BCA1_YEAST
ID BCA1_YEAST Reviewed; 393 AA.
AC P38891; D3DLF7;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 187.
DE RecName: Full=Branched-chain-amino-acid aminotransferase, mitochondrial;
DE Short=BCAT;
DE EC=2.6.1.42;
DE AltName: Full=Protein ECA39;
DE AltName: Full=Protein TWT1;
DE Flags: Precursor;
GN Name=BAT1; Synonyms=ECA39, TWT1; OrderedLocusNames=YHR208W;
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 [GENOMIC DNA], 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=8091229; DOI=10.1126/science.8091229;
RA Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z.,
RA Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T.,
RA Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P., Louis E.J.,
RA Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L.,
RA St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P.,
RA Waterston R., Wilson R., Vaudin M.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
RT VIII.";
RL Science 265:2077-2082(1994).
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [5]
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 [6]
RP REGULATION BY GCN4.
RX PubMed=8934531;
RA Ben-Yosef T., Yanuka O., Benvenisty N.;
RT "ECA39 is regulated by c-Myc in human and by a Jun/Fos homolog, GCN4, in
RT yeast.";
RL Oncogene 13:1859-1866(1996).
RN [7]
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 [8]
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-315, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [10]
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: Involved in the biosynthesis of the branched chain amino
CC acids leucine, isoleucine, and valine. Catalyzes the formation of
CC methionine from 2-keto-4-methylthiobutyrate (KMTB) in the methionine
CC salvage pathway primarily using branched chain amino acids (leucine,
CC isoleucine, and valine) as the amino donors. Appears to be involved in
CC the regulation of the transition from G1 to S phase in the cell cycle.
CC High copy suppressor of a temperature-sensitive mutation in the ABC
CC transporter, ATM1. {ECO:0000269|PubMed:18625006,
CC 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 P38891; P47176: BAT2; NbExp=3; IntAct=EBI-3455, EBI-3462;
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000269|PubMed:21267457}.
CC -!- DEVELOPMENTAL STAGE: Highly expressed during logarithmic phase of
CC growth. Down-regulated during the stationary phase.
CC -!- INDUCTION: Mainly expressed on ammonium-glucose exponential cultures
CC (biosynthetic conditions), and repressed in the presence of leucine,
CC isoleucine or valine. {ECO:0000269|PubMed:21267457}.
CC -!- MISCELLANEOUS: Present with 87300 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}.
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DR EMBL; X78961; CAA55556.1; -; Genomic_DNA.
DR EMBL; U00029; AAB69733.1; -; Genomic_DNA.
DR EMBL; AY558111; AAS56437.1; -; Genomic_DNA.
DR EMBL; BK006934; DAA06901.1; -; Genomic_DNA.
DR PIR; S48989; S48989.
DR RefSeq; NP_012078.3; NM_001179339.3.
DR AlphaFoldDB; P38891; -.
DR SMR; P38891; -.
DR BioGRID; 36642; 112.
DR DIP; DIP-6475N; -.
DR IntAct; P38891; 8.
DR STRING; 4932.YHR208W; -.
DR iPTMnet; P38891; -.
DR MaxQB; P38891; -.
DR PaxDb; P38891; -.
DR PRIDE; P38891; -.
DR EnsemblFungi; YHR208W_mRNA; YHR208W; YHR208W.
DR GeneID; 856615; -.
DR KEGG; sce:YHR208W; -.
DR SGD; S000001251; BAT1.
DR VEuPathDB; FungiDB:YHR208W; -.
DR eggNOG; KOG0975; Eukaryota.
DR GeneTree; ENSGT00390000009532; -.
DR HOGENOM; CLU_031922_0_1_1; -.
DR InParanoid; P38891; -.
DR OMA; LTEVFAC; -.
DR BioCyc; MetaCyc:YHR208W-MON; -.
DR BioCyc; YEAST:YHR208W-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:P38891; -.
DR Proteomes; UP000002311; Chromosome VIII.
DR RNAct; P38891; protein.
DR GO; GO:0005759; C:mitochondrial matrix; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; 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; Mitochondrion; Phosphoprotein;
KW Pyridoxal phosphate; Reference proteome; Transferase; Transit peptide.
FT TRANSIT 1..16
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 17..393
FT /note="Branched-chain-amino-acid aminotransferase,
FT mitochondrial"
FT /id="PRO_0000001281"
FT MOD_RES 219
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
FT MOD_RES 315
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18407956"
SQ SEQUENCE 393 AA; 43596 MW; E76604F326A7C674 CRC64;
MLQRHSLKLG KFSIRTLATG APLDASKLKI TRNPNPSKPR PNEELVFGQT FTDHMLTIPW
SAKEGWGTPH IKPYGNLSLD PSACVFHYAF ELFEGLKAYR TPQNTITMFR PDKNMARMNK
SAARICLPTF ESEELIKLTG KLIEQDKHLV PQGNGYSLYI RPTMIGTSKG LGVGTPSEAL
LYVITSPVGP YYKTGFKAVR LEATDYATRA WPGGVGDKKL GANYAPCILP QLQAAKRGYQ
QNLWLFGPEK NITEVGTMNV FFVFLNKVTG KKELVTAPLD GTILEGVTRD SVLTLARDKL
DPQEWDINER YYTITEVATR AKQGELLEAF GSGTAAVVSP IKEIGWNNED IHVPLLPGEQ
CGALTKQVAQ WIADIQYGRV NYGNWSKTVA DLN
