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The annotation and conditions in this rule are derived from the following entries: B3L2V1 (PSD_PLAKH), P39006 (PSD1_YEAST)

If a protein meets these conditions... i

Common conditions

    • Matches HAMAP signature MF_03208
    • taxon = Eukaryota
    • fragment ≠ the sequence is fragmented

Special conditions

    • taxon ≠ Plasmodiidae
    • Subsequence at position @NTER@ - 17 aligns to entry B3L2V1 (individually applies "Mitochondrial matrix")
    • Subsequence at position 37 - @CTER@ aligns to entry B3L2V1 (individually applies "Mitochondrial intermembrane")
    • Subsequence at position 308 - 308 aligns to "S" in entry B3L2V1 (individually applies "Charge relay system; for autoendoproteolytic cleavage activity")
    • Subsequence at position 308 - 308 aligns to "S" in entry B3L2V1 (individually applies "Schiff-base intermediate with substrate; via pyruvic acid; for decarboxylase activity")
    • Subsequence at position 198 - 198 aligns to "H" in entry B3L2V1 (individually applies "Charge relay system; for autoendoproteolytic cleavage activity")
    • Subsequence at position 307 - 308 aligns to "G-S" in entry B3L2V1 (individually applies "Cleavage (non-hydrolytic); by autocatalysis")
    • Subsequence at position 139 - 139 aligns to "D" in entry B3L2V1 (individually applies "Charge relay system; for autoendoproteolytic cleavage activity")
    • Subsequence at position 308 - 308 aligns to "S" in entry B3L2V1 (individually applies "Pyruvic acid (Ser); by autocatalysis")

... then these annotations are applied i

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi

Cleaved chain(s) or included domain(s)i

  • Cleaved chain:
    Recommended name:
    Phosphatidylserine decarboxylase beta chain
  • Cleaved chain:
    Recommended name:
    Phosphatidylserine decarboxylase alpha chain
  • Cleaved chain:
    Recommended name:
    Phosphatidylserine decarboxylase 1 beta chain
  • Cleaved chain:
    Recommended name:
    Phosphatidylserine decarboxylase 1 alpha chain

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi

  • Name:PSD1
  • Name:PISD
  • Name:psd-1

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> describes the function(s) of a protein.<p><a href='/help/function' target='_top'>More...</a></p>Functioni

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

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

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

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

  • 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.

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei

  • Charge relay system; for autoendoproteolytic cleavage activity (to residues corresponding to position 308)
  • Schiff-base intermediate with substrate; via pyruvic acid; for decarboxylase activity (to residues corresponding to position 308)
  • Charge relay system; for autoendoproteolytic cleavage activity (to residues corresponding to position 198)
  • Charge relay system; for autoendoproteolytic cleavage activity (to residues corresponding to position 139)

<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini

  • Mitochondrial matrix (to residues corresponding to positions @NTER@i - 17)
  • Mitochondrial intermembrane (to residues corresponding to positions 37 - @CTER@i)

<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei

  • Cleavage (non-hydrolytic); by autocatalysis (to residues corresponding to positions 307 - 308)

<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei

  • Pyruvic acid (Ser); by autocatalysis (to residues corresponding to position 308)

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO (Gene Ontology) termsi

  • GO:0004609 phosphatidylserine decarboxylase activity
  • GO:0006646 phosphatidylethanolamine biosynthetic process
  • GO:0016540 protein autoprocessing
  • GO:0030176 integral component of endoplasmic reticulum membrane
  • GO:0031305 integral component of mitochondrial inner membrane
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