BCAT2_PONAB
ID BCAT2_PONAB Reviewed; 392 AA.
AC Q5REP0;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 76.
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;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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; CR857482; CAH89767.1; -; mRNA.
DR RefSeq; NP_001124808.1; NM_001131336.1.
DR AlphaFoldDB; Q5REP0; -.
DR SMR; Q5REP0; -.
DR STRING; 9601.ENSPPYP00000011426; -.
DR GeneID; 100171664; -.
DR KEGG; pon:100171664; -.
DR CTD; 587; -.
DR eggNOG; KOG0975; Eukaryota.
DR InParanoid; Q5REP0; -.
DR OrthoDB; 853728at2759; -.
DR Proteomes; UP000001595; Unplaced.
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.
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 2: Evidence at transcript 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..392
FT /note="Branched-chain-amino-acid aminotransferase,
FT mitochondrial"
FT /id="PRO_0000281867"
FT BINDING 168
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O15382"
FT MOD_RES 229
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:O15382"
FT MOD_RES 321
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O15382"
SQ SEQUENCE 392 AA; 44221 MW; 173C84A7D9052431 CRC64;
MAAAALGQIW ARKFLSVPWL LCGPRRYASS SFKAADLQLE MTQKPHKKPG PGEPLVFGKT
FTDHMLMVEW SDKGWGQPRI QPFQNLTLHP ASSSLHYSLQ LFEGMKAFKG KDQQVRLFRP
WLNMDRMLRS AMRLCLPSFD KLELLECIRR LIEVDKDWVP DAAGTSLYVR PVLIGNEPSL
GVSQPTRALL FVILCPVGTY FPGGSVTPVS LLADPAFIRA WVGGVGNYKL GGNYGPTVLV
QQEALKQGCE QVLWLYGPDH QLTEVGTMNI FVYWTHEDGV LELVTPPLNG VILPGVVRQS
LLDLAQTWGE FRVVERTITT KQLLQALEEG RVREVFGSGT ACQVCPVHRI LYKDRNLHIP
TMENGPELIL RFQKELKEIQ YGIRAHEWMF PV
