A0A0C3HRV6 · A0A0C3HRV6_OIDMZ

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 site811Charge relay system; for autoendoproteolytic cleavage activity
Active site869Charge relay system; for autoendoproteolytic cleavage activity
Site955-956Cleavage (non-hydrolytic); by autocatalysis
Active site956Charge relay system; for autoendoproteolytic cleavage activity
Active site956Schiff-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
      OIDMADRAFT_113969

Organism names

  • Taxonomic identifier
  • Strain
    • Zn
  • Taxonomic lineage
    Eukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Leotiomycetes > Leotiomycetes incertae sedis > Myxotrichaceae > Oidiodendron

Accessions

  • Primary accession
    A0A0C3HRV6

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_50233308831-955Phosphatidylserine decarboxylase 2 beta chain
Modified residue956Pyruvic acid (Ser); by autocatalysis
ChainPRO_5023330882956-1043Phosphatidylserine 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. Interacts with pstB2. This interaction may be a means to structurally tether the donor membrane (ER) harboring PstB2 to acceptor membranes (Golgi/endosomes) harboring PSD2 during PtdSer transport to the site of PtdEtn synthesis.

Protein-protein interaction databases

Family & Domains

Features

Showing features for region, compositional bias, domain.

Type
IDPosition(s)Description
Region13-42Disordered
Compositional bias14-41Polar residues
Domain31-149C2
Region201-250Disordered
Compositional bias222-239Acidic residues
Domain260-382C2
Compositional bias409-424Polar residues
Region409-436Disordered
Domain443-478EF-hand
Compositional bias546-591Polar residues
Region546-613Disordered
Region992-1043Disordered
Compositional bias1000-1025Basic and acidic residues

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
    1,043
  • Mass (Da)
    116,675
  • Last updated
    2015-04-01 v1
  • Checksum
    EDED622628B0783A
MVRIPLPHRLKSYGSYSAGNSRSTSPNPLGRSGTPLDTSGEPARTNGLILKVVVLKARNLAAKDKNGTSDPYLVLALGDSRHATQYSPKTLNPEWNVTIQMPISSANYLLLDCVCWDKDRFGKDYMGEFDLALEDIFQNEQIAQEPRWYPLKSKRPGVKKGNVSGEVLLQFTILDSGNIGATPQQIMEKFKILCGTESGDLLGPETPTSRASRLFAGDEQGDEDEYRSEEDEEPSDETDDQTKSESVEKRKRRLRLRGLRKKKQMRAYEFSGGSDVVGIVFLDIQKITDLPPERNMTRTSFDMDPFVVASLGKKTYRTRVIRHNLNPVFNEKMIFQVQRREQNYSLSFTIIDRDKLSGNDFIASAVLPITDITETAPEANPETGLYALKEPPEMGAITPTVSRSRFKLPLSRSSSSQSLNKLARPSMPPRSPTGTKYVPYPALRQQFWRAMLKQYDTDESGRISKVELTTMLDTLGSTLKESTIESFFKRFQGAENSGDETSCDLTVDEAVICLEDQLYEKSRPPATITEKVKSLVPEAAMFKSHKASQLGQTITTSASSQTDLSTDTSPSASENTTLVDQPQQSVDSQRVEGLRTPGEDGDDADREDLNDKDEEHVVEIRECPICHQPRLNKRSDADIITHVATCASQDWRQVNSIVMAGFVTPSQAQRKWYSKVITKISYGGYRLGANSANILVQDRITGQISEERMSVYVRLGIRLLYKGLKSKDMEKKRIRKLLRGLSFKQGIKYDDPASKTEIQKFINFHKLDMSEVLLPIESFKNFNEFFYRQLKVGARPCSAPDQPKIVVSPADCRSVVFNRIDDATRIWVKGREFSIERLLGNAYPEDAKRYIGGALGIFRLAPQDYHRFHIPVDGIMGTPKTIEGEYYTVNPMAIRSALDVYGENVRVVLPIDSVAHGRVMVICVGAMMVGSTVITRHAGETVKRAEELGYFKFGGSTILLLFEEGTMQFDDDLVDNSNGALETLIRVGMSIGHHPSQPQYTPDMRKKEDDITESEIEDAKRRIEGSSAQPKIPGKTPLASLAG

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias14-41Polar residues
Compositional bias222-239Acidic residues
Compositional bias409-424Polar residues
Compositional bias546-591Polar residues
Compositional bias1000-1025Basic and acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
KN832871
EMBL· GenBank· DDBJ
KIN05750.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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