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The annotation and conditions in this rule are derived from the following entries: P23721 (SERC_ECOLI), Q59196 (SERC_BACCI), P52878 (SERC_METBF), Q9RME2 (SERC_BACAO), P80862 (SERC_BACSU)

If a protein meets these conditions... i

Common conditions

Special conditions

    • Subsequence at position 9 - 9 aligns to "S" in entry P23721 (individually applies "L-glutamate")
    • Subsequence at position 153 - 153 aligns to "T" in entry P23721 (individually applies "Pyridoxal phosphate")
    • Subsequence at position 198 - 198 aligns to "K" in entry P23721 (individually applies "N6-(pyridoxal phosphate)lysine")
    • Subsequence at position 42 - 42 aligns to "R" in entry P23721 (individually applies "L-glutamate")
    • Subsequence at position 102 - 102 aligns to "[WF]" in entry P23721 (individually applies "Pyridoxal phosphate")
    • Subsequence at position 197 - 197 aligns to "Q" in entry P23721 (individually applies "Pyridoxal phosphate")
    • Subsequence at position 76 - 77 aligns to "[GA]-[RST]" in entry P23721 (individually applies "Pyridoxal phosphate binding")
    • Subsequence at position 174 - 174 aligns to "D" in entry P23721 (individually applies "Pyridoxal phosphate")
    • Subsequence at position 239 - 240 aligns to "N-T" in entry P23721 (individually applies "Pyridoxal phosphate binding")

... 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 namei

  • Recommended name:
    Phosphoserine aminotransferase (EC:2.6.1.52)
    Alternative name(s):
    Phosphohydroxythreonine aminotransferase
    Short name:
    PSAT

<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 namei

  • Name:serC

<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

  • Pathwayi: L-serine biosynthesis

    This protein is involved in step 2 of the subpathway that synthesizes L-serine from 3-phospho-D-glycerate. This subpathway is part of the pathway L-serine biosynthesis, which is itself part of Amino-acid biosynthesis.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-serine from 3-phospho-D-glycerate, the pathway L-serine biosynthesis and in Amino-acid biosynthesis.
  • Pathwayi: pyridoxine 5'-phosphate biosynthesis

    This protein is involved in step 3 of the subpathway that synthesizes pyridoxine 5'-phosphate from D-erythrose 4-phosphate. This subpathway is part of the pathway pyridoxine 5'-phosphate biosynthesis, which is itself part of Cofactor biosynthesis.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes pyridoxine 5'-phosphate from D-erythrose 4-phosphate, the pathway pyridoxine 5'-phosphate biosynthesis and in Cofactor biosynthesis.

<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 <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

  • Homodimer.

<p>This section describes the function(s) of a protein.<p><a href='/help/function' target='_top'>More...</a></p>Functioni

  • Catalyzes the reversible conversion of 3-phosphohydroxypyruvate to phosphoserine and of 3-hydroxy-2-oxo-4-phosphonooxybutanoate to phosphohydroxythreonine.

<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 ‘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 ‘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

  • N6-(pyridoxal phosphate)lysine (to residues corresponding to position 198)

<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni

  • Pyridoxal phosphate binding (to residues corresponding to positions 76 - 77)
  • Pyridoxal phosphate binding (to residues corresponding to positions 239 - 240)

<p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei

  • L-glutamate (to residues corresponding to position 9)
  • Pyridoxal phosphate (to residues corresponding to position 153)
  • L-glutamate (to residues corresponding to position 42)
  • Pyridoxal phosphate (to residues corresponding to position 102)
  • Pyridoxal phosphate (to residues corresponding to position 197)
  • Pyridoxal phosphate (to residues corresponding to position 174)

<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

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