BCAT2_ARATH
ID BCAT2_ARATH Reviewed; 388 AA.
AC Q9M439; O80598;
DT 06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Branched-chain-amino-acid aminotransferase 2, chloroplastic;
DE Short=Atbcat-2;
DE EC=2.6.1.42;
DE Flags: Precursor;
GN Name=BCAT2; OrderedLocusNames=At1g10070; ORFNames=T27I1.9;
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=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.-D., 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.-P., 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 [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 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 2-oxoglutarate
CC as an amino acceptor, but no activity for D-isomers of Leu, Ile, Val,
CC Asp, Glu or Ala. {ECO:0000269|PubMed:18318836}.
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:18318836};
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:18318836};
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:18318836};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.71 mM for L-leucine {ECO:0000269|PubMed:18318836};
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 -!- 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=Q9M439-1; Sequence=Displayed;
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=AAC34333.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AJ271731; CAB93128.1; -; mRNA.
DR EMBL; AC004122; AAC34333.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE28537.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE28538.1; -; Genomic_DNA.
DR EMBL; AY051038; AAK93715.1; -; mRNA.
DR EMBL; AF370135; AAK43950.1; -; mRNA.
DR PIR; T00626; T00626.
DR RefSeq; NP_001031015.1; NM_001035938.2. [Q9M439-1]
DR RefSeq; NP_001031016.2; NM_001035939.3.
DR RefSeq; NP_172478.1; NM_100881.3. [Q9M439-1]
DR AlphaFoldDB; Q9M439; -.
DR SMR; Q9M439; -.
DR BioGRID; 22783; 9.
DR IntAct; Q9M439; 2.
DR STRING; 3702.AT1G10070.1; -.
DR iPTMnet; Q9M439; -.
DR PaxDb; Q9M439; -.
DR PRIDE; Q9M439; -.
DR ProteomicsDB; 240641; -. [Q9M439-1]
DR EnsemblPlants; AT1G10070.1; AT1G10070.1; AT1G10070. [Q9M439-1]
DR EnsemblPlants; AT1G10070.2; AT1G10070.2; AT1G10070. [Q9M439-1]
DR GeneID; 837543; -.
DR Gramene; AT1G10070.1; AT1G10070.1; AT1G10070. [Q9M439-1]
DR Gramene; AT1G10070.2; AT1G10070.2; AT1G10070. [Q9M439-1]
DR KEGG; ath:AT1G10070; -.
DR Araport; AT1G10070; -.
DR TAIR; locus:2201921; AT1G10070.
DR eggNOG; KOG0975; Eukaryota.
DR InParanoid; Q9M439; -.
DR OMA; EQRWIPT; -.
DR PhylomeDB; Q9M439; -.
DR BRENDA; 2.6.1.42; 399.
DR SABIO-RK; Q9M439; -.
DR UniPathway; UPA00047; UER00058.
DR UniPathway; UPA00048; UER00073.
DR UniPathway; UPA00049; UER00062.
DR PRO; PR:Q9M439; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9M439; baseline and differential.
DR Genevisible; Q9M439; AT.
DR GO; GO:0009507; C:chloroplast; IDA: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:0071669; P:plant-type cell wall organization or biogenesis; IMP:TAIR.
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..22
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 23..388
FT /note="Branched-chain-amino-acid aminotransferase 2,
FT chloroplastic"
FT /id="PRO_0000001276"
FT MOD_RES 235
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 388 AA; 42591 MW; C457DBADF362DCF0 CRC64;
MIKTITSLRK TLVLPLHLHI RTLQTFAKYN AQAASALREE RKKPLYQNGD DVYADLDWDN
LGFGLNPADY MYVMKCSKDG EFTQGELSPY GNIQLSPSAG VLNYGQAIYE GTKAYRKENG
KLLLFRPDHN AIRMKLGAER MLMPSPSVDQ FVNAVKQTAL ANKRWVPPAG KGTLYIRPLL
MGSGPILGLG PAPEYTFIVY ASPVGNYFKE GMAALNLYVE EEYVRAAPGG AGGVKSITNY
APVLKALSRA KSRGFSDVLY LDSVKKKYLE EASSCNVFVV KGRTISTPAT NGTILEGITR
KSVMEIASDQ GYQVVEKAVH VDEVMDADEV FCTGTAVVVA PVGTITYQEK RVEYKTGDES
VCQKLRSVLV GIQTGLIEDN KGWVTDIN
