A0A0F5PGD5 · A0A0F5PGD5_9SPHN

  • 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.

Type
IDPosition(s)Description
Site202-203Cleavage (non-hydrolytic); by autocatalysis
Active site203Schiff-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
      WP12_02975

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • SRS2
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Alphaproteobacteria > Sphingomonadales > Sphingomonadaceae > Sphingomonas

Accessions

  • Primary accession
    A0A0F5PGD5

Proteomes

Subcellular Location

Cell membrane
; Peripheral membrane protein

Features

Showing features for transmembrane.

TypeIDPosition(s)Description
Transmembrane28-61Helical

Keywords

PTM/Processing

Features

Showing features for chain, modified residue.

Type
IDPosition(s)Description
ChainPRO_50232387071-202Phosphatidylserine decarboxylase beta chain
Modified residue203Pyruvic acid (Ser); by autocatalysis
ChainPRO_5023238711203-244Phosphatidylserine 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.

Protein-protein interaction databases

Family & Domains

Sequence similarities

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

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    244
  • Mass (Da)
    26,218
  • Last updated
    2015-06-24 v1
  • MD5 Checksum
    87014EFFD8C9C828D4A8C6EA8B21276F
MTSLDKPDIGTTSVKWRWPGVHPEGRKFVLLAAVIALVFALLAWETLAWPMAGITVWVAAFFRDPIRTTPTGEGLVIAPADGLVTMITTVPPPREMAGEDGLGDAPMTRVSIFMSVFDVHINRTPIAGTVRKVAYIPGSFLNADLDKASEENERQHILVEAIDGTRIGFTQIAGLVARRIVPFVKAGDIVGLGQRIGLIRFGSRVDVYLPAGTGHRVTLGQRTIAGETVIARLGESDRTVGAAQ

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
LARW01000050
EMBL· GenBank· DDBJ
KKC27470.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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