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ADE16 bifunctional phosphoribosylaminoimidazolecarboxamide formyltransferase/IMP cyclohydrolase ADE16 [ Saccharomyces cerevisiae S288C ]

Gene ID: 850715, updated on 2-Nov-2024

Summary

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Official Symbol
ADE16
Official Full Name
bifunctional phosphoribosylaminoimidazolecarboxamide formyltransferase/IMP cyclohydrolase ADE16
Primary source
SGD:S000004018
Locus tag
YLR028C
See related
AllianceGenome:SGD:S000004018; FungiDB:YLR028C; VEuPathDB:YLR028C
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 IMP cyclohydrolase activity and phosphoribosylaminoimidazolecarboxamide formyltransferase activity. Involved in 'de novo' IMP biosynthetic process. Located in cytosol. Human ortholog(s) of this gene implicated in purine-pyrimidine metabolic disorder. Orthologous to human ATIC (5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase/IMP cyclohydrolase). [provided by Alliance of Genome Resources, Nov 2024]
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Genomic context

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See ADE16 in Genome Data Viewer
Location:
chromosome: XII
Exon count:
1
Sequence:
Chromosome: XII; NC_001144.5 (199540..201315, complement)

Chromosome XII - NC_001144.5Genomic Context describing neighboring genes Neighboring gene aspartate transaminase AAT2 Neighboring gene ncRNA Neighboring gene ribosomal 60S subunit protein L15A Neighboring gene uncharacterized protein

Genomic regions, transcripts, and products

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Genomic Sequence:
NC_001144.5

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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Related articles in PubMed

  1. Saccharomyces cerevisiae expresses two genes encoding isozymes of 5-aminoimidazole-4-carboxamide ribonucleotide transformylase. Tibbetts AS, et al. Arch Biochem Biophys, 1997 Apr 15. PMID 9143321
  2. Characterization of two 5-aminoimidazole-4-carboxamide ribonucleotide transformylase/inosine monophosphate cyclohydrolase isozymes from Saccharomyces cerevisiae. Tibbetts AS, et al. J Biol Chem, 2000 Jul 7. PMID 10877846
  3. Physiological and toxic effects of purine intermediate 5-amino-4-imidazolecarboxamide ribonucleotide (AICAR) in yeast. Hürlimann HC, et al. J Biol Chem, 2011 Sep 2. PMID 21757731, Free PMC Article
  4. Dysregulation of purine nucleotide biosynthesis pathways modulates cisplatin cytotoxicity in Saccharomyces cerevisiae. Kowalski D, et al. Mol Pharmacol, 2008 Oct. PMID 18612078, Free PMC Article
  5. Role of the myb-like protein bas1p in Saccharomyces cerevisiae: a proteome analysis. Denis V, et al. Mol Microbiol, 1998 Nov. PMID 9822821

See all (49) citations in PubMed

GeneRIFs: Gene References Into Functions

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

Gene Ontology Provided by SGD

Function Evidence Code Pubs
enables IMP cyclohydrolase activity IBA
Inferred from Biological aspect of Ancestor
more info
  
enables IMP cyclohydrolase activity IDA
Inferred from Direct Assay
more info
 PubMed 
enables IMP cyclohydrolase activity IEA
Inferred from Electronic Annotation
more info
  
enables hydrolase activity IEA
Inferred from Electronic Annotation
more info
  
enables hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amidines IEA
Inferred from Electronic Annotation
more info
  
enables phosphoribosylaminoimidazolecarboxamide formyltransferase activity IBA
Inferred from Biological aspect of Ancestor
more info
  
enables phosphoribosylaminoimidazolecarboxamide formyltransferase activity IDA
Inferred from Direct Assay
more info
 PubMed 
enables phosphoribosylaminoimidazolecarboxamide formyltransferase activity IEA
Inferred from Electronic Annotation
more info
  
enables transferase activity IEA
Inferred from Electronic Annotation
more info
  
Process Evidence Code Pubs
involved_in 'de novo' IMP biosynthetic process IBA
Inferred from Biological aspect of Ancestor
more info
  
involved_in 'de novo' IMP biosynthetic process IDA
Inferred from Direct Assay
more info
 PubMed 
involved_in 'de novo' IMP biosynthetic process IEA
Inferred from Electronic Annotation
more info
  
involved_in 'de novo' IMP biosynthetic process IMP
Inferred from Mutant Phenotype
more info
 PubMed 
involved_in nucleobase-containing compound biosynthetic process IEA
Inferred from Electronic Annotation
more info
  
involved_in purine nucleotide biosynthetic process IDA
Inferred from Direct Assay
more info
 PubMed 
involved_in purine nucleotide biosynthetic process IEA
Inferred from Electronic Annotation
more info
  
involved_in purine nucleotide biosynthetic process IMP
Inferred from Mutant Phenotype
more info
 PubMed 
Component Evidence Code Pubs
located_in cytoplasm IEA
Inferred from Electronic Annotation
more info
  
is_active_in cytosol IBA
Inferred from Biological aspect of Ancestor
more info
  
located_in cytosol IDA
Inferred from Direct Assay
more info
 PubMed 
located_in cytosol IEA
Inferred from Electronic Annotation
more info
  

General protein information

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Preferred Names
bifunctional phosphoribosylaminoimidazolecarboxamide formyltransferase/IMP cyclohydrolase ADE16
NP_013128.1
  • Enzyme of 'de novo' purine biosynthesis; contains both 5-aminoimidazole-4-carboxamide ribonucleotide transformylase and inosine monophosphate cyclohydrolase activities; ADE16 has a paralog, ADE17, that arose from the whole genome duplication; ade16 ade17 mutants require adenine and histidine

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_001144.5 Reference assembly

    Range
    199540..201315 complement
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NM_001181915.1 → NP_013128.1  TPA: bifunctional phosphoribosylaminoimidazolecarboxamide formyltransferase/IMP cyclohydrolase ADE16 [Saccharomyces cerevisiae S288C]

    See identical proteins and their annotated locations for NP_013128.1

    Status: REVIEWED

    UniProtKB/Swiss-Prot
    D6VY30, E9PAG6, P54113
    UniProtKB/TrEMBL
    A7A0T4, B3LT01, B5VMW6, C7GXH4, G2WIM2
    Conserved Domains (1) summary
    COG0138
    Location:4 → 591
    PurH; AICAR transformylase/IMP cyclohydrolase PurH [Nucleotide transport and metabolism]
Nucleotide Protein
Heading Accession and Version
Protein Accession Links
GenPept Link UniProtKB Link
P54113.1

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