A0A090CBN0 · A0A090CBN0_PODAN

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 site878Charge relay system; for autoendoproteolytic cleavage activity
Active site937Charge relay system; for autoendoproteolytic cleavage activity
Site1023-1024Cleavage (non-hydrolytic); by autocatalysis
Active site1024Charge relay system; for autoendoproteolytic cleavage activity
Active site1024Schiff-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

Organism names

Accessions

  • Primary accession
    A0A090CBN0

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_50235572401-1023Phosphatidylserine decarboxylase 2 beta chain
Modified residue1024Pyruvic acid (Ser); by autocatalysis
ChainPRO_50235572411024-1135Phosphatidylserine 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 region, compositional bias, domain.

TypeIDPosition(s)Description
Region182-251Disordered
Compositional bias214-234Acidic residues
Domain255-376C2
Region404-424Disordered
Domain527-562EF-hand
Region629-656Disordered
Compositional bias1079-1096Basic and acidic residues
Region1079-1135Disordered

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
    1,135
  • Mass (Da)
    125,706
  • Last updated
    2014-11-26 v1
  • Checksum
    EA0269C4D03A6C7B
MARFIPNRLKPGYSNSAANSASNSRRRACWCRYRFYGYEGHTPSPSPSPPSPPSLPSWCQGVASHTDLLKIQAKDLAAKDRGGTSDPSLLLDVNCWDKDRFGKDYLGEFDLALEEIFADEKIEQPPTWYKLKSKRPGKKTGVVSGEVLLQFSLLDTSNKDASPQQIYEKFAAIAKSAPAIDASLTPTPSRTPVLAPTKGKVPSPAPSLGGRVTDDADEDDDYDYEDETPEDEDPTKPETAEKRRRRLRIKGLKRKKRQNPYEFINGGSDVVGIIFLEICKITDLPPESNVTRTSFDMDPFVVASLGKKTYRTKTIRHNLDPVFNEKMIFQVLNHEQQYQFAFTVIDHDKYSGNDFIASVNFPVQEIISKAPKADPATGLYNLKEVAEFSAPAQRTRFMRLGLSRTNSTQSLSKQARPALSKNPSTLTNVSSLVATPALGSGQQLHEVPEGAQTPAINAPIPAGLVQPGEGGVAAAAANTAENASPETEDPDFFPYTLPLRMKNLEKWEDKHNPQLYIRAKYMPYAALRQQFWRALLKQYDADESGLISKVELTTMLDSLGSTLRESTIDSFFLRFPHKAGDNEDVEDLTMDEAVICLEDQLESKVRTPGVAERVKNILPDAAEKVKNLLPIPGKESHPDTVQPPSESDLGGTDSITVPELATPGEEGDYLDRDDLNASNTEEHVVEIRECPICHQPRLNKRKDADIITHIATCASQDWRQVNNLMMGGFVTSSQAQRKWYSKVITKISYGGYKLGANSANILVQDRITGQINEEKMSVYVRLGIRLLYKGLKSNNMEKKRIRKLLKSLSIKQGKKYDDPASKAEIPKFIAFHGLDLSEVLLPLDQFKNFNEFFYRALKPDARPVSAPNNPRIVVSPADCRSVVFNRVDIATKVWIKGREFSVKRLLGDACPEDAHRYEAGGALGIFRLAPQDYHRFHIPVDGVMREPKTIAGEYYTVNPMAIRSALDVYGENVRIVVPIDSPEFGRVMVICIGAMMVGSTVITKKEGDEVKRGDELGYFKFGGSTLVVLFESGKMVFDDDLVDNSNTALETLIRVGMSVGHAPSEPQWTPDMRKDDAQITEADKQDAKRRIQGQVAEESPNDDSGSGLDVDGEGDGEVTVKVPHLGTTNGPAVTA

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias214-234Acidic residues
Compositional bias1079-1096Basic and acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
FO904937
EMBL· GenBank· DDBJ
CDP25131.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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