A0A067PD06 · A0A067PD06_9AGAM

  • 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.

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 site953Charge relay system; for autoendoproteolytic cleavage activity
Active site1011Charge relay system; for autoendoproteolytic cleavage activity
Site1097-1098Cleavage (non-hydrolytic); by autocatalysis
Active site1098Charge relay system; for autoendoproteolytic cleavage activity
Active site1098Schiff-base intermediate with substrate; via pyruvic acid; for decarboxylase activity

GO annotations

AspectTerm
Cellular Componentendosome membrane
Cellular ComponentGolgi membrane
Cellular ComponentGolgi stack
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
      JAAARDRAFT_39909

Organism names

  • Taxonomic identifier
  • Strain
    • MUCL 33604
  • Taxonomic lineage
    Eukaryota > Fungi > Dikarya > Basidiomycota > Agaricomycotina > Agaricomycetes > Agaricomycetidae > Jaapiales > Jaapiaceae > Jaapia

Accessions

  • Primary accession
    A0A067PD06

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_50233022881-1097Phosphatidylserine decarboxylase 2 beta chain
Modified residue1098Pyruvic acid (Ser); by autocatalysis
ChainPRO_50233022891098-1162Phosphatidylserine 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, compositional bias, region.

TypeIDPosition(s)Description
Domain28-153C2
Compositional bias207-230Polar residues
Region207-271Disordered
Compositional bias232-250Acidic residues
Region286-369Disordered
Compositional bias336-361Polar residues
Domain379-499C2
Region620-680Disordered
Compositional bias631-649Polar residues
Region701-756Disordered
Compositional bias722-756Polar residues
Region1142-1162Disordered
Compositional bias1145-1162Polar 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
    1,162
  • Mass (Da)
    128,269
  • Last updated
    2014-09-03 v1
  • Checksum
    285E1D333706856A
MVAAPKKALKIRRALRSAARLPIRVTSGKGYNTRAFTPIPGETPIVILRVQVIGCKELLAKDKNGSSDPFVVVSLSSTKFQTPVVKRSLNPTYAAKDATFDFPIYLSLAERLGVVELVLWDKDMLKKDYLGEVGISLEDWFKDGNAFAFDDPYNKPFSSNVLSTRASTPATGTVQIKLGFVAPYNTQSLMEFDEVYAELIRRSQPSLVSAPPTEGIGTIRSHQTGPQFEDDGLSSDEGENDIEGEGGTDDEEDRSPFNELFIPPPTALTYEPMPLTFAPPIDLNLNLSPPTPTTPTTPTIGGFEKDKSTPVPSRPSTPGFRVPKVPKILRRPVVTPSASYDSTASPSVPPTPRTQSSTEVPGVGAGDKKKKFRKSWGGKLVEYNFSAANDIVGIVMLEIKSASDLPKLKNMTRTGWDMDPFVVISFGKKVFRTRVIRHSLNPNWDEKLLFHVRRYETSFKVKLTVLDWDKLTSNDHVGDASFNVSELLVDVPEKDPETGLYKAGETGDTPMREFVLGLETDKEVKWEGKHNPTISFKAKYQPYDALRQRFWRQYLKQYDTDDTSTLSHLELTSMLDSLGSTLAAETVNSFFTRHGKKPQEDDLTIPEAVQCLEMELCKPPSEKKRIDSDTALLSGDTSMPATPSLMTMEGSQGFPLDMSKIDFSGPPMQPPIEAYPWDPLRKPSLPPAYATERSEQPLIDAAAGVGPGPTRIVPPSYPGPSIPAMHSSSPSSSDAEDSSGGSPSNTSPSEYTSSGSLERVINVKNCPLCHRPRLNSKAEMDIVTHLAVCASQDWASVDRIVVGNFVTASQAQRKWYTKMISKVSSGNYKLGANSANIIVQNRMNGQLEEEKMQVYVRLGIRLLYKAMRSRMEGGRARRLLKSLSIKQGLKYDSPESARDIVPFIEFHNLKVDEILEPISSFKNFNEFFYRKLKPDARPVENPDNPYRLVSAADCRLMCFETVNEATKLWIKGREFTVARLLGDQYKDQAEKYHGGALCIFRLAPQDYHRFHVPVDGTIGPMTYIPGEYYTVNPQAIRTGLDVYGENVRKIVPIDSPEFGRVMCVCVGAMMVGTIRTTVEEGQQVKRGQEFGYFAFGGSTIVILFERGVVEWDEDLLINGHACLETLVRVGMGIGKSVRSPHGTPAAVAGSSNGNGHGLGNGA

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias207-230Polar residues
Compositional bias232-250Acidic residues
Compositional bias336-361Polar residues
Compositional bias631-649Polar residues
Compositional bias722-756Polar residues
Compositional bias1145-1162Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
KL197738
EMBL· GenBank· DDBJ
KDQ52654.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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