ProRule PRU00948
General rule information
[?]
| Accession | PRU00948 |
| Dates | 14-DEC-2011 (Created)
19-NOV-2022 (Last updated, Version 10) |
| Data class | Domain; |
| Predictors |
case c? <Length>=211> and <Length<=317>
PROSITE; PS51616; SAM_NNMT_PNMT_TEMT_2 end case
|
Name | Amine N-methyltransferase |
| Function | Amine N-methyltransferase (EC 2.1.1.49) is an enzyme that transfers a methyl group from S-adenosyl-L-methionine (SAM) to an amine to form a methylated amine and S-adenosyl-L-homocysteine. |
| Scope(s) |
Eukaryota Euarchontoglires |
| Example(s) | O97972 (INMT_RABIT); |
Propagated annotation
[?]
Identifier, protein and gene names
[?]
| Protein name | + RecName: EC=2.1.1.49; |
Comments
[?]
| CATALYTIC ACTIVITY | Reaction=a tertiary amine + S-adenosyl-L-methionine = a methylated tertiary amine + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:53928, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:137982, ChEBI:CHEBI:137983; EC=2.1.1.49; |
| CATALYTIC ACTIVITY | Reaction=a secondary amine + S-adenosyl-L-methionine = a methylated secondary amine + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:53924, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:137419, ChEBI:CHEBI:137984; EC=2.1.1.49; |
| CATALYTIC ACTIVITY | Reaction=a primary amine + S-adenosyl-L-methionine = a methylated primary amine + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:23136, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:65296, ChEBI:CHEBI:131823; EC=2.1.1.49; |
| SIMILARITY | Belongs to the class I-like SAM-binding methyltransferase superfamily. NNMT/PNMT/TEMT family. |
Keywords
[?]
Gene Ontology
[?]
| GO:0030748; Molecular function:amine N-methyltransferase activity |
| GO:0032259; Biological process:methylation |
| GO:0046500; Biological process:S-adenosylmethionine metabolic process |
Features
[?]
| From: PS51616 | ||||||||||||
| Key | From | To | Description | Tag | Condition | FTGroup | ||||||
| BINDING | 64 | 65 | /ligand="S-adenosyl-L-methionine" /ligand_id="ChEBI:CHEBI:59789" |
|||||||||
| BINDING | 143 | 144 | /ligand="S-adenosyl-L-methionine" /ligand_id="ChEBI:CHEBI:59789" |
|||||||||
| BINDING | 21 | 21 | /ligand="S-adenosyl-L-methionine" /ligand_id="ChEBI:CHEBI:59789" |
Y | ||||||||
| BINDING | 26 | 26 | /ligand="S-adenosyl-L-methionine" /ligand_id="ChEBI:CHEBI:59789" |
Y | ||||||||
| BINDING | 70 | 70 | /ligand="S-adenosyl-L-methionine" /ligand_id="ChEBI:CHEBI:59789" |
Y | ||||||||
| BINDING | 86 | 86 | /ligand="S-adenosyl-L-methionine" /ligand_id="ChEBI:CHEBI:59789" |
D | ||||||||
| BINDING | 91 | 91 | /ligand="S-adenosyl-L-methionine" /ligand_id="ChEBI:CHEBI:59789" |
N | ||||||||
| BINDING | 164 | 164 | /ligand="S-adenosyl-L-methionine" /ligand_id="ChEBI:CHEBI:59789" |
[FLT] | ||||||||
Additional information
[?]
| Size range | unlimited amino acids |
| Related rules |
None |
| Fusion | None |
| Repeats | 1 |
| Topology | Undefined |
PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see prosite_license.html.