A0A223NQZ6 · A0A223NQZ6_9SPHI

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

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

Features

Showing features for site, active site.

TypeIDPosition(s)Description
Site187-188Cleavage (non-hydrolytic); by autocatalysis
Active site188Schiff-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
      MuYL_0267

Organism names

  • Taxonomic identifier
  • Strain
    • BJC16-A31
  • Taxonomic lineage
    Bacteria > Bacteroidota > Sphingobacteriia > Sphingobacteriales > Sphingobacteriaceae > Mucilaginibacter

Accessions

  • Primary accession
    A0A223NQZ6

Proteomes

Subcellular Location

Cell membrane
; Peripheral membrane protein

Features

Showing features for transmembrane.

TypeIDPosition(s)Description
Transmembrane7-29Helical
Transmembrane35-54Helical

Keywords

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_50234178771-187Phosphatidylserine decarboxylase beta chain
Modified residue188Pyruvic acid (Ser); by autocatalysis
ChainPRO_5023417876188-257Phosphatidylserine 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

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    257
  • Mass (Da)
    28,982
  • Last updated
    2017-10-25 v1
  • Checksum
    3650E4166D9FBF4C
MTFHKEGYTSLAICILFIFVLNFLVSFYFPEAHVLKWIVYILSFFLFVTIVQFFRSPKITIDAHDKYVLCPADGKVVVIEETEETEFLKDRRIQLSVFMSPINVHINRNPIAGVVKYFKYNPGKYLVAWHPKSSTENERTTIAIENKAGVIVLFRQIAGALARRIVWYVKEGDVVEQGEQFGFIKFGSRVDVFLPLGTEIKVELGQVVKGGKTILAELADKPAAVKTTAAKEAATSEADDAFEKVKAARPVKNTIKK

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP022743
EMBL· GenBank· DDBJ
ASU32170.1
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.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp