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Identification
NameBranched-chain-amino-acid aminotransferase, mitochondrial
Synonyms
  • BCAT
  • Protein ECA39
  • Protein TWT1
Gene NameBAT1
Enzyme Class
Biological Properties
General FunctionInvolved in catalytic activity
Specific FunctionCatalyzes the first reaction in the catabolism of the essential branched chain amino acids leucine, isoleucine, and valine. Appears to be involved in the regulation of the transition from G1 to S phase in the cell cycle. High copy suppressor of a temperature-sensitive mutation in the ABC transporter, ATM1
Cellular LocationMitochondrion matrix
Pathways
  • Valine, leucine and isoleucine degradation00280
  • Valine, leucine and isoleucine biosynthesis00290
  • Pantothenate and CoA biosynthesis00770
Reactions
  • L-leucine + 2-oxoglutarate = 4-methyl-2-oxopentanoate + L-glutamate.
  • 2-oxoglutaric acid + L-isoleucine = (S)-3-methyl-2-oxopentanoic acid + L-glutamic acid.
  • 2-oxoglutaric acid + L-valine = 3-methyl-2-oxobutanoic acid + L-glutamic acid.
Metabolites
YMDB IDNameView
YMDB00038L-IsoleucineShow
YMDB00152L-ValineShow
YMDB00153Oxoglutaric acidShow
YMDB00168(S)-3-methyl-2-oxovaleric acidShow
YMDB00271L-Glutamic acidShow
YMDB00365Alpha-Ketoisovaleric acidShow
YMDB00387L-LeucineShow
YMDB00388KetoleucineShow
YMDB00449(2S)-2-Isopropyl-3-oxosuccinateShow
YMDB00862hydronShow
YMDB00912Carbon dioxideShow
GO Classification
Component
Not Available
Function
branched-chain-amino-acid transaminase activity
catalytic activity
transferase activity
transferase activity, transferring nitrogenous groups
transaminase activity
Process
branched chain family amino acid metabolic process
metabolic process
cellular metabolic process
cellular amino acid and derivative metabolic process
cellular amino acid metabolic process
Gene Properties
Chromosome Locationchromosome 8
LocusYHR208W
Gene Sequence
>1182 bp
ATGTTGCAGAGACATTCCTTGAAGTTGGGGAAATTCTCCATCAGAACACTCGCTACTGGT
GCCCCATTAGATGCATCCAAACTAAAAATTACTAGAAACCCAAATCCATCCAAGCCAAGA
CCAAATGAAGAATTAGTGTTCGGCCAGACATTCACCGATCATATGTTGACCATTCCTTGG
TCAGCCAAAGAAGGGTGGGGCACTCCACACATCAAGCCTTACGGTAATCTTTCTCTTGAC
CCATCTGCTTGTGTATTCCATTATGCATTTGAATTATTTGAAGGTTTGAAAGCCTACAGA
ACTCCTCAAAATACTATCACCATGTTCCGTCCGGATAAGAACATGGCCCGTATGAACAAG
TCTGCCGCTAGAATTTGTTTGCCAACTTTCGAATCTGAAGAATTGATCAAACTTACCGGG
AAATTGATCGAACAAGATAAACACTTGGTTCCTCAAGGTAATGGTTACTCATTATACATC
AGACCAACAATGATTGGTACATCCAAGGGTTTAGGTGTTGGCACTCCCTCCGAGGCTCTT
CTTTATGTTATTACTTCTCCAGTCGGTCCTTATTATAAGACTGGTTTCAAAGCCGTACGT
CTTGAAGCAACAGACTATGCTACAAGAGCTTGGCCAGGTGGTGTTGGCGACAAAAAATTG
GGTGCTAACTATGCCCCATGCATCTTACCTCAACTACAAGCTGCCAAAAGAGGGTACCAA
CAAAATCTATGGTTGTTCGGCCCAGAAAAGAACATCACTGAGGTTGGTACTATGAACGTG
TTCTTCGTTTTCCTCAACAAAGTCACTGGCAAGAAGGAATTGGTTACCGCTCCATTAGAT
