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The annotation and conditions in this rule are derived from the following entries: P14193 (KPRS_BACSU), P0A717 (KPRS_ECOLI), Q97CA5 (KPRS_THEVO), Q58761 (KPRS_METJA), P9WKE3 (KPRS_MYCTU)

If a protein meets these conditions... i

Common conditions

    • Matches HAMAP signature MF_00583_A
    • taxon = Archaea
    • fragment ≠ the sequence is fragmented

Special conditions

    • taxon = Bacteria Subsequence at position 198 - 198 aligns to "K" in entry P14193
    • taxon = Bacteria Subsequence at position 175 - 175 aligns to "D" in entry P14193
    • taxon = Bacteria
    • Subsequence at position 198 - 198 aligns to "K" in entry P14193
    • taxon = Bacteria
    • Subsequence at position 175 - 175 aligns to "D" in entry P14193
    • taxon = Bacteria
    • Subsequence at position 200 - 200 aligns to "R" in entry P14193 (individually applies "Ribose-5-phosphate")
    • Subsequence at position 136 - 136 aligns to "H" in entry P14193 (individually applies "Magnesium")
    • Subsequence at position 224 - 224 aligns to "D" in entry P14193 (individually applies "Ribose-5-phosphate")
    • Subsequence at position 228 - 232 aligns to "[DN]-[TS]-[AG]-x-[TS]" in entry P14193 (individually applies "Ribose-5-phosphate binding")
    • Subsequence at position 102 - 103 aligns to "R-Q" in entry P14193 (individually applies "ATP")
    • Subsequence at position 43 - 45 aligns to "[DN]-x-[EN]" in entry P14193 (individually applies "ATP")
    • taxon = Archaea
    • Subsequence at position 161 - 161 aligns to "D" in entry Q97CA5 (individually applies "Magnesium 2")
    • Subsequence at position 184 - 184 aligns to "K" in entry Q97CA5 (individually applies "")
    • Subsequence at position 210 - 210 aligns to "D" in entry Q97CA5 (individually applies "Ribose-5-phosphate")
    • Subsequence at position 124 - 124 aligns to "H" in entry Q97CA5 (individually applies "Magnesium 1")
    • Subsequence at position 214 - 218 aligns to "S-T-G-x-T" in entry Q97CA5 (individually applies "Ribose-5-phosphate binding")
    • Subsequence at position 34 - 36 aligns to "D-x-E" in entry Q97CA5 (individually applies "ATP")
    • Subsequence at position 91 - 92 aligns to "R-Q" in entry Q97CA5 (individually applies "ATP")
    • Subsequence at position 186 - 186 aligns to "R" in entry Q97CA5 (individually applies "Ribose-5-phosphate")

... then these annotations are applied i

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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

  • Alternative name(s):
    5-phospho-D-ribosyl alpha-1-diphosphate
    Phosphoribosyl diphosphate synthase
    Phosphoribosyl pyrophosphate synthase
    Short name:
    P-Rib-PP synthase
    Short name:
    PRPP synthase
    Short name:
    PRPPase
  • Recommended name:
    Ribose-phosphate pyrophosphokinase (EC:2.7.6.1)
    Short name:
    RPPK
  • Recommended name:
    Putative ribose-phosphate pyrophosphokinase (EC:2.7.6.1)
    Short name:
    RPPK

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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:prs

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'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/function%5Fsection">Function</a> describes the function(s) of a protein.<p><a href='/help/function' target='_top'>More...</a></p>Functioni

  • Involved in the biosynthesis of the central metabolite phospho-alpha-D-ribosyl-1-pyrophosphate (PRPP) via the transfer of pyrophosphoryl group from ATP to 1-hydroxyl of ribose-5-phosphate (Rib-5-P).

<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/interaction%5Fsection">'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%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

  • Homohexamer.

<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 reports a variety of possible errors and/or grounds for confusion relevant to different aspects of the information provided on the protein. Note that errors concerning the protein sequence are reported in the <a href="http://www.uniprot.org/help/sequence%5Fcaution">'Sequence caution'</a> subsection.<p><a href='/help/caution' target='_top'>More...</a></p>Cautioni

  • Part of a set of proteins in which some residues (ACT_SITE, NP_BIND, REGION and BINDING) are not conserved.

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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%5Fsection">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

  • Magnesium (to residues corresponding to position 175)
  • Magnesium (to residues corresponding to position 136)
  • Magnesium 2 (to residues corresponding to position 161)
  • Magnesium 1 (to residues corresponding to position 124)

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi

  • ATP (to residues corresponding to positions 102 - 103)
  • ATP (to residues corresponding to positions 43 - 45)
  • ATP (to residues corresponding to positions 34 - 36)
  • ATP (to residues corresponding to positions 91 - 92)

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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

  • Ribose-5-phosphate (to residues corresponding to position 200)
  • Ribose-5-phosphate (to residues corresponding to position 224)
  • Ribose-5-phosphate (to residues corresponding to position 210)
  • Ribose-5-phosphate (to residues corresponding to position 186)

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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

  • (to residues corresponding to position 198)
  • (to residues corresponding to position 184)

<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

  • Ribose-5-phosphate binding (to residues corresponding to positions 228 - 232)
  • Ribose-5-phosphate binding (to residues corresponding to positions 214 - 218)

<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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