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UniRule: UR000100757

Source Rule HAMAP: MF_01139

View all proteins annotated by this ruleRemove highlights

The annotation and conditions in this rule are derived from the following entries: P60472 (UPPS_ECOLI), O82827 (UPPS_MICLU), Q9HH76 (UPPS_SULAC), P9WFF7 (DPDS_MYCTU), A0R0S4 (DPDS_MYCS2), P9WFF5 (ZFPP_MYCTU), A0R2W4 (ZFPP_MYCS2), Q47SS3 (ZFPP_THEFY), Q47RM6 (DPDP_THEFY)

If a protein meets these conditions... i

Common conditions

Special conditions

    • Subsequence at position 26 - 26 aligns to "D" in entry P60472 (individually applies "")
    • Subsequence at position 27 - 30 aligns to "G-N-x-[RK]" in entry P60472 (individually applies "Substrate binding")
    • Subsequence at position 31 - 31 aligns to "[WF]" in entry P60472 (individually applies "Substrate")
    • Subsequence at position 194 - 194 aligns to "R" in entry P60472 (individually applies "Substrate")
    • Subsequence at position 71 - 73 aligns to "S-x-[ED]" in entry P60472 (individually applies "Substrate binding")
    • Subsequence at position 26 - 26 aligns to "D" in entry P60472 (individually applies "Magnesium")
    • Subsequence at position 39 - 39 aligns to "[RK]" in entry P60472 (individually applies "Substrate")
    • Subsequence at position 75 - 75 aligns to "[WF]" in entry P60472 (individually applies "Substrate")
    • Subsequence at position 43 - 43 aligns to "H" in entry P60472 (individually applies "Substrate")
    • Subsequence at position 77 - 77 aligns to "[RK]" in entry P60472 (individually applies "Substrate")
    • Subsequence at position 74 - 74 aligns to "N" in entry P60472 (individually applies "Proton acceptor")
    • Subsequence at position 213 - 213 aligns to "E" in entry P60472 (individually applies "Magnesium")
    • Subsequence at position 200 - 202 aligns to "R-x-S" in entry P60472 (individually applies "Substrate binding")

... 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

  • Recommended name:
    Tritrans,polycis-undecaprenyl-diphosphate synthase (geranylgeranyl-diphosphate specific) (EC:2.5.1.89)
    Alternative name(s):
    Undecaprenyl diphosphate synthase
    Short name:
    UDS
    Undecaprenyl pyrophosphate synthase
    Short name:
    UPP synthase
  • Recommended name:
    Ditrans,polycis-undecaprenyl-diphosphate synthase ((2E,6E)-farnesyl-diphosphate specific) (EC:2.5.1.31)
    Alternative name(s):
    Ditrans,polycis-undecaprenylcistransferase
    Undecaprenyl diphosphate synthase
    Short name:
    UDS
    Undecaprenyl pyrophosphate synthase
    Short name:
    UPP synthase
  • Recommended name:
    Isoprenyl transferase (EC:2.5.1.-)

<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:uppS

<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

  • Catalyzes the sequential condensation of isopentenyl diphosphate (IPP) with geranylgeranyl diphosphate (GGPP) to yield (2Z,6Z,10Z,14Z,18Z,22Z,26Z,30E,34E,38E)-undecaprenyl diphosphate (tritrans,heptacis-UPP). It is probably the precursor of glycosyl carrier lipids.
  • Catalyzes the sequential condensation of isopentenyl diphosphate (IPP) with (2E,6E)-farnesyl diphosphate (E,E-FPP) to yield (2Z,6Z,10Z,14Z,18Z,22Z,26Z,30Z,34E,38E)-undecaprenyl diphosphate (di-trans,octa-cis-UPP). UPP is the precursor of glycosyl carrier lipid in the biosynthesis of bacterial cell wall polysaccharide components such as peptidoglycan and lipopolysaccharide.
  • Catalyzes the condensation of isopentenyl diphosphate (IPP) with allylic pyrophosphates generating different type of terpenoids.

<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

  • Homodimer.

<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 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 31)
  • Substrate (to residues corresponding to position 194)
  • Substrate (to residues corresponding to position 39)
  • Substrate (to residues corresponding to position 75)
  • Substrate (to residues corresponding to position 43)
  • Substrate (to residues corresponding to position 77)

<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 26)
  • Proton acceptor (to residues corresponding to position 74)

<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 27 - 30)
  • Substrate binding (to residues corresponding to positions 71 - 73)
  • Substrate binding (to residues corresponding to positions 200 - 202)

<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 199)
  • Magnesium (to residues corresponding to position 26)
  • Magnesium (to residues corresponding to position 213)

<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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