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The annotation and conditions in this rule are derived from the following entries: P24232 (HMP_ECOLI), P39662 (HMP_CUPNH), P26353 (HMP_SALTY)

If a protein meets these conditions... i

Common conditions

    • Matches HAMAP signature MF_01252
    • taxon = Bacteria
    • fragment ≠ the sequence is fragmented

Special conditions

    • Subsequence at position 268 - 273 aligns to "G-[VI]-G-[QILAV]-T-P" in entry P24232 (individually applies "NADP")
    • Subsequence at position 95 - 95 aligns to "Y" in entry P24232 (individually applies "Charge relay system")
    • Subsequence at position 135 - 135 aligns to "E" in entry P24232 (individually applies "Charge relay system")
    • Subsequence at position 188 - 188 aligns to "Y" in entry P24232 (individually applies "FAD")
    • Subsequence at position 204 - 207 aligns to "R-[QN]-Y-S" in entry P24232 (individually applies "FAD")
    • Subsequence at position 389 - 392 aligns to "[CLFVT]-F-G-[PST]" in entry P24232 (individually applies "FAD")
    • Subsequence at position 388 - 388 aligns to "E" in entry P24232 (individually applies "Influences the redox potential of the prosthetic heme and FAD groups")
    • Subsequence at position 259 - @CTER@ aligns to entry P24232 (individually applies "NAD or NADP-binding")
    • Subsequence at position 147 - @CTER@ aligns to entry P24232 (individually applies "Reductase")
    • Subsequence at position 29 - 29 aligns to "Y" in entry P24232 (individually applies "Involved in heme-bound ligand stabilization and O-O bond activation")
    • Subsequence at position 84 - 84 aligns to "K" in entry P24232 (individually applies "Influences the redox potential of the prosthetic heme and FAD groups")
    • Subsequence at position 85 - 85 aligns to "H" in entry P24232 (individually applies "Iron (heme proximal ligand)")

... 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:
    Flavohemoprotein
    Alternative name(s):
    Flavohemoglobin
    Hemoglobin-like protein
    Nitric oxide dioxygenase (EC:1.14.12.17)
    Short name:
    NO oxygenase
    Short name:
    NOD

<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:hmp

<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 '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

  • Is involved in NO detoxification in an aerobic process, termed nitric oxide dioxygenase (NOD) reaction that utilizes O2 and NAD(P)H to convert NO to nitrate, which protects the bacterium from various noxious nitrogen compounds. Therefore, plays a central role in the inducible response to nitrosative stress.

<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

  • Consists of two distinct domains; an N-terminal heme-containing oxygen-binding domain and a C-terminal reductase domain with binding sites for FAD and NAD(P)H.

<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

  • Influences the redox potential of the prosthetic heme and FAD groups (to residues corresponding to position 388)
  • Involved in heme-bound ligand stabilization and O-O bond activation (to residues corresponding to position 29)
  • Influences the redox potential of the prosthetic heme and FAD groups (to residues corresponding to position 84)

<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

  • Iron (heme proximal ligand) (to residues corresponding to position 85)

<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 268 - 273)
  • FAD (to residues corresponding to positions 204 - 207)
  • FAD (to residues corresponding to positions 389 - 392)

<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

  • FAD (to residues corresponding to position 188)

<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

  • NAD or NADP-binding (to residues corresponding to positions 259 - @CTER@i)
  • Reductase (to residues corresponding to positions 147 - @CTER@i)

<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

  • Charge relay system (to residues corresponding to position 95)
  • Charge relay system (to residues corresponding to position 135)

<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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