Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9LE06 (BCAT4_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 104. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Methionine aminotransferase BCAT4

EC=2.6.1.88
Alternative name(s):
Branched-chain-amino-acid aminotransferase 4
Short name=Atbcat-4
Methionine-oxo-acid transaminase BCAT4
Gene names
Name:BCAT4
Ordered Locus Names:At3g19710
ORF Names:MMB12_16
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length354 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Convert 2-oxo acids to branched-chain amino acids. Acts on methionine and its derivatives and the corresponding 2-oxo acids. Catalyzes the initial deamination of methionine to 4-methylthio-2-oxobutyrate as well as the transamination of other typical intermediates of the methionine chain elongation pathway. Ref.6

Catalytic activity

L-methionine + a 2-oxo acid = 2-oxo-4-methylthiobutanoate + an L-amino acid. Ref.6

Cofactor

Pyridoxal phosphate Probable.

Subcellular location

Cytoplasm Ref.1 Ref.6.

Tissue specificity

Mostly expressed in phloem. Ref.6

Induction

Transient induction by wounding. Follows a diurnal rhythm. Ref.6

Post-translational modification

Ubiquitinated.

Disruption phenotype

Reduced methionine-derived aliphatic glucosinolate accumulation, but increased levels of free methionine and S-methylmethionine. Ref.6

Miscellaneous

Although all the other members of the family possess a branched-chain amino acid aminotransferase activity, the exact function of BCAT4 remains unclear at present.

Sequence similarities

Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family.

Biophysicochemical properties

Kinetic parameters:

KM=0.045 mM for 2-oxo acid 4-methylthio-2-oxobutyrate (MTOB) Ref.6

KM=0.93 mM for methionine

KM=4.86 mM for leucine

Vmax=2.7 µmol/min/mg enzyme with MTOB as substrate

Vmax=0.089 µmol/min/mg enzyme with methionine as substrate

Vmax=0.11 µmol/min/mg enzyme with leucine as substrate

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 354354Methionine aminotransferase BCAT4
PRO_0000103297

Amino acid modifications

Modified residue1981N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9LE06 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 313EA4C5B5AE1898

FASTA35439,019
        10         20         30         40         50         60 
MAPSAQPLPV SVSDEKYANV KWEELAFKFV RTDYMYVAKC NHGESFQEGK ILPFADLQLN 

        70         80         90        100        110        120 
PCAAVLQYGQ GLYEGLKAYR TEDGRILLFR PDQNGLRLQA GADRLYMPYP SVDQFVSAIK 

       130        140        150        160        170        180 
QVALANKKWI PPPGKGTLYI RPILFGSGPI LGSFPIPETT FTAFACPVGR YHKDNSGLNL 

       190        200        210        220        230        240 
KIEDQFRRAF PSGTGGVKSI TNYCPVWIPL AEAKKQGFSD ILFLDAATGK NIEELFAANV 

       250        260        270        280        290        300 
FMLKGNVVST PTIAGTILPG VTRNCVMELC RDFGYQVEER TIPLVDFLDA DEAFCTGTAS 

       310        320        330        340        350 
IVTSIASVTF KDKKTGFKTG EETLAAKLYE TLSDIQTGRV EDTKGWTVEI DRQG 

« Hide

References

« Hide 'large scale' references
[1]"The branched-chain amino acid transaminase gene family in Arabidopsis encodes plastid and mitochondrial proteins."
Diebold R., Schuster J., Daschner K., Binder S.
Plant Physiol. 129:540-550(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION.
Strain: cv. Columbia.
[2]"Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC clones."
Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.
DNA Res. 7:217-221(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[3]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[4]"Empirical analysis of transcriptional activity in the Arabidopsis genome."
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. expand/collapse author list , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
[5]"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."
Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K. expand/collapse author list , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K.
Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
[6]"Branched-chain aminotransferase4 is part of the chain elongation pathway in the biosynthesis of methionine-derived glucosinolates in Arabidopsis."
Schuster J., Knill T., Reichelt M., Gershenzon J., Binder S.
Plant Cell 18:2664-2679(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE, CATALYTIC ACTIVITY, INDUCTION BY WOUNDING, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, BIOPHYSICOCHEMICAL PROPERTIES.
[7]"Tandem affinity purification and mass spectrometric analysis of ubiquitylated proteins in Arabidopsis."
Saracco S.A., Hansson M., Scalf M., Walker J.M., Smith L.M., Vierstra R.D.
Plant J. 59:344-358(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ271732 mRNA. Translation: CAB93129.1.
AP000417 Genomic DNA. Translation: BAB02558.1.
CP002686 Genomic DNA. Translation: AEE76278.1.
AY052676 mRNA. Translation: AAK96580.1.
AF446892 mRNA. Translation: AAL38625.1.
AK226525 mRNA. Translation: BAE98664.1.
PIRT52401.
RefSeqNP_188605.1. NM_112861.3.
UniGeneAt.22630.
At.25237.

3D structure databases

ProteinModelPortalQ9LE06.
SMRQ9LE06. Positions 20-350.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid6841. 1 interaction.
STRING3702.AT3G19710.1-P.

Proteomic databases

PaxDbQ9LE06.
PRIDEQ9LE06.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT3G19710.1; AT3G19710.1; AT3G19710.
GeneID821508.
KEGGath:AT3G19710.

Organism-specific databases

TAIRAT3G19710.

Phylogenomic databases

eggNOGCOG0115.
HOGENOMHOG000276704.
InParanoidQ9LE06.
KOK00826.
OMAKWEELAF.
PhylomeDBQ9LE06.

Enzyme and pathway databases

BioCycARA:AT3G19710-MONOMER.
MetaCyc:AT3G19710-MONOMER.
BRENDA2.6.1.42. 401.

Gene expression databases

GenevestigatorQ9LE06.

Family and domain databases

InterProIPR001544. Aminotrans_IV.
IPR005786. B_amino_transII.
[Graphical view]
PANTHERPTHR11825. PTHR11825. 1 hit.
PfamPF01063. Aminotran_4. 1 hit.
[Graphical view]
PIRSFPIRSF006468. BCAT1. 1 hit.
SUPFAMSSF56752. SSF56752. 1 hit.
TIGRFAMsTIGR01123. ilvE_II. 1 hit.
ProtoNetSearch...

Entry information

Entry nameBCAT4_ARATH
AccessionPrimary (citable) accession number: Q9LE06
Secondary accession number(s): Q0WW34
Entry history
Integrated into UniProtKB/Swiss-Prot: December 6, 2002
Last sequence update: October 1, 2000
Last modified: May 14, 2014
This is version 104 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names