Aspartate-semialdehyde dehydrogenase (P13663)

Identification
NameAspartate-semialdehyde dehydrogenase
Synonyms
  • ASA DH
  • ASA dehydrogenase
Gene NameHOM2
Enzyme Class
Biological Properties
General FunctionInvolved in aspartate-semialdehyde dehydrogenase activity
Specific FunctionThis enzyme catalyzes the second step in the common metabolic pathway to synthesize Thr and Met from Asp
Cellular LocationNot Available
SMPDB Pathways
Cysteine MetabolismPW002383 ThumbThumb?image type=greyscaleThumb?image type=simple
Methionine metabolism and salvagePW002384 ThumbThumb?image type=greyscaleThumb?image type=simple
KEGG Pathways
Cysteine and methionine metabolismec00270 Map00270
Glycine, serine and threonine metabolismec00260 Map00260
Lysine biosynthesisec00300 Map00300
SMPDB Reactions
4-Phospho-L-aspartic acid + hydron + NADPH → phosphate + NADP + L-aspartic 4-semialdehyde
4-Phospho-L-aspartic acid + NADPH + hydron → phosphate + NADP + L-aspartic 4-semialdehyde
KEGG Reactions
4-Phospho-L-aspartic acid + NADPH + hydron → NADP + phosphate + L-aspartic 4-semialdehyde
Metabolites
YMDB IDNameView
YMDB00034L-aspartic 4-semialdehydeShow
YMDB001134-Phospho-L-aspartic acidShow
YMDB00426NADPHShow
YMDB00427NADPShow
YMDB00862hydronShow
YMDB00907phosphateShow
GO Classification
Component
intracellular part
cytoplasm
cell part
Function
protein dimerization activity
NADP or NADPH binding
oxidoreductase activity, acting on the aldehyde or oxo group of donors
binding
oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
aspartate-semialdehyde dehydrogenase activity
nucleotide binding
oxidoreductase activity
protein binding
catalytic activity
NAD or NADH binding
Process
cellular metabolic process
cellular amino acid and derivative metabolic process
cellular amino acid metabolic process
threonine metabolic process
threonine biosynthetic process
oxidation reduction
aspartate family amino acid metabolic process
cellular amino acid biosynthetic process
sulfur amino acid metabolic process
sulfur amino acid biosynthetic process
metabolic process
methionine biosynthetic process
Gene Properties
Chromosome Locationchromosome 4
LocusYDR158W
Gene Sequence>1098 bp ATGGCTGGAAAGAAAATTGCTGGTGTTTTGGGTGCTACTGGTTCCGTTGGTCAACGTTTC ATTCTGTTGTTGGCAAATCACCCTCATTTCGAACTGAAAGTTCTTGGTGCCTCTTCTAGA TCAGCTGGCAAGAAATACGTTGACGCTGTGAACTGGAAGCAAACCGATTTGCTACCGGAA TCTGCTACCGATATTATTGTTTCCGAATGTAAATCTGAATTCTTTAAAGAGTGTGACATC GTCTTTTCCGGATTGGATGCTGACTATGCTGGCGCTATCGAAAAGGAATTCATGGAAGCT GGTATCGCCATTGTTTCCAATGCCAAGAATTATAGAAGAGAACAAGATGTGCCATTGATT GTTCCTGTTGTCAATCCTGAGCATTTGGATATTGTAGCTCAAAAGCTTGACACCGCCAAG GCTCAAGGTAAGCCAAGACCAGGGTTCATTATCTGTATTTCCAATTGTTCCACTGCAGGT TTGGTTGCACCATTGAAGCCTTTGATTGAAAAATTCGGTCCTATTGATGCTTTGACCACT ACTACTTTGCAAGCAATCTCAGGTGCTGGTTTCTCCCCAGGTGTACCAGGTATTGATATT