BAT1 branched-chain-amino-acid transaminase BAT1 [Saccharomyces cerevisiae S288C] - Gene

Summary

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Official Symbol: BAT1
Official Full Name: branched-chain-amino-acid transaminase BAT1
Primary source: SGD:S000001251
Locus tag: YHR208W
See related: AllianceGenome:SGD:S000001251; FungiDB:YHR208W; VEuPathDB:YHR208W
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: ECA39; TWT1
Summary: Enables branched-chain-amino-acid transaminase activity. Involved in branched-chain amino acid biosynthetic process and branched-chain amino acid catabolic process. Located in mitochondrial matrix. Human ortholog(s) of this gene implicated in hypervalinemia and hyperleucine-isoleucinemia. Orthologous to several human genes including BCAT2 (branched chain amino acid transaminase 2). [provided by Alliance of Genome Resources, Nov 2024]
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Genomic context

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See BAT1 in Genome Data Viewer

Location:: chromosome: VIII

Exon count:: 1

Sequence:: Chromosome: VIII; NC_001140.6 (517532..518713)

Chromosome VIII - NC_001140.6 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:: NC_001140.6

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

BAT1 and BAT2 differential expression and subcellular relocalization has resulted in distribution of the biosynthetic and catabolic roles of ancestral BCAT in two isozymes improving BCAA metabolism and constituting an adaptation to facultative metabolism.
Title: Saccharomyces cerevisiae Bat1 and Bat2 aminotransferases have functionally diverged from the ancestral-like Kluyveromyces lactis orthologous enzyme.
adjustment of BAT gene expression could play an important role in assisting winemakers in their endeavour to produce wines with specific flavour profiles.
Title: The effect of increased branched-chain amino acid transaminase activity in yeast on the production of higher alcohols and on the flavour profiles of wine and distillates.

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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 L-isoleucine-2-oxoglutarate transaminase activity	IEA Inferred from Electronic Annotation more info
enables L-leucine-2-oxoglutarate transaminase activity	IEA Inferred from Electronic Annotation more info
enables L-valine-2-oxoglutarate transaminase activity	IEA Inferred from Electronic Annotation more info
enables branched-chain-amino-acid transaminase activity	IBA Inferred from Biological aspect of Ancestor more info
enables branched-chain-amino-acid transaminase activity	IDA Inferred from Direct Assay more info	PubMed
enables branched-chain-amino-acid transaminase activity	IEA Inferred from Electronic Annotation more info
enables transaminase activity	IEA Inferred from Electronic Annotation more info

Process	Evidence Code	Pubs
involved_in L-leucine biosynthetic process	IBA Inferred from Biological aspect of Ancestor more info
involved_in L-leucine biosynthetic process	IEA Inferred from Electronic Annotation more info
involved_in L-methionine salvage from methylthioadenosine	IEA Inferred from Electronic Annotation more info
involved_in L-valine biosynthetic process	IBA Inferred from Biological aspect of Ancestor more info
involved_in L-valine biosynthetic process	IEA Inferred from Electronic Annotation more info
involved_in amino acid biosynthetic process	IEA Inferred from Electronic Annotation more info
involved_in branched-chain amino acid biosynthetic process	IDA Inferred from Direct Assay more info	PubMed
involved_in branched-chain amino acid biosynthetic process	IEA Inferred from Electronic Annotation more info
involved_in branched-chain amino acid biosynthetic process	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in branched-chain amino acid catabolic process	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in branched-chain amino acid metabolic process	IEA Inferred from Electronic Annotation more info
involved_in isoleucine biosynthetic process	IEA Inferred from Electronic Annotation more info

Component	Evidence Code	Pubs
located_in mitochondrial matrix	IDA Inferred from Direct Assay more info	PubMed
located_in mitochondrial matrix	IEA Inferred from Electronic Annotation more info
located_in mitochondrion	HDA more info	PubMed
is_active_in mitochondrion	IBA Inferred from Biological aspect of Ancestor more info
located_in mitochondrion	IEA Inferred from Electronic Annotation more info

General protein information

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Preferred Names: branched-chain-amino-acid transaminase BAT1

NP_012078.3

EC 2.6.1.42

Mitochondrial branched-chain amino acid (BCAA) aminotransferase; preferentially involved in BCAA biosynthesis; homolog of murine ECA39; highly expressed during logarithmic phase and repressed during stationary phase; BAT1 has a paralog, BAT2, that arose from the whole genome duplication

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_001140.6 Reference assembly

Range

517532..518713

Download

GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

NM_001179339.3 → NP_012078.3 TPA: branched-chain-amino-acid transaminase BAT1 [Saccharomyces cerevisiae S288C]

See identical proteins and their annotated locations for NP_012078.3

Status: REVIEWED

UniProtKB/Swiss-Prot

D3DLF7, P38891

UniProtKB/TrEMBL

A6ZTB5, B3LSW9, C7GN93, C8ZA09, G2WFT2, N1P4Y5

Conserved Domains (1) summary

cd01557
Location:78 → 378

BCAT_beta_family; Branched-chain aminotransferase catalyses the transamination of the branched-chain amino acids leusine, isoleucine and valine to their respective alpha-keto acids, alpha-ketoisocaproate, alpha-keto-beta-methylvalerate and alpha-ketoisovalerate. The ...