ID A0A1P8APB7_ARATH Unreviewed; 405 AA.
AC A0A1P8APB7;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=Branched-chain-amino-acid aminotransferase {ECO:0000256|RuleBase:RU004517};
DE EC=2.6.1.42 {ECO:0000256|RuleBase:RU004517};
GN Name=BCAT-1 {ECO:0000313|EMBL:ANM58499.1, ECO:0000313|TAIR:AT1G10060};
GN Synonyms=ATBCAT-1 {ECO:0000313|EMBL:ANM58499.1}, BCAT1
GN {ECO:0000313|EMBL:ANM58499.1};
GN OrderedLocusNames=At1g10060 {ECO:0000313|Araport:AT1G10060,
GN ECO:0000313|EMBL:ANM58499.1};
GN ORFNames=T27I1.8 {ECO:0000313|EMBL:ANM58499.1}, T27I1_8
GN {ECO:0000313|EMBL:ANM58499.1};
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:ANM58499.1, ECO:0000313|Proteomes:UP000006548};
RN [1] {ECO:0000313|EMBL:ANM58499.1, ECO:0000313|Proteomes:UP000006548}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia {ECO:0000313|Proteomes:UP000006548};
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [2] {ECO:0000313|Proteomes:UP000006548}
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia {ECO:0000313|Proteomes:UP000006548};
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
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}.
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DR EMBL; CP002684; ANM58499.1; -; Genomic_DNA.
DR RefSeq; NP_001320928.1; NM_001331882.1.
DR AlphaFoldDB; A0A1P8APB7; -.
DR SMR; A0A1P8APB7; -.
DR ProteomicsDB; 200227; -.
DR EnsemblPlants; AT1G10060.6; AT1G10060.6; AT1G10060.
DR GeneID; 837542; -.
DR Gramene; AT1G10060.6; AT1G10060.6; AT1G10060.
DR Araport; AT1G10060; -.
DR TAIR; AT1G10060; BCAT-1.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; A0A1P8APB7; baseline and differential.
DR GO; GO:0052656; F:L-isoleucine transaminase activity; IEA:RHEA.
DR GO; GO:0050048; F:L-leucine:2-oxoglutarate aminotransferase activity; IEA:RHEA.
DR GO; GO:0052655; F:L-valine transaminase activity; IEA:RHEA.
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 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 PANTHER; PTHR42825; AMINO ACID AMINOTRANSFERASE; 1.
DR PANTHER; PTHR42825:SF34; BRANCHED-CHAIN-AMINO-ACID AMINOTRANSFERASE 1, MITOCHONDRIAL; 1.
DR Pfam; PF01063; Aminotran_4; 1.
DR SUPFAM; SSF56752; D-aminoacid aminotransferase-like PLP-dependent enzymes; 1.
DR PROSITE; PS00770; AA_TRANSFER_CLASS_4; 1.
PE 1: Evidence at protein level;
KW Amino-acid biosynthesis {ECO:0000256|RuleBase:RU004517};
KW Aminotransferase {ECO:0000256|RuleBase:RU004517};
KW Branched-chain amino acid biosynthesis {ECO:0000256|RuleBase:RU004517};
KW Proteomics identification {ECO:0007829|PeptideAtlas:A0A1P8APB7,
KW ECO:0007829|ProteomicsDB:A0A1P8APB7};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU004516};
KW Reference proteome {ECO:0000313|Proteomes:UP000006548};
KW Transferase {ECO:0000256|RuleBase:RU004517}.
SQ SEQUENCE 405 AA; 44848 MW; 31EA83D5C8FF8866 CRC64;
MYSQSPIDIF EGIFVVTYKS WLRNLNTEKE NASNFPSSLY IFQPLSVSLP LCSFSNIFFR
VGTTSLIIIF STPINKRYIL EFHFGAQTKL VQHSSYMALR RCLPQYSTTS SYLSKIWGFR
MHGTKAAASV VEEHVSGAER EDEEYADVDW DNLGFSLVRT DFMFATKSCR DGNFEQGYLS
RYGNIELNPA AGILNYGQGL IEGMKAYRGE DGRVLLFRPE LNAMRMKIGA ERMCMHSPSV
HQFIEGVKQT VLANRRWVPP PGKGSLYLRP LLFGSGASLG VAAASEYTFL VFGSPVQNYF
KEGTAALNLY VEEVIPRAYL GGTGGVKAIS NYGPVLEVMR RAKSRGFSDV LYLDADTGKN
IEEVSAANIF LVKGNTIVTP ATSGTILGGI TRGRTKCSGR RTEGS
//
