U.S. flag

An official website of the United States government

Format

Send to:

Choose Destination

CHA1 L-serine/L-threonine ammonia-lyase CHA1 [ Saccharomyces cerevisiae S288C ]

Gene ID: 850295, updated on 4-Jan-2025

Summary

Official Symbol
CHA1
Official Full Name
L-serine/L-threonine ammonia-lyase CHA1
Primary source
SGD:S000000569
Locus tag
YCL064C
See related
AllianceGenome:SGD:S000000569; FungiDB:YCL064C; VEuPathDB:YCL064C
Gene type
protein coding
RefSeq status
REVIEWED
Organism
Saccharomyces cerevisiae S288C (strain: S288C)
Lineage
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces
Summary
Enables L-serine ammonia-lyase activity and threonine deaminase activity. Involved in L-serine catabolic process and threonine catabolic process. Located in mitochondrial nucleoid. Orthologous to human SDS (serine dehydratase) and SDSL (serine dehydratase like). [provided by Alliance of Genome Resources, Jan 2025]
NEW
Try the new Gene table
Try the new Transcript table

Genomic context

See CHA1 in Genome Data Viewer
Location:
chromosome: III
Exon count:
1
Sequence:
Chromosome: III; NC_001135.5 (15798..16880, complement)

Chromosome III - NC_001135.5Genomic Context describing neighboring genes Neighboring gene homeodomain mating type protein alpha2 Neighboring gene transcriptional co-activator mating type protein alpha Neighboring gene Vac17p Neighboring gene chromatin-modulating protein MRC1

Bibliography

GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Pathways from PubChem

Interactions

Products Interactant Other Gene Complex Source Pubs Description

General gene information

Gene Ontology Provided by SGD

Function Evidence Code Pubs
enables L-serine ammonia-lyase activity IBA
Inferred from Biological aspect of Ancestor
more info
 
enables L-serine ammonia-lyase activity IDA
Inferred from Direct Assay
more info
PubMed 
enables L-serine ammonia-lyase activity IEA
Inferred from Electronic Annotation
more info
 
enables lyase activity IEA
Inferred from Electronic Annotation
more info
 
enables pyridoxal phosphate binding IEA
Inferred from Electronic Annotation
more info
 
enables threonine deaminase activity IDA
Inferred from Direct Assay
more info
PubMed 
enables threonine deaminase activity IEA
Inferred from Electronic Annotation
more info
 
Process Evidence Code Pubs
involved_in L-serine catabolic process IBA
Inferred from Biological aspect of Ancestor
more info
 
involved_in L-serine catabolic process IGI
Inferred from Genetic Interaction
more info
PubMed 
involved_in amino acid metabolic process IEA
Inferred from Electronic Annotation
more info
 
involved_in threonine catabolic process IGI
Inferred from Genetic Interaction
more info
PubMed 
Component Evidence Code Pubs
located_in mitochondrial nucleoid IDA
Inferred from Direct Assay
more info
PubMed 
located_in mitochondrion HDA PubMed 
located_in mitochondrion IEA
Inferred from Electronic Annotation
more info
 

General protein information

Preferred Names
L-serine/L-threonine ammonia-lyase CHA1
NP_001018030.1
  • Catabolic L-serine (L-threonine) deaminase; catalyzes the degradation of both L-serine and L-threonine; required to use serine or threonine as the sole nitrogen source, transcriptionally induced by serine and threonine

NCBI Reference Sequences (RefSeq)

NEW Try the new Transcript table

Genome Annotation

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference assembly

Genomic

  1. NC_001135.5 Reference assembly

    Range
    15798..16880 complement
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NM_001178706.1NP_001018030.1  TPA: L-serine/L-threonine ammonia-lyase CHA1 [Saccharomyces cerevisiae S288C]

    See identical proteins and their annotated locations for NP_001018030.1

    Status: REVIEWED

    UniProtKB/Swiss-Prot
    D6VQV4, P25379
    UniProtKB/TrEMBL
    A6ZTD3, B3LU22, C7GT17, C8Z427, G2W9W5, N1P7Z9
    Conserved Domains (1) summary
    cd06448
    Location:7333
    L-Ser-dehyd; Serine dehydratase is a pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the conversion of L- , D-serine, or L-threonine to pyruvate/ketobutyrate and ammonia.