A0A0E9NMF1 · A0A0E9NMF1_SAICN
- ProteinPhosphatidyl-N-methylethanolamine N-methyltransferase
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids407 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
Function
function
Catalyzes the second two steps of the methylation pathway of phosphatidylcholine biosynthesis, the SAM-dependent methylation of phosphatidylmonomethylethanolamine (PMME) to phosphatidyldimethylethanolamine (PDME) and of PDME to phosphatidylcholine (PC).
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 | |
Biological Process | methylation | |
Biological Process | phosphatidylcholine biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePhosphatidyl-N-methylethanolamine N-methyltransferase
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Taphrinomycotina > Taphrinomycotina incertae sedis > Saitoella
Accessions
- Primary accessionA0A0E9NMF1
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, intramembrane, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-26 | Lumenal | ||||
Sequence: MADLDKYLLLTKFYAQDAFSSIDWSQ | ||||||
Intramembrane | 27-47 | Helical | ||||
Sequence: PSLYISVASILFNPIWWNVVA | ||||||
Transmembrane | 29-46 | Helical | ||||
Sequence: LYISVASILFNPIWWNVV | ||||||
Topological domain | 48-59 | Lumenal | ||||
Sequence: RMEYHNKTLTKL | ||||||
Transmembrane | 66-85 | Helical | ||||
Sequence: YGCYGLAVAIFSLGIIRDFL | ||||||
Transmembrane | 108-135 | Helical | ||||
Sequence: LAVALFLTGNILVLTSMYALGVTGTYLG | ||||||
Topological domain | 131-173 | Lumenal | ||||
Sequence: GTYLGDYFGILMDARVTGFPFNVTDNPMYWGSAMSFLGTALWY | ||||||
Transmembrane | 172-195 | Helical | ||||
Sequence: WYGRPAGVVLSVVVVVMYKIALAF | ||||||
Topological domain | 195-407 | Cytoplasmic | ||||
Sequence: FEEPFTGWCEGPVSFLPLGSIVGALLLQSTWRTDVAASSGVAGERRNSTFCLLWIIIFGSFTGSSGVIHLFNKGSSCFFDTIPNIRKEIYDTCIATHFITSQTTHSMMNENDRISGTAQVTKLHVKVQSMAGSVRTPWPSNSKERAGRGLWMKLWRHHFRKLGELKKKKNQRKRDMSANPSFNLVSMKHTPYLALNTPHPHAPCPSTQNKDSP | ||||||
Transmembrane | 207-225 | Helical | ||||
Sequence: VSFLPLGSIVGALLLQSTW | ||||||
Transmembrane | 245-265 | Helical | ||||
Sequence: CLLWIIIFGSFTGSSGVIHLF |
Keywords
- Cellular component
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 388-407 | Disordered | ||||
Sequence: ALNTPHPHAPCPSTQNKDSP |
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
- Length407
- Mass (Da)45,270
- Last updated2015-06-24 v1
- ChecksumFB041E3E1E1235D2
Keywords
- Technical term