LYS1/YIR034C Summary Help

Standard Name LYS1
Systematic Name YIR034C
Feature Type ORF, Verified
Description Saccharopine dehydrogenase (NAD+, L-lysine-forming); catalyzes the conversion of saccharopine to L-lysine, which is the final step in the lysine biosynthesis pathway; also has mRNA binding activity (1, 2 and see Summary Paragraph)
Name Description LYSine requiring
Chromosomal Location
ChrIX:420736 to 419615 | ORF Map | GBrowse
Note: this feature is encoded on the Crick strand.
Gbrowse
Genetic position: 40 cM
Gene Ontology Annotations All LYS1 GO evidence and references
  View Computational GO annotations for LYS1
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
High-throughput
Regulators 7 genes
Resources
Pathways
Classical genetics
unspecified
Large-scale survey
null
overexpression
Resources
26 total interaction(s) for 20 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 11
  • Affinity Capture-RNA: 2
  • PCA: 1
  • Protein-peptide: 3
  • Reconstituted Complex: 1
  • Two-hybrid: 3

Genetic Interactions
  • Dosage Lethality: 1
  • Negative Genetic: 1
  • Synthetic Lethality: 2
  • Synthetic Rescue: 1

Resources
Expression Summary
histogram
Resources
Length (a.a.) 373
Molecular Weight (Da) 41,464
Isoelectric Point (pI) 9.82
Localization
Phosphorylation PhosphoGRID | PhosphoPep Database
Structure
Homologs
sequence information
ChrIX:420736 to 419615 | ORF Map | GBrowse
Note: this feature is encoded on the Crick strand.
SGD ORF map
Genetic position: 40 cM
Last Update Coordinates: 2011-02-03 | Sequence: 1994-12-10
Subfeature details
Relative
Coordinates
Chromosomal
Coordinates
Most Recent Updates
Coordinates Sequence
CDS 1..1122 420736..419615 2011-02-03 1994-12-10
Retrieve sequences
Analyze Sequence
S288C only
S288C vs. other species
S288C vs. other strains
Resources
External Links All Associated Seq | E.C. | Entrez Gene | Entrez RefSeq Protein | MIPS | Search all NCBI (Entrez) | UniProtKB
Primary SGDIDS000001473
SUMMARY PARAGRAPH for LYS1

About lysine biosynthesis

S. cerevisiae synthesizes the essential amino acid L-lysine via the L-alpha-aminoadipic acid pathway instead of the diaminopmelate pathway (3). Originally proposed to be characteristic of fungi, recent studies suggest prokaryotes also synthesize lysine via the alpha-aminoadipic acid pathway (4). Intermediates in this pathway are often incorporated into secondary metabolites. For example, it has been well- studied that alpha-aminoadipate is required for penicillin production (3). Regulation of the lysine biosynthetic pathway in S. cerevisiae is an interaction between general amino acid control (via Gcn4p) (5), feedback inhibition of homocitrate synthase activity by lysine (6), and induction of Lys14p by alpha-aminoadipate semialdehyde (7).

Last updated: 2007-10-04 Contact SGD

References cited on this page View Complete Literature Guide for LYS1
1) Ogawa H and Fujioka M  (1978) Purification and characterization of saccharopine dehydrogenase from baker's yeast. J Biol Chem 253(10):3666-70
2) Tsvetanova NG, et al.  (2010) Proteome-Wide Search Reveals Unexpected RNA-Binding Proteins in Saccharomyces cerevisiae.LID - e12671 [pii] PLoS One 5(9)
3) Zabriskie TM and Jackson MD  (2000) Lysine biosynthesis and metabolism in fungi. Nat Prod Rep 17(1):85-97
4) Nishida H and Nishiyama M  (2000) What is characteristic of fungal lysine synthesis through the alpha-aminoadipate pathway? J Mol Evol 51(3):299-302
5) Hinnebusch A  (1992) "General and Pathway-specific Regulatory Mechanisms Controlling the Synthesis of Amino Acid Biosynthetic Enzymes in Saccharomyces cerevisiae". Pp. 319-414 in The Molecular and Cellular Biology of the Yeast Saccharomyces: Gene Expression, edited by Jones EW, Pringle JR and Broach JR. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press
6) Feller A, et al.  (1999) In Saccharomyces cerevisae, feedback inhibition of homocitrate synthase isoenzymes by lysine modulates the activation of LYS gene expression by Lys14p. Eur J Biochem 261(1):163-70
7) El Alami M, et al.  (2000) Characterisation of a tripartite nuclear localisation sequence in the regulatory protein Lys14 of Saccharomyces cerevisiae. Curr Genet 38(2):78-86