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MDE1 methylthioribulose 1-phosphate dehydratase MDE1 [ Saccharomyces cerevisiae S288C ]

Gene ID: 853481, updated on 9-Dec-2024

Summary

Official Symbol
MDE1
Official Full Name
methylthioribulose 1-phosphate dehydratase MDE1
Primary source
SGD:S000003785
Locus tag
YJR024C
See related
AllianceGenome:SGD:S000003785; FungiDB:YJR024C; VEuPathDB:YJR024C
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 methylthioribulose 1-phosphate dehydratase activity. Involved in L-methionine salvage from methylthioadenosine. Located in cytoplasm. Orthologous to human APIP (APAF1 interacting protein). [provided by Alliance of Genome Resources, Dec 2024]
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Genomic context

See MDE1 in Genome Data Viewer
Location:
chromosome: X
Exon count:
1
Sequence:
Chromosome: X; NC_001142.9 (470230..470964, complement)

Chromosome X - NC_001142.9Genomic Context describing neighboring genes Neighboring gene Rec107p Neighboring gene U4/U6-U5 snRNP complex subunit LSM8 Neighboring gene 3-hydroxyanthranilate 3,4-dioxygenase Neighboring gene gag protein Neighboring gene gag-pol fusion protein

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 lyase activity IEA
Inferred from Electronic Annotation
more info
 
enables metal ion binding IEA
Inferred from Electronic Annotation
more info
 
enables methylthioribulose 1-phosphate dehydratase activity IBA
Inferred from Biological aspect of Ancestor
more info
 
enables methylthioribulose 1-phosphate dehydratase activity IEA
Inferred from Electronic Annotation
more info
 
enables methylthioribulose 1-phosphate dehydratase activity IMP
Inferred from Mutant Phenotype
more info
PubMed 
enables zinc ion binding IEA
Inferred from Electronic Annotation
more info
 
enables zinc ion binding RCA
inferred from Reviewed Computational Analysis
more info
PubMed 
Process Evidence Code Pubs
involved_in L-methionine salvage from methylthioadenosine IBA
Inferred from Biological aspect of Ancestor
more info
 
involved_in L-methionine salvage from methylthioadenosine IEA
Inferred from Electronic Annotation
more info
 
involved_in L-methionine salvage from methylthioadenosine IMP
Inferred from Mutant Phenotype
more info
PubMed 
involved_in methionine biosynthetic process IEA
Inferred from Electronic Annotation
more info
 
Component Evidence Code Pubs
located_in cytoplasm HDA PubMed 
is_active_in cytoplasm IBA
Inferred from Biological aspect of Ancestor
more info
 
located_in cytoplasm IEA
Inferred from Electronic Annotation
more info
 

General protein information

Preferred Names
methylthioribulose 1-phosphate dehydratase MDE1
NP_012558.3
  • 5'-methylthioribulose-1-phosphate dehydratase; acts in the methionine salvage pathway; potential Smt3p sumoylation substrate; expression downregulated by caspofungin and deletion mutant is caspofungin resistant

NCBI Reference Sequences (RefSeq)

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Genome Annotation

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

Reference assembly

Genomic

  1. NC_001142.9 Reference assembly

    Range
    470230..470964 complement
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NM_001181682.3NP_012558.3  TPA: methylthioribulose 1-phosphate dehydratase MDE1 [Saccharomyces cerevisiae S288C]

    See identical proteins and their annotated locations for NP_012558.3

    Status: REVIEWED

    UniProtKB/Swiss-Prot
    B3LQB9, B5VLI6, D6VWJ7, P47095
    UniProtKB/TrEMBL
    D3UF85, G2WH34, N1P8N0
    Conserved Domains (1) summary
    cd00398
    Location:14238
    Aldolase_II; Class II Aldolase and Adducin head (N-terminal) domain. Aldolases are ubiquitous enzymes catalyzing central steps of carbohydrate metabolism. Based on enzymatic mechanisms, this superfamily has been divided into two distinct classes (Class I and II). ...