BCA2_YEAST
ID BCA2_YEAST Reviewed; 376 AA.
AC P47176; D6VWW6; Q07124;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 187.
DE RecName: Full=Branched-chain-amino-acid aminotransferase, cytosolic;
DE Short=BCAT;
DE EC=2.6.1.42;
DE AltName: Full=Protein TWT2;
GN Name=BAT2; Synonyms=TWT2; OrderedLocusNames=YJR148W; ORFNames=J2209;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND CHARACTERIZATION.
RX PubMed=8798704; DOI=10.1074/jbc.271.40.24458;
RA Kispal G., Steiner H., Court D.A., Rolinski B., Lill R.;
RT "Mitochondrial and cytosolic branched-chain amino acid transaminases from
RT yeast, homologs of the myc oncogene-regulated Eca39 protein.";
RL J. Biol. Chem. 271:24458-24464(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL EMBO J. 15:2031-2049(1996).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP CHARACTERIZATION.
RX PubMed=8702755; DOI=10.1074/jbc.271.34.20242;
RA Eden A., Simchen G., Benvenisty N.;
RT "Two yeast homologs of ECA39, a target for c-Myc regulation, code for
RT cytosolic and mitochondrial branched-chain amino acid aminotransferases.";
RL J. Biol. Chem. 271:20242-20245(1996).
RN [5]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [6]
RP FUNCTION.
RX PubMed=18625006; DOI=10.1111/j.1742-4658.2008.06552.x;
RA Pirkov I., Norbeck J., Gustafsson L., Albers E.;
RT "A complete inventory of all enzymes in the eukaryotic methionine salvage
RT pathway.";
RL FEBS J. 275:4111-4120(2008).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND INDUCTION.
RX PubMed=21267457; DOI=10.1371/journal.pone.0016099;
RA Colon M., Hernandez F., Lopez K., Quezada H., Gonzalez J., Lopez G.,
RA Aranda C., Gonzalez A.;
RT "Saccharomyces cerevisiae Bat1 and Bat2 aminotransferases have functionally
RT diverged from the ancestral-like Kluyveromyces lactis orthologous enzyme.";
RL PLoS ONE 6:E16099-E16099(2011).
CC -!- FUNCTION: Catalyzes the first reaction in the catabolism of the
CC essential branched chain amino acids leucine, isoleucine, and valine.
CC Catalyzes the formation of methionine from 2-keto-4-methylthiobutyrate
CC (KMTB) in the methionine salvage pathway primarily using branched chain
CC amino acids (leucine, isoleucine, and valine) as well as lysine and
CC proline as the amino donors. Involved in cell cycle regulation.
CC {ECO:0000269|PubMed:18625006, ECO:0000269|PubMed:21267457}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + L-leucine = 4-methyl-2-oxopentanoate + L-
CC glutamate; Xref=Rhea:RHEA:18321, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:17865, ChEBI:CHEBI:29985, ChEBI:CHEBI:57427; EC=2.6.1.42;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + L-isoleucine = (S)-3-methyl-2-oxopentanoate +
CC L-glutamate; Xref=Rhea:RHEA:24801, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:35146, ChEBI:CHEBI:58045; EC=2.6.1.42;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + L-valine = 3-methyl-2-oxobutanoate + L-
CC glutamate; Xref=Rhea:RHEA:24813, ChEBI:CHEBI:11851,
CC ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:57762; EC=2.6.1.42;
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-
CC isoleucine from 2-oxobutanoate: step 4/4.
CC -!- PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine
CC from 3-methyl-2-oxobutanoate: step 4/4.
CC -!- PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine from
CC pyruvate: step 4/4.
CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via salvage
CC pathway; L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate:
CC step 6/6.
CC -!- INTERACTION:
CC P47176; P38891: BAT1; NbExp=3; IntAct=EBI-3462, EBI-3455;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21267457}.
CC -!- DEVELOPMENTAL STAGE: Highly expressed during stationary phase, down-
CC regulated during logarithmic phase of growth.
CC -!- INDUCTION: Down-regulated in the presence of repressive nitrogen
CC sources (glutamine) and derepressed in secondary non-repressive
CC nitrogen sources such as GABA. Highly expressed on cultures with
CC isoleucine, leucine and valine as sole nitrogen source (catabolic
CC conditions). {ECO:0000269|PubMed:21267457}.
CC -!- MISCELLANEOUS: Present with 25900 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the class-IV pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA60376.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAA60376.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; X86568; CAA60376.1; ALT_SEQ; mRNA.
DR EMBL; Z49648; CAA89681.1; -; Genomic_DNA.
DR EMBL; BK006943; DAA08932.1; -; Genomic_DNA.
DR PIR; S57177; S57177.
DR RefSeq; NP_012682.1; NM_001181806.1.
DR AlphaFoldDB; P47176; -.
DR SMR; P47176; -.
DR BioGRID; 33903; 161.
DR DIP; DIP-2151N; -.
DR IntAct; P47176; 8.
DR MINT; P47176; -.
DR STRING; 4932.YJR148W; -.
DR iPTMnet; P47176; -.
DR MaxQB; P47176; -.
DR PaxDb; P47176; -.
DR PRIDE; P47176; -.
DR EnsemblFungi; YJR148W_mRNA; YJR148W; YJR148W.
DR GeneID; 853613; -.
DR KEGG; sce:YJR148W; -.
DR SGD; S000003909; BAT2.
DR VEuPathDB; FungiDB:YJR148W; -.
DR eggNOG; KOG0975; Eukaryota.
DR GeneTree; ENSGT00390000009532; -.
DR HOGENOM; CLU_031922_0_2_1; -.
DR InParanoid; P47176; -.
DR OMA; PVGSYYK; -.
DR BioCyc; YEAST:YJR148W-MON; -.
DR BRENDA; 2.6.1.42; 984.
DR Reactome; R-SCE-70895; Branched-chain amino acid catabolism.
DR UniPathway; UPA00047; UER00058.
DR UniPathway; UPA00048; UER00073.
DR UniPathway; UPA00049; UER00062.
DR UniPathway; UPA00904; UER00879.
DR PRO; PR:P47176; -.
DR Proteomes; UP000002311; Chromosome X.
DR RNAct; P47176; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0004084; F:branched-chain-amino-acid transaminase activity; IDA:SGD.
DR GO; GO:0052656; F:L-isoleucine transaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0052654; F:L-leucine transaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0050048; F:L-leucine:2-oxoglutarate aminotransferase activity; IEA:RHEA.
DR GO; GO:0052655; F:L-valine transaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0009082; P:branched-chain amino acid biosynthetic process; IDA:SGD.
DR GO; GO:0009083; P:branched-chain amino acid catabolic process; IMP:SGD.
DR GO; GO:0009097; P:isoleucine biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0019509; P:L-methionine salvage from methylthioadenosine; IEA:UniProtKB-UniPathway.
DR GO; GO:0009098; P:leucine biosynthetic process; IBA:GO_Central.
DR GO; GO:0009099; P:valine biosynthetic process; IBA:GO_Central.
DR CDD; cd01557; BCAT_beta_family; 1.
DR Gene3D; 3.20.10.10; -; 1.
DR Gene3D; 3.30.470.10; -; 1.
DR InterPro; IPR001544; Aminotrans_IV.
DR InterPro; IPR018300; Aminotrans_IV_CS.
DR InterPro; IPR036038; Aminotransferase-like.
DR InterPro; IPR005786; B_amino_transII.
DR InterPro; IPR043132; BCAT-like_C.
DR InterPro; IPR043131; BCAT-like_N.
DR InterPro; IPR033939; BCAT_family.
DR PANTHER; PTHR11825; PTHR11825; 1.
DR Pfam; PF01063; Aminotran_4; 1.
DR PIRSF; PIRSF006468; BCAT1; 1.
DR SUPFAM; SSF56752; SSF56752; 1.
DR TIGRFAMs; TIGR01123; ilvE_II; 1.
DR PROSITE; PS00770; AA_TRANSFER_CLASS_4; 1.
PE 1: Evidence at protein level;
KW Amino-acid biosynthesis; Aminotransferase;
KW Branched-chain amino acid biosynthesis; Cytoplasm; Pyridoxal phosphate;
KW Reference proteome; Transferase.
FT CHAIN 1..376
FT /note="Branched-chain-amino-acid aminotransferase,
FT cytosolic"
FT /id="PRO_0000103302"
FT MOD_RES 202
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
FT CONFLICT 148..149
FT /note="IG -> MA (in Ref. 1; CAA60376)"
FT /evidence="ECO:0000305"
FT CONFLICT 194..195
FT /note="WP -> CA (in Ref. 1; CAA60376)"
FT /evidence="ECO:0000305"
FT CONFLICT 224
FT /note="Q -> E (in Ref. 1; CAA60376)"
FT /evidence="ECO:0000305"
FT CONFLICT 313
FT /note="F -> K (in Ref. 1; CAA60376)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 376 AA; 41625 MW; 12B1BF6D58DFDE6B CRC64;
MTLAPLDASK VKITTTQHAS KPKPNSELVF GKSFTDHMLT AEWTAEKGWG TPEIKPYQNL
SLDPSAVVFH YAFELFEGMK AYRTVDNKIT MFRPDMNMKR MNKSAQRICL PTFDPEELIT
LIGKLIQQDK CLVPEGKGYS LYIRPTLIGT TAGLGVSTPD RALLYVICCP VGPYYKTGFK
AVRLEATDYA TRAWPGGCGD KKLGANYAPC VLPQLQAASR GYQQNLWLFG PNNNITEVGT
MNAFFVFKDS KTGKKELVTA PLDGTILEGV TRDSILNLAK ERLEPSEWTI SERYFTIGEV
TERSKNGELL EAFGSGTAAI VSPIKEIGWK GEQINIPLLP GEQTGPLAKE VAQWINGIQY
GETEHGNWSR VVTDLN
