A0A0D0B9W4 · A0A0D0B9W4_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.

Type
IDPosition(s)Description
Active site987Charge relay system; for autoendoproteolytic cleavage activity
Active site1045Charge relay system; for autoendoproteolytic cleavage activity
Site1131-1132Cleavage (non-hydrolytic); by autocatalysis
Active site1132Charge relay system; for autoendoproteolytic cleavage activity
Active site1132Schiff-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
      CY34DRAFT_804151

Organism names

  • Taxonomic identifier
  • Strain
    • UH-Slu-Lm8-n1
  • Taxonomic lineage
    Eukaryota > Fungi > Dikarya > Basidiomycota > Agaricomycotina > Agaricomycetes > Agaricomycetidae > Boletales > Suillineae > Suillaceae > Suillus

Accessions

  • Primary accession
    A0A0D0B9W4

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_50234253001-1131Phosphatidylserine decarboxylase 2 beta chain
Modified residue1132Pyruvic acid (Ser); by autocatalysis
ChainPRO_50234252991132-1181Phosphatidylserine 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 region, domain, compositional bias.

Type
IDPosition(s)Description
Region1-38Disordered
Domain24-154C2
Region215-292Disordered
Compositional bias241-262Acidic residues
Compositional bias274-288Basic and acidic residues
Region305-348Disordered
Compositional bias321-347Polar residues
Region353-372Disordered
Domain412-534C2
Domain590-625EF-hand
Region744-787Disordered
Compositional bias749-787Polar 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
    1,181
  • Mass (Da)
    130,676
  • Last updated
    2015-04-29 v1
  • Checksum
    9EE6CA77B05078C8
MAPAVPKKAQKLGRALKSAARFPGRGSGRNHYSPSPGEQPVVLLRVQVIGCRGLARARNGAQAKEGDLNPLVVVSLLNNRHHTPVLKRTPNPVYASKDATFDFPIYLSLADRLGSVELVVWDKDTLKLKKEYVGEVALTLESWFRDVDGNLLVSGLGFSSETNQPQSVNLVSTRANTHASGMAVVKLGFVTPPGAQSPMAFERVFAELVKRSRPSLVSAPPTEGIGTLRSHLTGPAYEDDGGISSDEEDDDAVEEGEDEDEDLSRLYLSPSRLQDQTREDEEPETARPTVARCDLPRLHLHCSPTLSHVQPEEREPEITPQLPPVTSTTPTTTPPAMHSTTSASKSRLPKLFPRRPNLITTPSYDTNTPPTDRLHRRSVSAGAIAPLPSPISPGPSSAVYQTQKKIFRKSWSSKKVDYNFSAANSNDIVGIVMLEIQGATDLPKLKNMTRTGFDMDPFVVISFSKKIFRTRIIRHSLNPTWDEKLLFHVRRYETSFKVQMTVLDWDKLSSNDHVGDIWLDVGELVRDAPQPDPRTGLYADVCGENDAEGGEGREMKQFCLPLTTAKEMPWEAKHNPTISFRAKFQPYAELRQRFWAQYLKQYDTDDTGSISHVELTSMLDSLGSTLSAQTIDSFFTRHRKRPAEDELTIEESIQCLETELIRPACEKKRIDVIDTFMDRDSSASASESITPGEEIGLNIAFGRPFLGGLDFSGPPLSAILGDDSPTDLGRSVFVTESSDRPLLSVCVPEPSSAASTPGGSRSDNARQNSASSSELDDATSAQASSSSSDTFERVINIKNCPLCHRPRLNSKAEMDIITHLAICASQDWAKVDRIVVGNFVTASQAQRKWYTKVISKVSNGNYRIGANSANIIVQNRMTGQLQEEKMQVYVRLGIRLLYKGARGRMEGARARRLLKSLSIKQGAKYDSPESARDIPSFIEFHGLKVDEILEPISSFKTFNDFFYRKLKPSARPTESPDDPRRLVSAADCRLMVFETVSEATKLWIKGREFSIARLLGDVYREEAERYVGGPLAIFRLAPQDYHRFHVPVDGKIGEMRDVKGEYYTVNPQAVRSALDVYGENVRKIVPIDSPQFGRVMVVCVGAMMVGSIKITVEEGQDVKRGQELGYFAFGGSTIVVLFERGAVEWDEDLVINGRACLETLVRVGMGIGTCRRNGPSYGGRA

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias241-262Acidic residues
Compositional bias274-288Basic and acidic residues
Compositional bias321-347Polar residues
Compositional bias749-787Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
KN835220
EMBL· GenBank· DDBJ
KIK43147.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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