A0A9P8C183 · A0A9P8C183_9HELO

  • Protein
    Phosphatidylserine decarboxylase proenzyme 2
  • Gene
    PSD2
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    4/5

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.

Caution

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

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 site866Charge relay system; for autoendoproteolytic cleavage activity
Active site924Charge relay system; for autoendoproteolytic cleavage activity
Site1010-1011Cleavage (non-hydrolytic); by autocatalysis
Active site1011Charge relay system; for autoendoproteolytic cleavage activity
Active site1011Schiff-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
      BJ875DRAFT_218607

Organism names

  • Taxonomic identifier
  • Strain
    • TRa018bII
  • Taxonomic lineage
    Eukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Leotiomycetes > Helotiales > Helotiales incertae sedis > Amylocarpus

Accessions

  • Primary accession
    A0A9P8C183

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_50405522671-1010Phosphatidylserine decarboxylase 2 beta chain
Modified residue1011Pyruvic acid (Ser); by autocatalysis
ChainPRO_50405522681011-1099Phosphatidylserine 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.

Family & Domains

Features

Showing features for domain, region, compositional bias.

Type
IDPosition(s)Description
Domain32-150C2
Region197-249Disordered
Compositional bias217-233Acidic residues
Domain254-377C2
Region392-426Disordered
Compositional bias401-426Polar residues
Domain516-551EF-hand
Region598-665Disordered
Compositional bias622-648Polar residues
Region1048-1099Disordered
Compositional bias1053-1078Basic and acidic residues
Compositional bias1083-1099Polar 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

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    1,099
  • Mass (Da)
    122,169
  • Last updated
    2023-09-13 v1
  • Checksum
    AFAC8AB0B4EDE250
MVRNILPNRLKSFANPNPYPNIRSTSPSPVIKRSNTSDSFLDMSKAAMLCLKVVVLRARDLAAKDRSGTSDPYLVLTLGDAKDATQPVYKTLNPEWNISMQFPITGVNSLLLDCVCWDKDRFGKDYLGEFDLSLEDVFCRGQNEVGPNWYPLRSKRPGGRKSSNVSGDVFLQFTLFDSSNPSATSDQVMDKFRSLTGGEVSEVGTPLPRMGSHGQEEEDDDFDDDEDPSDETDDPTKPENAEKRRRKLRLRGLRKKKQAAAYEFNSESEVVGIVFLEIGKITDLPPERNMTRTSFDMDPFVVASLGKKTYRTRVIRHNLNPVFHEKMIFQVLRHEQTYSISFTVIDRDKLSGNDFIASTVIPLTEITDTAPSADSETGLYELKEPELNAVVPEKQNRSRFKLPLSRSSSSQSLSRLGRPQLTPNKSRDAFYTSGSNSGATTPHLGVPPTSNPGGGPAGDLAPPTNAVDEDDGYHGRGDPDLHPFTIPLKLKNAEKWEAKHSPVLDIQAKYVPYPALRQQFWRSMLRQYDTDESGRISKVELTTMLDTLGSTLKESTIDGFFARFGKNQASLNDGDADLSFDEAVICLEDQLLEKSKSQSVADRLRSHLPTHMGGTPARPPPSLRTEDSTASSRSQTLVDQTETQDVQDLGTPGEEGDALDNNDLNDKGEEHVVEIRECPICHQPRLNKRSDTDIITHIATCASQDWRQVNSIVMAGFVTSSQAQRKWYSKVITKISYGGYKLGANSANILVQDRITGQINEERMSVYVRLGIRLLYKGLKSKDMEKKRIRKLLRGLSFKQGVKYDDPASAAEIEKFVAFHQLDMSEVLLPLNEFKSFNEFFYRALTPEARPCSAPDNPKIIVSPADCRSVVFNKMDVATTIWVKGREFSVERLLGNAYPEDAKRYKNGALGIFRLAPQDYHRFHIPVDGVMGTPKPIDGEYYTVNPMAIRSALDVYGENLRVIVPIDSVAHGRVMVICVGAMMVGSTVITRKGGEQVKRAEELGYFKFGGSTILLLFEDGAMRFDDDLVDNSNGALETLIRVGMSIGHHPDQGQHTPDMRKKDADISEAERAEAKRRIEGSILGPSATSTPTSGMGGSL

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias217-233Acidic residues
Compositional bias401-426Polar residues
Compositional bias622-648Polar residues
Compositional bias1053-1078Basic and acidic residues
Compositional bias1083-1099Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
MU251848
EMBL· GenBank· DDBJ
KAG9228871.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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