I3V6A7 · SOMT1_PAPSO
- ProteinScoulerine-9-O-methyltransferase 1
- GeneSOMT1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids390 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Methyltransferase involved in the biosynthesis of the benzylisoquinoline alkaloid noscapine (PubMed:22535422, PubMed:22653730, PubMed:29610307).
Catalyzes the conversion of (S)-scoulerine to (S)-tetrahydrocolumbamine (PubMed:22535422, PubMed:22653730).
Can convert (S)-tetrahydrocolumbamine to tetrahydropalmatine (PubMed:22535422).
Can convert (S)-norreticuline to (S)-norcodamine (PubMed:22535422).
Can convert (S)-reticuline to (S)-codamine (PubMed:22535422).
Substrate preference is (S)-scoulerine > (S)-tetrahydrocolumbamine > (S)-norreticuline > (S)-reticuline (PubMed:22535422).
Catalyzes the conversion of (S)-scoulerine to (S)-tetrahydrocolumbamine (PubMed:22535422, PubMed:22653730).
Can convert (S)-tetrahydrocolumbamine to tetrahydropalmatine (PubMed:22535422).
Can convert (S)-norreticuline to (S)-norcodamine (PubMed:22535422).
Can convert (S)-reticuline to (S)-codamine (PubMed:22535422).
Substrate preference is (S)-scoulerine > (S)-tetrahydrocolumbamine > (S)-norreticuline > (S)-reticuline (PubMed:22535422).
Catalytic activity
- (S)-scoulerine + S-adenosyl-L-methionine = (S)-tetrahydrocolumbamine + H+ + S-adenosyl-L-homocysteineThis reaction proceeds in the forward direction.
- (S)-norreticuline + S-adenosyl-L-methionine = (S)-norcodamine + H+ + S-adenosyl-L-homocysteineThis reaction proceeds in the forward direction.
- (S)-reticuline + S-adenosyl-L-methionine = (S)-codamine + H+ + S-adenosyl-L-homocysteineThis reaction proceeds in the forward direction.
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
28.5 μM | (S)-scoulerine | |||||
70.3 μM | (S)-reticuline | |||||
19 μM | S-adenosyl-L-methionine |
Vmax | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|
2036 nmol/min/mg | with (S)-scoulerine as substrate | ||||
184.4 nmol/min/mg | with (S)-reticuline as substrate | ||||
1290 nmol/min/mg | with S-adenosyl-L-methionine as substrate |
Pathway
Alkaloid biosynthesis.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 153 | substrate | ||||
Sequence: E | ||||||
Binding site | 207 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: M | ||||||
Binding site | 211 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 235 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 258 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 278-279 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: DM | ||||||
Binding site | 292 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Active site | 296 | Proton acceptor | ||||
Sequence: H | ||||||
Binding site | 296-297 | substrate | ||||
Sequence: HD |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | (S)-scoulerine 9-O-methyltransferase activity | |
Molecular Function | methyltransferase activity | |
Molecular Function | O-methyltransferase activity | |
Molecular Function | protein dimerization activity | |
Molecular Function | tetrahydrocolumbamine 2-O-methyltransferase activity | |
Biological Process | benzyl isoquinoline alkaloid biosynthetic process | |
Biological Process | methylation |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameScoulerine-9-O-methyltransferase 1
- EC number
- Short namesPsSOMT1
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > Ranunculales > Papaveraceae > Papaveroideae > Papaver
Accessions
- Primary accessionI3V6A7
- Secondary accessions
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 296 | Loss of enzymatic activity. | ||||
Sequence: H → A |
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000447591 | 1-390 | Scoulerine-9-O-methyltransferase 1 | |||
Sequence: MATNGEIFNTYGHNRQTATVTKITASNESSNGVCYLSETANLGKLICIPMALRAAMELNVFQLISKFGTDAKVSASEIASKMPNAKNNPEAAMYLDRILRLLGASSILSVSTTKKSINRGGDDVVVHEKLYGLTNSSCCLVPRQEDGVSLVEELLFTSDKVVVDSFFKLKCVVEEKDSVPFEVAHGAKIFEYAATEPRMNQVFNDGMAVFSIVVFEAVFRFYDGFLDMKELLDVGGGIGTSVSKIVAKYPLIRGVNFDLPHVISVAPQYPGVEHVAGDMFEEVPKGQNMLLKWVLHDWGDERCVKLLKNCWNSLPVGGKVLIIEFVLPNELGNNAESFNALIPDLLLMALNPGGKERTISEYDDLGKAAGFIKTIPIPISNGLHVIEFHK |
Interaction
Subunit
Homodimer.
Structure
Family & Domains
Sequence similarities
Belongs to the class I-like SAM-binding methyltransferase superfamily. Cation-independent O-methyltransferase family. COMT subfamily.
Family and domain databases
Sequence
- Sequence statusComplete
- Length390
- Mass (Da)42,699
- Last updated2012-09-05 v1
- ChecksumC3E59F1D7F78BE01
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 15-17 | in Ref. 2; AFB74611 | ||||
Sequence: RQT → HQS | ||||||
Sequence conflict | 221 | in Ref. 2; AFB74611 | ||||
Sequence: F → V |
Keywords
- Technical term