BCAT2_MOUSE
ID BCAT2_MOUSE Reviewed; 393 AA.
AC O35855; Q8VD03;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 2.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Branched-chain-amino-acid aminotransferase, mitochondrial;
DE Short=BCAT(m);
DE EC=2.6.1.42 {ECO:0000250|UniProtKB:O15382};
DE Flags: Precursor;
GN Name=Bcat2; Synonyms=Bcatm, Eca40;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Kidney, and Salivary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-275.
RX PubMed=9165094; DOI=10.1016/s0167-4838(97)00044-7;
RA Bledsoe R.K., Dawson P.A., Hutson S.M.;
RT "Cloning of the rat and human mitochondrial branched chain
RT aminotransferases (BCATm).";
RL Biochim. Biophys. Acta 1339:9-13(1997).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Pancreas, Spleen,
RC and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Catalyzes the first reaction in the catabolism of the
CC essential branched chain amino acids leucine, isoleucine, and valine
CC (By similarity). May also function as a transporter of branched chain
CC alpha-keto acids (By similarity). {ECO:0000250|UniProtKB:O15382,
CC ECO:0000250|UniProtKB:O35854}.
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 Evidence={ECO:0000250|UniProtKB:O15382};
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 Evidence={ECO:0000250|UniProtKB:O15382};
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 Evidence={ECO:0000250|UniProtKB:O15382};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250|UniProtKB:O15382};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:O15382}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:O35854}.
CC -!- SIMILARITY: Belongs to the class-IV pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
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DR EMBL; BC017688; AAH17688.1; -; mRNA.
DR EMBL; BC048072; AAH48072.1; -; mRNA.
DR EMBL; U68526; AAB67674.1; -; mRNA.
DR CCDS; CCDS21252.1; -.
DR RefSeq; NP_033867.1; NM_009737.3.
DR AlphaFoldDB; O35855; -.
DR SMR; O35855; -.
DR STRING; 10090.ENSMUSP00000033098; -.
DR iPTMnet; O35855; -.
DR PhosphoSitePlus; O35855; -.
DR SwissPalm; O35855; -.
DR REPRODUCTION-2DPAGE; O35855; -.
DR EPD; O35855; -.
DR jPOST; O35855; -.
DR PaxDb; O35855; -.
DR PeptideAtlas; O35855; -.
DR PRIDE; O35855; -.
DR ProteomicsDB; 273476; -.
DR Antibodypedia; 31810; 273 antibodies from 31 providers.
DR DNASU; 12036; -.
DR Ensembl; ENSMUST00000033098; ENSMUSP00000033098; ENSMUSG00000030826.
DR GeneID; 12036; -.
DR KEGG; mmu:12036; -.
DR UCSC; uc009gwc.2; mouse.
DR CTD; 587; -.
DR MGI; MGI:1276534; Bcat2.
DR VEuPathDB; HostDB:ENSMUSG00000030826; -.
DR eggNOG; KOG0975; Eukaryota.
DR GeneTree; ENSGT00390000009532; -.
DR InParanoid; O35855; -.
DR OMA; GTAWFIT; -.
DR OrthoDB; 853728at2759; -.
DR PhylomeDB; O35855; -.
DR TreeFam; TF300882; -.
DR BRENDA; 2.6.1.42; 3474.
DR Reactome; R-MMU-70895; Branched-chain amino acid catabolism.
DR BioGRID-ORCS; 12036; 1 hit in 74 CRISPR screens.
DR ChiTaRS; Bcat2; mouse.
DR PRO; PR:O35855; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; O35855; protein.
DR Bgee; ENSMUSG00000030826; Expressed in hindlimb stylopod muscle and 199 other tissues.
DR ExpressionAtlas; O35855; baseline and differential.
DR Genevisible; O35855; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0004084; F:branched-chain-amino-acid transaminase activity; IDA:MGI.
DR GO; GO:0052656; F:L-isoleucine transaminase activity; ISO:MGI.
DR GO; GO:0052654; F:L-leucine transaminase activity; ISO:MGI.
DR GO; GO:0050048; F:L-leucine:2-oxoglutarate aminotransferase activity; IEA:RHEA.
DR GO; GO:0052655; F:L-valine transaminase activity; ISO:MGI.
DR GO; GO:0009083; P:branched-chain amino acid catabolic process; IMP:MGI.
DR GO; GO:0009081; P:branched-chain amino acid metabolic process; IMP:MGI.
DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEP:MGI.
DR GO; GO:0006550; P:isoleucine catabolic process; IMP:MGI.
DR GO; GO:0006549; P:isoleucine metabolic process; IMP:MGI.
DR GO; GO:0009098; P:leucine biosynthetic process; ISO:MGI.
DR GO; GO:0006551; P:leucine metabolic process; IMP:MGI.
DR GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0010817; P:regulation of hormone levels; IMP:MGI.
DR GO; GO:0009099; P:valine biosynthetic process; IBA:GO_Central.
DR GO; GO:0006573; P:valine metabolic process; IMP:MGI.
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 Acetylation; Amino-acid biosynthesis; Aminotransferase;
KW Branched-chain amino acid biosynthesis; Lipid metabolism; Mitochondrion;
KW Pyridoxal phosphate; Reference proteome; Transferase; Transit peptide.
FT TRANSIT 1..27
FT /note="Mitochondrion"
FT /evidence="ECO:0000250|UniProtKB:O35854"
FT CHAIN 28..393
FT /note="Branched-chain-amino-acid aminotransferase,
FT mitochondrial"
FT /id="PRO_0000001272"
FT BINDING 169
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O15382"
FT MOD_RES 230
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:O15382"
FT MOD_RES 322
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O15382"
FT CONFLICT 199
FT /note="G -> A (in Ref. 2; AAB67674)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 393 AA; 44127 MW; 7D2ACF7C743B1978 CRC64;
MAAATLGQVW ARKLLPVPWL LCGSKRCVSS IFKAADLQIQ MTKEPQKKPA PSQALLFGKT
FTDHMLMVEW NNKAGWGPPR IQPFQNLTLH PACSGLHYSL QLFEGLKAYK GGDQQVRLFR
PWLNMDRMLR SARRLCLPDF DKQELLECIR QLIEVDKDWV PDGNGTSLYV RPVLIGNEPS
LGVGMVTQAL LYVILCPVGS YFPGDSMTPV SLLADPSFVR AWIGGVGDCK LGGNYGPTVA
VQREAQKRGC EQVLWLYGPD HQLTEVGTMN IFVYWTHEDG VLELVTPPLN GVILPGVVRQ
SLLDLARTWG EFRVAERKVT MKELKRALEE GRVREVFGSG TACQVCPVHQ ILYEGKQLHI
PTMENGPELI LRFQKELKAI QYGASAHDWM FRV
