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Protein

Branched-chain-amino-acid aminotransferase, mitochondrial

Gene

BAT1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in the biosynthesis of the branched chain amino acids leucine, isoleucine, and valine. Catalyzes the formation of methionine from 2-keto-4-methylthiobutyrate (KMTB) in the methionine salvage pathway primarily using branched chain amino acids (leucine, isoleucine, and valine) as the amino donors. 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, ATM1.2 Publications

Catalytic activityi

L-leucine + 2-oxoglutarate = 4-methyl-2-oxopentanoate + L-glutamate.
L-isoleucine + 2-oxoglutarate = (S)-3-methyl-2-oxopentanoate + L-glutamate.
L-valine + 2-oxoglutarate = 3-methyl-2-oxobutanoate + L-glutamate.

Cofactori

Pathwayi: L-isoleucine biosynthesis

This protein is involved in step 4 of the subpathway that synthesizes L-isoleucine from 2-oxobutanoate.
Proteins known to be involved in the 4 steps of the subpathway in this organism are:
  1. Acetolactate synthase small subunit, mitochondrial (ILV6), Acetolactate synthase catalytic subunit, mitochondrial (ILV2)
  2. Ketol-acid reductoisomerase, mitochondrial (ILV5)
  3. Dihydroxy-acid dehydratase, mitochondrial (ILV3)
  4. Branched-chain-amino-acid aminotransferase, cytosolic (BAT2), Branched-chain-amino-acid aminotransferase, mitochondrial (BAT1)
This subpathway is part of the pathway L-isoleucine biosynthesis, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-isoleucine from 2-oxobutanoate, the pathway L-isoleucine biosynthesis and in Amino-acid biosynthesis.

Pathwayi: L-leucine biosynthesis

This protein is involved in step 4 of the subpathway that synthesizes L-leucine from 3-methyl-2-oxobutanoate.
Proteins known to be involved in the 4 steps of the subpathway in this organism are:
  1. 2-isopropylmalate synthase (LEU4), 2-isopropylmalate synthase 2, mitochondrial (LEU9)
  2. 3-isopropylmalate dehydratase (LEU1)
  3. 3-isopropylmalate dehydrogenase (LEU2)
  4. Branched-chain-amino-acid aminotransferase, cytosolic (BAT2), Branched-chain-amino-acid aminotransferase, mitochondrial (BAT1)
This subpathway is part of the pathway L-leucine biosynthesis, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-leucine from 3-methyl-2-oxobutanoate, the pathway L-leucine biosynthesis and in Amino-acid biosynthesis.

Pathwayi: L-valine biosynthesis

This protein is involved in step 4 of the subpathway that synthesizes L-valine from pyruvate.
Proteins known to be involved in the 4 steps of the subpathway in this organism are:
  1. Acetolactate synthase small subunit, mitochondrial (ILV6), Acetolactate synthase catalytic subunit, mitochondrial (ILV2)
  2. Ketol-acid reductoisomerase, mitochondrial (ILV5)
  3. Dihydroxy-acid dehydratase, mitochondrial (ILV3)
  4. Branched-chain-amino-acid aminotransferase, cytosolic (BAT2), Branched-chain-amino-acid aminotransferase, mitochondrial (BAT1)
This subpathway is part of the pathway L-valine biosynthesis, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-valine from pyruvate, the pathway L-valine biosynthesis and in Amino-acid biosynthesis.

Pathwayi: L-methionine biosynthesis via salvage pathway

This protein is involved in step 6 of the subpathway that synthesizes L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate.
Proteins known to be involved in the 6 steps of the subpathway in this organism are:
  1. Methylthioribose-1-phosphate isomerase (MRI1)
  2. Methylthioribulose-1-phosphate dehydratase (MDE1)
  3. Enolase-phosphatase E1 (UTR4)
  4. Enolase-phosphatase E1 (UTR4)
  5. 1,2-dihydroxy-3-keto-5-methylthiopentene dioxygenase (ADI1)
  6. Branched-chain-amino-acid aminotransferase, cytosolic (BAT2), Aromatic amino acid aminotransferase 2 (ARO9), Branched-chain-amino-acid aminotransferase, mitochondrial (BAT1), Aromatic/aminoadipate aminotransferase 1 (ARO8)
This subpathway is part of the pathway L-methionine biosynthesis via salvage pathway, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate, the pathway L-methionine biosynthesis via salvage pathway and in Amino-acid biosynthesis.

