BCAT3_ARATH
ID BCAT3_ARATH Reviewed; 413 AA.
AC Q9M401; Q8LAT6; Q9M2Z0;
DT 06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Branched-chain-amino-acid aminotransferase 3, chloroplastic {ECO:0000303|PubMed:12068099};
DE Short=Atbcat-3;
DE EC=2.6.1.42;
DE EC=2.6.1.88;
DE Flags: Precursor;
GN Name=BCAT3 {ECO:0000303|PubMed:12068099};
GN OrderedLocusNames=At3g49680 {ECO:0000312|Araport:AT3G49680};
GN ORFNames=T16K5.30 {ECO:0000303|PubMed:11130713};
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 CHARACTERIZATION.
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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE
RP SPECIFICITY, INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=18162591; DOI=10.1104/pp.107.111609;
RA Knill T., Schuster J., Reichelt M., Gershenzon J., Binder S.;
RT "Arabidopsis branched-chain aminotransferase 3 functions in both amino acid
RT and glucosinolate biosynthesis.";
RL Plant Physiol. 146:1028-1039(2008).
RN [7]
RP SUBCELLULAR LOCATION, AND ACTIVITY REGULATION.
RX PubMed=25070638; DOI=10.1105/tpc.114.126854;
RA Niehaus T.D., Nguyen T.N., Gidda S.K., ElBadawi-Sidhu M., Lambrecht J.A.,
RA McCarty D.R., Downs D.M., Cooper A.J., Fiehn O., Mullen R.T., Hanson A.D.;
RT "Arabidopsis and Maize RidA proteins preempt reactive enamine/imine damage
RT to branched-chain amino acid biosynthesis in plastids.";
RL Plant Cell 26:3010-3022(2014).
CC -!- FUNCTION: Converts 2-oxo acids to branched-chain amino acids. Acts on
CC leucine, isoleucine and valine. Also involved in methionine chain
CC elongation cycle of aliphatic glucosinolate formation. Catalyzes the
CC conversion of 5-methylthiopentyl-2-oxo and 6-methylthiohexyl-2-oxo
CC acids to their respective Met derivatives, homomethionine and dihomo-
CC methionine, respectively. {ECO:0000269|PubMed:18162591}.
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:0000269|PubMed:18162591};
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:0000269|PubMed:18162591};
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:0000269|PubMed:18162591};
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:18162591};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC -!- ACTIVITY REGULATION: Inhibited by Ser- or Thr-derived imine.
CC {ECO:0000269|PubMed:25070638}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.14 mM for 4-methyl-2-oxopentanoate (4MOP)
CC {ECO:0000269|PubMed:18162591};
CC KM=0.14 mM for (S)-3-methyl-2-oxopentanoate (3MOP)
CC {ECO:0000269|PubMed:18162591};
CC KM=1.38 mM for 3-methyl-2-oxobutanoate (3MOB)
CC {ECO:0000269|PubMed:18162591};
CC KM=1.92 mM for 2-oxo-4-methylthiobutanoate (MTOB)
CC {ECO:0000269|PubMed:18162591};
CC Vmax=27.42 umol/min/mg enzyme with 4-methyl-2-oxopentanoate as
CC substrate {ECO:0000269|PubMed:18162591};
CC Vmax=13.33 umol/min/mg enzyme with (S)-3-methyl-2-oxopentanoate as
CC substrate {ECO:0000269|PubMed:18162591};
CC Vmax=14.79 umol/min/mg enzyme with 3-methyl-2-oxobutanoate as
CC substrate {ECO:0000269|PubMed:18162591};
CC Vmax=21.01 umol/min/mg enzyme with 2-oxo-4-methylthiobutanoate as
CC substrate {ECO:0000269|PubMed:18162591};
CC -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-
CC isoleucine from 2-oxobutanoate: step 4/4.
CC -!- PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine
CC from 3-methyl-2-oxobutanoate: step 4/4.
CC -!- PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine from
CC pyruvate: step 4/4.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:25070638}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q9M401-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed in the phloem cells.
CC {ECO:0000269|PubMed:18162591}.
CC -!- INDUCTION: Diurnally expressed. {ECO:0000303|PubMed:18162591}.