CTAGACAATATTATTCCATACATTGGTGGTGAAGAAGACAAGATGGAATGGGAGACCAAG AAAATCTTGGCTCCATTAGCAGAAGACAAGACACACGTCAAACTATTGACTCCAGAAGAA ATCAAAGTCTCTGCTCAATGTAACAGAGTCGCTGTTTCCGATGGGCACACCGAATGTATC TCTTTGAGGTTCAAGAACAGACCTGCTCCATCCGTCGAGCAAGTCAAGACATGCCTAAAA GAATACGTCTGCGATGCCTACAAATTAGGCTGTCATTCTGCTCCAAAGCAAACTATTCAT GTTTTGGAACAACCAGACAGACCTCAACCAAGGTTGGACAGGAACAGAGACAGCGGTTAC GGTGTTTCCGTTGGTAGAATCAGAGAAGACCCATTGTTAGATTTCAAAATGGTTGTCCTT TCCCACAACACCATTATTGGTGCCGCTGGTTCTGGTGTCTTGATTGCCGAAATCTTACTA GCAAGAAACTTGATTTAA
Protein Properties
Pfam Domain Function
Protein Residues365
Protein Molecular Weight39543.30078
Protein Theoretical pI6.71
Signalling Regions
  • None
Transmembrane Regions
  • None
Protein Sequence>Aspartate-semialdehyde dehydrogenase MAGKKIAGVLGATGSVGQRFILLLANHPHFELKVLGASSRSAGKKYVDAVNWKQTDLLPE SATDIIVSECKSEFFKECDIVFSGLDADYAGAIEKEFMEAGIAIVSNAKNYRREQDVPLI VPVVNPEHLDIVAQKLDTAKAQGKPRPGFIICISNCSTAGLVAPLKPLIEKFGPIDALTT TTLQAISGAGFSPGVPGIDILDNIIPYIGGEEDKMEWETKKILAPLAEDKTHVKLLTPEE IKVSAQCNRVAVSDGHTECISLRFKNRPAPSVEQVKTCLKEYVCDAYKLGCHSAPKQTIH VLEQPDRPQPRLDRNRDSGYGVSVGRIREDPLLDFKMVVLSHNTIIGAAGSGVLIAEILL ARNLI
References
External Links
ResourceLink
Saccharomyces Genome Database HOM2
Uniprot IDP13663
Uniprot NameDHAS_YEAST
GenBank Gene IDAY557698
Genebank Protein ID45269289
General Reference
  • Thomas, D., Surdin-Kerjan, Y. (1989). "Structure of the HOM2 gene of Saccharomyces cerevisiae and regulation of its expression." Mol Gen Genet 217:149-154.2570346
  • Jacq, C., Alt-Morbe, J., Andre, B., Arnold, W., Bahr, A., Ballesta, J. P., Bargues, M., Baron, L., Becker, A., Biteau, N., Blocker, H., Blugeon, C., Boskovic, J., Brandt, P., Bruckner, M., Buitrago, M. J., Coster, F., Delaveau, T., del Rey, F., Dujon, B., Eide, L. G., Garcia-Cantalejo, J. M., Goffeau, A., Gomez-Peris, A., Zaccaria, P., et, a. l. .. (1997). "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV." Nature 387:75-78.9169867
  • Hu, Y., Rolfs, A., Bhullar, B., Murthy, T. V., Zhu, C., Berger, M. F., Camargo, A. A., Kelley, F., McCarron, S., Jepson, D., Richardson, A., Raphael, J., Moreira, D., Taycher, E., Zuo, D., Mohr, S., Kane, M. F., Williamson, J., Simpson, A., Bulyk, M. L., Harlow, E., Marsischky, G., Kolodner, R. D., LaBaer, J. (2007). "Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae." Genome Res 17:536-543.17322287
  • 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
  • Li, X., Gerber, S. A., Rudner, A. D., Beausoleil, S. A., Haas, W., Villen, J., Elias, J. E., Gygi, S. P. (2007). "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae." J Proteome Res 6:1190-1197.17330950
  • Smolka, M. B., Albuquerque, C. P., Chen, S. H., Zhou, H. (2007). "Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Proc Natl Acad Sci U S A 104:10364-10369.17563356
  • 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