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The annotation and conditions in this rule are derived from the following entries: Q08368 (ACDA1_METTE), Q46G04 (ACDA1_METBF)

If a protein meets these conditions... i

Common conditions

    • Matches HAMAP signature MF_01137
    • taxon = Archaea
    • fragment ≠ the sequence is fragmented

Special conditions

    • Subsequence at position 323 - 323 aligns to "C" in entry Q46G04 Subsequence at position 278 - 278 aligns to "C" in entry Q46G04 Subsequence at position 523 - 523 aligns to "C" in entry Q46G04 Subsequence at position 552 - 552 aligns to "C" in entry Q46G04 Subsequence at position 587 - 587 aligns to "C" in entry Q46G04 Subsequence at position 250 - 250 aligns to "H" in entry Q46G04
    • Subsequence at position 73 - 73 aligns to "C" in entry Q46G04 Subsequence at position 77 - 77 aligns to "C" in entry Q46G04
    • Subsequence at position 94 - 94 aligns to "C" in entry Q46G04 Subsequence at position 84 - 84 aligns to "C" in entry Q46G04 Subsequence at position 79 - 79 aligns to "C" in entry Q46G04 Subsequence at position 76 - 76 aligns to "C" in entry Q46G04
    • Subsequence at position 417 - 417 aligns to "C" in entry Q46G04 Subsequence at position 423 - 423 aligns to "C" in entry Q46G04 Subsequence at position 465 - 465 aligns to "C" in entry Q46G04 Subsequence at position 420 - 420 aligns to "C" in entry Q46G04
    • Subsequence at position 458 - 458 aligns to "C" in entry Q46G04 Subsequence at position 461 - 461 aligns to "C" in entry Q46G04 Subsequence at position 455 - 455 aligns to "C" in entry Q46G04 Subsequence at position 427 - 427 aligns to "C" in entry Q46G04
    • Subsequence at position 73 - 73 aligns to "C" in entry Q46G04 Subsequence at position 77 - 77 aligns to "C" in entry Q46G04
    • Subsequence at position 94 - 94 aligns to "C" in entry Q46G04 Subsequence at position 84 - 84 aligns to "C" in entry Q46G04 Subsequence at position 79 - 79 aligns to "C" in entry Q46G04 Subsequence at position 76 - 76 aligns to "C" in entry Q46G04
    • Subsequence at position 323 - 323 aligns to "C" in entry Q46G04 Subsequence at position 278 - 278 aligns to "C" in entry Q46G04 Subsequence at position 523 - 523 aligns to "C" in entry Q46G04 Subsequence at position 552 - 552 aligns to "C" in entry Q46G04 Subsequence at position 587 - 587 aligns to "C" in entry Q46G04 Subsequence at position 250 - 250 aligns to "H" in entry Q46G04
    • Subsequence at position 417 - 417 aligns to "C" in entry Q46G04 Subsequence at position 423 - 423 aligns to "C" in entry Q46G04 Subsequence at position 465 - 465 aligns to "C" in entry Q46G04 Subsequence at position 420 - 420 aligns to "C" in entry Q46G04
    • Subsequence at position 458 - 458 aligns to "C" in entry Q46G04 Subsequence at position 461 - 461 aligns to "C" in entry Q46G04 Subsequence at position 455 - 455 aligns to "C" in entry Q46G04 Subsequence at position 427 - 427 aligns to "C" in entry Q46G04
  • Subsequence at position 94 - 94 aligns to "C" in entry Q46G04 (applies "Iron-sulfur 2 (4Fe-4S)") Subsequence at position 84 - 84 aligns to "C" in entry Q46G04 (applies "Iron-sulfur 2 (4Fe-4S)") Subsequence at position 79 - 79 aligns to "C" in entry Q46G04 (applies "Iron-sulfur 2 (4Fe-4S)") Subsequence at position 76 - 76 aligns to "C" in entry Q46G04 (applies "Iron-sulfur 2 (4Fe-4S)")
  • Subsequence at position 458 - 458 aligns to "C" in entry Q46G04 (applies "Iron-sulfur 4 (4Fe-4S)") Subsequence at position 461 - 461 aligns to "C" in entry Q46G04 (applies "Iron-sulfur 4 (4Fe-4S)") Subsequence at position 455 - 455 aligns to "C" in entry Q46G04 (applies "Iron-sulfur 4 (4Fe-4S)") Subsequence at position 427 - 427 aligns to "C" in entry Q46G04 (applies "Iron-sulfur 4 (4Fe-4S)")
    • Subsequence at position 117 - 117 aligns to "H" in entry Q46G04
  • Subsequence at position 417 - 417 aligns to "C" in entry Q46G04 (applies "Iron-sulfur 3 (4Fe-4S)") Subsequence at position 423 - 423 aligns to "C" in entry Q46G04 (applies "Iron-sulfur 3 (4Fe-4S)") Subsequence at position 465 - 465 aligns to "C" in entry Q46G04 (applies "Iron-sulfur 3 (4Fe-4S)") Subsequence at position 420 - 420 aligns to "C" in entry Q46G04 (applies "Iron-sulfur 3 (4Fe-4S)")
  • Subsequence at position 73 - 73 aligns to "C" in entry Q46G04 (applies "Iron-sulfur 1 (4Fe-4S); shared with dimeric partner") Subsequence at position 77 - 77 aligns to "C" in entry Q46G04 (applies "Iron-sulfur 1 (4Fe-4S); shared with dimeric partner")
  • Subsequence at position 323 - 323 aligns to "C" in entry Q46G04 (applies "Nickel-iron-sulfur (Ni-4Fe-4S)") Subsequence at position 278 - 278 aligns to "C" in entry Q46G04 (applies "Nickel-iron-sulfur (Ni-4Fe-4S)") Subsequence at position 523 - 523 aligns to "C" in entry Q46G04 (applies "Nickel-iron-sulfur (Ni-4Fe-4S)") Subsequence at position 552 - 552 aligns to "C" in entry Q46G04 (applies "Nickel-iron-sulfur (Ni-4Fe-4S)") Subsequence at position 587 - 587 aligns to "C" in entry Q46G04 (applies "Nickel-iron-sulfur (Ni-4Fe-4S)") Subsequence at position 250 - 250 aligns to "H" in entry Q46G04 (applies "Nickel-iron-sulfur (Ni-4Fe-4S); via tele 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:
    Acetyl-CoA decarbonylase/synthase complex subunit alpha (EC:1.2.7.4)
    Short name:
    ACDS complex subunit alpha
    Alternative name(s):
    ACDS complex carbon monoxide dehydrogenase subunit alpha
    Short name:
    ACDS CODH subunit alpha