GO - Molecular functioni

GO - Biological processi

  • branched-chain amino acid biosynthetic process Source: SGD
  • branched-chain amino acid catabolic process Source: SGD
  • cellular response to UV Source: MGI
  • isoleucine biosynthetic process Source: UniProtKB-UniPathway
  • leucine biosynthetic process Source: UniProtKB-UniPathway
  • L-methionine biosynthetic process from methylthioadenosine Source: UniProtKB-UniPathway
  • mitotic G1 DNA damage checkpoint Source: MGI
  • valine biosynthetic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Aminotransferase, Transferase

Keywords - Biological processi

Amino-acid biosynthesis, Branched-chain amino acid biosynthesis

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-11720.
YEAST:YHR208W-MONOMER.
BRENDAi2.6.1.42. 984.
ReactomeiR-SCE-70895. Branched-chain amino acid catabolism.
UniPathwayiUPA00047; UER00058.
UPA00048; UER00073.
UPA00049; UER00062.
UPA00904; UER00879.

Names & Taxonomyi

Protein namesi
Recommended name:
Branched-chain-amino-acid aminotransferase, mitochondrial (EC:2.6.1.42)
Short name:
BCAT
Alternative name(s):
Protein ECA39
Protein TWT1
Gene namesi
Name:BAT1
Synonyms:ECA39, TWT1
Ordered Locus Names:YHR208W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome VIII

Organism-specific databases

EuPathDBiFungiDB:YHR208W.
SGDiS000001251. BAT1.

Subcellular locationi

GO - Cellular componenti

  • mitochondrial matrix Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 1616MitochondrionSequence analysisAdd
BLAST
Chaini17 – 393377Branched-chain-amino-acid aminotransferase, mitochondrialPRO_0000001281Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei219 – 2191N6-(pyridoxal phosphate)lysineBy similarity
Modified residuei315 – 3151PhosphothreonineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP38891.
PeptideAtlasiP38891.

PTM databases

iPTMnetiP38891.

Expressioni

Developmental stagei

Highly expressed during logarithmic phase of growth. Down-regulated during the stationary phase.

Inductioni

Mainly expressed on ammonium-glucose exponential cultures (biosynthetic conditions), and repressed in the presence of leucine, isoleucine or valine.1 Publication

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
DVL2O146413EBI-3455,EBI-740850From a different organism.

Protein-protein interaction databases

BioGridi36642. 83 interactions.
DIPiDIP-6475N.
IntActiP38891. 6 interactions.
MINTiMINT-665576.

Structurei

3D structure databases

ProteinModelPortaliP38891.
SMRiP38891. Positions 38-379.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

GeneTreeiENSGT00390000009532.
HOGENOMiHOG000276704.
InParanoidiP38891.
KOiK00826.
OMAiWIADIQY.
OrthoDBiEOG769ZVJ.

Family and domain databases

InterProiIPR001544. Aminotrans_IV.
IPR018300. Aminotrans_IV_CS.
IPR005786. B_amino_transII.
[Graphical view]
PANTHERiPTHR11825. PTHR11825. 1 hit.
PfamiPF01063. Aminotran_4. 1 hit.
[Graphical view]
PIRSFiPIRSF006468. BCAT1. 1 hit.
SUPFAMiSSF56752. SSF56752. 1 hit.
TIGRFAMsiTIGR01123. ilvE_II. 1 hit.
PROSITEiPS00770. AA_TRANSFER_CLASS_4. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P38891-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLQRHSLKLG KFSIRTLATG APLDASKLKI TRNPNPSKPR PNEELVFGQT
60 70 80 90 100
FTDHMLTIPW SAKEGWGTPH IKPYGNLSLD PSACVFHYAF ELFEGLKAYR
110 120 130 140 150
TPQNTITMFR PDKNMARMNK SAARICLPTF ESEELIKLTG KLIEQDKHLV
160 170 180 190 200
PQGNGYSLYI RPTMIGTSKG LGVGTPSEAL LYVITSPVGP YYKTGFKAVR
210 220 230 240 250
LEATDYATRA WPGGVGDKKL GANYAPCILP QLQAAKRGYQ QNLWLFGPEK
260 270 280 290 300
NITEVGTMNV FFVFLNKVTG KKELVTAPLD GTILEGVTRD SVLTLARDKL
310 320 330 340 350
DPQEWDINER YYTITEVATR AKQGELLEAF GSGTAAVVSP IKEIGWNNED
360 370 380 390
IHVPLLPGEQ CGALTKQVAQ WIADIQYGRV NYGNWSKTVA DLN
Length:393
Mass (Da):43,596
Last modified:February 1, 1995 - v1
Checksum:iE76604F326A7C674
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X78961 Genomic DNA. Translation: CAA55556.1.
U00029 Genomic DNA. Translation: AAB69733.1.
AY558111 Genomic DNA. Translation: AAS56437.1.
BK006934 Genomic DNA. Translation: DAA06901.1.
PIRiS48989.
RefSeqiNP_012078.3. NM_001179339.3.

Genome annotation databases

EnsemblFungiiYHR208W; YHR208W; YHR208W.
GeneIDi856615.
KEGGisce:YHR208W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X78961 Genomic DNA. Translation: CAA55556.1.
U00029 Genomic DNA. Translation: AAB69733.1.
AY558111 Genomic DNA. Translation: AAS56437.1.
BK006934 Genomic DNA. Translation: DAA06901.1.
PIRiS48989.
RefSeqiNP_012078.3. NM_001179339.3.

3D structure databases

ProteinModelPortaliP38891.
SMRiP38891. Positions 38-379.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi36642. 83 interactions.
DIPiDIP-6475N.
IntActiP38891. 6 interactions.
MINTiMINT-665576.

PTM databases

iPTMnetiP38891.

Proteomic databases

MaxQBiP38891.
PeptideAtlasiP38891.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYHR208W; YHR208W; YHR208W.
GeneIDi856615.
KEGGisce:YHR208W.

Organism-specific databases

EuPathDBiFungiDB:YHR208W.
SGDiS000001251. BAT1.

Phylogenomic databases

GeneTreeiENSGT00390000009532.
HOGENOMiHOG000276704.
InParanoidiP38891.
KOiK00826.
OMAiWIADIQY.
OrthoDBiEOG769ZVJ.

Enzyme and pathway databases

UniPathwayiUPA00047; UER00058.
UPA00048; UER00073.
UPA00049; UER00062.
UPA00904; UER00879.
BioCyciMetaCyc:MONOMER-11720.
YEAST:YHR208W-MONOMER.
BRENDAi2.6.1.42. 984.
ReactomeiR-SCE-70895. Branched-chain amino acid catabolism.

Miscellaneous databases

PROiP38891.

Family and domain databases

InterProiIPR001544. Aminotrans_IV.
IPR018300. Aminotrans_IV_CS.
IPR005786. B_amino_transII.
[Graphical view]
PANTHERiPTHR11825. PTHR11825. 1 hit.
PfamiPF01063. Aminotran_4. 1 hit.
[Graphical view]
PIRSFiPIRSF006468. BCAT1. 1 hit.
SUPFAMiSSF56752. SSF56752. 1 hit.
TIGRFAMsiTIGR01123. ilvE_II. 1 hit.
PROSITEiPS00770. AA_TRANSFER_CLASS_4. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Mitochondrial and cytosolic branched-chain amino acid transaminases from yeast, homologs of the myc oncogene-regulated Eca39 protein."
    Kispal G., Steiner H., Court D.A., Rolinski B., Lill R.
    J. Biol. Chem. 271:24458-24464(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  5. "Two yeast homologs of ECA39, a target for c-Myc regulation, code for cytosolic and mitochondrial branched-chain amino acid aminotransferases."
    Eden A., Simchen G., Benvenisty N.
    J. Biol. Chem. 271:20242-20245(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  6. "ECA39 is regulated by c-Myc in human and by a Jun/Fos homolog, GCN4, in yeast."
    Ben-Yosef T., Yanuka O., Benvenisty N.
    Oncogene 13:1859-1866(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: REGULATION BY GCN4.
  7. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  8. "A complete inventory of all enzymes in the eukaryotic methionine salvage pathway."
    Pirkov I., Norbeck J., Gustafsson L., Albers E.
    FEBS J. 275:4111-4120(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  9. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
    Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
    Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-315, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "Saccharomyces cerevisiae Bat1 and Bat2 aminotransferases have functionally diverged from the ancestral-like Kluyveromyces lactis orthologous enzyme."
    Colon M., Hernandez F., Lopez K., Quezada H., Gonzalez J., Lopez G., Aranda C., Gonzalez A.
    PLoS ONE 6:E16099-E16099(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INDUCTION.

Entry informationi

Entry nameiBCA1_YEAST
AccessioniPrimary (citable) accession number: P38891
Secondary accession number(s): D3DLF7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: June 8, 2016
This is version 147 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 87300 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome VIII
    Yeast (Saccharomyces cerevisiae) chromosome VIII: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.