A0AAJ8W4T5 · A0AAJ8W4T5_CANPA

  • Protein
    Phosphatidylserine decarboxylase proenzyme 2
  • Gene
    PSD2
  • 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). 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.

TypeIDPosition(s)Description
Active site840Charge relay system; for autoendoproteolytic cleavage activity
Active site902Charge relay system; for autoendoproteolytic cleavage activity
Site988-989Cleavage (non-hydrolytic); by autocatalysis
Active site989Charge relay system; for autoendoproteolytic cleavage activity
Active site989Schiff-base intermediate with substrate; via pyruvic acid; for decarboxylase activity

GO annotations

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

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

Gene names

    • Name
      PSD2

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Fungi > Dikarya > Ascomycota > Saccharomycotina > Saccharomycetes > Saccharomycetales > Debaryomycetaceae > Candida/Lodderomyces clade > Candida

Accessions

  • Primary accession
    A0AAJ8W4T5

Subcellular Location

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

Keywords

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_50423021821-988Phosphatidylserine decarboxylase 2 beta chain
Modified residue989Pyruvic acid (Ser); by autocatalysis
ChainPRO_5042302181989-1110Phosphatidylserine 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 region, domain, compositional bias.

TypeIDPosition(s)Description
Region1-25Disordered
Domain34-163C2
Region315-337Disordered
Domain344-468C2
Region1091-1110Disordered
Compositional bias1092-1110Polar residues

Domain

The C2 domains have an essential, but non-catalytic function. They may facilitate interaction with PstB2 and are required for lipid transport function.

Sequence similarities

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    1,110
  • Mass (Da)
    125,741
  • Last updated
    2024-07-24 v1
  • Checksum
    3E24C0DB5A70E71F
MGDRFQDQSKSGSGSNSSSNSTSYASLRNIENNENSKINVDINQNSSSPYKLYLKINANRAADLVTTTDSEKEANAGKHSSRKFINPVLVAKINDKKKVTQRKTNTNQPSWDDELNLSLKRGDLSSILVISVWDKHKRYKNYLGELRLSLEKLFLKDDGTFTEKTELKWYGLSSNSTVHAFVTGSVLLSFELFVKRRKSRTITGKKEVGANVGAQMQDLRLNMTEQEFKTWLRSLIEPDSKALHSLTPDEQGFYDEAMTDISDMESLATKKSAGSILSNDRPANKIKKDNFLSVRGNDRYASSFSEQSSYLSTDAYSDGNLSQGGGERKDKPKRRLGIRKTGRAHSDLFKSKKFELSGRQVLGVLFIEIVSCEDLPPVSNFTRTSFDMDPFVVVTFGKKTFRTSWKRHTLSPIFNERVAFEVMAHESNYTVQFSVLDRDRFSFHDDVAHIKLALRDLIELSPFQSLMDHGLSSSDLSANPEPGYSTGDLDASSNSNVKILEEDNIVKSVRRGRFSNRRKIVESTVDTSKFKVMSLSLDLHDQKYLGKYSPKLKIRVRFETYNDLRKEFWKVLLKQYDLGETKQEETYDFMELVSLLDALGTKDAESLVEEFYRNLGKDATADSLAYDEIIEQLEIHVSLNDQNSNRIFVFDTCPLCSQKRLSKKQDTDIITHFAICASKDWSIVNKLLVSSYATPRHATKKWYSKALIKLTYGKYKLGGNTANIFVQDRLTGIIVEEKMSVYVRLGIRLLYKGLDKAKSKRVRLLLSSLSKKQGRKFDSPSSKADIASFIKFHKLSLDDCLIEDPEGYPTFNEFFYRKLKPNARVIEDKKNKGIVSSPADCRCTVFDSVDDATNLWIKGRNFTLAKLFNGNFQNLNTTNLYKSDQCSLGIFRLAPQDYHRFHSPVSGTIGPIKYIEGEYYTVNPMAIRSELDVFGENVRSIIPIQTKEYGMVIMIAVGAMMVGSICLTKQEGDSIERGEEVGYFKFGGSTIILLFDRTKFTFDSDLVSNSKSCIETLVRVGQSIGHSPDVNEFKRDHVEFDQLPQTTKLQLIRVLTGGDLTDKHQLSNWEANRTTGLEEVDEEEDYYVSDSNISFGADSSMEEEGSITSE

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias1092-1110Polar residues

Genome annotation databases

Similar Proteins

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