A0A2M8HGK2 · A0A2M8HGK2_9LEPT

  • Protein
    Phosphatidylserine decarboxylase proenzyme
  • Gene
    psd
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    4/5

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

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 site544Charge relay system; for autoendoproteolytic cleavage activity
Active site600Charge relay system; for autoendoproteolytic cleavage activity
Site703-704Cleavage (non-hydrolytic); by autocatalysis
Active site704Charge relay system; for autoendoproteolytic cleavage activity
Active site704Schiff-base intermediate with substrate; via pyruvic acid; for decarboxylase activity

GO annotations

AspectTerm
Cellular Componentplasma membrane
Molecular Functionamino acid:sodium symporter activity
Molecular Functionphosphatidylserine decarboxylase activity
Biological Processphosphatidylethanolamine biosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

Gene names

    • Name
      psd
    • ORF names
      CK427_15160

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • FW.030
  • Taxonomic lineage
    Bacteria > Spirochaetota > Spirochaetia > Leptospirales > Leptospiraceae > Leptospira

Accessions

  • Primary accession
    A0A2M8HGK2

Proteomes

Subcellular Location

Cell membrane
; Multi-pass membrane protein
Cell membrane
; Peripheral membrane protein

Features

Showing features for transmembrane.

TypeIDPosition(s)Description
Transmembrane22-49Helical
Transmembrane70-94Helical
Transmembrane100-121Helical
Transmembrane148-176Helical
Transmembrane182-204Helical
Transmembrane211-232Helical
Transmembrane252-274Helical
Transmembrane300-322Helical
Transmembrane342-363Helical
Transmembrane384-401Helical
Transmembrane413-434Helical
Transmembrane459-482Helical

Keywords

PTM/Processing

Features

Showing features for chain, modified residue.

Type
IDPosition(s)Description
ChainPRO_50233719371-703Phosphatidylserine decarboxylase beta chain
Modified residue704Pyruvic acid (Ser); by autocatalysis
ChainPRO_5023371938704-746Phosphatidylserine 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 coiled coil.

TypeIDPosition(s)Description
Coiled coil497-524

Sequence similarities

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    746
  • Mass (Da)
    83,189
  • Last updated
    2018-04-25 v1
  • MD5 Checksum
    E9795624593E94F5FCB8AB9C61A97D1F
MKNNIFELTDFGFLGQDILNPYFYLIFFAGLVISIRLGFPQFRFFFLGLKILTGNMDEKGSKGQIVHSQSFFAGVGSSLLLGSFLGTALALMIGGIGALFWIWIAAIFIMPVRFVSSTLSIRFRQKLPSGRYLSGPVYFIEKALKAKWLSLSFGIGSLFTILLFGATYPMVAITYIAQKGLLIKGMAFPILVSVILVFIVLGGIRRVGKTAGYLAISGIVLFILSYFLLFYGKNSGLGFFSAVFSEAFRIESLTAGGIFILMKSMASSTGLFFLSTETGIGKSAGVSGSVRTDYPAKHGLVSMLSTFFEAFLVSPLFAYILFSNGAIGMEDQLVFYSGLLSNPLTIGSLCLYISLVAFGILSLTGWFYTGEQNSYYILGDRLSNVYRILFVITILSTAFLIDKFGGLMLPYLFNYSFTLAVITSVPLLVSLILLSKTARVELKKFISESGMKYEIIQDFYLVLLSILPKNLISKIFGIISMLRLPRFLMIPILKAFAKTYKVNLDEAELEIQEYNSLNQFFTRALRAEARIIDSAANALVSPVDARISAFGDIKEKSVIQAKGIDYSVSELIGVERYAKDFINGKFITFYLSPQDYHRIHSPFYGKVLGYYYEPGKLFPVNELAVLNIQSLFPKNERLITFLQTEYGKVAVVKVGASNVGKIRVTYDNKIVTNSWIRFSKEHEYKDISILIDKGAELGRFEMGSTVILIFEKDTMDLSPKLTLNEKTQYGNEIGFFRKKLINLPKN

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
PEQN01000057
EMBL· GenBank· DDBJ
PJD99920.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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