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Protein

Branched-chain-amino-acid aminotransferase, cytosolic

Gene

BAT2

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

Functioni

Catalyzes the first reaction in the catabolism of the essential 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 well as lysine and proline as the amino donors. Involved in cell cycle regulation.2 Publications

Miscellaneous

Present with 25900 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

BioCyciYEAST:YJR148W-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, cytosolic (EC:2.6.1.42)
Short name:
BCAT
Alternative name(s):
Protein TWT2
Gene namesi
Name:BAT2
Synonyms:TWT2
Ordered Locus Names:YJR148W
ORF Names:J2209
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome X

Organism-specific databases

EuPathDBiFungiDB:YJR148W
SGDiS000003909 BAT2

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

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001033021 – 376Branched-chain-amino-acid aminotransferase, cytosolicAdd BLAST376

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei202N6-(pyridoxal phosphate)lysineBy similarity1

Proteomic databases

MaxQBiP47176
PaxDbiP47176
PRIDEiP47176

PTM databases

iPTMnetiP47176

Expressioni

Developmental stagei

Highly expressed during stationary phase, down-regulated during logarithmic phase of growth.

Inductioni

Down-regulated in the presence of repressive nitrogen sources (glutamine) and derepressed in secondary non-repressive nitrogen sources such as GABA. Highly expressed on cultures with isoleucine, leucine and valine as sole nitrogen source (catabolic conditions).1 Publication

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
BAT1P388913EBI-3462,EBI-3455

Protein-protein interaction databases

BioGridi33903, 152 interactors
DIPiDIP-2151N
IntActiP47176, 8 interactors
MINTiP47176
STRINGi4932.YJR148W

Structurei

3D structure databases

ProteinModelPortaliP47176
SMRiP47176
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

GeneTreeiENSGT00390000009532
HOGENOMiHOG000276704
InParanoidiP47176
KOiK00826
OMAiQTAYANK
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.

P47176-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTLAPLDASK VKITTTQHAS KPKPNSELVF GKSFTDHMLT AEWTAEKGWG
60 70 80 90 100
TPEIKPYQNL SLDPSAVVFH YAFELFEGMK AYRTVDNKIT MFRPDMNMKR
110 120 130 140 150
MNKSAQRICL PTFDPEELIT LIGKLIQQDK CLVPEGKGYS LYIRPTLIGT
160 170 180 190 200
TAGLGVSTPD RALLYVICCP VGPYYKTGFK AVRLEATDYA TRAWPGGCGD
210 220 230 240 250
KKLGANYAPC VLPQLQAASR GYQQNLWLFG PNNNITEVGT MNAFFVFKDS
260 270 280 290 300
KTGKKELVTA PLDGTILEGV TRDSILNLAK ERLEPSEWTI SERYFTIGEV
310 320 330 340 350
TERSKNGELL EAFGSGTAAI VSPIKEIGWK GEQINIPLLP GEQTGPLAKE
360 370
VAQWINGIQY GETEHGNWSR VVTDLN
Length:376
Mass (Da):41,625
Last modified:February 1, 1996 - v1
Checksum:i12B1BF6D58DFDE6B
GO

Sequence cautioni

The sequence CAA60376 differs from that shown. Reason: Frameshift at positions 1, 170, 199, 207, 210 and 214.Curated
The sequence CAA60376 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti148 – 149IG → MA in CAA60376 (PubMed:8798704).Curated2
Sequence conflicti194 – 195WP → CA in CAA60376 (PubMed:8798704).Curated2
Sequence conflicti224Q → E in CAA60376 (PubMed:8798704).Curated1
Sequence conflicti313F → K in CAA60376 (PubMed:8798704).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X86568 mRNA Translation: CAA60376.1 Sequence problems.
Z49648 Genomic DNA Translation: CAA89681.1
BK006943 Genomic DNA Translation: DAA08932.1
PIRiS57177
RefSeqiNP_012682.1, NM_001181806.1

Genome annotation databases

EnsemblFungiiYJR148W; YJR148W; YJR148W
GeneIDi853613
KEGGisce:YJR148W

Similar proteinsi

Entry informationi

Entry nameiBCA2_YEAST
AccessioniPrimary (citable) accession number: P47176
Secondary accession number(s): D6VWW6, Q07124
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: May 23, 2018
This is version 162 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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