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The annotation and conditions in this rule are derived from the following entries: P67910 (HLDD_ECOLI)

If a protein meets these conditions... i

Common conditions

    • Matches HAMAP signature MF_01601
    • taxon = Bacteria
    • fragment ≠ the sequence is fragmented

Special conditions

    • Subsequence at position 272 - 272 aligns to "Y" in entry P67910 (individually applies "Substrate")
    • Subsequence at position 170 - 170 aligns to "[VI]" in entry P67910 (individually applies "NADP; via amide nitrogen")
    • Subsequence at position 201 - 204 aligns to entry P67910 (individually applies "Substrate binding")
    • Subsequence at position 38 - 38 aligns to "[KQR]" in entry P67910 (individually applies "NADP")
    • Subsequence at position 169 - 169 aligns to "N" in entry P67910 (individually applies "Substrate")
    • Subsequence at position 187 - 187 aligns to "[HKQ]" in entry P67910 (individually applies "Substrate")
    • Subsequence at position 209 - 209 aligns to "[HR]" in entry P67910 (individually applies "Substrate")
    • Subsequence at position 92 - 92 aligns to "N" in entry P67910 (individually applies "NADP")
    • Subsequence at position 180 - 180 aligns to "x" in entry P67910 (individually applies "Substrate; via carbonyl oxygen")
    • Subsequence at position 31 - 32 aligns to entry P67910 (individually applies "NADP")
    • Subsequence at position 75 - 79 aligns to entry P67910 (individually applies "NADP")
    • Subsequence at position 53 - 53 aligns to "[KQR]" in entry P67910 (individually applies "NADP")
    • Subsequence at position 10 - 11 aligns to entry P67910 (individually applies "NADP")
    • Subsequence at position 144 - 144 aligns to "K" in entry P67910 (individually applies "NADP")
    • Subsequence at position 178 - 178 aligns to "K" in entry P67910 (individually applies "Proton acceptor")
    • Subsequence at position 140 - 140 aligns to "Y" in entry P67910 (individually applies "Proton acceptor")
    • Subsequence at position 178 - 178 aligns to "K" in entry P67910 (individually applies "NADP")

... 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:
    ADP-L-glycero-D-manno-heptose-6-epimerase (EC:5.1.3.20)
    Alternative name(s):
    ADP-L-glycero-beta-D-manno-heptose-6-epimerase
    Short name:
    ADP-glyceromanno-heptose 6-epimerase
    Short name:
    ADP-hep 6-epimerase
    Short name:
    AGME

<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:hldD

<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 ‘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 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_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

  • Homopentamer.

<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

  • Catalyzes the interconversion between ADP-D-glycero-beta-D-manno-heptose and ADP-L-glycero-beta-D-manno-heptose via an epimerization at carbon 6 of the heptose.

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

  • Contains a large N-terminal NADP-binding domain, and a smaller C-terminal substrate-binding domain.

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

  • NADP (to residues corresponding to positions 31 - 32)
  • NADP (to residues corresponding to positions 75 - 79)
  • NADP (to residues corresponding to positions 10 - 11)

<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 272)
  • NADP; via amide nitrogen (to residues corresponding to position 170)
  • NADP (to residues corresponding to position 38)
  • Substrate (to residues corresponding to position 169)
  • Substrate (to residues corresponding to position 187)
  • Substrate (to residues corresponding to position 209)
  • NADP (to residues corresponding to position 92)
  • Substrate; via carbonyl oxygen (to residues corresponding to position 180)
  • NADP (to residues corresponding to position 53)
  • NADP (to residues corresponding to position 144)
  • NADP (to residues corresponding to position 178)

<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 178)
  • Proton acceptor (to residues corresponding to position 140)

<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 201 - 204)

<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

  • N6-acetyllysine (to residues corresponding to position 267)

<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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