A0A8H7PWB4 · A0A8H7PWB4_MORIS

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 site819Charge relay system; for autoendoproteolytic cleavage activity
Active site875Charge relay system; for autoendoproteolytic cleavage activity
Site961-962Cleavage (non-hydrolytic); by autocatalysis
Active site962Charge relay system; for autoendoproteolytic cleavage activity
Active site962Schiff-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
      INT43_008510

Organism names

Accessions

  • Primary accession
    A0A8H7PWB4

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_50350165481-961Phosphatidylserine decarboxylase 2 beta chain
Modified residue962Pyruvic acid (Ser); by autocatalysis
ChainPRO_5035016547962-1003Phosphatidylserine 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.

Family & Domains

Features

Showing features for domain, region, compositional bias.

TypeIDPosition(s)Description
Domain1-106C2
Region180-199Disordered
Compositional bias185-199Polar residues
Domain242-362C2
Compositional bias512-528Basic and acidic residues
Region512-533Disordered
Region552-578Disordered
Compositional bias561-578Basic and acidic 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

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    1,003
  • Mass (Da)
    113,259
  • Last updated
    2022-01-19 v1
  • Checksum
    A0B7A15756569AFF
MTNDTVEELILRCSVIKAQDLVSKDSNGFSDPYAIVSNGKDFHSSEVVPKNLNPEWDFTCDLTLTPGDSQISIVLWDKDSFKSDFLGQISFDVQDLFKSGQAIAFHDDNNEPRWYELLDRDTRRSKILRRKKKLADQPKPMSSGKVLVKLGLVERYGTAAPENWESIWDAFLNSAARSDAIEKPDQPSTADQKSQNTATAKRALLQKYRTTSNKSIDTSTAKFHGEDLMGIMYIEVTCASDLPPEKNGKLHVNDPIANKYILAYLDTRSTNVVILMIHTTFDMDPFVVVTFGRSTFRTKALRHTLNPTWNEKLYFHVNDDDINYKLKFSVYDKDKVSGNDFVAGNEVSILDIINKSLESGKLALKPASTVGAGNKGTDEEDHIRLTLGNSSEGSAAKDIGSDMEMHTIDLKLANQAKWEGRHQPTLTFRAKYVPYEEIRKMFWLTLTKTYDADSNGRMSHMEVQTMLESLGSTISDSTIDEFWSHFNKTEDQELEFEELIDRLEAHIVYSDRRRREAKKAREPTEGLDRSDTSNSLFLDPIKFYQYDSEMSSDNFNDNSDSEDTLNDKDHASFASSDHDEPLAEAHGVQYGVHDNHEQTYDVSSDKDVKLKDDDVMENENDNIEKVIHVKECPICHRPNLNRKSQMDIITHIATCAADDWTTVDKFVMGNFITEAYAQRKWFVKMISKVGYGKYSLGTDNANIIVQDRQTGQLIEEKMAVYVRLGMRLLYRGSKTTVHTKRAQKILENMSMKQGKRFDSPMSARDIKPFIQFHKLDMTEVLDPMESFKTFNQFFYRKLKPDARPCDSADDPNVAVSAADARMMAFATIDDATRIWIKGMNFSVGKLLGDEELGKSYVGGSLAIFRLAPQDYHRFHSPVDGVVSEVKHIPGEYYTVNPMAIRTTLDVYGENTRSVLSIDSPTFGKVAVACIGAMMVGSIEITAKPGSTLKRTDELGYFAFGGSTLVAIWPPNSIQFDKDLLMNAQEPLETLTRVGQHIGKAVSK

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias185-199Polar residues
Compositional bias512-528Basic and acidic residues
Compositional bias561-578Basic and acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JAEPQZ010000005
EMBL· GenBank· DDBJ
KAG2180930.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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