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The annotation and conditions in this rule are derived from the following entries: Q9X519 (GPMI_GEOSE), P39773 (GPMI_BACSU), P37689 (GPMI_ECOLI)

If a protein meets these conditions... i

Common conditions

    • Matches HAMAP signature MF_01038
    • gene location = Plastid
    • fragment ≠ the sequence is fragmented

Special conditions

    • Subsequence at position 407 - 407 aligns to "H" in entry Q9X519 Subsequence at position 444 - 444 aligns to "D" in entry Q9X519 Subsequence at position 445 - 445 aligns to "H" in entry Q9X519 Subsequence at position 403 - 403 aligns to "D" in entry Q9X519 Subsequence at position 462 - 462 aligns to "H" in entry Q9X519 Subsequence at position 62 - 62 aligns to "S" in entry Q9X519 Subsequence at position 12 - 12 aligns to "D" in entry Q9X519
    • gene location = Plastid; Chloroplast
  • Subsequence at position 407 - 407 aligns to "H" in entry Q9X519 (applies "Manganese 1") Subsequence at position 444 - 444 aligns to "D" in entry Q9X519 (applies "Manganese 2") Subsequence at position 445 - 445 aligns to "H" in entry Q9X519 (applies "Manganese 2") Subsequence at position 403 - 403 aligns to "D" in entry Q9X519 (applies "Manganese 1") Subsequence at position 462 - 462 aligns to "H" in entry Q9X519 (applies "Manganese 1") Subsequence at position 62 - 62 aligns to "S" in entry Q9X519 (applies "Manganese 2") Subsequence at position 12 - 12 aligns to "D" in entry Q9X519 (applies "Manganese 2")
    • Subsequence at position 261 - 264 aligns to "R-x-x-R" in entry Q9X519 (individually applies "Substrate binding")
    • Subsequence at position 62 - 62 aligns to "S" in entry Q9X519 (individually applies "Phosphoserine intermediate")
    • Subsequence at position 191 - 191 aligns to "[RK]" in entry Q9X519 (individually applies "Substrate")
    • Subsequence at position 336 - 336 aligns to "K" in entry Q9X519 (individually applies "Substrate")
    • Subsequence at position 185 - 185 aligns to "R" in entry Q9X519 (individually applies "Substrate")
    • Subsequence at position 123 - 123 aligns to "H" in entry Q9X519 (individually applies "Substrate")
    • Subsequence at position 153 - 154 aligns to "R-D" in entry Q9X519 (individually applies "Substrate 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:
    2,3-bisphosphoglycerate-independent phosphoglycerate mutase (EC:5.4.2.12)
    Short name:
    BPG-independent PGAM
    Short name:
    Phosphoglyceromutase
    Short name:
    iPGM

<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:gpmI

<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

  • Monomer.

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

  • Essential for rapid growth and for sporulation. Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate.
  • Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate.

<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 metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi

  • Pathwayi: glycolysis

    This protein is involved in step 3 of the subpathway that synthesizes pyruvate from D-glyceraldehyde 3-phosphate. This subpathway is part of the pathway glycolysis, which is itself part of Carbohydrate degradation.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes pyruvate from D-glyceraldehyde 3-phosphate, the pathway glycolysis and in Carbohydrate degradation.

<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/function_section">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi

  • Manganese 1 (to residues corresponding to position 407)
  • Manganese 2 (to residues corresponding to position 444)
  • Manganese 2 (to residues corresponding to position 445)
  • Manganese 1 (to residues corresponding to position 403)
  • Manganese 1 (to residues corresponding to position 462)
  • Manganese 2 (to residues corresponding to position 62)
  • Manganese 2 (to residues corresponding to position 12)

<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

  • Phosphoserine intermediate (to residues corresponding to position 62)

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> 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

  • Substrate (to residues corresponding to position 191)
  • Substrate (to residues corresponding to position 336)
  • Substrate (to residues corresponding to position 185)
  • Substrate (to residues corresponding to position 123)

<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

  • Substrate binding (to residues corresponding to positions 261 - 264)
  • Substrate binding (to residues corresponding to positions 153 - 154)

<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

  • Phosphotyrosine (to residues corresponding to position 36)

<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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