CC -!- DISRUPTION PHENOTYPE: No effect on the levels of free amino acids in
CC seeds, but reduced levels of Val, Ser and Thr in leaves. Increased
CC levels of Met-derived glucosinolates in leaves.
CC {ECO:0000269|PubMed:18162591}.
CC -!- MISCELLANEOUS: Branched-chain amino acids are synthesized in
CC chloroplasts, whereas the degradation takes place in mitochondria.
CC -!- SIMILARITY: Belongs to the class-IV pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB66906.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AJ276124; CAB93131.1; -; mRNA.
DR EMBL; AL132965; CAB66906.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE78575.1; -; Genomic_DNA.
DR EMBL; AF446355; AAL48229.1; -; mRNA.
DR EMBL; AY097417; AAM19933.1; -; mRNA.
DR EMBL; AY087619; AAM65160.1; -; mRNA.
DR PIR; T46034; T46034.
DR RefSeq; NP_566923.1; NM_114828.6. [Q9M401-1]
DR AlphaFoldDB; Q9M401; -.
DR SMR; Q9M401; -.
DR BioGRID; 9448; 2.
DR STRING; 3702.AT3G49680.1; -.
DR PaxDb; Q9M401; -.
DR PRIDE; Q9M401; -.
DR ProteomicsDB; 241207; -. [Q9M401-1]
DR EnsemblPlants; AT3G49680.1; AT3G49680.1; AT3G49680. [Q9M401-1]
DR GeneID; 824130; -.
DR Gramene; AT3G49680.1; AT3G49680.1; AT3G49680. [Q9M401-1]
DR KEGG; ath:AT3G49680; -.
DR Araport; AT3G49680; -.
DR TAIR; locus:2097320; AT3G49680.
DR eggNOG; KOG0975; Eukaryota.
DR InParanoid; Q9M401; -.
DR OrthoDB; 853728at2759; -.
DR PhylomeDB; Q9M401; -.
DR BioCyc; ARA:AT3G49680-MON; -.
DR BioCyc; MetaCyc:AT3G49680-MON; -.
DR BRENDA; 2.6.1.42; 399.
DR SABIO-RK; Q9M401; -.
DR UniPathway; UPA00047; UER00058.
DR UniPathway; UPA00048; UER00073.
DR UniPathway; UPA00049; UER00062.
DR PRO; PR:Q9M401; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9M401; baseline and differential.
DR Genevisible; Q9M401; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0004084; F:branched-chain-amino-acid transaminase activity; IBA:GO_Central.
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:0009097; P:isoleucine biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0009098; P:leucine biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0009099; P:valine biosynthetic process; IEA:UniProtKB-UniPathway.
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; 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.
DR PROSITE; PS00770; AA_TRANSFER_CLASS_4; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Amino-acid biosynthesis; Aminotransferase;
KW Branched-chain amino acid biosynthesis; Chloroplast; Plastid;
KW Pyridoxal phosphate; Reference proteome; Transferase; Transit peptide.
FT TRANSIT 1..60
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 61..413
FT /note="Branched-chain-amino-acid aminotransferase 3,
FT chloroplastic"
FT /id="PRO_0000001277"
FT MOD_RES 259
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
FT CONFLICT 74
FT /note="T -> P (in Ref. 5; AAM65160)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 413 AA; 44972 MW; C9AF31F56589916B CRC64;
MERAAILPSV NQNYLLCPSR AFSTRLHSST RNLSPPSFAS IKLQHSSSSV SSNGGISLTR
CNAVSSNSSS TLVTELADID WDTVGFGLKP ADYMYVMKCN IDGEFSKGEL QRFGNIEISP
SAGVLNYGQG LFEGLKAYRK KDGNNILLFR PEENAKRMRN GAERMCMPAP TVEQFVEAVT
ETVLANKRWV PPPGKGSLYV RPLLMGTGAV LGLAPAPEYT FIIYVSPVGN YFKEGVAPIN
LIVENEFHRA TPGGTGGVKT IGNYAAVLKA QSIAKAKGYS DVLYLDCIYK RYLEEVSSCN
IFIVKDNVIS TPEIKGTILP GITRKSMIDV ARTQGFQVEE RNVTVDELLE ADEVFCTGTA
VVVSPVGSVT YKGKRVSYGE GTFGTVSKQL YTVLTSLQMG LIEDNMKWTV NLS
