BCAT6_ARATH
ID BCAT6_ARATH Reviewed; 356 AA.
AC Q9LPM9; Q42148; Q8L961;
DT 06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Branched-chain-amino-acid aminotransferase 6;
DE Short=Atbcat-6;
DE EC=2.6.1.42;
GN Name=BCAT6; OrderedLocusNames=At1g50110; ORFNames=F2J10.4;
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].
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 16-140.
RC STRAIN=cv. Columbia;
RX PubMed=8580968; DOI=10.1046/j.1365-313x.1996.09010101.x;
RA Cooke R., Raynal M., Laudie M., Grellet F., Delseny M., Morris P.-C.,
RA Guerrier D., Giraudat J., Quigley F., Clabault G., Li Y.-F., Mache R.,
RA Krivitzky M., Gy I.J.-J., Kreis M., Lecharny A., Parmentier Y., Marbach J.,
RA Fleck J., Clement B., Philipps G., Herve C., Bardet C., Tremousaygue D.,
RA Lescure B., Lacomme C., Roby D., Jourjon M.-F., Chabrier P.,
RA Charpenteau J.-L., Desprez T., Amselem J., Chiapello H., Hoefte H.;
RT "Further progress towards a catalogue of all Arabidopsis genes: analysis of
RT a set of 5000 non-redundant ESTs.";
RL Plant J. 9:101-124(1996).
CC -!- FUNCTION: Converts 2-oxo acids to branched-chain amino acids. Acts on
CC leucine, isoleucine and valine (By similarity). {ECO:0000250}.
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 -!- 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 -!- 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 -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
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: Cytoplasm.
CC -!- SIMILARITY: Belongs to the class-IV pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
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DR EMBL; AJ312747; CAC37393.1; -; mRNA.
DR EMBL; AC015445; AAF76437.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE32516.1; -; Genomic_DNA.
DR EMBL; AY088621; AAM66943.1; -; mRNA.
DR EMBL; Z26805; CAA81418.1; -; mRNA.
DR PIR; D96537; D96537.
DR RefSeq; NP_175431.1; NM_103897.4.
DR AlphaFoldDB; Q9LPM9; -.
DR SMR; Q9LPM9; -.
DR STRING; 3702.AT1G50110.1; -.
DR iPTMnet; Q9LPM9; -.
DR PaxDb; Q9LPM9; -.
DR PRIDE; Q9LPM9; -.
DR ProteomicsDB; 240776; -.
DR EnsemblPlants; AT1G50110.1; AT1G50110.1; AT1G50110.
DR GeneID; 841433; -.
DR Gramene; AT1G50110.1; AT1G50110.1; AT1G50110.
DR KEGG; ath:AT1G50110; -.
DR Araport; AT1G50110; -.
DR TAIR; locus:2031030; AT1G50110.
DR eggNOG; KOG0975; Eukaryota.
DR HOGENOM; CLU_031922_4_0_1; -.
DR InParanoid; Q9LPM9; -.
DR OrthoDB; 853728at2759; -.
DR PhylomeDB; Q9LPM9; -.
DR BioCyc; ARA:AT1G50110-MON; -.
DR BRENDA; 2.6.1.42; 399.
DR UniPathway; UPA00047; UER00058.
DR UniPathway; UPA00048; UER00073.
DR UniPathway; UPA00049; UER00062.
DR PRO; PR:Q9LPM9; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9LPM9; baseline and differential.
DR Genevisible; Q9LPM9; 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:0052656; F:L-isoleucine transaminase activity; IDA:TAIR.
DR GO; GO:0052654; F:L-leucine transaminase activity; IDA:TAIR.
DR GO; GO:0050048; F:L-leucine:2-oxoglutarate aminotransferase activity; IEA:RHEA.
DR GO; GO:0052655; F:L-valine transaminase activity; IDA:TAIR.
DR GO; GO:0010326; F:methionine-oxo-acid transaminase activity; IDA:TAIR.
DR GO; GO:0033506; P:glucosinolate biosynthetic process from homomethionine; IGI:TAIR.
DR GO; GO:0009097; P:isoleucine biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0071267; P:L-methionine salvage; IGI:TAIR.
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 Amino-acid biosynthesis; Aminotransferase;
KW Branched-chain amino acid biosynthesis; Cytoplasm; Pyridoxal phosphate;
KW Reference proteome; Transferase.
FT CHAIN 1..356
FT /note="Branched-chain-amino-acid aminotransferase 6"
FT /id="PRO_0000103298"
FT MOD_RES 199
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
FT CONFLICT 135..140
FT /note="GKGTLY -> VKELCI (in Ref. 5; CAA81418)"
FT /evidence="ECO:0000305"
FT CONFLICT 145
FT /note="L -> P (in Ref. 4; AAM66943)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 356 AA; 38861 MW; C3F1A506BD3B82BF CRC64;
MAPSSSPLRT TSETDEKYAN VKWEELGFAL TPIDYMYVAK CRQGESFTQG KIVPYGDISI
SPCSPILNYG QGLFEGLKAY RTEDDRIRIF RPDQNALRMQ TGAERLCMTP PTLEQFVEAV
KQTVLANKKW VPPPGKGTLY IRPLLLGSGA TLGVAPAPEY TFLIYASPVG DYHKVSSGLN
LKVDHKYHRA HSGGTGGVKS CTNYSPVVKS LLEAKSAGFS DVLFLDAATG RNIEELTACN
IFIVKGNIVS TPPTSGTILP GVTRKSISEL AHDIGYQVEE RDVSVDELLE AEEVFCTGTA
VVVKAVETVT FHDKKVKYRT GEAALSTKLH SMLTNIQMGV VEDKKGWMVD IDPCQG
