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

Summary

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Gene symbol: MDE1
Gene description: methylthioribulose 1-phosphate dehydratase MDE1
Primary source: FungiDB:YJR024C
Locus tag: YJR024C
See related: SGD:S000003785; AllianceGenome:SGD:S000003785; 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, Apr 2022]
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Genomic context

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See MDE1 in Genome Data Viewer

Location:: chromosome: X

Exon count:: 1

Sequence:: Chromosome: X; NC_001142.9 (470230..470964, complement)

Chromosome X - NC_001142.9 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:: NC_001142.9

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

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Pathways from PubChem

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Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Homology

Orthologs from OrthoDB

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 S-adenosylmethionine	IEA Inferred from Electronic Annotation more info
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 more info	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

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Preferred Names: methylthioribulose 1-phosphate dehydratase MDE1

NP_012558.3

EC 4.2.1.109

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

NC_001142.9 Reference assembly

Range

470230..470964 complement

Download

GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

NM_001181682.3 → NP_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:14 → 238

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). ...