A0AAN1H9Z7 · A0AAN1H9Z7_9ENTR

  • 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).

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 site90Charge relay system; for autoendoproteolytic cleavage activity
Active site147Charge relay system; for autoendoproteolytic cleavage activity
Site253-254Cleavage (non-hydrolytic); by autocatalysis
Active site254Charge relay system; for autoendoproteolytic cleavage activity
Active site254Schiff-base intermediate with substrate; via pyruvic acid; for decarboxylase activity

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

Gene names

    • Name
      psd
    • ORF names
      CU081_01545

Organism names

  • Taxonomic identifier
  • Strain
    • CRENT-193
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Enterobacter

Accessions

  • Primary accession
    A0AAN1H9Z7

Proteomes

Subcellular Location

Cell membrane
; Peripheral membrane protein

Keywords

PTM/Processing

Features

Showing features for chain, modified residue.

Type
IDPosition(s)Description
ChainPRO_50426532971-253Phosphatidylserine decarboxylase beta chain
Modified residue254Pyruvic acid (Ser); by autocatalysis
ChainPRO_5042653296254-322Phosphatidylserine 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 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.

Type
IDPosition(s)Description
Region294-322Disordered
Compositional bias301-322Basic and acidic residues

Sequence similarities

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    322
  • Mass (Da)
    35,835
  • Last updated
    2024-10-02 v1
  • Checksum
    C87920E834B30F86
MLNSFKLSLQYILPKLWLTRLAGWGASKRAGWLTKLVIDLFVKYYKVDMKEAQKPDTASYRTFNEFFVRPLRDEVRPLNTDPNVLVMPADGVISQLGKIEDDKILQAKGHNYSLEALLAGNYIMADLFRNGTFATTYLSPRDYHRVHMPCNGILREMIYVPGDLFSVNHLTAQNVPNLFARNERVICLFDTEFGPMAQILVGATIVGSIETVWAGTITPPREGVIKRWTWPAGEEEGSVALLKGQEMGRFKLGSTVINLFAPGKVNLVDELESLSVTKLGQPLAVSTEVFATPDVAPAPLPEDEIKAEHDASPLVDDKKDEG

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias301-322Basic and acidic residues

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP024812
EMBL· GenBank· DDBJ
ATW94577.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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