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The annotation and conditions in this rule are derived from the following entries: P0ACC7 (GLMU_ECOLI), Q97R46 (GLMU_STRPN), P9WMN3 (GLMU_MYCTU)

If a protein meets these conditions... i

Common conditions

    • Matches HAMAP signature MF_01631
    • taxon = Bacteria
    • fragment ≠ the sequence is fragmented

Special conditions

    • Subsequence at position 380 - 380 aligns to "A" in entry P0ACC7 (individually applies "Acetyl-CoA; via amide nitrogen")
    • Subsequence at position 103 - 105 aligns to "[SY]-G-D" in entry P0ACC7 (individually applies "UDP-GlcNAc binding")
    • Subsequence at position 227 - 227 aligns to "N" in entry P0ACC7 (individually applies "UDP-GlcNAc")
    • Subsequence at position 366 - 366 aligns to "Y" in entry P0ACC7 (individually applies "UDP-GlcNAc")
    • Subsequence at position 169 - 169 aligns to "N" in entry P0ACC7 (individually applies "UDP-GlcNAc")
    • Subsequence at position 230 - 250 aligns to entry P0ACC7 (individually applies "Linker")
    • Subsequence at position 227 - 227 aligns to "N" in entry P0ACC7 (individually applies "Magnesium")
    • Subsequence at position 386 - 387 aligns to "N-Y" in entry P0ACC7 (individually applies "Acetyl-CoA binding")
    • Subsequence at position 405 - 405 aligns to "S" in entry P0ACC7 (individually applies "Acetyl-CoA")
    • Subsequence at position 251 - @CTER@ aligns to entry P0ACC7 (individually applies "N-acetyltransferase")
    • Subsequence at position 11 - 14 aligns to "L-A-A-G" in entry P0ACC7 (individually applies "UDP-GlcNAc binding")
    • Subsequence at position 363 - 363 aligns to "H" in entry P0ACC7 (individually applies "Proton acceptor")
    • Subsequence at position 76 - 76 aligns to "Q" in entry P0ACC7 (individually applies "UDP-GlcNAc")
    • Subsequence at position 81 - 82 aligns to "G-T" in entry P0ACC7 (individually applies "UDP-GlcNAc binding")
    • Subsequence at position @NTER@ - 229 aligns to entry P0ACC7 (individually applies "Pyrophosphorylase")
    • Subsequence at position 351 - 351 aligns to "K" in entry P0ACC7 (individually applies "UDP-GlcNAc")
    • Subsequence at position 377 - 377 aligns to "N" in entry P0ACC7 (individually applies "UDP-GlcNAc")
    • Subsequence at position 25 - 25 aligns to "K" in entry P0ACC7 (individually applies "UDP-GlcNAc")
    • Subsequence at position 154 - 154 aligns to "E" in entry P0ACC7 (individually applies "UDP-GlcNAc")
    • Subsequence at position 423 - 423 aligns to "[ACGST]" in entry P0ACC7 (individually applies "Acetyl-CoA; via amide nitrogen")
    • Subsequence at position 333 - 333 aligns to "R" in entry P0ACC7 (individually applies "UDP-GlcNAc")
    • Subsequence at position 440 - 440 aligns to "R" in entry P0ACC7 (individually applies "Acetyl-CoA")
    • Subsequence at position 105 - 105 aligns to "D" in entry P0ACC7 (individually applies "Magnesium")
    • Subsequence at position 140 - 140 aligns to "G" in entry P0ACC7 (individually applies "UDP-GlcNAc; via amide nitrogen")

... 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:
    Bifunctional protein GlmU

Cleaved chain(s) or included domain(s)i

  • Includes domain:
    Recommended name:
    UDP-N-acetylglucosamine pyrophosphorylase (EC:2.7.7.23)
    Alternative name(s):
    N-acetylglucosamine-1-phosphate uridyltransferase
  • Includes domain:
    Recommended name:
    Glucosamine-1-phosphate N-acetyltransferase (EC:2.3.1.157)

<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:glmU

<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 ‘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 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 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/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

  • Homotrimer.

<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

<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

  • Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C-terminal domain catalyzes the transfer of acetyl group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N-acetylglucosamine-1-phosphate (GlcNAc-1-P), which is converted into UDP-GlcNAc by the transfer of uridine 5-monophosphate (from uridine 5-triphosphate), a reaction catalyzed by the N-terminal domain.

<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

  • Proton acceptor (to residues corresponding to position 363)

<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

  • Magnesium (to residues corresponding to position 227)
  • Magnesium (to residues corresponding to position 105)

<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

  • UDP-GlcNAc binding (to residues corresponding to positions 103 - 105)
  • Linker (to residues corresponding to positions 230 - 250)
  • Acetyl-CoA binding (to residues corresponding to positions 386 - 387)
  • N-acetyltransferase (to residues corresponding to positions 251 - @CTER@i)
  • UDP-GlcNAc binding (to residues corresponding to positions 11 - 14)
  • UDP-GlcNAc binding (to residues corresponding to positions 81 - 82)
  • Pyrophosphorylase (to residues corresponding to positions @NTER@i - 229)

<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

  • Acetyl-CoA; via amide nitrogen (to residues corresponding to position 380)
  • UDP-GlcNAc (to residues corresponding to position 227)
  • UDP-GlcNAc (to residues corresponding to position 366)
  • UDP-GlcNAc (to residues corresponding to position 169)
  • Acetyl-CoA (to residues corresponding to position 405)
  • UDP-GlcNAc (to residues corresponding to position 76)
  • UDP-GlcNAc (to residues corresponding to position 351)
  • UDP-GlcNAc (to residues corresponding to position 377)
  • UDP-GlcNAc (to residues corresponding to position 25)
  • UDP-GlcNAc (to residues corresponding to position 154)
  • Acetyl-CoA; via amide nitrogen (to residues corresponding to position 423)
  • UDP-GlcNAc (to residues corresponding to position 333)
  • Acetyl-CoA (to residues corresponding to position 440)
  • UDP-GlcNAc; via amide nitrogen (to residues corresponding to position 140)

<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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