B6SU46 · AAMT2_MAIZE

  • Protein
    Anthranilate O-methyltransferase 2
  • Gene
    AAMT2
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    3/5

Function

function

Methyltransferase involved in the biosynthesis of methyl anthranilate in response to stresses. Utilizes anthranilic acid as substrate. Produces exclusively the O-methyl ester.

Catalytic activity

Kinetics

KM SUBSTRATE pH TEMPERATURE[C] NOTES EVIDENCE
311 μManthranilic acid
94 μMS-adenosyl-L-methionine
kcat is 0.37 sec-1 with anthranilic acid as substrate.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site18S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site25substrate
Binding site58-60S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site98S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site142-144S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site164substrate

GO annotations

AspectTerm
Molecular FunctionS-adenosylmethionine-dependent methyltransferase activity
Biological Processdefense response
Biological Processmethylation

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Anthranilate O-methyltransferase 2
  • EC number
  • Alternative names
    • Anthranilic acid methyltransferase 2
    • Benzoate carboxyl methyltransferase
    • O-methyltransferase 2

Gene names

    • Name
      AAMT2
    • Synonyms
      OMT2

Organism names

  • Taxonomic identifier
  • Strain
    • cv. Delprim
  • Taxonomic lineage
    Eukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > Liliopsida > Poales > Poaceae > PACMAD clade > Panicoideae > Andropogonodae > Andropogoneae > Tripsacinae > Zea

Accessions

  • Primary accession
    B6SU46

Proteomes

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00004239121-374Anthranilate O-methyltransferase 2

Proteomic databases

Expression

Induction

Slightly up-regulated by herbivory and jasmonic acid, but not by salicylic acid.

Gene expression databases

Interaction

Protein-protein interaction databases

Structure

Family & Domains

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    374
  • Mass (Da)
    42,666
  • Last updated
    2008-12-16 v1
  • Checksum
    23989DE46CC0F004
MRIERDLHMATGDGETSYTKNSRIQEKTMFQIKPVLEEATRAVYTALHPQTMVVADLGCSSGPNTLRFVSEVIGIIARHCKEYGRQHDHTQLQFFLNDLPGNDFNNLFQLIQQFNKSTAINHKSEAAEALPPPCYISGLPGSYYTRIFPSESVHLFHSLFCLQWRSEAPEGNKKTCLDIYITKTMSPSMVKLFQQQFQKDFSLFLRLRYEELVSGGQMVLTFIGRKHENVFTGESNHLYGLLAQSLKSLVDEGLVEKEKLESFYLPMYSPSVGEVEAILKQVGLFNMNHVKVFQTNWDPYDDLESDVVHNSIRSGENVAKCLRAVMQPLVASQFGEPILDKLFKEYARRVAKHLENEKTKHAIIVLSIEKAIHL

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
HM242246
EMBL· GenBank· DDBJ
ADI87451.1
EMBL· GenBank· DDBJ
mRNA
EU956261
EMBL· GenBank· DDBJ
ACG28379.1
EMBL· GenBank· DDBJ
mRNA

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp