ProRule PRU00932
General rule information
[?]
Accession | PRU00932 |
Dates | 6-MAR-2012 (Created)
19-NOV-2022 (Last updated, Version 13) |
Data class | Domain; |
Predictors |
PROSITE; PS51600; SAM_GNMT |
Name | Glycine and glycine/sarcosine N-methyltransferase |
Function | Glycine N-methyltransferase (EC 2.1.1.20) is an enzyme that transfers a methyl group from S-adenosyl-L-methionine (SAM) to glycine to form sarcosine and S-adenosyl-L-homocysteine. Glycine/sarcosine N-methyltransferase (EC 2.1.1.156) is an enzyme that transfers a methyl group from S-adenosyl-L-methionine (SAM) to glycine to form sarcosine and S-adenosyl-L-homocysteine AND transfers a methyl group from S-adenosyl-L-methionine (SAM) to sarcosine to form N,N-dimethylglycine and S-adenosyl-L-homocysteine. |
Scope(s) |
Eukaryota Eutheria Bacteria |
Example(s) | P13255 (GNMT_RAT); |
Propagated annotation
[?]
Identifier, protein and gene names
[?]
case <FTGroup:1> and (<OC:Bacteria> or <OC:Archaea>) | |
Protein name | + RecName: EC=2.1.1.156; |
else case <FTGroup:1> | |
Protein name | + RecName: EC=2.1.1.20; |
end case |
Comments
[?]
case <FTGroup:1> and (<OC:Bacteria> or <OC:Archaea>) | |
CATALYTIC ACTIVITY | Reaction=glycine + 2 S-adenosyl-L-methionine = 2 H(+) + N,N- dimethylglycine + 2 S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:32463, ChEBI:CHEBI:15378, ChEBI:CHEBI:57305, ChEBI:CHEBI:57856, ChEBI:CHEBI:58251, ChEBI:CHEBI:59789; EC=2.1.1.156; |
else case <FTGroup:1> | |
CATALYTIC ACTIVITY | Reaction=glycine + S-adenosyl-L-methionine = H(+) + S-adenosyl-L- homocysteine + sarcosine; Xref=Rhea:RHEA:19937, ChEBI:CHEBI:15378, ChEBI:CHEBI:57305, ChEBI:CHEBI:57433, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789; EC=2.1.1.20; |
end case | |
SIMILARITY | Belongs to the class I-like SAM-binding methyltransferase superfamily. Glycine N-methyltransferase family. |
Keywords
[?]
case <FTGroup:1> | |
Methyltransferase | |
S-adenosyl-L-methionine | |
Transferase | |
end case |
Gene Ontology
[?]
case <FTGroup:1> | |
GO:0017174; Molecular function:glycine N-methyltransferase activity | |
end case | |
case <FTGroup:1> and (<OCellular component:Bacteria> or <OC:Archaea>) | |
GO:0052730; Molecular function:sarcosine N-methyltransferase activity | |
end case | |
case <FTGroup:1> | |
GO:0032259; Biological process:methylation | |
GO:0046500; Biological process:S-adenosylmethionine metabolic process | |
end case |
Features
[?]
From: PS51600 | ||||||||||||
Key | From | To | Description | Tag | Condition | FTGroup | ||||||
case <FTGroup:1> | ||||||||||||
BINDING | 122 | 123 | /ligand="S-adenosyl-L-methionine" /ligand_id="ChEBI:CHEBI:59789" |
[DN]-W | ||||||||
end case | ||||||||||||
BINDING | 27 | 27 | /ligand="S-adenosyl-L-methionine" /ligand_id="ChEBI:CHEBI:59789" |
Y | 1 | |||||||
case <FTGroup:1> | ||||||||||||
BINDING | 36 | 36 | /ligand="S-adenosyl-L-methionine" /ligand_id="ChEBI:CHEBI:59789" |
[WY] | ||||||||
BINDING | 39 | 39 | /ligand="substrate" | Y | ||||||||
BINDING | 46 | 46 | /ligand="S-adenosyl-L-methionine" /ligand_id="ChEBI:CHEBI:59789" |
R | ||||||||
BINDING | 70 | 70 | /ligand="S-adenosyl-L-methionine" /ligand_id="ChEBI:CHEBI:59789" |
[AS] | ||||||||
BINDING | 91 | 91 | /ligand="S-adenosyl-L-methionine" /ligand_id="ChEBI:CHEBI:59789" |
D | ||||||||
BINDING | 143 | 143 | /ligand="S-adenosyl-L-methionine" /ligand_id="ChEBI:CHEBI:59789" |
[FMLQ] | ||||||||
BINDING | 145 | 145 | /ligand="substrate" | [NS] | ||||||||
end case | ||||||||||||
BINDING | 179 | 179 | /ligand="substrate" | R | 1 | |||||||
case <FTGroup:1> | ||||||||||||
BINDING | 223 | 223 | /ligand="substrate" | |||||||||
end case |
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.
UniProtKB rule member sequences
[?]
- UniProtKB/Swiss-Prot sets
Bacteria [4] Eukaryota [5] All [ 9 ]
- Retrieve set of proteins with 3D structure for this domain