A0A370PGJ6 · A0A370PGJ6_ASPPH

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.

TypeIDPosition(s)Description
Active site849Charge relay system; for autoendoproteolytic cleavage activity
Active site907Charge relay system; for autoendoproteolytic cleavage activity
Site993-994Cleavage (non-hydrolytic); by autocatalysis
Active site994Charge relay system; for autoendoproteolytic cleavage activity
Active site994Schiff-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
      M752DRAFT_217103

Organism names

  • Taxonomic identifier
  • Strain
    • ATCC 13157
  • Taxonomic lineage
    Eukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Eurotiomycetes > Eurotiomycetidae > Eurotiales > Aspergillaceae > Aspergillus

Accessions

  • Primary accession
    A0A370PGJ6

Proteomes

Subcellular Location

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

Keywords

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_50235540271-993Phosphatidylserine decarboxylase 2 beta chain
Modified residue994Pyruvic acid (Ser); by autocatalysis
ChainPRO_5023554026994-1075Phosphatidylserine 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 region, compositional bias, domain.

TypeIDPosition(s)Description
Region1-35Disordered
Compositional bias9-33Polar residues
Domain22-139C2
Region188-225Disordered
Domain239-363C2
Region363-460Disordered
Compositional bias389-434Polar residues
Domain502-537EF-hand
Compositional bias577-600Polar residues
Region577-646Disordered
Compositional bias607-636Polar 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
    1,075
  • Mass (Da)
    120,066
  • Last updated
    2018-11-07 v1
  • Checksum
    E8877FEE3B3A500E
MVRLPLPQRLSSHLSTKSNNPTPGQSRSTSPMRMPEQKPLILKVSVIRGRDLAAKDRGGTSDPYLVVTLGDARQSTPTIPKTLNPEWNVTFEMPVVGVPLLECICWDHDRFGKDYLGEFDIPLEDIFQNGDVHQQPKWYTLKSKRKPTKKKDSMVSGEILLQFSLLDSSNPTASPTDTYHKFRTLVSSGDEEDDFPQIPSITLDDADREEETSDETDDPTKPEVVEKRRRRLRLKRLKRKSLAARAYQFSGAGNGVQGIVFMEIVKVTDLPPERNVTRTSFDMDPFVVTSLGRKTLRTPVVRHNLNPIYNEKMVFQVMKHEQSYTIGFTVMDRDKFSGNDFVASASFPVQTLIKSAPEADPETGLYKFVDPTLDPAGAERGHSSRPSEIRIAISRSPSANSLSTSPKFGTTPRGSSTSLSSQTLLEQSSTLLPPRSIPEVPESSQPSTPTTAGFEGDPIGPLESNGLQVYRIQLALKNKERWEDKHFPELFVKAKYMPYRALRQQFWRLMLRQYDADESGRIDKVELTTMLDTLGSTLKESTIDSFFERFSLENQPSETMDLTFDQAVICLEDTLQALQKDPSSPPKKLSPTPSTASRESDEQSSGDELTMEPGSHNANPQTTSVPTLPTDEQPSSTEEDLLPDDLGDERGVEHVIELRECPLCHQPRLSSRSDADIITHIATCASRDWRQVDNLVMGGFVTSSQAQRKWYTKVITKISYGGYKLGANSANILVQDRITGQINEERMSVYVRLGIRLLYKGLKSREMEKKRIRKILKSLSIKQGRKYDDPASASQIRDFINFHQLDMSEVLLPVEKFKTFNEFFYRALKPGARPCSAPDEPGIVVSPADCRAVVFDRMEEATGIWVKGREFSVARLLGDAYPEDVQRFKNGALGIFRLAPQDYHRFHIPVDGVLGEPKTIEGEYYTVNPMAIRSALDVYGENVRVLVPIDSVAHGRVMVVCVGAMMVGSTVITRQAGEKVSRAEELGYFKFGGSTLLLLFEEGAVNFDSDLVDNSKGPLETLIRVGMSVGHSPGVAQFEPDMPKKSEDVSLEEMQAAKRRIEGSLAPPTDAAAFE

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias9-33Polar residues
Compositional bias389-434Polar residues
Compositional bias577-600Polar residues
Compositional bias607-636Polar residues

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
KZ851855
EMBL· GenBank· DDBJ
RDK41327.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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