A0A175JDR5 · A0A175JDR5_ENTHI
- ProteinPhosphatidylethanolamine N-methyltransferase
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids205 (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 > Amoebozoa > Evosea > Archamoebae > Mastigamoebida > Entamoebidae > Entamoeba
Accessions
- Primary accessionA0A175JDR5
Proteomes
Organism-specific databases
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 | 1-7 | Lumenal | ||||
Sequence: MFEFVMD | ||||||
Intramembrane | 8-28 | Helical | ||||
Sequence: QYATLSALFIFASPAVWNTLA | ||||||
Transmembrane | 12-30 | Helical | ||||
Sequence: LSALFIFASPAVWNTLAHI | ||||||
Topological domain | 29-40 | Lumenal | ||||
Sequence: HIEYFTHKISQL | ||||||
Transmembrane | 51-70 | Helical | ||||
Sequence: FVMCIIISMQIIRNIFFYIA | ||||||
Transmembrane | 90-112 | Helical | ||||
Sequence: TLVNIVAIPIQIFGWVLSISSFY | ||||||
Topological domain | 118-160 | Lumenal | ||||
Sequence: GTYEGDCFGFLFDEMITSFPFGFVPHPMYFGGALLFISSALYY | ||||||
Transmembrane | 168-192 | Helical | ||||
Sequence: LSIWSIVVYCIFSYLVEQPLTILIY | ||||||
Topological domain | 183-205 | Cytoplasmic | ||||
Sequence: VEQPLTILIYSNKKTQHDEKKEE |
Keywords
- Cellular component
Structure
Sequence
- Sequence statusComplete
- Length205
- Mass (Da)23,486
- Last updated2016-09-07 v1
- ChecksumD99470E97D34796B
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
BDEQ01000001 EMBL· GenBank· DDBJ | GAT91624.1 EMBL· GenBank· DDBJ | Genomic DNA |