A0A5C6GFM8 · A0A5C6GFM8_9HYPO

  • Protein
    Phosphatidylserine decarboxylase proenzyme 1, mitochondrial
  • Gene
    PSD1
  • 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.

Type
IDPosition(s)Description
Active site214Charge relay system; for autoendoproteolytic cleavage activity
Active site360Charge relay system; for autoendoproteolytic cleavage activity
Site487-488Cleavage (non-hydrolytic); by autocatalysis
Active site488Charge relay system; for autoendoproteolytic cleavage activity
Active site488Schiff-base intermediate with substrate; via pyruvic acid; for decarboxylase activity

GO annotations

AspectTerm
Cellular Componentmitochondrial inner membrane
Molecular Functionphosphatidylserine decarboxylase activity
Biological Processphosphatidylethanolamine biosynthetic process
Biological Processprotein autoprocessing

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

Gene names

    • Name
      PSD1
    • ORF names
      ED733_004779

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • Cep018-CH2
  • Taxonomic lineage
    Eukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Sordariomycetes > Hypocreomycetidae > Hypocreales > Clavicipitaceae > Metarhizium

Accessions

  • Primary accession
    A0A5C6GFM8

Proteomes

Subcellular Location

Phosphatidylserine decarboxylase 1 alpha chain

Mitochondrion inner membrane
; Peripheral membrane protein
Note: Anchored to the mitochondrial inner membrane through its interaction with the integral membrane beta chain.

Phosphatidylserine decarboxylase 1 beta chain

Mitochondrion inner membrane
; Single-pass membrane protein

Features

Showing features for topological domain.

TypeIDPosition(s)Description
Topological domain1-78Mitochondrial matrix
Topological domain98-533Mitochondrial intermembrane

Keywords

PTM/Processing

Features

Showing features for chain, modified residue.

Type
IDPosition(s)Description
ChainPRO_50233065701-487Phosphatidylserine decarboxylase 1 beta chain
Modified residue488Pyruvic acid (Ser); by autocatalysis
ChainPRO_5023306568488-533Phosphatidylserine decarboxylase 1 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 compositional bias, region.

Type
IDPosition(s)Description
Compositional bias105-124Basic and acidic residues
Region105-126Disordered

Sequence similarities

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    533
  • Mass (Da)
    58,792
  • Last updated
    2019-11-13 v1
  • Checksum
    48335E98FE4B358D
MAALGVGSGQLLRRHALANLRRPCSSCADQHMATLMLTSRSTLRTPIVVRNFSSRSNQRPRFSQRLGEALRNSKITWYHIPVGVGIGFLGLVQFYKVTAREQEKQRQADGGAADQPKRRQRIRPEGPWQVQVMSTLPLKAISRLWGKFNELTIPYYLRVPGFKLYSFIFGVNLDEVSEPDLHIYPNLAAFFYRTLKPGARPLDPDSHALLSPSDGKLLQYGRIEGGDIEQVKGMTYSVDALLGQNTPTASIASGQSSVSDRSSGSVAHGDEAVVRQEEEFAKMNGISYTLPDLLSGQADSQGPHRATDESTEVSARAVSEVRAELALGEKPWYDVVSADKSTSLYYAVIYLAPGDYHRFHSPTDWVVERRRHFAGELYSVSPYLQRTLPGLFTLNERVVLLGRWRYGFFGYVPVGATNVGSIRINFDRELRTNSLLTDTAAGLAAEQAAERGEPYTGFAEATYEGASPVLHGHALRRGEEMGGFQLGSTIVLVFEAPSEKAQGEGKPASGWHWAVDKGQTVKMGQALGRVVEQ

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias105-124Basic and acidic residues

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
SBHS01000010
EMBL· GenBank· DDBJ
TWU74693.1
EMBL· GenBank· DDBJ
Genomic DNA

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.
Help