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Database: UniProt
Entry: A0A5E4CBY4_MARMO
LinkDB: A0A5E4CBY4_MARMO
Original site: A0A5E4CBY4_MARMO 
ID   A0A5E4CBY4_MARMO        Unreviewed;       284 AA.
AC   A0A5E4CBY4;
DT   13-NOV-2019, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2019, sequence version 1.
DT   08-NOV-2023, entry version 16.
DE   RecName: Full=branched-chain-amino-acid transaminase {ECO:0000256|ARBA:ARBA00013053};
DE            EC=2.6.1.42 {ECO:0000256|ARBA:ARBA00013053};
GN   ORFNames=GHT09_018718 {ECO:0000313|EMBL:KAF7469821.1}, MONAX_5E004831
GN   {ECO:0000313|EMBL:VTJ79363.1};
OS   Marmota monax (Woodchuck).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Sciuromorpha; Sciuridae;
OC   Xerinae; Marmotini; Marmota.
OX   NCBI_TaxID=9995 {ECO:0000313|EMBL:VTJ79363.1, ECO:0000313|Proteomes:UP000335636};
RN   [1] {ECO:0000313|EMBL:VTJ79363.1, ECO:0000313|Proteomes:UP000335636}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Alioto T., Alioto T.;
RL   Submitted (APR-2019) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KAF7469821.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=WC2-LM {ECO:0000313|EMBL:KAF7469821.1};
RC   TISSUE=Liver {ECO:0000313|EMBL:KAF7469821.1};
RA   Shumante A., Zimin A.V., Puiu D., Salzberg S.L.;
RL   Submitted (AUG-2020) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00000627};
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:0000256|ARBA:ARBA00000995};
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:0000256|ARBA:ARBA00001745};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
CC   -!- SIMILARITY: Belongs to the class-IV pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|ARBA:ARBA00009320}.
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DR   EMBL; WJEC01007593; KAF7469821.1; -; Genomic_DNA.
DR   EMBL; CABDUW010001175; VTJ79363.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A5E4CBY4; -.
DR   Proteomes; UP000335636; Unassembled WGS sequence.
DR   Proteomes; UP000662637; Unassembled WGS sequence.
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:0052655; F:L-valine transaminase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008652; P:amino acid biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0009081; P:branched-chain amino acid metabolic process; IEA:InterPro.
DR   Gene3D; 3.30.470.10; -; 1.
DR   Gene3D; 3.20.10.10; D-amino Acid Aminotransferase, subunit A, domain 2; 1.
DR   InterPro; IPR001544; Aminotrans_IV.
DR   InterPro; IPR036038; Aminotransferase-like.
DR   InterPro; IPR005786; B_amino_transII.
DR   InterPro; IPR043132; BCAT-like_C.
DR   InterPro; IPR043131; BCAT-like_N.
DR   PANTHER; PTHR11825:SF70; BRANCHED-CHAIN-AMINO-ACID AMINOTRANSFERASE, CYTOSOLIC; 1.
DR   PANTHER; PTHR11825; SUBGROUP IIII AMINOTRANSFERASE; 1.
DR   Pfam; PF01063; Aminotran_4; 1.
DR   PIRSF; PIRSF006468; BCAT1; 1.
DR   SUPFAM; SSF56752; D-aminoacid aminotransferase-like PLP-dependent enzymes; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW   Aminotransferase {ECO:0000313|EMBL:KAF7469821.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000335636};
KW   Transferase {ECO:0000313|EMBL:KAF7469821.1}.
FT   MOD_RES         222
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006468-1"
SQ   SEQUENCE   284 AA;  31782 MW;  8A9E43EB04B94792 CRC64;
     MKDCSNGCSA EYPGEGGSKE VVETFRAKDL IITPATILKE KPDPNTLVFG TVFTDHMLTV
     EWSSEFGWEK PHIKPFQNLS LHPGSSTLHY AVELFEGLKA FRGVDNKIRL FRPELNMERM
     CKSAVRATLP VFDKEELLEC IQQLVQLDQE WVPYSTSGSL YIRPTFIGTE PSLGVKKPTK
     ALLFVILSPV GPYFSSGTFN PVSLWANPKY VRAWKGGTGD CKMGGNYGSS LFAQCEAAEN
     GCQQVLWLYG EDNQITEVGT MNLFLYWINE DGGNTLRFQL CAMF
//
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