D3ZAW2 · PISD_RAT

  • Protein
    Phosphatidylserine decarboxylase proenzyme, mitochondrial
  • Gene
    Pisd
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

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. May be involved in lipid droplet biogenesis at the endoplasmic reticulum membrane (By similarity).

Catalytic activity

Cofactor

pyruvate (UniProtKB | Rhea| CHEBI:15361 )

Note: Binds 1 pyruvoyl group covalently per subunit.

Activity regulation

Inhibited by hydroxylamine.

Kinetics

KM SUBSTRATE pH TEMPERATURE[C] NOTES EVIDENCE
67 μMphosphatidylserine
Vmax pH TEMPERATURE[C] NOTES EVIDENCE
77 nmol/h/mg

pH Dependence

Optimum pH is 5.

Pathway

Phospholipid metabolism; phosphatidylethanolamine biosynthesis.

Features

Showing features for active site, site.

TypeIDPosition(s)Description
Active site188Charge relay system; for autoendoproteolytic cleavage activity
Active site264Charge relay system; for autoendoproteolytic cleavage activity
Site374-375Cleavage (non-hydrolytic); by autocatalysis
Active site375Charge relay system; for autoendoproteolytic cleavage activity
Active site375Schiff-base intermediate with substrate; via pyruvic acid; for decarboxylase activity

GO annotations

AspectTerm
Cellular Componentlipid droplet
Cellular Componentmitochondrial inner membrane
Cellular Componentmitochondrion
Molecular Functionphosphatidylserine decarboxylase activity
Biological Processlipid droplet formation
Biological Processmitochondrial protein catabolic process
Biological Processphosphatidylethanolamine biosynthetic process
Biological Processprotein autoprocessing
Biological Processregulation of mitochondrion organization

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

Gene names

    • Name
      Pisd

Organism names

  • Taxonomic identifier
  • Strain
    • Brown Norway
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Rattus

Accessions

  • Primary accession
    D3ZAW2

Proteomes

Organism-specific databases

Subcellular Location

Lipid droplet
Note: Predominantly localizes to lipid droplets in lipid-replete conditions, and to mitochondria in lipid-deplete conditions.

Phosphatidylserine decarboxylase beta chain

Mitochondrion inner membrane
; Single-pass membrane protein

Phosphatidylserine decarboxylase alpha chain

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

Features

Showing features for topological domain, transmembrane.

TypeIDPosition(s)Description
Topological domain50-60Mitochondrial matrix
Transmembrane61-79Helical
Topological domain80-406Mitochondrial intermembrane

Keywords

PTM/Processing

Features

Showing features for transit peptide, chain, modified residue.

TypeIDPosition(s)Description
Transit peptide1-49Mitochondrion
ChainPRO_000043557550-374Phosphatidylserine decarboxylase beta chain
ChainPRO_000043557450-406Phosphatidylserine decarboxylase proenzyme, mitochondrial
Modified residue375Pyruvic acid (Ser); by autocatalysis
ChainPRO_0000435576375-406Phosphatidylserine 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

Proteomic databases

PTM databases

Expression

Gene expression databases

Interaction

Subunit

Heterodimer of a large membrane-associated beta subunit and a small pyruvoyl-containing alpha subunit.

Protein-protein interaction databases

Structure

Family & Domains

Sequence similarities

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    406
  • Mass (Da)
    45,824
  • Last updated
    2015-07-22 v3
  • Checksum
    5358A6A2A6D72EE7
MAVAGGRGCVRSLREGVLWRSSPCHCDYTATRHFLGALQKLPLQAWVRKVHTAPLRTLFLLRPVPILLAAGGGYAGYRQYEKYRERQLEKLGLEIPPKLASHWEVSLYKSVPTRLLSRACGRLNQVELPSWLRRPVYSLYIWTFGVNMTEAAVEDLQHYRNLSEFFRRKLKPQARPVCGLHSVISPSDGKILTFGQVKNSEVEQVKGVTYSLESFLGPRACTEDLPFPPASSCDSFRNQLVTREGNELYHCVIYLAPGDYHCFHSPTDWTVSHRRHFPGSLMSVNPGMARWIKELFCHNERVVLTGDWKHGFFSLTAVGATNVGSIRIHFDQDLHTNSPSYSKGSYNDLSFVTHANKEGIPMRKGEPLGEFNLGSTIVLIFEAPKDFNFRLKAGQKILFGEALGSL

Computationally mapped potential isoform sequences

There are 5 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
A0A0G2JTF7A0A0G2JTF7_RATPisd375
A0A0G2K0F9A0A0G2K0F9_RATPisd262
A0A8I6GLT0A0A8I6GLT0_RATPisd409
A0A8I5ZNJ4A0A8I5ZNJ4_RATPisd365
A0A8L2QDB1A0A8L2QDB1_RATPisd388

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AC105515
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.

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