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The annotation and conditions in this rule are derived from the following entries: Q56224 (NQO9_THET8), P0AFD6 (NUOI_ECOLI)

If a protein meets these conditions... i

Common conditions

    • Matches HAMAP signature MF_01351
    • taxon = Bacteria
    • fragment ≠ the sequence is fragmented
    • Matches HAMAP signature MF_01351
    • gene location = Plastid
    • fragment ≠ the sequence is fragmented

Special conditions

... 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 namesi

  • Recommended name:
    NAD(P)H-quinone oxidoreductase subunit I, chloroplastic (EC:7.1.1.-)
    Alternative name(s):
    NAD(P)H dehydrogenase subunit I
    Short name:
    NDH subunit I
    NADH-plastoquinone oxidoreductase subunit I
  • Recommended name:
    NAD(P)H-quinone oxidoreductase subunit I (EC:7.1.1.-)
    Alternative name(s):
    NAD(P)H dehydrogenase I subunit I
    NDH-1 subunit I
    Short name:
    NDH-I
  • Recommended name:
    NADH-quinone oxidoreductase subunit I (EC:7.1.1.-)
    Alternative name(s):
    NADH dehydrogenase I subunit I
    NDH-1 subunit I

<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 namesi

  • Name:ndhI
  • Name:nuoI

<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 describes the function(s) of a protein.<p><a href='/help/function' target='_top'>More...</a></p>Functioni

  • NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient.
  • NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient.
  • NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be menaquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.
  • NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.

<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

  • NDH is composed of at least 16 different subunits, 5 of which are encoded in the nucleus.
  • NDH-1 is composed of 15 different subunits. Subunits NuoA, H, J, K, L, M, N constitute the membrane sector of the complex.
  • NDH-1 is composed of at least 11 different subunits.
  • NDH-1 is composed of 13 different subunits. Subunits NuoA, H, J, K, L, M, N constitute the membrane sector of the complex.
  • NDH-1 is composed of 14 different subunits. Subunits NuoA, H, J, K, L, M, N constitute the membrane sector of the complex.

<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 ‘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 ‘Function’ 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-sulfur 2 (4Fe-4S) (to residues corresponding to position 104)
  • Iron-sulfur 2 (4Fe-4S) (to residues corresponding to position 63)
  • Iron-sulfur 2 (4Fe-4S) (to residues corresponding to position 98)
  • Iron-sulfur 2 (4Fe-4S) (to residues corresponding to position 101)
  • Iron-sulfur 1 (4Fe-4S) (to residues corresponding to position 108)
  • Iron-sulfur 1 (4Fe-4S) (to residues corresponding to position 59)
  • Iron-sulfur 1 (4Fe-4S) (to residues corresponding to position 56)
  • Iron-sulfur 1 (4Fe-4S) (to residues corresponding to position 53)

<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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