BCAT2_BOVIN
ID BCAT2_BOVIN Reviewed; 393 AA.
AC Q5EA40; Q0V8P3;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 111.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Testis;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (FEB-2006) 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; BT020729; AAX08746.1; -; mRNA.
DR EMBL; BT021163; AAX31345.1; -; mRNA.
DR EMBL; BT026175; ABG67014.1; -; mRNA.
DR EMBL; BC114055; AAI14056.1; -; mRNA.
DR RefSeq; NP_001013611.2; NM_001013593.2.
DR AlphaFoldDB; Q5EA40; -.
DR SMR; Q5EA40; -.
DR STRING; 9913.ENSBTAP00000031858; -.
DR PaxDb; Q5EA40; -.
DR PRIDE; Q5EA40; -.
DR Ensembl; ENSBTAT00000066914; ENSBTAP00000066987; ENSBTAG00000009172.
DR GeneID; 281643; -.
DR KEGG; bta:281643; -.
DR CTD; 587; -.
DR VEuPathDB; HostDB:ENSBTAG00000009172; -.
DR VGNC; VGNC:26440; BCAT2.
DR eggNOG; KOG0975; Eukaryota.
DR GeneTree; ENSGT00390000009532; -.
DR HOGENOM; CLU_031922_0_3_1; -.
DR InParanoid; Q5EA40; -.
DR OMA; GTAWFIT; -.
DR OrthoDB; 853728at2759; -.
DR TreeFam; TF300882; -.
DR Proteomes; UP000009136; Chromosome 18.
DR Bgee; ENSBTAG00000009172; Expressed in diaphragm and 105 other tissues.
DR ExpressionAtlas; Q5EA40; baseline and differential.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0004084; F:branched-chain-amino-acid transaminase activity; IBA:GO_Central.
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:0009098; P:leucine biosynthetic process; IBA:GO_Central.
DR GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
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 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..393
FT /note="Branched-chain-amino-acid aminotransferase,
FT mitochondrial"
FT /id="PRO_0000236190"
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 288
FT /note="P -> S (in Ref. 1; ABG67014)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 393 AA; 44648 MW; 86809C05C27DABA3 CRC64;
MATAALRQIW IPRFLPVPWF LCGSRRYASS SFKAADLQLE MTQEPHKKPD PSQPLLFGKT
FTDHMLMVEW NQEKGWGQPR IQPFQNLTLH PACSALHYSL QLFEGMKAFK GGDQRVRLFR
PWLNMERMLR SALRLCLPSF DKIELLECIR RLVEVDQDWV PGSMGTSLYV RPVLIGNEPS
LGVGHPTRAL LFVILSPVGA YFPGDALKPV SLLADPSFIR AWVGGVGNYK LGGNYGPTVL
VQQEAQKKGC EQVLWLYGPD HELTEVGTMN IFVFWTYEDG VLELVTPPLD GIILPGIVRQ
SLLDLARTWG EFRVVERKIT MKEFLRALKD GRVREVFGSG TACQVCPVHQ ILYQGKHFHI
PTMENGPQLI LRFHKELKAI QYGSKAHEWM LPV
