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R8BXU1 · R8BXU1_PHAM7

Function

function

Catalyzes the formation of phosphatidylethanolamine (PtdEtn) from phosphatidylserine (PtdSer). Plays a central role in phospholipid metabolism and in the interorganelle trafficking of phosphatidylserine.

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 site881Charge relay system; for autoendoproteolytic cleavage activity
Active site939Charge relay system; for autoendoproteolytic cleavage activity
Site1025-1026Cleavage (non-hydrolytic); by autocatalysis
Active site1026Charge relay system; for autoendoproteolytic cleavage activity
Active site1026Schiff-base intermediate with substrate; via pyruvic acid; for decarboxylase activity

GO annotations

AspectTerm
Cellular Componentendosome membrane
Cellular ComponentGolgi membrane
Cellular ComponentGolgi stack
Molecular Functioncalcium ion binding
Molecular Functionphosphatidylserine decarboxylase activity
Biological Processphosphatidylethanolamine biosynthetic process
Biological Processprotein autoprocessing

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

Gene names

    • Name
      PSD2
    • ORF names
      UCRPA7_311

Organism names

Accessions

  • Primary accession
    R8BXU1

Proteomes

Subcellular Location

Golgi apparatus membrane
; Peripheral membrane protein
Endosome membrane
; Peripheral membrane protein

Keywords

PTM/Processing

Features

Showing features for chain, modified residue.

Type
IDPosition(s)Description
ChainPRO_50233306631-1025Phosphatidylserine decarboxylase 2 beta chain
Modified residue1026Pyruvic acid (Ser); by autocatalysis
ChainPRO_50233306621026-1120Phosphatidylserine decarboxylase 2 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. Interacts with pstB2. This interaction may be a means to structurally tether the donor membrane (ER) harboring PstB2 to acceptor membranes (Golgi/endosomes) harboring PSD2 during PtdSer transport to the site of PtdEtn synthesis.

Family & Domains

Features

Showing features for domain, region, compositional bias.

Type
IDPosition(s)Description
Domain1-117C2
Region166-239Disordered
Compositional bias167-187Polar residues
Compositional bias207-226Acidic residues
Domain248-369C2
Region362-381Disordered
Compositional bias393-429Polar residues
Region393-441Disordered
Domain524-559EF-hand
Region628-676Disordered
Compositional bias643-664Polar residues
Region1059-1120Disordered
Compositional bias1070-1098Basic and acidic residues

Domain

The C2 domains have an essential, but non-catalytic function. They may facilitate interactions with other proteins and are required for lipid transport function.

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    1,120
  • Mass (Da)
    124,215
  • Last updated
    2013-07-24 v1
  • MD5 Checksum
    47EBDA8CF886929A0AB940C036275FFE
MRSKDPVSPEGPKEGLLLSIVVLKARNLAAKDRGGTSDPYLVLTLGDAKHITSSQSKTLNPEWNEQCQMPVTGVQHMLLSVCCWDKDRFGKDYLGEFDLALEEIFADGKFEQLPKWFPLKSKRPGKKTSLVSGEVLLQFTLYDAANPNATDQQVAEKFGTLVKAVPEAESTSRNPTPTLTPVLAPTSAPGKSPSPPLTRRATDRTDVDDDDDYDVYDDETPEDEDPTKPEAIEKKKRRLRIKGLKRKKRENPYEFTNGGSNDVMGIIFLEICNITDLPPESNFTKTGFDMDPFVVASLGKKTYRTKVVRHNLNPVFNEKMLFQVLEHEKNYSFAFMVIDRDRYSGNDFIASTSLPLKELIDRSPKADPETGLYDLRDPPEYVPSQRSRFARLGLSRSSSAQSLGKLSRPPLSKNPSTVSNVSQIAPTTPAPTSAPGPQLSGDGIMEASQPLPSPGLLAPTISGGSGGGNGASVTSAAGELLPDSEDGDFSSISLPLKMKNIDKWEAKHSPTLALRAKYMPYPALRQQFWRALLKQYDTDESGRISKVELTTMLDTLGSTLRDSTINRFFQRFPHKGTNGDDLSDLTIDEAVICLEDQLEAESKPPTVGDRVKSMLPDLTQAKDYLGIPTKSGAEIPQPPSDASSEVLGPSASQTSTSTLTIPELNTPGEEGDLLNKDDLNDREEEHVVEIRECPICHQPRLNKRKDADIITHIATCASQDWRQVNNLMMAGFVTASQAQRKWYSKVITKISYGGYKLGANSANILVQDRLTGQINEEKMSVYVRLGIRLLYKGLKSNNMENKRIRKMLKGLSIKQGKKYDDPASKSEIEGFIKFHGLDMSEVLRPIEEFKNFNEFFYRELKPDARPCSAPDNPNIIVSPADCRSVVFNRIDVAQKIWIKGREFSVKRLLGDAYPEDAKRYENGALGIFRLAPQDYHRFHIPVDGTLLKPKLIAGEYYTVNPMAIRSALDVYGENVRVICPIDSVKHGRVMVVCVGAMMVGSTVITRKEGEQVKRAEELGYFKFGGSTIVLLFEDGKMKFDDDLVDNSTGALETLIRAGTSVGHSPNESQWTPDMRKDEKDVTEQDKKDAKRRIQGSLSLEESPEDSDDSPVPSQGIQGPI

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias167-187Polar residues
Compositional bias207-226Acidic residues
Compositional bias393-429Polar residues
Compositional bias643-664Polar residues
Compositional bias1070-1098Basic and acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
KB932799
EMBL· GenBank· DDBJ
EOO04145.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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