ID A0A7G2E154_ARATH Unreviewed; 358 AA. AC A0A7G2E154; DT 10-FEB-2021, integrated into UniProtKB/TrEMBL. DT 10-FEB-2021, sequence version 1. DT 03-MAY-2023, entry version 10. DE RecName: Full=Branched-chain-amino-acid aminotransferase {ECO:0000256|RuleBase:RU004517}; DE EC=2.6.1.42 {ECO:0000256|RuleBase:RU004517}; GN ORFNames=AT9943_LOCUS3500 {ECO:0000313|EMBL:CAD5315105.1}; OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis. OX NCBI_TaxID=3702 {ECO:0000313|EMBL:CAD5315105.1, ECO:0000313|Proteomes:UP000516314}; RN [1] {ECO:0000313|EMBL:CAD5315105.1, ECO:0000313|Proteomes:UP000516314} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Cdm-0 {ECO:0000313|Proteomes:UP000516314}; RA Ashkenazy H.; RL Submitted (SEP-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|RuleBase:RU004517}; 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|RuleBase:RU004517}; 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|RuleBase:RU004517}; CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC Evidence={ECO:0000256|ARBA:ARBA00001933, CC ECO:0000256|RuleBase:RU004516}; CC -!- SIMILARITY: Belongs to the class-IV pyridoxal-phosphate-dependent CC aminotransferase family. {ECO:0000256|ARBA:ARBA00009320, CC ECO:0000256|RuleBase:RU004106}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; LR881466; CAD5315105.1; -; Genomic_DNA. DR AlphaFoldDB; A0A7G2E154; -. DR Proteomes; UP000516314; Chromosome 1. 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:0009082; P:branched-chain amino acid biosynthetic process; IEA:UniProtKB-KW. DR CDD; cd01557; BCAT_beta_family; 1. 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; 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; PTHR42825; AMINO ACID AMINOTRANSFERASE; 1. DR PANTHER; PTHR42825:SF28; BRANCHED-CHAIN-AMINO-ACID AMINOTRANSFERASE 7-RELATED; 1. DR Pfam; PF01063; Aminotran_4; 1. DR PIRSF; PIRSF006468; BCAT1; 1. DR SUPFAM; SSF56752; D-aminoacid aminotransferase-like PLP-dependent enzymes; 1. DR TIGRFAMs; TIGR01123; ilvE_II; 1. DR PROSITE; PS00770; AA_TRANSFER_CLASS_4; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis {ECO:0000256|RuleBase:RU004517}; KW Aminotransferase {ECO:0000256|ARBA:ARBA00022576, KW ECO:0000256|RuleBase:RU004517}; KW Branched-chain amino acid biosynthesis {ECO:0000256|RuleBase:RU004517}; KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898, KW ECO:0000256|RuleBase:RU004516}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004517}. SQ SEQUENCE 358 AA; 39049 MW; 7E8BA7335947E64A CRC64; MAPSVHPSSS PLFTSKADEK YANVKWDELG FALIPTDYMY VAKCKQGESF STGEIVPYGD ISISPCAGIL NYGQGLFEGL KAYRTEDGRI TLFRPDQNAI RMQTGADRLC MTPPSPEQFV EAVKQTVLAN NKWVPPPGKG ALYIRPLLIG TGAVLGVASA PEYTFIIYTS PVGNYHKASS SLNLKVDHNH RRAHFGGTGG VVKSLIEAKS SGFSDVLFLD AATGKNIEEV STCNIFILKG NIVSTPPTSG TILPGITRKS ICELARDIGY EVQERDVSVD ELLEAEEVFC TGTAVVIKAV ETVTFHDKRV KYRTGEEAFS TKLHLILTNI QMGVVEDKKG WMMEIDHLVG TDSFPDET //