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The annotation and conditions in this rule are derived from the following entries: P0A6I6 (COAD_ECOLI), O26010 (COAD_HELPY), P9WPA5 (COAD_MYCTU), P63820 (COAD_STAAW), Q8DNE6 (COAD_STRR6), O34797 (COAD_BACSU), Q3JW91 (COAD_BURP1), Q831P9 (COAD_ENTFA), B7V2S6 (COAD_PSEA8), P63819 (COAD_STAAN), Q9WZK0 (COAD_THEMA), Q5SJS9 (COAD_THET8), Q8ZJN9 (COAD_YERPE)

If a protein meets these conditions... i

Common conditions

    • Matches HAMAP signature MF_00151
    • taxon = Bacteria
    • fragment ≠ the sequence is fragmented

Special conditions

    • Subsequence at position 88 - 88 aligns to "[RK]" in entry P0A6I6 (individually applies "Substrate")
    • Subsequence at position 10 - 11 aligns to "[TS]-[FYL]" in entry P0A6I6 (individually applies "ATP")
    • Subsequence at position 18 - 18 aligns to "H" in entry P0A6I6 (individually applies "Transition state stabilizer")
    • Subsequence at position 42 - 42 aligns to "K" in entry P0A6I6 (individually applies "Substrate")
    • Subsequence at position 99 - 99 aligns to "E" in entry P0A6I6 (individually applies "ATP")
    • Subsequence at position 10 - 10 aligns to "[TS]" in entry P0A6I6 (individually applies "Substrate")
    • Subsequence at position 89 - 91 aligns to "G-x-R" in entry P0A6I6 (individually applies "ATP")
    • Subsequence at position 18 - 18 aligns to "H" in entry P0A6I6 (individually applies "ATP")
    • Subsequence at position 74 - 74 aligns to "[MLVIATS]" in entry P0A6I6 (individually applies "Substrate; via amide nitrogen")
    • Subsequence at position 124 - 130 aligns to entry P0A6I6 (individually applies "ATP")

... 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 namei

  • Recommended name:
    Phosphopantetheine adenylyltransferase (EC:2.7.7.3)
    Alternative name(s):
    Dephospho-CoA pyrophosphorylase
    Pantetheine-phosphate adenylyltransferase
    Short name:
    PPAT

<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:coaD

<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 '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 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%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 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

  • Pathwayi: coenzyme A biosynthesis

    This protein is involved in step 4 of the subpathway that synthesizes CoA from (R)-pantothenate. This subpathway is part of the pathway coenzyme A 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 CoA from (R)-pantothenate, the pathway coenzyme A biosynthesis and in Cofactor biosynthesis.

<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

  • Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate.

<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%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 10 - 11)
  • ATP (to residues corresponding to positions 89 - 91)
  • ATP (to residues corresponding to positions 124 - 130)

<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

  • Transition state stabilizer (to residues corresponding to position 18)

<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

  • Substrate (to residues corresponding to position 88)
  • Substrate (to residues corresponding to position 42)
  • ATP (to residues corresponding to position 99)
  • Substrate (to residues corresponding to position 10)
  • ATP (to residues corresponding to position 18)
  • Substrate; via amide nitrogen (to residues corresponding to position 74)

<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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