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The annotation and conditions in this rule are derived from the following entries: P21177 (FADB_ECOLI), P28793 (FADB_PSEFR)

If a protein meets these conditions... i

Common conditions

Special conditions

    • Subsequence at position 401 - 403 aligns to "[VI]-[VT]-E" in entry P28793 (individually applies "NAD")
    • Subsequence at position 430 - 430 aligns to "S" in entry P28793 (individually applies "NAD")
    • Subsequence at position 325 - 325 aligns to "M" in entry P28793 (individually applies "NAD; via amide nitrogen")
    • Subsequence at position 660 - 660 aligns to "Y" in entry P28793 (individually applies "Substrate")
    • Subsequence at position 408 - 408 aligns to "K" in entry P28793 (individually applies "NAD")
    • Subsequence at position 454 - 454 aligns to "N" in entry P28793 (individually applies "NAD")
    • Subsequence at position 451 - 451 aligns to "H" in entry P28793 (individually applies "For 3-hydroxyacyl-CoA dehydrogenase activity")
    • Subsequence at position 297 - 297 aligns to "D" in entry P28793 (individually applies "Substrate")
    • Subsequence at position 312 - @CTER@ aligns to entry P28793 (individually applies "3-hydroxyacyl-CoA dehydrogenase")
    • Subsequence at position 501 - 501 aligns to "N" in entry P28793 (individually applies "Substrate")
    • Subsequence at position 120 - 120 aligns to "E" in entry P28793 (individually applies "Important for catalytic activity")
    • Subsequence at position 140 - 140 aligns to "E" in entry P28793 (individually applies "Important for catalytic activity")
    • Subsequence at position @NTER@ - 190 aligns to entry P28793 (individually applies "Enoyl-CoA hydratase/isomerase")
    • Subsequence at position 344 - 344 aligns to "D" in entry P28793 (individually applies "NAD")

... 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:
    Fatty acid oxidation complex subunit alpha

Cleaved chain(s) or included domain(s)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 namei

  • Name:fadB

<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: fatty acid beta-oxidation

    This protein is involved in the pathway fatty acid beta-oxidation, which is part of Lipid metabolism.
    View all proteins of this organism that are known to be involved in the pathway fatty acid beta-oxidation and in Lipid metabolism.

<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

  • Involved in the aerobic and anaerobic degradation of long-chain fatty acids via beta-oxidation cycle. Catalyzes the formation of 3-oxoacyl-CoA from enoyl-CoA via L-3-hydroxyacyl-CoA. It can also use D-3-hydroxyacyl-CoA and cis-3-enoyl-CoA as substrate.

<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/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 chains (FadB) and two beta chains (FadA).

<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

  • Important for catalytic activity (to residues corresponding to position 120)
  • Important for catalytic activity (to residues corresponding to position 140)

<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

  • NAD (to residues corresponding to positions 401 - 403)

<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

  • For 3-hydroxyacyl-CoA dehydrogenase activity (to residues corresponding to position 451)

<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

  • NAD (to residues corresponding to position 430)
  • NAD; via amide nitrogen (to residues corresponding to position 325)
  • Substrate (to residues corresponding to position 660)
  • NAD (to residues corresponding to position 408)
  • NAD (to residues corresponding to position 454)
  • Substrate (to residues corresponding to position 297)
  • Substrate (to residues corresponding to position 501)
  • NAD (to residues corresponding to position 344)

<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

  • 3-hydroxyacyl-CoA dehydrogenase (to residues corresponding to positions 312 - @CTER@i)
  • Enoyl-CoA hydratase/isomerase (to residues corresponding to positions @NTER@i - 190)

<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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