A0A8H4RSC0 · A0A8H4RSC0_9HELO

  • Protein
    Phosphatidyl-N-methylethanolamine N-methyltransferase
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    3/5

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).

Caution

The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

Catalytic activity

Pathway

Phospholipid metabolism; phosphatidylcholine biosynthesis.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site597-599S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site679-680S-adenosyl-L-methionine (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentendoplasmic reticulum membrane
Cellular Componentmitochondrial membrane
Molecular Functionphosphatidyl-N-dimethylethanolamine N-methyltransferase activity
Molecular Functionphosphatidyl-N-methylethanolamine N-methyltransferase activity
Biological Processmethylation
Biological Processphosphatidylcholine biosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Phosphatidyl-N-methylethanolamine N-methyltransferase
  • EC number
  • Alternative names
    • Phospholipid methyltransferase
      (PLMT
      )

Gene names

    • ORF names
      G7Y89_g4065

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • DSM 108380
  • Taxonomic lineage
    Eukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Leotiomycetes > Helotiales > Tricladiaceae > Cudoniella

Accessions

  • Primary accession
    A0A8H4RSC0

Proteomes

Subcellular Location

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.

TypeIDPosition(s)Description
Topological domain1-510Lumenal
Intramembrane511-531Helical
Topological domain532-543Lumenal
Transmembrane553-569Helical
Topological domain566-592Cytoplasmic
Transmembrane590-608Helical
Topological domain614-656Lumenal
Transmembrane655-675Helical
Topological domain678-701Cytoplasmic

Keywords

Family & Domains

Features

Showing features for domain, compositional bias, region.

TypeIDPosition(s)Description
Domain36-177Transcriptional regulatory protein RXT2 N-terminal
Compositional bias218-262Polar residues
Region218-308Disordered
Compositional bias270-298Polar residues

Sequence similarities

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    701
  • Mass (Da)
    77,660
  • Last updated
    2022-01-19 v1
  • Checksum
    A7E16980AB48FC1E
MASQAAIFAETIAGMKKAIKRKLYDSESDSSIEQLTNRGNKLRKKARFVHEGQLAPPTGPNVYKRKIEHAGFYRDIISQNPPLIDEEGYEVDSDDDDERAQIAMTSAAEFDPYADVKIDQLLMPLTAASDLPDHLTLSKPFTSRTLTELTQNAREMVQKEKASLWRIKHLLTRLSGDNTWIPCESLVTDNDIALFLDVRDKNRATMLGRLQVKDDADQASTGTLVSDDAEQPPNLLNSEGHISEPPQNTMQSATSNPIENGDELAQARNGTIGKESTGQTETNKTIEPRNSTESHDNLALKNGARIPLRNDFEPATEENVEMGGAVKPPSGESSENQGMAVDEITELDVVGSMEELGDNAAPRRMRTRAQAQAASDNTASSRTRSATPEFNNDTFIHPYFLAPITSHPDRDVGLPQPEAEETRRLLQLYIQKQEEVCRGAQKIYEGLLRADRYRKLVLKWAKAEAHVGVNRDMSDGEDWYDKGEWGLDEDLKKGQDEEEEDAATTAKKTRTLLRAKVREAKLLPNSTMLIPFSEYHNKVLTKLAGGNSRNACYGLAVAIFSLGIFRDFLYERALRAQPSHPALENPLASYIAYALLATGNVLVLSSMWALGVTGTYLGDYFGILMDKMVMGFPFNICSAPMYYGSTMSFLGTAILFGKPAGILLTAEVLVVYMIALRFEDPFTAGIYAKREKDQKKGGKKA

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias218-262Polar residues
Compositional bias270-298Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JAAMPI010000212
EMBL· GenBank· DDBJ
KAF4634059.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp