A0A8H4RSC0 · A0A8H4RSC0_9HELO
- ProteinPhosphatidyl-N-methylethanolamine N-methyltransferase
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids701 (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
- 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
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
- Organism
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Leotiomycetes > Helotiales > Tricladiaceae > Cudoniella
Accessions
- Primary accessionA0A8H4RSC0
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 | 1-510 | Lumenal | ||||
Sequence: MASQAAIFAETIAGMKKAIKRKLYDSESDSSIEQLTNRGNKLRKKARFVHEGQLAPPTGPNVYKRKIEHAGFYRDIISQNPPLIDEEGYEVDSDDDDERAQIAMTSAAEFDPYADVKIDQLLMPLTAASDLPDHLTLSKPFTSRTLTELTQNAREMVQKEKASLWRIKHLLTRLSGDNTWIPCESLVTDNDIALFLDVRDKNRATMLGRLQVKDDADQASTGTLVSDDAEQPPNLLNSEGHISEPPQNTMQSATSNPIENGDELAQARNGTIGKESTGQTETNKTIEPRNSTESHDNLALKNGARIPLRNDFEPATEENVEMGGAVKPPSGESSENQGMAVDEITELDVVGSMEELGDNAAPRRMRTRAQAQAASDNTASSRTRSATPEFNNDTFIHPYFLAPITSHPDRDVGLPQPEAEETRRLLQLYIQKQEEVCRGAQKIYEGLLRADRYRKLVLKWAKAEAHVGVNRDMSDGEDWYDKGEWGLDEDLKKGQDEEEEDAATTAKKTR | ||||||
Intramembrane | 511-531 | Helical | ||||
Sequence: TLLRAKVREAKLLPNSTMLIP | ||||||
Topological domain | 532-543 | Lumenal | ||||
Sequence: FSEYHNKVLTKL | ||||||
Transmembrane | 553-569 | Helical | ||||
Sequence: YGLAVAIFSLGIFRDFL | ||||||
Topological domain | 566-592 | Cytoplasmic | ||||
Sequence: RDFLYERALRAQPSHPALENPLASYIA | ||||||
Transmembrane | 590-608 | Helical | ||||
Sequence: YIAYALLATGNVLVLSSMW | ||||||
Topological domain | 614-656 | Lumenal | ||||
Sequence: GTYLGDYFGILMDKMVMGFPFNICSAPMYYGSTMSFLGTAILF | ||||||
Transmembrane | 655-675 | Helical | ||||
Sequence: LFGKPAGILLTAEVLVVYMIA | ||||||
Topological domain | 678-701 | Cytoplasmic | ||||
Sequence: FEDPFTAGIYAKREKDQKKGGKKA |
Keywords
- Cellular component
Structure
Family & Domains
Features
Showing features for domain, compositional bias, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 36-177 | Transcriptional regulatory protein RXT2 N-terminal | ||||
Sequence: TNRGNKLRKKARFVHEGQLAPPTGPNVYKRKIEHAGFYRDIISQNPPLIDEEGYEVDSDDDDERAQIAMTSAAEFDPYADVKIDQLLMPLTAASDLPDHLTLSKPFTSRTLTELTQNAREMVQKEKASLWRIKHLLTRLSGD | ||||||
Compositional bias | 218-262 | Polar residues | ||||
Sequence: QASTGTLVSDDAEQPPNLLNSEGHISEPPQNTMQSATSNPIENGD | ||||||
Region | 218-308 | Disordered | ||||
Sequence: QASTGTLVSDDAEQPPNLLNSEGHISEPPQNTMQSATSNPIENGDELAQARNGTIGKESTGQTETNKTIEPRNSTESHDNLALKNGARIPL | ||||||
Compositional bias | 270-298 | Polar residues | ||||
Sequence: GTIGKESTGQTETNKTIEPRNSTESHDNL |
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
- Length701
- Mass (Da)77,660
- Last updated2022-01-19 v1
- ChecksumA7E16980AB48FC1E
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 218-262 | Polar residues | ||||
Sequence: QASTGTLVSDDAEQPPNLLNSEGHISEPPQNTMQSATSNPIENGD | ||||||
Compositional bias | 270-298 | Polar residues | ||||
Sequence: GTIGKESTGQTETNKTIEPRNSTESHDNL |
Keywords
- Technical term