A0A167YBF6 · A0A167YBF6_9HYPO

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.

TypeIDPosition(s)Description
Active site863Charge relay system; for autoendoproteolytic cleavage activity
Active site921Charge relay system; for autoendoproteolytic cleavage activity
Site1007-1008Cleavage (non-hydrolytic); by autocatalysis
Active site1008Charge relay system; for autoendoproteolytic cleavage activity
Active site1008Schiff-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
      AAL_06849

Organism names

  • Taxonomic identifier
  • Strain
    • RCEF 2490
  • Taxonomic lineage
    Eukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Sordariomycetes > Hypocreomycetidae > Hypocreales > Clavicipitaceae > Moelleriella

Accessions

  • Primary accession
    A0A167YBF6

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_50234490681-1007Phosphatidylserine decarboxylase 2 beta chain
Modified residue1008Pyruvic acid (Ser); by autocatalysis
ChainPRO_50234490671008-1114Phosphatidylserine 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 compositional bias, region, domain.

TypeIDPosition(s)Description
Compositional bias1-29Polar residues
Region1-37Disordered
Domain26-145C2
Compositional bias197-216Polar residues
Region197-261Disordered
Compositional bias223-241Acidic residues
Domain265-386C2
Region385-478Disordered
Compositional bias408-466Polar residues
Domain516-551EF-hand
Region614-668Disordered
Region1078-1114Disordered

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
    1,114
  • Mass (Da)
    124,012
  • Last updated
    2016-07-06 v1
  • Checksum
    31C917395F7CA3D4
MRIKPNRLLSSSSINSVNNHNTSPMRSNKTDYHGGPGTEAATGLTLKLVILKARNLAAKDRSGTSDPYLVITCGDTRIVTHSVPKTLNPEWNAIEQFPINSVQNLLLDVICWDKDRFGKDYMGEFDLALEEVFQNERTEIEPRWFPLKSKRPGKKTGKVSGEVQLQFTLFDATHLGAPSREILGKFHALISAIPGSTPSTTPLLTSSTTKSASSRLSGQDEHFDDDEDGLSEFDDDESEDASKPDTAEKAEKRRRRLRIKGLKKRRRDNPYAFNNSSSDVVGIIFLEISKITDLPPESNLTRTSFDMDPFVVASLGKKTYRTRRVRHNLNPVYNEKMIFHVQSHEQSYSFSFTVIDHDKYSGNDFIAACSLPIHELVERAPQADPETGLYGLREPPDHVPSAARSRFKKLSVSRSSSTQSLTKLIRPQLSKNPSSTNVSPQGTTAELGQTHSANGSVTSDVQAPNAADNSDAVAEGDDGDFHEYVVPLKMKNLDKWESKHSPKIYLKAKYMPYPALRQQFWRAMLRQYDTDESGQISRVELTTMLDTLGSTLRESTIDSFFHRFPHKAADNEDGWDLTMDEAVICLEDQLAGKGKPKTVVDKVKSLVPDLRQLGISNKAPSADEPARPAASGTSTPAVAEPKTAVDTTDGKGSGEEDSDENGEREEEHVVEIRECPICHQPRLNKRSDTDIITHIATCASQDWRQVNTVLMGGFVTASQAQRKWYSKVITKISYGGYKLGANSANILVQDRITGQINEEKMSVYVRLGIRLLYKGLKSRDMENKRIRKMLKNLSIKQGKKFDDPASRDEIEKFIAFHGLDMSEVLLPLEEFKNFNEFFYRALKPEARPCSAPDNPKIIVSPADCRSVVFDQISQATQIWVKGREFNLKRLLGDAYPQDAARYEDGALGIFRLAPQDYHRFHIPVDGILGKPVTIAGEYYTVNPMAIRSSLDVYGENVRVVVPIDSVKHGRVMVICVGAMMVGSTVITRSAGEEVRRAEELGYFKFGGSTVLLLFEPGKMQFDDDLADNSSTALETLIRVGMSIGHSPDEGQWTPDMRKSEGDITEADKQEAMRRIQGNFAMEGSAHDSGSDDDGGPKRRMARAPTMNTFAASAM

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias1-29Polar residues
Compositional bias197-216Polar residues
Compositional bias223-241Acidic residues
Compositional bias408-466Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AZGY01000019
EMBL· GenBank· DDBJ
KZZ91108.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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