A0AA91TXH2 · A0AA91TXH2_WOLPI

  • Protein
    Phosphatidylserine decarboxylase proenzyme
  • Gene
    psd
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    3/5

Function

function

Catalyzes the formation of phosphatidylethanolamine (PtdEtn) from phosphatidylserine (PtdSer).

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

Phospholipid metabolism; phosphatidylethanolamine biosynthesis; phosphatidylethanolamine from CDP-diacylglycerol: step 2/2.

Features

Showing features for site, active site.

TypeIDPosition(s)Description
Site185-186Cleavage (non-hydrolytic); by autocatalysis
Active site186Schiff-base intermediate with substrate; via pyruvic acid

GO annotations

AspectTerm
Cellular Componentplasma membrane
Molecular Functionphosphatidylserine decarboxylase activity
Biological Processphosphatidylethanolamine biosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

Gene names

    • Name
      psd
    • ORF names
      BTO27_04555

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • wAus
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Alphaproteobacteria > Rickettsiales > Anaplasmataceae > Wolbachieae > Wolbachia

Accessions

  • Primary accession
    A0AA91TXH2

Proteomes

Subcellular Location

Cell membrane
; Peripheral membrane protein

Features

Showing features for transmembrane.

TypeIDPosition(s)Description
Transmembrane12-34Helical

Keywords

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_50415067781-185Phosphatidylserine decarboxylase beta chain
Modified residue186Pyruvic acid (Ser); by autocatalysis
ChainPRO_5041506779186-227Phosphatidylserine decarboxylase 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 post-translation cleavage follows an unusual pathway, termed non-hydrolytic serinolysis, 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.

Keywords

Interaction

Subunit

Heterodimer of a large membrane-associated beta subunit and a small pyruvoyl-containing alpha subunit.

Family & Domains

Sequence similarities

Belongs to the phosphatidylserine decarboxylase family. PSD-A subfamily.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    227
  • Mass (Da)
    25,349
  • Last updated
    2024-03-27 v1
  • Checksum
    2B72A8B5B27C204D
MCFGLPNINREGYLFIVVSFIVTCIAFSISWGAGITCLFPTLLCTYFFRDPARAVPNNKDFILSPADGVISKIEEVSYSLSEENEEEKKFTLVSIFLSVLNVHVNRIPISGTIKEMSYKKGKFVSAMSNRSSNENEKQIIVIEYEKGKEIIVEQIAGFIARRIVCNLRTSQSVKAGERFGIIRFGSRVNIYIPAGIEVRVSEGQTVIGGETVIADLNKQEKLTFDIV

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
MRWX01000047
EMBL· GenBank· DDBJ
PBQ26534.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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