YSA1 ADP-ribose diphosphatase [Saccharomyces cerevisiae S288C] - Gene

Summary

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Official Symbol: YSA1
Official Full Name: ADP-ribose diphosphatase
Primary source: SGD:S000000315
Locus tag: YBR111C
See related: AllianceGenome:SGD:S000000315; FungiDB:YBR111C; VEuPathDB:YBR111C
Gene type: protein coding
RefSeq status: REVIEWED
Organism: Saccharomyces cerevisiae S288C (strain: S288C)
Lineage: Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces
Also known as: RMA2
Summary: Enables ADP-ribose diphosphatase activity. Involved in ribose phosphate metabolic process. Located in mitochondrion. Orthologous to human NUDT5 (nudix hydrolase 5). [provided by Alliance of Genome Resources, Dec 2024]
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Genomic context

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See YSA1 in Genome Data Viewer

Location:: chromosome: II

Exon count:: 1

Sequence:: Chromosome: II; NC_001134.8 (461178..461873, complement)

Chromosome II - NC_001134.8 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:: NC_001134.8

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

the Nudix (nucleoside diphosphate linked to another moiety X) hydrolase Ysa1 from Saccharomyces cerevisiae is a major regulator of cellular ADPr and O-acetyl-ADP-ribose (OAADPr)
Title: Hydrolase regulates NAD+ metabolites and modulates cellular redox.

Submit: New GeneRIF Correction

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 ADP-ribose diphosphatase activity	IBA Inferred from Biological aspect of Ancestor more info
enables ADP-ribose diphosphatase activity	IDA Inferred from Direct Assay more info	PubMed
enables ADP-ribose diphosphatase activity	IEA Inferred from Electronic Annotation more info
enables hydrolase activity	IEA Inferred from Electronic Annotation more info
enables metal ion binding	IEA Inferred from Electronic Annotation more info

Process	Evidence Code	Pubs
involved_in nucleoside phosphate metabolic process	IBA Inferred from Biological aspect of Ancestor more info
involved_in ribose phosphate metabolic process	IBA Inferred from Biological aspect of Ancestor more info
involved_in ribose phosphate metabolic process	IDA Inferred from Direct Assay more info	PubMed

Component	Evidence Code	Pubs
located_in cytoplasm	HDA more info	PubMed
is_active_in cytosol	IBA Inferred from Biological aspect of Ancestor more info
located_in mitochondrion	HDA more info	PubMed
located_in mitochondrion	IDA Inferred from Direct Assay more info	PubMed
located_in nucleus	HDA more info	PubMed
is_active_in nucleus	IBA Inferred from Biological aspect of Ancestor more info

General protein information

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Preferred Names: ADP-ribose diphosphatase

NP_009669.1

EC 3.6.1.13

Nudix hydrolase family member with ADP-ribose pyrophosphatase activity; shown to metabolize O-acetyl-ADP-ribose to AMP and acetylated ribose 5'-phosphate

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_001134.8 Reference assembly

Range

461178..461873 complement

Download

GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

NM_001178459.1 → NP_009669.1 TPA: ADP-ribose diphosphatase [Saccharomyces cerevisiae S288C]

See identical proteins and their annotated locations for NP_009669.1

Status: REVIEWED

UniProtKB/Swiss-Prot

D6VQB0, Q01976

UniProtKB/TrEMBL

A6ZL56, B3LN42, B5VE73, C7GUK9, D3UEK4, G2W9B6, N1PAT0

Conserved Domains (1) summary

cd03424
Location:76 → 213

ADPRase_NUDT5; ADP-ribose pyrophosphatase (ADPRase) catalyzes the hydrolysis of ADP-ribose and a variety of additional ADP-sugar conjugates to AMP and ribose-5-phosphate. Like other members of the Nudix hydrolase superfamily, it requires a divalent cation, such as Mg2+, ...