D4VP53 · D4VP53_9BACE

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
Site196-197Cleavage (non-hydrolytic); by autocatalysis
Active site197Schiff-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
      BN890_31800

Organism names

Accessions

  • Primary accession
    D4VP53

Proteomes

Subcellular Location

Cell membrane
; Peripheral membrane protein

Features

Showing features for transmembrane.

TypeIDPosition(s)Description
Transmembrane20-38Helical
Transmembrane44-62Helical

Keywords

PTM/Processing

Features

Showing features for chain, modified residue.

Type
IDPosition(s)Description
ChainPRO_50232145921-196Phosphatidylserine decarboxylase beta chain
Modified residue197Pyruvic acid (Ser); by autocatalysis
ChainPRO_5023214593197-228Phosphatidylserine 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
    228
  • Mass (Da)
    25,838
  • Last updated
    2010-06-15 v1
  • MD5 Checksum
    A28D33561666A52419E317C9E7DC1E9F
MGRLKKLKKIRIHREGTHILWASFLLLLLINAALYWGIDCKIPFYVVAVASIAVYLLMVNFFRCPIRLFGQDTEKIVVAPADGKIVVIEEVDENEYFHDRRLMVSIFMSIVNVHANWYPVDGTIKKVAHHNGNFMKAWLPKASTENERSTVVIETPEGVEILTRQIAGAVARRIVTYAEVGEECYIDEHMGFIKFGSRVDVYLPIGTEICVKMGQLTTGNQTVIAKLK

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CBXG010000038
EMBL· GenBank· DDBJ
CDM05587.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
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