UniProt ID: Q7ZVZ2 |
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. {ECO:0000256|HAMAP-Rule:MF_03216}. CATALYTIC ACTIVITY: Reaction=1,2-diacyl-sn-glycero-3-phospho-N,N-dimethylethanolamine + S- adenosyl-L-methionine = a 1,2-diacyl-sn-glycero-3-phosphocholine + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:32739, ChEBI:CHEBI:15378, ChEBI:CHEBI:57643, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:64572; Evidence={ECO:0000256|HAMAP- Rule:MF_03216}; CATALYTIC ACTIVITY: Reaction=1,2-diacyl-sn-glycero-3-phospho-N-methylethanolamine + S- adenosyl-L-methionine = 1,2-diacyl-sn-glycero-3-phospho-N,N- dimethylethanolamine + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:32735, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:64572, ChEBI:CHEBI:64573; EC=2.1.1.71; Evidence={ECO:0000256|HAMAP-Rule:MF_03216}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + S-adenosyl-L- methionine = 1,2-diacyl-sn-glycero-3-phospho-N-methylethanolamine + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:11164, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:64573, ChEBI:CHEBI:64612; EC=2.1.1.17; Evidence={ECO:0000256|HAMAP-Rule:MF_03216}; PATHWAY: Lipid metabolism. {ECO:0000256|ARBA:ARBA00005189}. PATHWAY: Phospholipid metabolism; phosphatidylcholine biosynthesis. {ECO:0000256|ARBA:ARBA00004969, ECO:0000256|HAMAP-Rule:MF_03216}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000256|HAMAP-Rule:MF_03216}; Multi-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_03216}. Mitochondrion membrane {ECO:0000256|HAMAP-Rule:MF_03216}; Multi-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_03216}. Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. Note=Found in endoplasmic reticulum where most PEMT activity is generated and in mitochondria. {ECO:0000256|HAMAP-Rule:MF_03216}. SIMILARITY: Belongs to the class VI-like SAM-binding methyltransferase superfamily. PEMT/PEM2 methyltransferase family. {ECO:0000256|HAMAP- Rule:MF_03216}. |
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