolic process
cellular amino acid and derivative metabolic process
cellular amino acid metabolic process
Gene Properties
Chromosome Locationchromosome 5
LocusYEL046C
Gene Sequence>1164 bp ATGACTGAATTCGAATTGCCTCCAAAATATATCACCGCTGCTAACGACTTGCGGTCAGAC ACATTCACCACTCCAACTGCAGAGATGATGGAGGCCGCTTTAGAGGCCTCTATCGGTGAC GCTGTCTACGGTGAAGATGTTGACACCGTTAGGCTCGAACAGACCGTTGCCCGCATGGCT GGCAAAGAAGCAGGTTTGTTCTGTGTCTCTGGGACTTTGTCCAACCAGATTGCCATCAGA ACTCACTTGATGCAACCTCCATACTCTATTCTATGTGATTACAGGGCTCACGTTTACACT CACGAAGCCGCTGGACTGGCGATCTTGTCTCAAGCGATGGTGGTTCCTGTGGTTCCTTCC AACGGTGACTACTTGACCTTGGAAGACATCAAGTCACACTACGTCCCAGACGACGGTGAT ATTCACGGTGCCCCCACCAGATTGATTTCTCTGGAAAACACTTTACACGGTATTGTTTAT CCATTGGAAGAACTGGTCCGCATCAAAGCTTGGTGTATGGAAAATGGTCTCAAACTACAT TGTGACGGTGCCAGAATCTGGAATGCCGCTGCACAATCTGGCGTGCCATTAAAGCAATAT GGGGAAATCTTCGACTCCATCTCCATCTGTCTATCCAAGTCTATGGGTGCTCCTATTGGG TCCGTCTTGGTTGGGAACCTTAAGTTTGTCAAGAAGGCCACCCATTTCAGAAAACAACAA GGTGGTGGTATTAGACAATCTGGTATGATGGCTAGAATAGCTCTTGTAAACATCAACAAC GATTGGAAGTCCCAATTGCTGTACTCGCACTCTTTGGCTCATGAATTAGCCGAATATTGT GAGGCAAAGGGCATCCCGCTAGAGTCTCCAGCAGACACCAACTTTGTCTTTATTAACCTG AAGGCCGCTAGAATGGACCCAGATGTCCTTGTTAAGAAGGGTTTGAAGTACAACGTTAAG CTAATGGGTGGTAGAGTCTCGTTCCACTATCAAGTCACCAGAGATACTTTGGAAAAAGTC AAATTGGCCATCTCCGAGGCCTTCGACTATGCTAAAGAACATCCTTTCGACTGTAACGGA CCTACCCAGATTTACCGTAGTGAATCCACCGAGGTCGACGTTGATGGCAACGCTATCCGC GAAATAAAAACCTACAAATACTGA
Protein Properties
Pfam Domain Function
Protein Residues387
Protein Molecular Weight42814.60156
Protein Theoretical pI6.24
Signalling Regions
  • None
Transmembrane Regions
  • None
Protein Sequence>Low specificity L-threonine aldolase MTEFELPPKYITAANDLRSDTFTTPTAEMMEAALEASIGDAVYGEDVDTVRLEQTVARMA GKEAGLFCVSGTLSNQIAIRTHLMQPPYSILCDYRAHVYTHEAAGLAILSQAMVVPVVPS NGDYLTLEDIKSHYVPDDGDIHGAPTRLISLENTLHGIVYPLEELVRIKAWCMENGLKLH CDGARIWNAAAQSGVPLKQYGEIFDSISICLSKSMGAPIGSVLVGNLKFVKKATHFRKQQ GGGIRQSGMMARMALVNINNDWKSQLLYSHSLAHELAEYCEAKGIPLESPADTNFVFINL KAARMDPDVLVKKGLKYNVKLMGGRVSFHYQVTRDTLEKVKLAISEAFDYAKEHPFDCNG PTQIYRSESTEVDVDGNAIREIKTYKY
References
External Links
ResourceLink
Saccharomyces Genome Database GLY1
Uniprot IDP37303
Uniprot NameGLY1_YEAST
GenBank Gene IDL28739
Genebank Protein ID453570
General Reference
  • McNeil, J. B., McIntosh, E. M., Taylor, B. V., Zhang, F. R., Tang, S., Bognar, A. L. (1994). "Cloning and molecular characterization of three genes, including two genes encoding serine hydroxymethyltransferases, whose inactivation is required to render yeast auxotrophic for glycine." J Biol Chem 269:9155-9165.8132653
  • Dietrich, F. S., Mulligan, J., Hennessy, K., Yelton, M. A., Allen, E., Araujo, R., Aviles, E., Berno, A., Brennan, T., Carpenter, J., Chen, E., Cherry, J. M., Chung, E., Duncan, M., Guzman, E., Hartzell, G., Hunicke-Smith, S., Hyman, R. W., Kayser, A., Komp, C., Lashkari, D., Lew, H., Lin, D., Mosedale, D., Davis, R. W., et, a. l. .. (1997). "The nucleotide sequence of Saccharomyces cerevisiae chromosome V." Nature 387:78-81.9169868
  • Liu, J. Q., Nagata, S., Dairi, T., Misono, H., Shimizu, S., Yamada, H. (1997). "The GLY1 gene of Saccharomyces cerevisiae encodes a low-specific L-threonine aldolase that catalyzes cleavage of L-allo-threonine and L-threonine to glycine--expression of the gene in Escherichia coli and purification and characterization of the enzyme." Eur J Biochem 245:289-293.9151955
  • Monschau, N., Stahmann, K. P., Sahm, H., McNeil, J. B., Bognar, A. L. (1997). "Identification of Saccharomyces cerevisiae GLY1 as a threonine aldolase: a key enzyme in glycine biosynthesis." FEMS Microbiol Lett 150:55-60.9163906
  • Ficarro, S. B., McCleland, M. L., Stukenberg, P. T., Burke, D. J., Ross, M. M., Shabanowitz, J., Hunt, D. F., White, F. M. (2002). "Phosphoproteome analysis by mass spectrometry and its application to Saccharomyces cerevisiae." Nat Biotechnol 20:301-305.11875433
  • 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
  • Peng, J., Schwartz, D., Elias, J. E., Thoreen, C. C., Cheng, D., Marsischky, G., Roelofs, J., Finley, D., Gygi, S. P. (2003). "A proteomics approach to understanding protein ubiquitination." Nat Biotechnol 21:921-926.12872131
  • Hitchcock, A. L., Auld, K., Gygi, S. P., Silver, P. A. (2003). "A subset of membrane-associated proteins is ubiquitinated in response to mutations in the endoplasmic reticulum degradation machinery." Proc Natl Acad Sci U S A 100:12735-12740.14557538
  • 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