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A0A4U9EJV6 · A0A4U9EJV6_GIBZA

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 site886Charge relay system; for autoendoproteolytic cleavage activity
Active site944Charge relay system; for autoendoproteolytic cleavage activity
Site1030-1031Cleavage (non-hydrolytic); by autocatalysis
Active site1031Charge relay system; for autoendoproteolytic cleavage activity
Active site1031Schiff-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
      FUG_LOCUS179002
      , MDCFG202_LOCUS127001

Organism names

Accessions

  • Primary accession
    A0A4U9EJV6

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_50414914611-1030Phosphatidylserine decarboxylase 2 beta chain
Modified residue1031Pyruvic acid (Ser); by autocatalysis
ChainPRO_50414914601031-1133Phosphatidylserine 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.

Type
IDPosition(s)Description
Region1-53Disordered
Compositional bias9-53Polar residues
Domain39-161C2
Region213-277Disordered
Compositional bias214-239Polar residues
Compositional bias240-260Acidic residues
Domain281-402C2
Region421-494Disordered
Compositional bias425-463Polar residues
Domain530-565EF-hand
Region629-689Disordered
Compositional bias631-666Polar residues
Compositional bias672-689Basic and acidic residues
Region1090-1133Disordered

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
    1,133
  • Mass (Da)
    125,981
  • Last updated
    2019-07-31 v1
  • MD5 Checksum
    B43A7ACBD171F19830D2E580D5926084
MVRIIPTRLKSVSRSSSSSSATISVTNGNSKKNRSNSPPMRSKNDSTSPSRDAGNGLALRVWIIRGKDLAAKDRSGTSDPPPQYIIVSTGESRIVTNDVPKTLNPEWNVSEEIPLTSVQNLLLSVICWDKDRFGKDYMGEFDLALEEIFNNGKVEQQPTWYRLKSKRPGKKTSVVSGEVQLQFSLFDSTNPSATTQEILEKFQTLVGAAPAGSRNVTPSMTPNLGPNAAPQSTANPQDSPSDDDEFDEDDSDSSDSDSGDDQDQDPTKRKRRLRIRGLKKRRRNNPYAFASNGFDTVGVIYLEVVKITDLPPESNLTRTSFDMDPFVVASLGKKTYRTRRIRHNLNPVFNEKMLFQIQSHEQKYSFSFTVIDHDKYSGNDFIASCNLPLHELLERSPQANPETGLYDLKVPAQAEALPSRSRFKKLAMSRSNSSSSISKMIRPPLSKHASSGSTTTAVPAPAPTSNPNMLAPADALANTGADPDSTAQDGGDSDFHEYTVPLKLKDLEKWEKKHNPILYLRAKYMPYDALRQQFWRAMLRQYDADESGRISRIELTTMLEALGSTLTEATIDTFFSRFPHRDADNEENWELTMDEVVICLEDQLQGKRRSSATAGDKLKHLVPDMKNLLHVSRPGNNNSNGGSENPSVLDLSATSGTQTPISNVPTLKTPADEEGDPLDKSDSGDDRGEEHVVEIRECPICHQPRLNKRKDADIITHIATCASQDWRQVNSVLVGGFVTASQAQRKWYSKVITKISYGGYKLGANSANILVQDRLTGQINEEKMSVYVRLGIRLLYKGLKSRDMENKRIRKLLKNLSVKQGKKFDDPASKDEIEKFIAFHGLDMSEVLLPLEEFNNFNEFFYRALKPDARPCSAPHNPHIIVSPADCRSVVFNSISTATKIWVKGREFNMKRLLGDAYPEDVSRFEGGALGIFRLAPQDYHRFHIPVDGVMGKPKTIEGEYYTVNPMAIRSALDVYGENVRVLVPIDSEAHGRVMVICVGAMMVGSTVITRNEGDKVQRAEELGYFKFGGSTILLLFEPGRMVFDDDLVDNGHDALETLVRVGMSVGHTPSEPQWTPDMRKNAENITEAEKRTAKRRIQGNVALQDSPDGSGEEEQAARSAKPTIDTMAASAM

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias9-53Polar residues
Compositional bias214-239Polar residues
Compositional bias240-260Acidic residues
Compositional bias425-463Polar residues
Compositional bias631-666Polar residues
Compositional bias672-689Basic and acidic residues

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CAJPIJ010000095
EMBL· GenBank· DDBJ
CAG1974123.1
EMBL· GenBank· DDBJ
Genomic DNA
CAAKMV010000121
EMBL· GenBank· DDBJ
VIO55694.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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