<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:cdhA

<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

  • Cluster B is an all-cysteinyl-liganded 4Fe-4S cluster; cluster C is a mixed Ni-Fe-S cluster which is the active site of CO oxidation. Cluster D is also an all-cysteinyl-liganded 4Fe-4S cluster that bridges the two subunits of the CODH dimer. Contains two additional 4Fe-4S clusters, dubbed E and F, that probably transport electrons from ferredoxin to the B cluster.

<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: methanogenesis from acetate

    This protein is involved in the pathway methanogenesis from acetate, which is part of One-carbon metabolism.
    View all proteins of this organism that are known to be involved in the pathway methanogenesis from acetate and in One-carbon metabolism.

<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

  • Heterotetramer of two alpha and two epsilon subunits. The ACDS complex is made up of alpha, epsilon, beta, gamma and delta subunits with a probable stoichiometry of (alpha2epsilon2)4-beta8-(gamma1delta1)8.

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

  • Part of the ACDS complex that catalyzes the reversible cleavage of acetyl-CoA, allowing growth on acetate as sole source of carbon and energy. The alpha-epsilon subcomponent functions as a carbon monoxide dehydrogenase.
  • Part of the ACDS complex that catalyzes the reversible cleavage of acetyl-CoA, allowing autotrophic growth from CO2. The alpha-epsilon subcomponent functions as a carbon monoxide dehydrogenase.

<p>This subsection of the ‘Function’ 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

  • Carbon monoxide; via tele nitrogen (to residues corresponding to position 117)

<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 94)
  • Iron-sulfur 2 (4Fe-4S) (to residues corresponding to position 84)
  • Iron-sulfur 2 (4Fe-4S) (to residues corresponding to position 79)
  • Iron-sulfur 2 (4Fe-4S) (to residues corresponding to position 76)
  • Iron-sulfur 4 (4Fe-4S) (to residues corresponding to position 458)
  • Iron-sulfur 4 (4Fe-4S) (to residues corresponding to position 461)
  • Iron-sulfur 4 (4Fe-4S) (to residues corresponding to position 455)
  • Iron-sulfur 4 (4Fe-4S) (to residues corresponding to position 427)
  • Iron-sulfur 3 (4Fe-4S) (to residues corresponding to position 417)
  • Iron-sulfur 3 (4Fe-4S) (to residues corresponding to position 423)
  • Iron-sulfur 3 (4Fe-4S) (to residues corresponding to position 465)
  • Iron-sulfur 3 (4Fe-4S) (to residues corresponding to position 420)
  • Iron-sulfur 1 (4Fe-4S); shared with dimeric partner (to residues corresponding to position 73)
  • Iron-sulfur 1 (4Fe-4S); shared with dimeric partner (to residues corresponding to position 77)
  • Nickel-iron-sulfur (Ni-4Fe-4S) (to residues corresponding to position 323)
  • Nickel-iron-sulfur (Ni-4Fe-4S) (to residues corresponding to position 278)
  • Nickel-iron-sulfur (Ni-4Fe-4S) (to residues corresponding to position 523)
  • Nickel-iron-sulfur (Ni-4Fe-4S) (to residues corresponding to position 552)
  • Nickel-iron-sulfur (Ni-4Fe-4S) (to residues corresponding to position 587)
  • Nickel-iron-sulfur (Ni-4Fe-4S); via tele nitrogen (to residues corresponding to position 250)

<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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