BCAT1_RAT
ID BCAT1_RAT Reviewed; 411 AA.
AC P54690;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Branched-chain-amino-acid aminotransferase, cytosolic;
DE Short=BCAT(c);
DE EC=2.6.1.42;
GN Name=Bcat1;
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], AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RX PubMed=8530459; DOI=10.1074/jbc.270.51.30344;
RA Hutson S.M., Bledsoe R.K., Hall T.R., Dawson P.A.;
RT "Cloning and expression of the mammalian cytosolic branched chain
RT aminotransferase isoenzyme.";
RL J. Biol. Chem. 270:30344-30352(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PROTEIN SEQUENCE OF 394-401, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RA Lubec G., Kang S.U., Lubec S.;
RL Submitted (SEP-2007) to UniProtKB.
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.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- TISSUE SPECIFICITY: Brain, low expression in ovary and placenta, but
CC not found in liver, kidney, and skeletal muscle.
CC -!- PTM: The N-terminus is blocked.
CC -!- SIMILARITY: Belongs to the class-IV pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
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DR EMBL; U35774; AAC52385.1; -; mRNA.
DR EMBL; BC087710; AAH87710.1; -; mRNA.
DR RefSeq; NP_058949.1; NM_017253.2.
DR AlphaFoldDB; P54690; -.
DR SMR; P54690; -.
DR BioGRID; 248224; 1.
DR STRING; 10116.ENSRNOP00000021193; -.
DR BindingDB; P54690; -.
DR ChEMBL; CHEMBL4678; -.
DR iPTMnet; P54690; -.
DR PhosphoSitePlus; P54690; -.
DR SwissPalm; P54690; -.
DR jPOST; P54690; -.
DR PaxDb; P54690; -.
DR PRIDE; P54690; -.
DR GeneID; 29592; -.
DR KEGG; rno:29592; -.
DR UCSC; RGD:2195; rat.
DR CTD; 586; -.
DR RGD; 2195; Bcat1.
DR VEuPathDB; HostDB:ENSRNOG00000015514; -.
DR eggNOG; KOG0975; Eukaryota.
DR InParanoid; P54690; -.
DR OMA; LTEVFAC; -.
DR OrthoDB; 853728at2759; -.
DR PhylomeDB; P54690; -.
DR TreeFam; TF300882; -.
DR Reactome; R-RNO-70895; Branched-chain amino acid catabolism.
DR SABIO-RK; P54690; -.
DR PRO; PR:P54690; -.
DR Proteomes; UP000002494; Chromosome 4.
DR Bgee; ENSRNOG00000015514; Expressed in cerebellum and 19 other tissues.
DR ExpressionAtlas; P54690; baseline and differential.
DR Genevisible; P54690; RN.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005829; C:cytosol; ISO:RGD.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0004084; F:branched-chain-amino-acid transaminase activity; IDA:RGD.
DR GO; GO:0042802; F:identical protein binding; IDA:RGD.
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:0009083; P:branched-chain amino acid catabolic process; ISO:RGD.
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 1: Evidence at protein level;
KW Amino-acid biosynthesis; Aminotransferase;
KW Branched-chain amino acid biosynthesis; Cytoplasm;
KW Direct protein sequencing; Lipid metabolism; Pyridoxal phosphate;
KW Reference proteome; Transferase.
FT CHAIN 1..411
FT /note="Branched-chain-amino-acid aminotransferase,
FT cytosolic"
FT /id="PRO_0000103294"
FT MOD_RES 247
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 411 AA; 46046 MW; 98030737376F1DB3 CRC64;
MAYLSRATAT LARQDCSNGC SASYAEEEEL EASTESYDEE GGSEASTQTF RAKDLIITKA
DVLKKKPDPS SLVFGASFTD HMLMVEWTSK YGWDKPHIKP FENLSIHPAA SVLHYAVELF
EGLKAFRGVD NKIRLFRPDL NMKRMCRSAV RTTLPEFDKE ELLQCVLQLI QLDREWVPYS
TSASLYIRPT FIGIEPSLGV KKPSKALLFV ILSPVGSYFS NGTFSPVSLW ANPKFVRSWK
GGTGDFKMGC NYGSSLLAQC EAAENGCHQV LWLYGKENRI TEVGTMNLFL YWINKDGEEE
LATPPLDGVI LPGVTRQSIL ELGEEWGEFK VCERHITMDD LSTALEENRV KEMFGSGTAC
VVCPVASILY KGQMLHIPTM ENGHKLSSRI MAKLTDIQYG RIKSEWTLEL P
