A0A167U1P0 · A0A167U1P0_9AGAM

Function

function

Catalyzes the formation of phosphatidylethanolamine (PtdEtn) from phosphatidylserine (PtdSer). Plays a central role in phospholipid metabolism and in the interorganelle trafficking of phosphatidylserine.

Catalytic activity

Cofactor

pyruvate (UniProtKB | Rhea| CHEBI:15361 )

Note: Binds 1 pyruvoyl group covalently per subunit.

Pathway

Lipid metabolism.
Phospholipid metabolism; phosphatidylethanolamine biosynthesis; phosphatidylethanolamine from CDP-diacylglycerol: step 2/2.

Features

Showing features for active site, site.

Type
IDPosition(s)Description
Active site574Charge relay system; for autoendoproteolytic cleavage activity
Active site632Charge relay system; for autoendoproteolytic cleavage activity
Site718-719Cleavage (non-hydrolytic); by autocatalysis
Active site719Charge relay system; for autoendoproteolytic cleavage activity
Active site719Schiff-base intermediate with substrate; via pyruvic acid; for decarboxylase activity

GO annotations

AspectTerm
Cellular Componentendosome membrane
Cellular ComponentGolgi membrane
Cellular ComponentGolgi stack
Molecular Functioncalcium ion binding
Molecular Functionphosphatidylserine decarboxylase activity
Biological Processphosphatidylethanolamine biosynthetic process
Biological Processprotein autoprocessing

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

Gene names

    • Name
      PSD2
    • ORF names
      FIBSPDRAFT_915298

Organism names

  • Taxonomic identifier
  • Strain
    • CBS 109695
  • Taxonomic lineage
    Eukaryota > Fungi > Dikarya > Basidiomycota > Agaricomycotina > Agaricomycetes > Agaricomycetidae > Atheliales > Atheliaceae > Fibularhizoctonia

Accessions

  • Primary accession
    A0A167U1P0

Proteomes

Subcellular Location

Golgi apparatus membrane
; Peripheral membrane protein
Endosome membrane
; Peripheral membrane protein

Keywords

PTM/Processing

Features

Showing features for chain, modified residue.

Type
IDPosition(s)Description
ChainPRO_50234370991-718Phosphatidylserine decarboxylase 2 beta chain
Modified residue719Pyruvic acid (Ser); by autocatalysis
ChainPRO_5023437098719-762Phosphatidylserine decarboxylase 2 alpha chain

Post-translational modification

Is synthesized initially as an inactive proenzyme. Formation of the active enzyme involves a self-maturation process in which the active site pyruvoyl group is generated from an internal serine residue via an autocatalytic post-translational modification. Two non-identical subunits are generated from the proenzyme in this reaction, and the pyruvate is formed at the N-terminus of the alpha chain, which is derived from the carboxyl end of the proenzyme. The autoendoproteolytic cleavage occurs by a canonical serine protease mechanism, in which the side chain hydroxyl group of the serine supplies its oxygen atom to form the C-terminus of the beta chain, while the remainder of the serine residue undergoes an oxidative deamination to produce ammonia and the pyruvoyl prosthetic group on the alpha chain. During this reaction, the Ser that is part of the protease active site of the proenzyme becomes the pyruvoyl prosthetic group, which constitutes an essential element of the active site of the mature decarboxylase.

Keywords

Interaction

Subunit

Heterodimer of a large membrane-associated beta subunit and a small pyruvoyl-containing alpha subunit.

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain, region, compositional bias.

Type
IDPosition(s)Description
Domain1-102C2
Domain155-190EF-hand
Region228-258Disordered
Region270-293Disordered
Compositional bias337-366Polar residues
Region337-372Disordered

Domain

The C2 domains have an essential, but non-catalytic function. They may facilitate interactions with other proteins and are required for lipid transport function.

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    762
  • Mass (Da)
    84,652
  • Last updated
    2016-07-06 v1
  • Checksum
    399793CE298B0FA5
MLEIQGATDLPRLKNMTRTGWDMDPFVVISFGKKVFRTRIIRHSLNPTWDEKLLFHVRAYEASFKVQLTVLDWDKLSSNDYVGDANFSVAELMGEGQGPQVDERTGLYSADADGKHPMKEFSVPLSVGKESVLPWEGKHHPVITFRAKYQPYAALRQQFWRQYLKEYDTEDTGLLSHLELTSMLDSLGSTLSAETISSFFTRNGKKAPEDELTMDEAVLCLETEVGRPREEKKRISPDEVQLDYSVPTTPGPGMGTGLSSMQVPQLAKLDFSGPASEPMDAETSAGEGEDLSRKTVGHPMYATEYSQQPLSDAAAPGGGIKTDLSSYPGTVLRAPAGQHQYSSAASSDAEEDLSGTNSNSYPFTPGGSSAGAAAEETLERVINVKNCPLCHRPRLNKKAEVDIVTHLAVCASGDWAKIDRIVVGNFVTASQAQRKWYTKIIGKVSSGDYRLGANSANIIVQNRMTGQLEEEKMQAYVRIGIRLFYKGAKSRMEGARARRLLKSMSIKQGIKYDDPASVRDIQPFIEFHRLDVTEIRDPIPSFKTFNQFFYRALKPEARPTEEPDNHHRIVSGADCRLMAFESVSEATRLWIKGREFTVARLLGDNYKDQVDHYHGGAVAIFRLAPQDYHRFHSPVDGVIGNMTYISGEYYTVNPQAIRTTLDVYGENARKIVPIDSPIFGRVMAVCVGAMMVGSIKTTLDEGDEVKRGQEFGYFAFGGSTIVLLFEKGVEWDEDLLINGRASLETLVRVGMGIGRSRRLPNP

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias337-366Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
KV418052
EMBL· GenBank· DDBJ
KZP03508.1
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.
Help