B6SU46 · AAMT2_MAIZE
- ProteinAnthranilate O-methyltransferase 2
- GeneAAMT2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids374 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score3/5
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
- anthranilate + S-adenosyl-L-methionine = O-methyl anthranilate + S-adenosyl-L-homocysteine
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
311 μM | anthranilic acid | |||||
94 μM | S-adenosyl-L-methionine |
kcat is 0.37 sec-1 with anthranilic acid as substrate.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 18 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 25 | substrate | ||||
Sequence: Q | ||||||
Binding site | 58-60 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: GCS | ||||||
Binding site | 98 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 142-144 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: SYY | ||||||
Binding site | 164 | substrate | ||||
Sequence: W |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | S-adenosylmethionine-dependent methyltransferase activity | |
Biological Process | defense response | |
Biological Process | methylation |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameAnthranilate O-methyltransferase 2
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > Liliopsida > Poales > Poaceae > PACMAD clade > Panicoideae > Andropogonodae > Andropogoneae > Tripsacinae > Zea
Accessions
- Primary accessionB6SU46
Proteomes
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000423912 | 1-374 | Anthranilate O-methyltransferase 2 | |||
Sequence: MRIERDLHMATGDGETSYTKNSRIQEKTMFQIKPVLEEATRAVYTALHPQTMVVADLGCSSGPNTLRFVSEVIGIIARHCKEYGRQHDHTQLQFFLNDLPGNDFNNLFQLIQQFNKSTAINHKSEAAEALPPPCYISGLPGSYYTRIFPSESVHLFHSLFCLQWRSEAPEGNKKTCLDIYITKTMSPSMVKLFQQQFQKDFSLFLRLRYEELVSGGQMVLTFIGRKHENVFTGESNHLYGLLAQSLKSLVDEGLVEKEKLESFYLPMYSPSVGEVEAILKQVGLFNMNHVKVFQTNWDPYDDLESDVVHNSIRSGENVAKCLRAVMQPLVASQFGEPILDKLFKEYARRVAKHLENEKTKHAIIVLSIEKAIHL |
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 statusComplete
- Length374
- Mass (Da)42,666
- Last updated2008-12-16 v1
- Checksum23989DE46CC0F004
Keywords
- Technical term