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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: -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

Miscellaneous

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

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

Keywordsi

Molecular functionAminotransferase, Transferase
Biological processAmino-acid biosynthesis, Branched-chain amino acid biosynthesis
LigandPyridoxal phosphate

Enzyme and pathway databases

BioCyciMetaCyc:YHR208W-MONOMER
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

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 16MitochondrionSequence analysisAdd BLAST16
ChainiPRO_000000128117 – 393Branched-chain-amino-acid aminotransferase, mitochondrialAdd BLAST377

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei219N6-(pyridoxal phosphate)lysineBy similarity1
Modified residuei315PhosphothreonineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP38891
PaxDbiP38891
PRIDEiP38891

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
BAT2P471763EBI-3455,EBI-3462

Protein-protein interaction databases

BioGridi36642, 108 interactors
DIPiDIP-6475N
IntActiP38891, 8 interactors
STRINGi4932.YHR208W

Structurei

3D structure databases

ProteinModelPortaliP38891
SMRiP38891
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

GeneTreeiENSGT00390000009532
HOGENOMiHOG000276704
InParanoidiP38891
KOiK00826
OMAiNFFGITH
OrthoDBiEOG092C2KT2

Family and domain databases

CDDicd01557 BCAT_beta_family, 1 hit
InterProiView protein in InterPro
IPR001544 Aminotrans_IV
IPR018300 Aminotrans_IV_CS
IPR036038 Aminotransferase-like
IPR005786 B_amino_transII
IPR033939 BCAT_family
PfamiView protein in Pfam
PF01063 Aminotran_4, 1 hit
PIRSFiPIRSF006468 BCAT1, 1 hit
SUPFAMiSSF56752 SSF56752, 1 hit
TIGRFAMsiTIGR01123 ilvE_II, 1 hit
PROSITEiView protein in PROSITE
PS00770 AA_TRANSFER_CLASS_4, 1 hit

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

Similar proteinsi

Entry informationi

Entry nameiBCA1_YEAST
AccessioniPrimary (citable) accession number: P38891
Secondary accession number(s): D3DLF7
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: May 23, 2018
This is version 164 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

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