BCAT1_ARATH
ID BCAT1_ARATH Reviewed; 384 AA.
AC Q93Y32; O80597;
DT 06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2002, sequence version 2.
DT 25-MAY-2022, entry version 152.
DE RecName: Full=Branched-chain-amino-acid aminotransferase 1, mitochondrial;
DE Short=Atbcat-1;
DE EC=2.6.1.42;
DE Flags: Precursor;
GN Name=BCAT1; OrderedLocusNames=At1g10060; ORFNames=T27I1.8;
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).
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 degradation; L-leucine degradation; 4-methyl-2-
CC oxopentanoate from L-leucine (aminotransferase route): step 1/1.
CC -!- PATHWAY: Amino-acid degradation; L-valine degradation.
CC -!- SUBCELLULAR LOCATION: Mitochondrion.
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=Q93Y32-1; 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=AAC34335.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AJ276123; CAB93130.1; -; mRNA.
DR EMBL; AC004122; AAC34335.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE28535.1; -; Genomic_DNA.
DR EMBL; AY054517; AAK96708.1; -; mRNA.
DR EMBL; AY128778; AAM91178.1; -; mRNA.
DR PIR; T00625; T00625.
DR RefSeq; NP_563859.1; NM_100880.3.
DR RefSeq; NP_849629.1; NM_179298.2. [Q93Y32-1]
DR AlphaFoldDB; Q93Y32; -.
DR SMR; Q93Y32; -.
DR BioGRID; 22782; 1.
DR STRING; 3702.AT1G10060.2; -.
DR iPTMnet; Q93Y32; -.
DR PaxDb; Q93Y32; -.
DR EnsemblPlants; AT1G10060.2; AT1G10060.2; AT1G10060. [Q93Y32-1]
DR GeneID; 837542; -.
DR Gramene; AT1G10060.2; AT1G10060.2; AT1G10060. [Q93Y32-1]
DR KEGG; ath:AT1G10060; -.
DR Araport; AT1G10060; -.
DR TAIR; locus:2201931; AT1G10060.
DR eggNOG; KOG0975; Eukaryota.
DR InParanoid; Q93Y32; -.
DR OMA; ITYQNTR; -.
DR PhylomeDB; Q93Y32; -.
DR BRENDA; 2.6.1.42; 399.
DR UniPathway; UPA00362; -.
DR UniPathway; UPA00363; UER00857.
DR PRO; PR:Q93Y32; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q93Y32; baseline and differential.
DR Genevisible; Q93Y32; AT.
DR GO; GO:0005739; C:mitochondrion; IDA:TAIR.
DR GO; GO:0004084; F:branched-chain-amino-acid transaminase activity; IDA:TAIR.
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:0006552; P:leucine catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006574; P:valine catabolic 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; Aminotransferase;
KW Branched-chain amino acid catabolism; Mitochondrion; Pyridoxal phosphate;
KW Reference proteome; Transferase; Transit peptide.
FT TRANSIT 1..18
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 19..384
FT /note="Branched-chain-amino-acid aminotransferase 1,
FT mitochondrial"
FT /id="PRO_0000001275"
FT MOD_RES 231
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 384 AA; 41934 MW; 324B55489ECFD7AF CRC64;
MALRRCLPQY STTSSYLSKI WGFRMHGTKA AASVVEEHVS GAEREDEEYA DVDWDNLGFS
LVRTDFMFAT KSCRDGNFEQ GYLSRYGNIE LNPAAGILNY GQGLIEGMKA YRGEDGRVLL
FRPELNAMRM KIGAERMCMH SPSVHQFIEG VKQTVLANRR WVPPPGKGSL YLRPLLFGSG
ASLGVAAASE YTFLVFGSPV QNYFKEGTAA LNLYVEEVIP RAYLGGTGGV KAISNYGPVL
EVMRRAKSRG FSDVLYLDAD TGKNIEEVSA ANIFLVKGNT IVTPATSGTI LGGITRKSII
EIALDLGYKV EERSVPVEEL KEAEEVFCTG TAAGVASVGS ITFKNTRTEY KVGDGIVTQQ
LRSILVGIQT GSIQDTKDWV LQIA
