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The annotation and conditions in this rule are derived from the following entries: P0A9Q5 (ACCD_ECOLI), Q5HF73 (ACCD_STAAC), Q2MI91 (ACCD_SOLLC), P18823 (ACCD_PEA)

If a protein meets these conditions... i

Common conditions

    • Matches HAMAP signature MF_01395
    • taxon = Bacteria
    • fragment ≠ the sequence is fragmented
    • Matches HAMAP signature MF_01395
    • gene location = Plastid
    • fragment ≠ the sequence is fragmented

Special conditions

    • taxon ≠ Mycobacterium Subsequence at position 46 - 46 aligns to "C" in entry P0A9Q5 Subsequence at position 27 - 27 aligns to "C" in entry P0A9Q5 Subsequence at position 49 - 49 aligns to "C" in entry P0A9Q5 Subsequence at position 30 - 30 aligns to "C" in entry P0A9Q5
    • gene location = Plastid; Chloroplast
    • gene location ≠ Plastid; Chloroplast
    • gene location = Plastid; Chloroplast
    • taxon ≠ Bacteria
  • taxon ≠ Mycobacterium Subsequence at position 46 - 46 aligns to "C" in entry P0A9Q5 (applies "Zinc") Subsequence at position 27 - 27 aligns to "C" in entry P0A9Q5 (applies "Zinc") Subsequence at position 49 - 49 aligns to "C" in entry P0A9Q5 (applies "Zinc") Subsequence at position 30 - 30 aligns to "C" in entry P0A9Q5 (applies "Zinc")
    • taxon ≠ Mycobacterium
    • Subsequence at position 27 - 49 aligns to "C-x(1,2)-C-x(12,18)-C-x(1,2)-C" in entry P0A9Q5

... 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:
    Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta, chloroplastic (EC:2.1.3.15)
    Short name:
    ACCase subunit beta
    Short name:
    Acetyl-CoA carboxylase carboxyltransferase subunit beta
  • Recommended name:
    Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta (EC:2.1.3.15)
    Short name:
    ACCase subunit beta
    Short name:
    Acetyl-CoA carboxylase carboxyltransferase subunit beta

<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:accD

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

  • Component of the acetyl coenzyme A carboxylase (ACC) complex. Biotin carboxylase (BC) catalyzes the carboxylation of biotin on its carrier protein (BCCP) and then the CO2 group is transferred by the transcarboxylase to acetyl-CoA to form malonyl-CoA.

<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/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

  • Acetyl-CoA carboxylase is a heterohexamer composed of biotin carboxyl carrier protein, biotin carboxylase and two subunits each of ACCase subunit alpha and ACCase plastid-coded subunit beta (accD).
  • Acetyl-CoA carboxylase is a heterohexamer composed of biotin carboxyl carrier protein (AccB), biotin carboxylase (AccC) and two subunits each of ACCase subunit alpha (AccA) and ACCase subunit beta (AccD).

<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 metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi

  • Pathwayi: malonyl-CoA biosynthesis

    This protein is involved in step 1 of the subpathway that synthesizes malonyl-CoA from acetyl-CoA. This subpathway is part of the pathway malonyl-CoA biosynthesis, which is itself part of Lipid metabolism.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes malonyl-CoA from acetyl-CoA, the pathway malonyl-CoA biosynthesis and in Lipid metabolism.

<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/function_section">Function</a> section specifies the position(s) and type(s) of zinc fingers within the protein.<p><a href='/help/zn_fing' target='_top'>More...</a></p>Zinc fingeri

  • C4-type (to residues corresponding to positions 27 - 49)

<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

  • Zinc (to residues corresponding to position 46)
  • Zinc (to residues corresponding to position 27)
  • Zinc (to residues corresponding to position 49)
  • Zinc (to residues corresponding to position 30)

<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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