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We are deeply saddened by the passing of Amos Bairoch (1957–2025), the creator of PROSITE. We wish to dedicate our latest paper, published shortly before his death, to him. He will always be a source of inspiration to us.
Our deepest condolences go out to his family and friends, and to all those who had the privilege of working with him. Rest in peace, Amos. Your work will live on long after you are gone.
Amos Bairoch

ProRule PRU00931


View rule in raw text format (no links)
PURL: https://purl.expasy.org/prosite/rule/PRU00931
General rule information [?]

Accession PRU00931
Dates 14-DEC-2011 (Created)
03-SEP-2024 (Last updated, Version 15)
Data class Domain;
Predictors PROSITE; PS51599; SAM_PEMT_PEM2
Name Phospholipid methyltransferases (EC 2.1.1.17 and EC=2.1.1.71) family
Function Phosphatidylethanolamine N-methyltransferase (EC 2.1.1.17) is an enzyme that transfers a methyl group from S-adenosyl-L-methionine (SAM) to phosphatidylethanolamine to form phosphatidyl-N-methylethanolamine and S- adenosyl-L-homocysteine. Phosphatidyl-N-methylethanolamine N-methyltransferase (EC 2.1.1.71) is an enzyme that transfers a methyl group from S-adenosyl-L-methionine (SAM) to phosphatidyl-N-methylethanolamine to form phosphatidyl-N- dimethylethanolamine and S-adenosyl-L-homocysteine. It also transfers a methyl group from S-adenosyl-L-methionine (SAM) to phosphatidyl-N- dimethylethanolamine to form phosphatidylcholine and S-adenosyl-L- homocysteine.
Scope(s) Eukaryota
Example(s) Q08388;

Propagated annotation [?]

Identifier, protein and gene names [?]

Protein name + RecName: EC=2.1.1.17;
+ RecName: EC=2.1.1.71;

Comments [?]

FUNCTIONCatalyzes three sequential methylation reactions of phosphatidylethanolamine (PE) by AdoMet, thereby producing phosphatidylcholine (PC).
CATALYTIC ACTIVITY Reaction=a 1,2-diacyl-sn-glycero-3-phospho-N-methylethanolamine + S- adenosyl-L-methionine = a 1,2-diacyl-sn-glycero-3-phospho-N,N- dimethylethanolamine + S-adenosyl-L-homocysteine + H(+); Xref=Rhea:RHEA:32735, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:64572, ChEBI:CHEBI:64573; EC=2.1.1.71;
CATALYTIC ACTIVITY Reaction=a 1,2-diacyl-sn-glycero-3-phospho-N,N-dimethylethanolamine + S-adenosyl-L-methionine = a 1,2-diacyl-sn-glycero-3-phosphocholine + S-adenosyl-L-homocysteine + H(+); Xref=Rhea:RHEA:32739, ChEBI:CHEBI:15378, ChEBI:CHEBI:57643, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:64572;
CATALYTIC ACTIVITY Reaction=a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + S-adenosyl-L- methionine = a 1,2-diacyl-sn-glycero-3-phospho-N-methylethanolamine + S-adenosyl-L-homocysteine + H(+); Xref=Rhea:RHEA:11164, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:64573, ChEBI:CHEBI:64612; EC=2.1.1.17;
PATHWAYPhospholipid metabolism; phosphatidylcholine biosynthesis.
SIMILARITYBelongs to the class VI-like SAM-binding methyltransferase superfamily. PEMT/PEM2 methyltransferase family.

Keywords [?]

Methyltransferase
S-adenosyl-L-methionine
Transferase
Lipid biosynthesis
Lipid metabolism
Phospholipid biosynthesis
Phospholipid metabolism

Gene Ontology [?]

GO:0004608; Molecular function:phosphatidylethanolamine N-methyltransferase activity
GO:0000773; Molecular function:phosphatidyl-N-methylethanolamine N-methyltransferase activity
GO:0006656; Biological process:phosphatidylcholine biosynthetic process

Features [?]


Additional information [?]

Size range 174-211 amino acids
Related rules None
Fusion None
Repeats 1
Topology Undefined

Copyright

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 [?]