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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: Annotation score: 5 out of 5-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

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

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

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

GO - Cellular componenti

  • cytoplasm Source: SGD
  • mitochondrion Source: GO_Central
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 376376Branched-chain-amino-acid aminotransferase, cytosolicPRO_0000103302Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei202 – 2021N6-(pyridoxal phosphate)lysineBy similarity

Proteomic databases

MaxQBiP47176.

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

Protein-protein interaction databases

BioGridi33903. 31 interactions.
DIPiDIP-2151N.
IntActiP47176. 8 interactions.
MINTiMINT-527696.

Structurei

3D structure databases

ProteinModelPortaliP47176.
SMRiP47176. Positions 21-372.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

GeneTreeiENSGT00390000009532.
HOGENOMiHOG000276704.
InParanoidiP47176.
KOiK00826.
OMAiSGTACMI.
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.

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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti148 – 1492IG → MA in CAA60376 (PubMed:8798704).Curated
Sequence conflicti194 – 1952WP → CA in CAA60376 (PubMed:8798704).Curated
Sequence conflicti224 – 2241Q → E in CAA60376 (PubMed:8798704).Curated
Sequence conflicti313 – 3131F → K in CAA60376 (PubMed:8798704).Curated

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.

Cross-referencesi

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.

3D structure databases

ProteinModelPortaliP47176.
SMRiP47176. Positions 21-372.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi33903. 31 interactions.
DIPiDIP-2151N.
IntActiP47176. 8 interactions.
MINTiMINT-527696.

PTM databases

iPTMnetiP47176.

Proteomic databases

MaxQBiP47176.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYJR148W; YJR148W; YJR148W.
GeneIDi853613.
KEGGisce:YJR148W.

Organism-specific databases

EuPathDBiFungiDB:YJR148W.
SGDiS000003909. BAT2.

Phylogenomic databases

GeneTreeiENSGT00390000009532.
HOGENOMiHOG000276704.
InParanoidiP47176.
KOiK00826.
OMAiSGTACMI.
OrthoDBiEOG769ZVJ.

Enzyme and pathway databases

UniPathwayiUPA00047; UER00058.
UPA00048; UER00073.
UPA00049; UER00062.
UPA00904; UER00879.
BioCyciYEAST:YJR148W-MONOMER.
BRENDAi2.6.1.42. 984.
ReactomeiR-SCE-70895. Branched-chain amino acid catabolism.

Miscellaneous databases

PROiP47176.

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 [MRNA], CHARACTERIZATION.
  2. "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X."
    Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C., Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D., Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J., Heumann K.
    , Hilger F., Hollenberg C.P., Huang M.-E., Jacq C., Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E., Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T., Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R., Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N., To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H., von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.
    EMBO J. 15:2031-2049(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. "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.
  5. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  6. "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.
  7. "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 nameiBCA2_YEAST
AccessioniPrimary (citable) accession number: P47176
Secondary accession number(s): D6VWW6, Q07124
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: July 6, 2016
This is version 146 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 25900 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 X
    Yeast (Saccharomyces cerevisiae) chromosome X: 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.