A0AA35RAB0 · A0AA35RAB0_GEOBA
- ProteinPhosphatidylethanolamine N-methyltransferase
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids214 (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
- 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
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-dimethylethanolamine N-methyltransferase activity | |
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
- Taxonomic lineageEukaryota > Metazoa > Porifera > Demospongiae > Heteroscleromorpha > Tetractinellida > Astrophorina > Geodiidae > Geodia
Accessions
- Primary accessionA0AA35RAB0
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Endoplasmic reticulum membrane ; Multi-pass membrane protein
Mitochondrion membrane ; Multi-pass membrane protein
Membrane ; Multi-pass membrane protein
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-26 | Lumenal | ||||
Sequence: MDGGPQDNTRVRRLEEMASALELLNE | ||||||
Transmembrane | 27-49 | Helical | ||||
Sequence: LASPSVLLACPLVMLNPLIWNLI | ||||||
Topological domain | 51-62 | Lumenal | ||||
Sequence: RHEYNTRSVSRL | ||||||
Transmembrane | 70-92 | Helical | ||||
Sequence: VVLVACIVMVNNSIRTSFFHYIV | ||||||
Transmembrane | 104-123 | Helical | ||||
Sequence: NVGATIAGYVIIGVGVLLVL | ||||||
Transmembrane | 130-153 | Helical | ||||
Sequence: GFFCTFLGDYFGILLDARVTGFPF | ||||||
Topological domain | 133-175 | Lumenal | ||||
Sequence: CTFLGDYFGILLDARVTGFPFNILNHPMFWGSFLIYVGDSVLC | ||||||
Transmembrane | 165-194 | Helical | ||||
Sequence: FLIYVGDSVLCASAVAFLLSLFIGLSYVLA | ||||||
Topological domain | 197-214 | Cytoplasmic | ||||
Sequence: FEVPFTAKIYAQKETKKI |
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
- Length214
- Mass (Da)23,535
- Last updated2024-01-24 v1
- Checksum290ADE69296398AB
Keywords
- Technical term