BCAT2_RAT
ID BCAT2_RAT Reviewed; 393 AA.
AC O35854;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Branched-chain-amino-acid aminotransferase, mitochondrial;
DE Short=BCAT(m);
DE EC=2.6.1.42 {ECO:0000269|PubMed:9165094};
DE Flags: Precursor;
GN Name=Bcat2; Synonyms=Bcatm, Eca40;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, CATALYTIC
RP ACTIVITY, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC STRAIN=Sprague-Dawley; TISSUE=Heart;
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 [2]
RP FUNCTION.
RX PubMed=8428987; DOI=10.1016/s0021-9258(18)53662-0;
RA Hutson S.M., Hall T.R.;
RT "Identification of the mitochondrial branched chain aminotransferase as a
RT branched chain alpha-keto acid transport protein.";
RL J. Biol. Chem. 268:3084-3091(1993).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Catalyzes the first reaction in the catabolism of the
CC essential branched chain amino acids leucine, isoleucine, and valine
CC (PubMed:9165094). May also function as a transporter of branched chain
CC alpha-keto acids (PubMed:8428987). {ECO:0000269|PubMed:8428987,
CC ECO:0000269|PubMed:9165094}.
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:0000269|PubMed:9165094};
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:0000269|PubMed:9165094};
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:0000269|PubMed:9165094};
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:0000269|PubMed:9165094}.
CC -!- TISSUE SPECIFICITY: Expressed in all tissues.
CC {ECO:0000269|PubMed:9165094}.
CC -!- SIMILARITY: Belongs to the class-IV pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
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DR EMBL; U68417; AAB67673.1; -; mRNA.
DR RefSeq; NP_071795.1; NM_022400.1.
DR AlphaFoldDB; O35854; -.
DR SMR; O35854; -.
DR IntAct; O35854; 1.
DR STRING; 10116.ENSRNOP00000028474; -.
DR BindingDB; O35854; -.
DR ChEMBL; CHEMBL3319; -.
DR iPTMnet; O35854; -.
DR PhosphoSitePlus; O35854; -.
DR jPOST; O35854; -.
DR PaxDb; O35854; -.
DR PRIDE; O35854; -.
DR GeneID; 64203; -.
DR KEGG; rno:64203; -.
DR UCSC; RGD:68948; rat.
DR CTD; 587; -.
DR RGD; 68948; Bcat2.
DR eggNOG; KOG0975; Eukaryota.
DR InParanoid; O35854; -.
DR OrthoDB; 853728at2759; -.
DR PhylomeDB; O35854; -.
DR Reactome; R-RNO-70895; Branched-chain amino acid catabolism.
DR SABIO-RK; O35854; -.
DR PRO; PR:O35854; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005739; C:mitochondrion; IDA:RGD.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0004084; F:branched-chain-amino-acid transaminase activity; IDA:RGD.
DR GO; GO:0052656; F:L-isoleucine transaminase activity; ISO:RGD.
DR GO; GO:0052654; F:L-leucine transaminase activity; ISO:RGD.
DR GO; GO:0050048; F:L-leucine:2-oxoglutarate aminotransferase activity; IEA:RHEA.
DR GO; GO:0052655; F:L-valine transaminase activity; ISO:RGD.
DR GO; GO:0009083; P:branched-chain amino acid catabolic process; IDA:RGD.
DR GO; GO:0009081; P:branched-chain amino acid metabolic process; ISO:RGD.
DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; ISO:RGD.
DR GO; GO:0006550; P:isoleucine catabolic process; IDA:RGD.
DR GO; GO:0006549; P:isoleucine metabolic process; ISO:RGD.
DR GO; GO:0007595; P:lactation; IEP:RGD.
DR GO; GO:0009098; P:leucine biosynthetic process; IDA:RGD.
DR GO; GO:0006551; P:leucine metabolic process; ISO:RGD.
DR GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0010817; P:regulation of hormone levels; ISO:RGD.
DR GO; GO:0009099; P:valine biosynthetic process; IBA:GO_Central.
DR GO; GO:0006573; P:valine metabolic process; ISO:RGD.
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; Direct protein sequencing;
KW Lipid metabolism; Mitochondrion; Pyridoxal phosphate; Reference proteome;
KW Transferase; Transit peptide.
FT TRANSIT 1..27
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:9165094"
FT CHAIN 28..393
FT /note="Branched-chain-amino-acid aminotransferase,
FT mitochondrial"
FT /id="PRO_0000001274"
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"
SQ SEQUENCE 393 AA; 44276 MW; ECB3704ED49A6C12 CRC64;
MSAAILGQVW TRKLLPIPWR LCVPGRCVSS NFKAADLQVQ VTREPQKKPA PSQPLLFGKT
FTDHMLMVEW NSKTGWGPPR IQPFQNLTLH PACSGLHYSL QLFEGLKAYK GRDKQVRLFR
PWLNMDRMLR SARRLCLPDF DKQELLECIR QLIEVDKDWV PDGNGTSLYV RPVLIGNEPS
LGVGMVTQAL LFVILCPVGS YFPGDSMTPV SLLADPSFVR AWIGGVGDCK LGGNYGPTVA
VQQEAQKKGC EQVLWLYGPD HQLTEVGTMN IFVYWTHEDG ELELATPPLD GIILPGVVRQ
SLLDLARTWG EFRVAERKVT MKELKRALEE GRVREVFGSG TACQVCPVHQ ILYEGKQLHI
PTMENGPELI LRFQKELKAI QYGTSAHDWM LRV
