BAT1/YHR208W Summary Help

Standard Name BAT1 1
Systematic Name YHR208W
Alias ECA39 2 , TWT1 3
Feature Type ORF, Verified
Description 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 (2, 4, 5 and see Summary Paragraph)
Name Description Branched-chain Amino acid Transaminase 1
Chromosomal Location
ChrVIII:517532 to 518713 | ORF Map | GBrowse
Gene Ontology Annotations All BAT1 GO evidence and references
  View Computational GO annotations for BAT1
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
Manually curated
Regulators 15 genes
Classical genetics
Large-scale survey
76 total interaction(s) for 68 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 12
  • Affinity Capture-RNA: 6

Genetic Interactions
  • Negative Genetic: 44
  • Phenotypic Enhancement: 3
  • Positive Genetic: 10
  • Synthetic Growth Defect: 1

Expression Summary
Length (a.a.) 393
Molecular Weight (Da) 43,596
Isoelectric Point (pI) 9.59
Phosphorylation PhosphoGRID | PhosphoPep Database
sequence information
ChrVIII:517532 to 518713 | ORF Map | GBrowse
Last Update Coordinates: 2005-11-07 | Sequence: 1996-07-31
Subfeature details
Most Recent Updates
Coordinates Sequence
CDS 1..1182 517532..518713 2005-11-07 1996-07-31
Retrieve sequences
Analyze Sequence
S288C only
S288C vs. other species
S288C vs. other strains
External Links All Associated Seq | E.C. | Entrez Gene | Entrez RefSeq Protein | MIPS | Search all NCBI (Entrez) | UniProtKB
Primary SGDIDS000001251

BAT1 and BAT2 respectively encode the mitochondrial and cytosolic branched-chain amino acid aminotransferases (BCAATases) (1). BCAATases are required for both branched-chain amino acid biosynthesis and Ehrlich pathway amino acid catabolism; Bat1p and Bat2p catalyze the transfer of amino groups between the amino acids valine, isoleucine, and leucine and their corresponding alpha-keto-acids. Alpha-keto-acids are biosynthetic precursors of fusel alcohols, which influence the aroma and flavor of yeast-derived fermentation products such as beer and bread (6 and references contained therein).

Bat1p and Bat2p are 77% identical to each other and orthologs have been identified in S. pombe, worm, mouse, and human (1, 7). BAT1 is highly expressed during logarithmic phase and repressed during stationary phase, while BAT2 is expressed during stationary phase and repressed during logarithmic growth (2). On glucose-containing media, single deletion of either BAT gene impairs neither cell growth nor fusel alcohol production, but deletion of both genes results in branched-chain amino acid auxotrophy and severe growth retardation (1).

Last updated: 2007-04-30 Contact SGD

References cited on this page View Complete Literature Guide for BAT1
1) Kispal G, et al.  (1996) Mitochondrial and cytosolic branched-chain amino acid transaminases from yeast, homologs of the myc oncogene-regulated Eca39 protein. J Biol Chem 271(40):24458-64
2) Eden A, et al.  (1996) Two yeast homologs of ECA39, a target for c-Myc regulation, code for cytosolic and mitochondrial branched-chain amino acid aminotransferases. J Biol Chem 271(34):20242-5
3) Dickinson JR  (2000) Pathways of leucine and valine catabolism in yeast. Methods Enzymol 324():80-92
4) Byrne KP and Wolfe KH  (2005) The Yeast Gene Order Browser: combining curated homology and syntenic context reveals gene fate in polyploid species. Genome Res 15(10):1456-61
5) Colon M, et al.  (2011) Saccharomyces cerevisiae Bat1 and Bat2 Aminotransferases Have Functionally Diverged from the Ancestral-Like Kluyveromyces lactis Orthologous Enzyme. PLoS One 6(1):e16099
6) Lilly M, et al.  (2006) 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. FEMS Yeast Res 6(5):726-43
7) Eden A and Benvenisty N  (1998) Characterization of a branched-chain amino-acid aminotransferase from Schizosaccharomyces pombe. Yeast 14(2):189-94