ARO8 bifunctional 2-aminoadipate transaminase/aromatic-amino-acid:2-oxoglutarate transaminase [Saccharomyces cerevisiae S288C] - Gene

Summary

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Official Symbol: ARO8
Official Full Name: bifunctional 2-aminoadipate transaminase/aromatic-amino-acid:2-oxoglutarate transaminase
Primary source: SGD:S000003170
Locus tag: YGL202W
See related: AllianceGenome:SGD:S000003170; FungiDB:YGL202W; VEuPathDB:YGL202W
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 2-aminoadipate transaminase activity and aromatic-amino-acid transaminase activity. Involved in L-phenylalanine biosynthetic process and tyrosine biosynthetic process. Located in cytoplasm. Orthologous to human AADAT (aminoadipate aminotransferase). [provided by Alliance of Genome Resources, Dec 2024]
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Genomic context

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See ARO8 in Genome Data Viewer

Location:: chromosome: VII

Exon count:: 1

Sequence:: Chromosome: VII; NC_001139.9 (116059..117561)

Chromosome VII - NC_001139.9 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:: NC_001139.9

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Study confirmed Aro8 and Aro9 as primary kynurenine aminotransferases (KATs) in S. cerevisiae and showed that the aro8Delta aro9Delta mutant cells lack kynurenic acid (KA) and showed that aro8Delta aro9Delta cells were sensitive to high concentrations of tryptophan (Trp). While expression of ARO9 rescued the sensitivity for Trp in the aro8Delta aro9Delta double mutant, addition of KA to the medium did not.
Title: Kynurenine aminotransferase activity of Aro8/Aro9 engage tryptophan degradation by producing kynurenic acid in Saccharomyces cerevisiae.
Deletion of ARO8 led to de novo production of phenylethanol during growth on a glucose synthetic medium.
Title: Deletion of the Saccharomyces cerevisiae ARO8 gene, encoding an aromatic amino acid transaminase, enhances phenylethanol production from glucose.
The aromatic aminotransferase Aro8 has been identified as an AAA-AT in Saccharomyces cerevisiae. This enzyme displays broad substrate selectivity, utilizing several amino acids and 2-oxo acids as substrates.
Title: Crystal structure of Saccharomyces cerevisiae Aro8, a putative α-aminoadipate aminotransferase.

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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 2-aminoadipate transaminase activity	IBA Inferred from Biological aspect of Ancestor more info
enables 2-aminoadipate transaminase activity	IDA Inferred from Direct Assay more info	PubMed
enables 2-aminoadipate transaminase activity	IEA Inferred from Electronic Annotation more info
enables 2-aminoadipate transaminase activity	IMP Inferred from Mutant Phenotype more info	PubMed
enables L-phenylalanine-2-oxoglutarate transaminase activity	IEA Inferred from Electronic Annotation more info
enables aromatic-amino-acid transaminase activity	IBA Inferred from Biological aspect of Ancestor more info
enables aromatic-amino-acid transaminase activity	IEA Inferred from Electronic Annotation more info
enables aromatic-amino-acid transaminase activity	IMP Inferred from Mutant Phenotype more info	PubMed
enables pyridoxal phosphate binding	IEA Inferred from Electronic Annotation more info
enables transaminase activity	IEA Inferred from Electronic Annotation more info

Process	Evidence Code	Pubs
involved_in L-methionine salvage from methylthioadenosine	IEA Inferred from Electronic Annotation more info
involved_in L-phenylalanine biosynthetic process	IEA Inferred from Electronic Annotation more info
involved_in L-phenylalanine biosynthetic process	IGI Inferred from Genetic Interaction more info	PubMed
involved_in aromatic amino acid family catabolic process	IBA Inferred from Biological aspect of Ancestor more info
involved_in aromatic amino acid metabolic process	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in biosynthetic process	IEA Inferred from Electronic Annotation more info
involved_in lysine biosynthetic process via aminoadipic acid	IBA Inferred from Biological aspect of Ancestor more info
involved_in lysine biosynthetic process via aminoadipic acid	IEA Inferred from Electronic Annotation more info
involved_in tyrosine biosynthetic process	IBA Inferred from Biological aspect of Ancestor more info
involved_in tyrosine biosynthetic process	IEA Inferred from Electronic Annotation more info
involved_in tyrosine biosynthetic process	IGI Inferred from Genetic Interaction more info	PubMed

Component	Evidence Code	Pubs
located_in cytoplasm	HDA more info	PubMed
located_in cytoplasm	IEA Inferred from Electronic Annotation more info

General protein information

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Preferred Names: bifunctional 2-aminoadipate transaminase/aromatic-amino-acid:2-oxoglutarate transaminase

NP_011313.1

EC 2.6.1.39

EC 2.6.1.57

Aromatic aminotransferase I; expression is regulated by general control of amino acid biosynthesis; involved with Aro9p in production of kynurenic acid to detoxify excess tryptophan

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_001139.9 Reference assembly

Range

116059..117561

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GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

NM_001181067.1 → NP_011313.1 TPA: bifunctional 2-aminoadipate transaminase/aromatic-amino-acid:2-oxoglutarate transaminase [Saccharomyces cerevisiae S288C]

See identical proteins and their annotated locations for NP_011313.1

Status: REVIEWED

UniProtKB/Swiss-Prot

D6VTV2, P53090

UniProtKB/TrEMBL

A0A166MTI9, A6ZTY7, B3LHQ0, C7GWZ3, C8Z853, G2WDQ5, M4WH72, M4WKD8, N1P482

Conserved Domains (1) summary

COG1167
Location:5 → 498

ARO8; DNA-binding transcriptional regulator, MocR family, contains an aminotransferase domain [Transcription, Amino acid transport and metabolism]