A0A7R7ZLN0 · A0A7R7ZLN0_ASPCH
- ProteinPhosphatidyl-N-methylethanolamine N-methyltransferase
- GeneOPI3
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids200 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
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
- 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 | |
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 > Pezizomycotina > Eurotiomycetes > Eurotiomycetidae > Eurotiales > Aspergillaceae > Aspergillus > Aspergillus subgen. Aspergillus
Accessions
- Primary accessionA0A7R7ZLN0
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 | 1-12 | Lumenal | ||||
Sequence: MAALTDFVDFSQ | ||||||
Intramembrane | 13-33 | Helical | ||||
Sequence: LSLQVTALSIAFNPIFWNIVA | ||||||
Transmembrane | 13-33 | Helical | ||||
Sequence: LSLQVTALSIAFNPIFWNIVA | ||||||
Topological domain | 34-45 | Lumenal | ||||
Sequence: RTEYRNHFLTRI | ||||||
Transmembrane | 45-66 | Helical | ||||
Sequence: IFGSPYYGCYFLAFTIFSLGIL | ||||||
Transmembrane | 86-108 | Helical | ||||
Sequence: QPILGAVLFGVGSVLVLSSMYAL | ||||||
Topological domain | 112-154 | Lumenal | ||||
Sequence: GTYLGDYFGILMDAPVTGFPFNVTGSPMYWGSTLNFLGVALYH | ||||||
Transmembrane | 115-132 | Helical | ||||
Sequence: LGDYFGILMDAPVTGFPF | ||||||
Transmembrane | 152-173 | Helical | ||||
Sequence: LYHGKVAGIALTAEVFILYWFA | ||||||
Topological domain | 176-200 | Cytoplasmic | ||||
Sequence: WEDPFTAGIYAKRERERAKQAGKSQ |
Keywords
- Cellular component
Structure
Sequence
- Sequence statusComplete
- Length200
- Mass (Da)22,292
- Last updated2021-06-02 v1
- Checksum24F6A504BEF259DA
Keywords
- Technical term