BCAT4_ARATH
ID BCAT4_ARATH Reviewed; 354 AA.
AC Q9LE06; Q0WW34;
DT 06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Methionine aminotransferase BCAT4;
DE EC=2.6.1.88;
DE AltName: Full=Branched-chain-amino-acid aminotransferase 4;
DE Short=Atbcat-4;
DE AltName: Full=Methionine-oxo-acid transaminase BCAT4;
GN Name=BCAT4; OrderedLocusNames=At3g19710; ORFNames=MMB12_16;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=12068099; DOI=10.1104/pp.001602;
RA Diebold R., Schuster J., Daschner K., Binder S.;
RT "The branched-chain amino acid transaminase gene family in Arabidopsis
RT encodes plastid and mitochondrial proteins.";
RL Plant Physiol. 129:540-550(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
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).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, CATALYTIC ACTIVITY, INDUCTION BY WOUNDING,
RP TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RX PubMed=17056707; DOI=10.1105/tpc.105.039339;
RA Schuster J., Knill T., Reichelt M., Gershenzon J., Binder S.;
RT "Branched-chain aminotransferase4 is part of the chain elongation pathway
RT in the biosynthesis of methionine-derived glucosinolates in Arabidopsis.";
RL Plant Cell 18:2664-2679(2006).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=18318836; DOI=10.1111/j.1742-4658.2008.06279.x;
RA Funakoshi M., Sekine M., Katane M., Furuchi T., Yohda M., Yoshikawa T.,
RA Homma H.;
RT "Cloning and functional characterization of Arabidopsis thaliana D-amino
RT acid aminotransferase--D-aspartate behavior during germination.";
RL FEBS J. 275:1188-1200(2008).
CC -!- FUNCTION: Converts 2-oxo acids to branched-chain amino acids. Shows
CC activity with L-Leu, L-Ile and L-Val as amino donors and alpha-keto-
CC glutarate as an amino acceptor, but no activity for D-isomers of Leu,
CC Ile, Val, Asp, Glu or Ala. Acts on methionine and its derivatives and
CC the corresponding 2-oxo acids. Catalyzes the initial deamination of
CC methionine to 4-methylthio-2-oxobutyrate as well as the transamination
CC of other typical intermediates of the methionine chain elongation
CC pathway. {ECO:0000269|PubMed:17056707, ECO:0000269|PubMed:18318836}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2-oxocarboxylate + L-methionine = 4-methylsulfanyl-2-
CC oxobutanoate + an L-alpha-amino acid; Xref=Rhea:RHEA:31763,
CC ChEBI:CHEBI:16723, ChEBI:CHEBI:35179, ChEBI:CHEBI:57844,
CC ChEBI:CHEBI:59869; EC=2.6.1.88;
CC Evidence={ECO:0000269|PubMed:17056707, ECO:0000269|PubMed:18318836};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000305};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.045 mM for 2-oxo acid 4-methylthio-2-oxobutyrate (MTOB)
CC {ECO:0000269|PubMed:17056707};
CC KM=0.93 mM for methionine {ECO:0000269|PubMed:17056707};
CC KM=4.86 mM for leucine {ECO:0000269|PubMed:17056707};
CC KM=1.61 mM for L-leucine {ECO:0000269|PubMed:18318836};
CC Vmax=2.7 umol/min/mg enzyme with MTOB as substrate
CC {ECO:0000269|PubMed:17056707};
CC Vmax=0.089 umol/min/mg enzyme with methionine as substrate
CC {ECO:0000269|PubMed:17056707};
CC Vmax=0.11 umol/min/mg enzyme with leucine as substrate
CC {ECO:0000269|PubMed:17056707};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12068099,
CC ECO:0000269|PubMed:17056707}.
CC -!- TISSUE SPECIFICITY: Mostly expressed in phloem.
CC {ECO:0000269|PubMed:17056707}.
CC -!- INDUCTION: Transient induction by wounding. Follows a diurnal rhythm.
CC {ECO:0000269|PubMed:17056707}.
CC -!- DISRUPTION PHENOTYPE: Reduced methionine-derived aliphatic
CC glucosinolate accumulation, but increased levels of free methionine and
CC S-methylmethionine. {ECO:0000269|PubMed:17056707}.
