HAMAP rule MF_03216
General rule information
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Accession | MF_03216 |
Dates | 7-JUL-2016 (Created)
3-SEP-2024 (Last updated, Version 10) |
Name | PLMT |
Scope(s) |
Eukaryota |
Template(s) | Q9UBM1 (PEMT_HUMAN); P05375 (PLMT_YEAST); Q7S5W9 (PLMT_NEUCR); Q61907 (PEMT_MOUSE); [ Recover all ] |
Triggered by |
HAMAP; MF_03216 (Get profile general information and statistics) |
Propagated annotation
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Identifier, protein and gene names
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case <OC:Fungi> or <OC:Viridiplantae> | |
Identifier | PLMT |
Protein name | RecName: Full=Phosphatidyl-N-methylethanolamine N-methyltransferase; EC=2.1.1.71; AltName: Full=Phospholipid methyltransferase; Short=PLMT; |
else | |
Identifier | PEMT |
Protein name | RecName: Full=Phosphatidylethanolamine N-methyltransferase; Short=PEAMT; Short=PEMT; EC=2.1.1.17; EC=2.1.1.71; AltName: Full=Phospholipid methyltransferase; Short=PLMT; |
end case | |
case <OC:Vertebrata> | |
Gene name | Name=PEMT; |
end case |
Comments
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case <OC:Fungi> or <OC:Viridiplantae> | |
FUNCTION | Catalyzes the second two steps of the methylation pathway of phosphatidylcholine biosynthesis, the SAM-dependent methylation of phosphatidylmonomethylethanolamine (PMME) to phosphatidyldimethylethanolamine (PDME) and of PDME to phosphatidylcholine (PC). |
else | |
FUNCTION | Catalyzes the three sequential steps of the methylation pathway for the biosynthesis of phosphatidylcholine, a critical and essential component for membrane structure. Uses S-adenosylmethionine (S-adenosyl-L-methionine, SAM or AdoMet) as the methyl group donor for the methylation of phosphatidylethanolamine (1,2-diacyl-sn-glycero-3- phosphoethanolamine, PE) to phosphatidylmonomethylethanolamine (1,2- diacyl-sn-glycero-3-phospho-N-methylethanolamine, PMME), PMME to phosphatidyldimethylethanolamine (1,2-diacyl-sn-glycero-3-phospho-N,N- dimethylethanolamine, PDME), and PDME to phosphatidylcholine (1,2- diacyl-sn-glycero-3-phosphocholine, PC), producing S-adenosyl-L- homocysteine in each step. |
end case | |
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; |
case not (<OC:Fungi> or <OC:Viridiplantae>) | |
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; |
end case | |
PATHWAY | Phospholipid metabolism; phosphatidylcholine biosynthesis. |
case <OC:Vertebrata> | |
SUBCELLULAR LOCATION | Endoplasmic reticulum membrane; Multi-pass membrane protein. Mitochondrion membrane; Multi-pass membrane protein. Note=Found in endoplasmic reticulum where most PEMT activity is generated and in mitochondria. |
else case <OC:Viridiplantae> | |
SUBCELLULAR LOCATION | Endoplasmic reticulum membrane; Multi-pass membrane protein. |
else | |
SUBCELLULAR LOCATION | Endoplasmic reticulum membrane; Multi-pass membrane protein. Mitochondrion membrane; Multi-pass membrane protein. |
end case | |
SIMILARITY | Belongs to the class VI-like SAM-binding methyltransferase superfamily. PEMT/PEM2 methyltransferase family. |
Keywords
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Gene Ontology
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GO:0005789; Cellular component:endoplasmic reticulum membrane | |
case not <OCellular component:Viridiplantae> | |
GO:0031966; Cellular component:mitochondrial membrane | |
end case | |
GO:0000773; Molecular function:phosphatidyl-N-methylethanolamine N-methyltransferase activity | |
case not <OCellular component:Fungi> | |
GO:0004608; Molecular function:phosphatidylethanolamine N-methyltransferase activity | |
end case | |
GO:0006656; Biological process:phosphatidylcholine biosynthetic process |
Cross-references
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PROSITE | PS51599; SAM_PEMT_PEM2; 1; |
PROSITE | PS50244; S5A_REDUCTASE; 1; |
Pfam | PF04191; PEMT; 1; |
PIRSF | PIRSF005444; PEMT; 1; |
Features
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From: PEMT_HUMAN (Q9UBM1) | ||||||||||||
Key | From | To | Description | Tag | Condition | FTGroup | ||||||
TOPO_DOM | Nter | 12 | /note="Lumenal" | |||||||||
INTRAMEM | 13 | 33 | /note="Helical" | |||||||||
TOPO_DOM | 34 | 45 | /note="Lumenal" | |||||||||
TRANSMEM | 46 | 66 | /note="Helical" | |||||||||
TOPO_DOM | 67 | 93 | /note="Cytoplasmic" | |||||||||
TRANSMEM | 94 | 114 | /note="Helical" | |||||||||
TOPO_DOM | 115 | 157 | /note="Lumenal" | |||||||||
TRANSMEM | 158 | 178 | /note="Helical" | |||||||||
TOPO_DOM | 179 | Cter | /note="Cytoplasmic" | |||||||||
BINDING | 98 | 100 | /ligand="S-adenosyl-L-methionine" /ligand_id="ChEBI:CHEBI:59789" |
x(2)-G | ||||||||
BINDING | 180 | 181 | /ligand="S-adenosyl-L-methionine" /ligand_id="ChEBI:CHEBI:59789" |
E-x |
Additional information
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Size range | 164-248 amino acids |
Related rules |
None |
Fusion | Nter: None Cter: None |