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

Gene ID: 856615, updated on 18-Sep-2024

Summary

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. Orthologous to human BCAT1 (branched chain amino acid transaminase 1) and BCAT2 (branched chain amino acid transaminase 2). [provided by Alliance of Genome Resources, Apr 2022]
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Genomic context

See BAT1 in Genome Data Viewer
Location:
chromosome: VIII
Exon count:
1
Sequence:
Chromosome: VIII; NC_001140.6 (517532..518713)

Chromosome VIII - NC_001140.6Genomic Context describing neighboring genes Neighboring gene kinase-regulated stress-responsive transcription factor SKN7 Neighboring gene S-adenosylmethionine-dependent methyltransferase Neighboring gene S-adenosylmethionine-dependent methyltransferase Neighboring gene aldose 1-epimerase superfamily protein

Bibliography

GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Pathways from PubChem

Interactions

Products Interactant Other Gene Complex Source Pubs Description

General gene information

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
 
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 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

Preferred Names
branched-chain-amino-acid transaminase BAT1
NP_012078.3
  • 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

  1. NC_001140.6 Reference assembly

    Range
    517532..518713
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NM_001179339.3NP_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:78378
    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 ...