A0A9C7PRP0 · A0A9C7PRP0_9RHOD
- ProteinPhosphatidylethanolamine N-methyltransferase
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids240 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
Function
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.
Catalytic activity
- 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+
Pathway
Lipid metabolism.
Phospholipid metabolism; phosphatidylcholine biosynthesis.
Features
Showing features for binding site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | endoplasmic reticulum membrane | |
Cellular Component | mitochondrial membrane | |
Molecular Function | phosphatidyl-N-methylethanolamine N-methyltransferase activity | |
Molecular Function | phosphatidylethanolamine N-methyltransferase activity | |
Biological Process | methylation | |
Biological Process | phosphatidylcholine biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePhosphatidylethanolamine N-methyltransferase
- EC number
- Short namesPEAMT ; PEMT
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Rhodophyta > Bangiophyceae > Galdieriales > Galdieriaceae > Galdieria
Accessions
- Primary accessionA0A9C7PRP0
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Endoplasmic reticulum membrane ; Multi-pass membrane protein
Mitochondrion membrane ; Multi-pass membrane protein
Features
Showing features for topological domain, intramembrane, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-52 | Lumenal | ||||
Sequence: MEMDLTVAKNNLKQVYHFIDAILSKRDYPLVQLLLHFFESLHLRSSVINFYD | ||||||
Intramembrane | 53-73 | Helical | ||||
Sequence: PKLARALIYTTLAPIIWNILA | ||||||
Transmembrane | 55-72 | Helical | ||||
Sequence: LARALIYTTLAPIIWNIL | ||||||
Topological domain | 74-85 | Lumenal | ||||
Sequence: RLEYFFHIISFL | ||||||
Transmembrane | 78-106 | Helical | ||||
Sequence: FFHIISFLFFGKRMGCYVLALWILLFSLY | ||||||
Topological domain | 107-133 | Cytoplasmic | ||||
Sequence: RDLLVMEAIQVQPTLKYLEETHLVALA | ||||||
Transmembrane | 127-149 | Helical | ||||
Sequence: THLVALAYILGALGGILVITSFL | ||||||
Topological domain | 155-197 | Lumenal | ||||
Sequence: GTFLGDYFGIYLEEKVSGFPFSFCSNPMYDGSTLLFISKALLA | ||||||
Transmembrane | 190-211 | Helical | ||||
Sequence: FISKALLASSPAGLLLAFWVYV | ||||||
Topological domain | 219-240 | Cytoplasmic | ||||
Sequence: FEEPFTDYIYRYRATNQAKKKR |
Keywords
- Cellular component
Structure
Family & Domains
Sequence similarities
Belongs to the class VI-like SAM-binding methyltransferase superfamily. PEMT/PEM2 methyltransferase family.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Length240
- Mass (Da)27,781
- Last updated2023-05-03 v1
- ChecksumECA5A3386C4647F7