A0A4R0R991 · A0A4R0R991_9APHY

  • 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.

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.

TypeIDPosition(s)Description
Active site1028Charge relay system; for autoendoproteolytic cleavage activity
Active site1086Charge relay system; for autoendoproteolytic cleavage activity
Site1172-1173Cleavage (non-hydrolytic); by autocatalysis
Active site1173Charge relay system; for autoendoproteolytic cleavage activity
Active site1173Schiff-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
      EIP91_004230

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • LE-BIN_3174
  • Taxonomic lineage
    Eukaryota > Fungi > Dikarya > Basidiomycota > Agaricomycotina > Agaricomycetes > Polyporales > Steccherinaceae > Steccherinum

Accessions

  • Primary accession
    A0A4R0R991

Proteomes

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_50232110171-1172Phosphatidylserine decarboxylase 2 beta chain
Modified residue1173Pyruvic acid (Ser); by autocatalysis
ChainPRO_50232110181173-1220Phosphatidylserine 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.

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain, compositional bias, region.

TypeIDPosition(s)Description
Domain30-143C2
Compositional bias199-222Polar residues
Region199-420Disordered
Compositional bias223-239Acidic residues
Compositional bias256-331Polar residues
Compositional bias332-354Pro residues
Compositional bias365-410Polar residues
Domain426-547C2
Domain597-632EF-hand
Region731-831Disordered
Compositional bias763-779Polar residues
Compositional bias794-831Polar 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

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    1,220
  • Mass (Da)
    133,073
  • Last updated
    2019-07-31 v1
  • Checksum
    46FD7DC89DA574EC
MVRAPQKALKIGRAIKSAARYPVQKVNIVKGSGSSFAPLPGEVPIVLLKVQVLSCSNLLAKDKNGFSDPVRHQTPVAKRTCNPAYSPKDATFDFPLFLSLADKLGVVELIVWDKDMLKKDYLGEVSIPLEDWFRNGSAFAFSDPENKPFDVPVVSTRVHTHAKGTIQVKLGFEYPTNIAALMEFSDVYDELIKLSRPSLTSAPPTEGIGTIRSHQTGPQFEDDGLSSDDESDDEDEDVAGPSGSPSLLKLFIPAVRSKSSTPTDFMPGKQRSVSASSSGLLLSDIRQPQPIPATATSPMTTPTPTTTQFPAIPPSMSTTSSNGTITPSTPNEQPVPLAPVIAKPQPPSKPPSPASGFSIPRIFPRRPTSTRSSSVDSTMVSSTLSSSSGAPQLSTPSTSLPGSGTSTPVTPRPKGKFRKSWVGGSKQAGYNFSAGSNDVVGIVMLEIAKASDLPKLRNLTRTGWDMDPFVVISFGKKVFRTRVIRHSLNPLWDEKLLFHVRRYETSFKLQLQVLDWDKLSSNDHVGDAYLDLPTLIEGAAQKDEKTGLYPIDMEEVASEGGMKEFTLALSTAKEMPWESKHNPQLFIRAKYQPYDALRQRFWRQYLKQYDTDDTGTISNLELTSMLDSLGSTLSRETIDSFFIRFGKKPHEDVLTMDETVMCLETELCRPPEEKKRINFDESGHDTSVPVTPSLVTTHDISSMPGLSGAGGANALNLDKLDFAGPVSNQASASVEHISGDMRKPAPPPPYATEPMQEPLGDVASAGSLSTPSGGGVGGTTPTPRTAHFERLPSGSGSGASSDAEDASPPNGSSSSGGSHSGSSSPSSSEDSFERVINVKNCPLCHRPRLSSKAEVDIVTHLAVCASQDWARVDRIVVGNFVTASQAQRKWYTKVISKVSAGNYKLGANSANIIVQNRMTGQLEEEKMQVYVRLGIRLLYKGWKSRMEGGRARRLLKSLSIKQGLKYDSPESARDIPAFIEFHNLKVDEILEPLQNFKTFNQFFYRKLKPDARPVENPDDPTRLVSGADCRLMAFETVQEATRLWIKGREFSVARLLGERYRAEADKYIGGALCIFRLAPQDYHRFHVPVDGVIGPMTDITGEYYTVNPQAIRTALDVYGENVRKIVPIDSPQFGRVMMVCVGAMMVGSIKMTVEEGQQVKRGQEFGYFAFGGSTIVVLFEKGAVVEWDEDLIVNSKACLETLVRVGMGIGRGRRVPASPA

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias199-222Polar residues
Compositional bias223-239Acidic residues
Compositional bias256-331Polar residues
Compositional bias332-354Pro residues
Compositional bias365-410Polar residues
Compositional bias763-779Polar residues
Compositional bias794-831Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
RWJN01000241
EMBL· GenBank· DDBJ
TCD64361.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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