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The annotation and conditions in this rule are derived from the following entries: P9WP79 (FBIB_MYCTU), Q7TWV3 (FBIB_MYCBO), A0QTG1 (FBIB_MYCS2)

If a protein meets these conditions... i

Common conditions

Special conditions

    • Subsequence at position 320 - 320 aligns to "D" in entry Q7TWV3 (individually applies "Coenzyme F420")
    • Subsequence at position 150 - 150 aligns to "D" in entry Q7TWV3 (individually applies "Divalent metal cation 1")
    • Subsequence at position 55 - 55 aligns to "K" in entry Q7TWV3 (individually applies "GTP")
    • Subsequence at position @NTER@ - 244 aligns to entry Q7TWV3 (individually applies "Coenzyme F420:L-glutamate ligase")
    • Subsequence at position 260 - 264 aligns to "R-x-S-x-R" in entry Q7TWV3 (individually applies "FMN")
    • Subsequence at position 288 - 288 aligns to "A" in entry Q7TWV3 (individually applies "FMN; via amide nitrogen and carbonyl oxygen")
    • Subsequence at position 399 - 399 aligns to "[GS]" in entry Q7TWV3 (individually applies "FMN; via amide nitrogen")
    • Subsequence at position 151 - 151 aligns to "[TS]" in entry Q7TWV3 (individually applies "Divalent metal cation 2")
    • Subsequence at position 109 - 109 aligns to "D" in entry Q7TWV3 (individually applies "Divalent metal cation 1")
    • Subsequence at position 245 - @CTER@ aligns to entry Q7TWV3 (individually applies "Dehydro-coenzyme F420-0 reductase")
    • Subsequence at position 50 - 50 aligns to "S" in entry Q7TWV3 (individually applies "GTP")
    • Subsequence at position 436 - 436 aligns to "R" in entry Q7TWV3 (individually applies "FMN")
    • Subsequence at position 20 - 23 aligns to "[LIMV]-P-x-[IVEF]" in entry Q7TWV3 (individually applies "GTP")
    • Subsequence at position 112 - 112 aligns to "N" in entry Q7TWV3 (individually applies "GTP")

... then these annotations are applied i

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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:
    Bifunctional F420 biosynthesis protein FbiB

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

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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:fbiB

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi

  • Pathwayi: coenzyme F420 biosynthesis

    This protein is involved in the pathway coenzyme F420 biosynthesis, which is part of Cofactor biosynthesis.
    View all proteins of this organism that are known to be involved in the pathway coenzyme F420 biosynthesis and in Cofactor biosynthesis.

<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 <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> describes the function(s) of a protein.<p><a href='/help/function' target='_top'>More...</a></p>Functioni

  • Bifunctional enzyme that catalyzes the GTP-dependent successive addition of multiple gamma-linked L-glutamates to the L-lactyl phosphodiester of 7,8-didemethyl-8-hydroxy-5-deazariboflavin (F420-0) to form polyglutamated F420 derivatives, and the FMNH2-dependent reduction of dehydro-F420-0 to form F420-0.
  • Bifunctional enzyme that catalyzes the GTP-dependent successive addition of two or more gamma-linked L-glutamates to the L-lactyl phosphodiester of 7,8-didemethyl-8-hydroxy-5-deazariboflavin (F420-0) to form polyglutamated F420 derivatives, and the FMNH2-dependent reduction of dehydro-F420-0 to form F420-0.

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni

  • Coenzyme F420:L-glutamate ligase (to residues corresponding to positions @NTER@i - 244)
  • Dehydro-coenzyme F420-0 reductase (to residues corresponding to positions 245 - @CTER@i)

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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

  • Coenzyme F420 (to residues corresponding to position 320)
  • GTP (to residues corresponding to position 55)
  • FMN; via amide nitrogen and carbonyl oxygen (to residues corresponding to position 288)
  • FMN; via amide nitrogen (to residues corresponding to position 399)
  • GTP (to residues corresponding to position 50)
  • FMN (to residues corresponding to position 436)
  • GTP (to residues corresponding to position 112)

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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

  • Divalent metal cation 1 (to residues corresponding to position 150)
  • Divalent metal cation 2 (to residues corresponding to position 151)
  • Divalent metal cation 1 (to residues corresponding to position 109)

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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

  • FMN (to residues corresponding to positions 260 - 264)
  • GTP (to residues corresponding to positions 20 - 23)

<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

  • GO:0009108 coenzyme biosynthetic process
  • GO:0052618 coenzyme F420-0:L-glutamate ligase activity
  • GO:0052619 coenzyme F420-1:gamma-L-glutamate ligase activity
  • GO:0052645 F420-0 metabolic process
  • GO:0052890 oxidoreductase activity, acting on the CH-CH group of donors, with a flavin as acceptor
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