AC   MF_03216;
DC   Protein; auto
TR   HAMAP; MF_03216; -; 1; level=0
XX
Names: PLMT
XX
case <OC:Fungi> or <OC:Viridiplantae>
ID   PLMT
DE   RecName: Full=Phosphatidyl-N-methylethanolamine N-methyltransferase;
DE            EC=2.1.1.71;
DE   AltName: Full=Phospholipid methyltransferase;
DE            Short=PLMT;
else
ID   PEMT
DE   RecName: Full=Phosphatidylethanolamine N-methyltransferase;
DE            Short=PEAMT;
DE            Short=PEMT;
DE            EC=2.1.1.17;
DE            EC=2.1.1.71;
DE   AltName: Full=Phospholipid methyltransferase;
DE            Short=PLMT;
end case
case <OC:Vertebrata>
GN   Name=PEMT;
end case
XX
case <OC:Fungi> or <OC:Viridiplantae>
CC   -!- FUNCTION: Catalyzes the second two steps of the methylation pathway of
CC       phosphatidylcholine biosynthesis, the SAM-dependent methylation of
CC       phosphatidylmonomethylethanolamine (PMME) to
CC       phosphatidyldimethylethanolamine (PDME) and of PDME to
CC       phosphatidylcholine (PC).
else
CC   -!- FUNCTION: Catalyzes the three sequential steps of the methylation
CC       pathway for the biosynthesis of phosphatidylcholine, a critical and
CC       essential component for membrane structure. Uses S-adenosylmethionine
CC       (S-adenosyl-L-methionine, SAM or AdoMet) as the methyl group donor for
CC       the methylation of phosphatidylethanolamine (1,2-diacyl-sn-glycero-3-
CC       phosphoethanolamine, PE) to phosphatidylmonomethylethanolamine (1,2-
CC       diacyl-sn-glycero-3-phospho-N-methylethanolamine, PMME), PMME to
CC       phosphatidyldimethylethanolamine (1,2-diacyl-sn-glycero-3-phospho-N,N-
CC       dimethylethanolamine, PDME), and PDME to phosphatidylcholine (1,2-
CC       diacyl-sn-glycero-3-phosphocholine, PC), producing S-adenosyl-L-
CC       homocysteine in each step.
end case
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1,2-diacyl-sn-glycero-3-phospho-N-methylethanolamine + S-
CC         adenosyl-L-methionine = 1,2-diacyl-sn-glycero-3-phospho-N,N-
CC         dimethylethanolamine + H(+) + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:32735, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:64572, ChEBI:CHEBI:64573; EC=2.1.1.71;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1,2-diacyl-sn-glycero-3-phospho-N,N-dimethylethanolamine + S-
CC         adenosyl-L-methionine = a 1,2-diacyl-sn-glycero-3-phosphocholine +
CC         H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:32739,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57643, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:64572;
case not (<OC:Fungi> or <OC:Viridiplantae>)
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + S-adenosyl-L-
CC         methionine = 1,2-diacyl-sn-glycero-3-phospho-N-methylethanolamine +
CC         H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:11164,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:64573, ChEBI:CHEBI:64612; EC=2.1.1.17;
end case
CC   -!- PATHWAY: Phospholipid metabolism; phosphatidylcholine biosynthesis.
case <OC:Vertebrata>
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass
CC       membrane protein. Mitochondrion membrane; Multi-pass membrane protein.
CC       Note=Found in endoplasmic reticulum where most PEMT activity is
CC       generated and in mitochondria.
else case <OC:Viridiplantae>
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass
CC       membrane protein.
else
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass
CC       membrane protein. Mitochondrion membrane; Multi-pass membrane protein.
end case
CC   -!- SIMILARITY: Belongs to the class VI-like SAM-binding methyltransferase
CC       superfamily. PEMT/PEM2 methyltransferase family.
XX
DR   PROSITE; PS51599; SAM_PEMT_PEM2; 1; trigger=no
DR   PROSITE; PS50244; S5A_REDUCTASE; 1; trigger=no
DR   Pfam; PF04191; PEMT; 1; trigger=no
DR   PIRSF; PIRSF005444; PEMT; 1; trigger=no
XX
KW   Endoplasmic reticulum
KW   Lipid biosynthesis
KW   Lipid metabolism
KW   Membrane
KW   Methyltransferase
case not <OC:Viridiplantae>
KW   Mitochondrion
end case
KW   Phospholipid biosynthesis
KW   Phospholipid metabolism
KW   S-adenosyl-L-methionine
KW   Transferase
KW   Transmembrane
KW   Transmembrane helix
XX
GO   GO:0005789; C:endoplasmic reticulum membrane
case not <OC:Viridiplantae>
GO   GO:0031966; C:mitochondrial membrane
end case
GO   GO:0080101; F:phosphatidyl-N-dimethylethanolamine N-methyltransferase activity
GO   GO:0000773; F:phosphatidyl-N-methylethanolamine N-methyltransferase activity
case not <OC:Fungi>
GO   GO:0004608; F:phosphatidylethanolamine N-methyltransferase activity
end case
GO   GO:0006656; P:phosphatidylcholine biosynthetic process
XX
FT   From: PEMT_HUMAN (Q9UBM1)
FT   TOPO_DOM        Nter..12
FT                   /note="Lumenal"
FT   INTRAMEM        13..33
FT                   /note="Helical"
FT   TOPO_DOM        34..45
FT                   /note="Lumenal"
FT   TRANSMEM        46..66
FT                   /note="Helical"
FT   TOPO_DOM        67..93
FT                   /note="Cytoplasmic"
FT   TRANSMEM        94..114
FT                   /note="Helical"
FT   TOPO_DOM        115..157
FT                   /note="Lumenal"
FT   TRANSMEM        158..178
FT                   /note="Helical"
FT   TOPO_DOM        179..Cter
FT                   /note="Cytoplasmic"
FT   BINDING         98..100
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT   Condition: x(2)-G
FT   BINDING         180..181
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT   Condition: E-x
XX
Size: 164-248;
Related: None;
Template: Q9UBM1; P05375; Q7S5W9; Q61907;
Scope:
 Eukaryota
Fusion:
 Nter: None
 Cter: None
Duplicate: None
Plasmid: None
Comments: None
XX
# Revision 1.8 2022/11/19
//