CC -!- MISCELLANEOUS: Although all the other members of the family possess a
CC branched-chain amino acid aminotransferase activity, the exact function
CC of BCAT4 remains unclear at present.
CC -!- SIMILARITY: Belongs to the class-IV pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
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DR EMBL; AJ271732; CAB93129.1; -; mRNA.
DR EMBL; AP000417; BAB02558.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE76278.1; -; Genomic_DNA.
DR EMBL; AY052676; AAK96580.1; -; mRNA.
DR EMBL; AF446892; AAL38625.1; -; mRNA.
DR EMBL; AK226525; BAE98664.1; -; mRNA.
DR PIR; T52401; T52401.
DR RefSeq; NP_188605.1; NM_112861.4.
DR AlphaFoldDB; Q9LE06; -.
DR SMR; Q9LE06; -.
DR BioGRID; 6841; 1.
DR STRING; 3702.AT3G19710.1; -.
DR iPTMnet; Q9LE06; -.
DR PaxDb; Q9LE06; -.
DR PRIDE; Q9LE06; -.
DR ProteomicsDB; 241130; -.
DR EnsemblPlants; AT3G19710.1; AT3G19710.1; AT3G19710.
DR GeneID; 821508; -.
DR Gramene; AT3G19710.1; AT3G19710.1; AT3G19710.
DR KEGG; ath:AT3G19710; -.
DR Araport; AT3G19710; -.
DR TAIR; locus:2091216; AT3G19710.
DR eggNOG; KOG0975; Eukaryota.
DR HOGENOM; CLU_031922_4_0_1; -.
DR InParanoid; Q9LE06; -.
DR OMA; ACISTTY; -.
DR OrthoDB; 853728at2759; -.
DR PhylomeDB; Q9LE06; -.
DR BioCyc; ARA:AT3G19710-MON; -.
DR BioCyc; MetaCyc:AT3G19710-MON; -.
DR BRENDA; 2.6.1.42; 399.
DR BRENDA; 2.6.1.88; 399.
DR SABIO-RK; Q9LE06; -.
DR PRO; PR:Q9LE06; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LE06; baseline and differential.
DR Genevisible; Q9LE06; AT.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0004084; F:branched-chain-amino-acid transaminase activity; IBA:GO_Central.
DR GO; GO:0010326; F:methionine-oxo-acid transaminase activity; IDA:TAIR.
DR GO; GO:0009081; P:branched-chain amino acid metabolic process; IEA:InterPro.
DR GO; GO:0019761; P:glucosinolate biosynthetic process; IMP:TAIR.
DR GO; GO:0009416; P:response to light stimulus; IEP:UniProtKB.
DR GO; GO:0009611; P:response to wounding; IEP:UniProtKB.
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; 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; PTHR42825; 1.
DR Pfam; PF01063; Aminotran_4; 1.
DR PIRSF; PIRSF006468; BCAT1; 1.
DR SUPFAM; SSF56752; SSF56752; 1.
DR TIGRFAMs; TIGR01123; ilvE_II; 1.
PE 1: Evidence at protein level;
KW Aminotransferase; Cytoplasm; Pyridoxal phosphate; Reference proteome;
KW Transferase.
FT CHAIN 1..354
FT /note="Methionine aminotransferase BCAT4"
FT /id="PRO_0000103297"
FT MOD_RES 198
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 354 AA; 39019 MW; 313EA4C5B5AE1898 CRC64;
MAPSAQPLPV SVSDEKYANV KWEELAFKFV RTDYMYVAKC NHGESFQEGK ILPFADLQLN
PCAAVLQYGQ GLYEGLKAYR TEDGRILLFR PDQNGLRLQA GADRLYMPYP SVDQFVSAIK
QVALANKKWI PPPGKGTLYI RPILFGSGPI LGSFPIPETT FTAFACPVGR YHKDNSGLNL
KIEDQFRRAF PSGTGGVKSI TNYCPVWIPL AEAKKQGFSD ILFLDAATGK NIEELFAANV
FMLKGNVVST PTIAGTILPG VTRNCVMELC RDFGYQVEER TIPLVDFLDA DEAFCTGTAS
IVTSIASVTF KDKKTGFKTG EETLAAKLYE TLSDIQTGRV EDTKGWTVEI DRQG
