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A0A804KUY4 · A0A804KUY4_MUSAM

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 site449Charge relay system; for autoendoproteolytic cleavage activity
Active site505Charge relay system; for autoendoproteolytic cleavage activity
Site592-593Cleavage (non-hydrolytic); by autocatalysis
Active site593Charge relay system; for autoendoproteolytic cleavage activity
Active site593Schiff-base intermediate with substrate; via pyruvic acid; for decarboxylase activity

GO annotations

AspectTerm
Cellular Componentmembrane
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
      104000763
    • Synonyms
      PSD2

Organism names

Accessions

  • Primary accession
    A0A804KUY4

Proteomes

Genome annotation databases

Subcellular Location

Keywords

  • Cellular component

PTM/Processing

Features

Showing features for chain, modified residue.

Type
IDPosition(s)Description
ChainPRO_50331828071-592Phosphatidylserine decarboxylase 2 beta chain
Modified residue593Pyruvic acid (Ser); by autocatalysis
ChainPRO_5033182806593-650Phosphatidylserine 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 region, compositional bias, domain.

Type
IDPosition(s)Description
Region1-47Disordered
Compositional bias22-36Basic residues
Domain26-151C2
Domain180-215EF-hand
Domain216-251EF-hand

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

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    650
  • Mass (Da)
    72,494
  • Last updated
    2021-09-29 v1
  • MD5 Checksum
    4E99D5AF54901F4CA2926C40DD701C31
MGHGSSRADASDDSSGDGHARHHHSRFSRFRRRFRSNRHDHGSDPPLVKNLAADDFAGIARIEIISAEMQFKDRWFACLSLGERTYRTETSDHTEKPIWRSEKKLVLEKDGPTIARISVIETNRLSKNNLVGYCEINLLEVLSQESENNIEELSLLDPSSSSTTVGSISILCYVEDPIETEKFFARRILSVVDLNGDGKLSYSEFAELINAFGNQVAAIKTEDLFKQADKNGDGVVDLDELATLIAVQQENEPLINNCPVCGESLGKLDKLNDMIHMTLCFDEGTGNQVMTGGFLTDKEASYGWIFKLSEWAHVSSYDIGLRSGSSASHILVVDRRTKGLVEEIIDGKIVLSMRAIYQSKVGLTLINTGVKDLLQNISEKQGKRMNSHESAKDIPKFIEFFIGQLKMDEAKYPIEYFKTFNEFFIRELKPGARPIAYPERDDIAVCAADCRLMAFNSANESLRFWIKGRKFSIQGLLGKDTCSSAFVDGSLVIFRLAPQDYHRFHVPVSGTIESFVDIPGYLYTVNPIAVNSKYCNVFTENKRVVSIISTSEFGKVAFVAIGATMVGSITFTKNEGDYVHKGDEFGYFSFGGSTVICVFEKDAIQIDEDLLSNSERSLETLVSVGMRLGISKRSGRIDELPNMETCKLEA

Computationally mapped potential isoform sequences

There is 1 potential isoform mapped to this entry

View all
EntryEntry nameGene nameLength
A0A804KUY5A0A804KUY5_MUSAM104000763719

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias22-36Basic residues

Keywords

Sequence databases

Genome annotation databases

Similar Proteins

Disclaimer

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