GGTACCATTTTAGAAGGTGTTACCAGAGACTCTGTTTTAACATTGGCTCGTGACAAACTA
GATCCTCAAGAATGGGACATCAACGAGCGTTATTACACTATTACTGAAGTCGCCACTAGA
GCAAAACAAGGTGAACTATTAGAAGCCTTCGGTTCTGGTACTGCTGCTGTCGTTTCACCT
ATCAAGGAAATTGGCTGGAACAACGAAGATATTCATGTTCCACTATTGCCTGGTGAACAA
TGTGGTGCATTGACCAAGCAAGTTGCTCAATGGATTGCTGATATCCAATACGGTAGAGTC
AATTATGGTAACTGGTCAAAAACTGTTGCCGACTTGAACTAA
Protein Properties
Pfam Domain Function
Protein Residues393
Protein Molecular Weight43595.69922
Protein Theoretical pI9.27
Signalling Regions
  • None
Transmembrane Regions
  • None
Protein Sequence
>Branched-chain-amino-acid aminotransferase, mitochondrial
MLQRHSLKLGKFSIRTLATGAPLDASKLKITRNPNPSKPRPNEELVFGQTFTDHMLTIPW
SAKEGWGTPHIKPYGNLSLDPSACVFHYAFELFEGLKAYRTPQNTITMFRPDKNMARMNK
SAARICLPTFESEELIKLTGKLIEQDKHLVPQGNGYSLYIRPTMIGTSKGLGVGTPSEAL
LYVITSPVGPYYKTGFKAVRLEATDYATRAWPGGVGDKKLGANYAPCILPQLQAAKRGYQ
QNLWLFGPEKNITEVGTMNVFFVFLNKVTGKKELVTAPLDGTILEGVTRDSVLTLARDKL
DPQEWDINERYYTITEVATRAKQGELLEAFGSGTAAVVSPIKEIGWNNEDIHVPLLPGEQ
CGALTKQVAQWIADIQYGRVNYGNWSKTVADLN
References
External Links
ResourceLink
Saccharomyces Genome Database BAT1
Uniprot IDP38891
Uniprot NameBCA1_YEAST
GenBank Gene IDAY558111
Genebank Protein ID45270112
General Reference
  • Kispal, G., Steiner, H., Court, D. A., Rolinski, B., Lill, R. (1996). "Mitochondrial and cytosolic branched-chain amino acid transaminases from yeast, homologs of the myc oncogene-regulated Eca39 protein." J Biol Chem 271:24458-24464.8798704
  • Johnston, M., Andrews, S., Brinkman, R., Cooper, J., Ding, H., Dover, J., Du, Z., Favello, A., Fulton, L., Gattung, S., et, a. l. .. (1994). "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome VIII." Science 265:2077-2082.8091229
  • Hu, Y., Rolfs, A., Bhullar, B., Murthy, T. V., Zhu, C., Berger, M. F., Camargo, A. A., Kelley, F., McCarron, S., Jepson, D., Richardson, A., Raphael, J., Moreira, D., Taycher, E., Zuo, D., Mohr, S., Kane, M. F., Williamson, J., Simpson, A., Bulyk, M. L., Harlow, E., Marsischky, G., Kolodner, R. D., LaBaer, J. (2007). "Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae." Genome Res 17:536-543.17322287
  • Eden, A., Simchen, G., Benvenisty, N. (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 271:20242-20245.8702755
  • Ben-Yosef, T., Yanuka, O., Benvenisty, N. (1996). "ECA39 is regulated by c-Myc in human and by a Jun/Fos homolog, Gcn4, in yeast." Oncogene 13:1859-1866.8934531
  • Ghaemmaghami, S., Huh, W. K., Bower, K., Howson, R. W., Belle, A., Dephoure, N., O'Shea, E. K., Weissman, J. S. (2003). "Global analysis of protein expression in yeast." Nature 425:737-741.14562106
  • Albuquerque, C. P., Smolka, M. B., Payne, S. H., Bafna, V., Eng, J., Zhou, H. (2008). "A multidimensional chromatography technology for in-depth phosphoproteome analysis." Mol Cell Proteomics 7:1389-1396.18407956