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BCAT1_SHEEP
ID   BCAT1_SHEEP             Reviewed;         385 AA.
AC   Q9GKM4;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   25-MAY-2022, entry version 91.
DE   RecName: Full=Branched-chain-amino-acid aminotransferase, cytosolic;
DE            Short=BCAT(c);
DE            EC=2.6.1.42;
GN   Name=BCAT1;
OS   Ovis aries (Sheep).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Caprinae; Ovis.
OX   NCBI_TaxID=9940;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND 3D-STRUCTURE MODELING.
RC   TISSUE=Brain;
RX   PubMed=11072075; DOI=10.1016/s0167-4781(00)00227-x;
RA   Bonfils J., Faure M., Gibrat J.-F., Glomot F., Papet I.;
RT   "Sheep cytosolic branched-chain amino acid aminotransferase: cDNA cloning,
RT   primary structure and molecular modelling and its unique expression in
RT   muscles.";
RL   Biochim. Biophys. Acta 1494:129-136(2000).
CC   -!- FUNCTION: Catalyzes the first reaction in the catabolism of the
CC       essential branched chain amino acids leucine, isoleucine, and valine.
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   -!- 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   -!- 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   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- TISSUE SPECIFICITY: Expressed in muscles.
CC       {ECO:0000269|PubMed:11072075}.
CC   -!- SIMILARITY: Belongs to the class-IV pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000305}.
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DR   EMBL; AF184916; AAG16994.1; -; mRNA.
DR   RefSeq; NP_001009444.1; NM_001009444.1.
DR   AlphaFoldDB; Q9GKM4; -.
DR   SMR; Q9GKM4; -.
DR   STRING; 9940.ENSOARP00000021583; -.
DR   GeneID; 443485; -.
DR   KEGG; oas:443485; -.
DR   CTD; 586; -.
DR   eggNOG; KOG0975; Eukaryota.
DR   OrthoDB; 853728at2759; -.
DR   BRENDA; 2.6.1.42; 2668.
DR   Proteomes; UP000002356; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; 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   Amino-acid biosynthesis; Aminotransferase;
KW   Branched-chain amino acid biosynthesis; Cytoplasm; Lipid metabolism;
KW   Pyridoxal phosphate; Reference proteome; Transferase.
FT   CHAIN           1..385
FT                   /note="Branched-chain-amino-acid aminotransferase,
FT                   cytosolic"
FT                   /id="PRO_0000103295"
FT   MOD_RES         221
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   385 AA;  43073 MW;  BF245858BBE684D2 CRC64;
     MDCNNGCSAE GTGEGGSKEP VETFKAEDLI ITRATILKEK PDPSTLVFGT VFTDHMLTVE
     WSLELGWEKP RIKPLQNLSL HPGSSALHYA VELFEGLKAF RGVDNKIRLF RPNLNMDRMY
     RSAMRATLPA FDKKELLECI QQLVKLDEEW VPYSTSASLY IRPTFIGTEP SLGVKKPTKA
     LLFVILSPVG PYFSSGSFNP VSLWANPKYV RAWKGGTGDC KMGGNYGSSL FAQCEAVENA
     CQQVLWLYGE ENQITEVGTM NLFLYWINED GEEELATPPL DGIILPGVMR QSILDLAHKW
     GEFKVSERYL TMDDLTTAVE ENRVREMFGS GTACVVCPVS TILYKDETIH IPTMENGPKL
     ASRILEKLTD IQYGREESDW TITVA
 
 
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