BCAT2_PIG
ID BCAT2_PIG Reviewed; 31 AA.
AC O19098;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 25-MAY-2022, entry version 100.
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; Fragment;
GN Name=BCAT2;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
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).
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; U68527; AAB67675.1; -; mRNA.
DR AlphaFoldDB; O19098; -.
DR STRING; 9823.ENSSSCP00000003396; -.
DR PaxDb; O19098; -.
DR eggNOG; KOG0975; Eukaryota.
DR HOGENOM; CLU_031922_0_3_1; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR Genevisible; O19098; SS.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
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; IEA:UniProtKB-KW.
DR GO; GO:0008652; P:cellular amino acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
PE 2: Evidence at transcript level;
KW 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..>31
FT /note="Branched-chain-amino-acid aminotransferase,
FT mitochondrial"
FT /id="PRO_0000001273"
FT NON_TER 31
SQ SEQUENCE 31 AA; 3517 MW; B4A8BA604E4328BF CRC64;
MAAAALRQIW ARKFLPVPWL LCGPRRYASS S
