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The annotation and conditions in this rule are derived from the following entries: P0AEA8 (CYSG_ECOLI), P25924 (CYSG_SALTY)

If a protein meets these conditions... i

Common conditions

Special conditions

    • Subsequence at position 128 - 128 aligns to "S" in entry P25924
    • Subsequence at position 128 - 128 aligns to "S" in entry P25924
    • Subsequence at position 306 - 306 aligns to "[IVL]" in entry P25924 (individually applies "S-adenosyl-L-methionine; via carbonyl oxygen")
    • Subsequence at position 43 - 44 aligns to entry P25924 (individually applies "NAD")
    • Subsequence at position 225 - 225 aligns to "P" in entry P25924 (individually applies "S-adenosyl-L-methionine; via carbonyl oxygen")
    • Subsequence at position 270 - 270 aligns to "K" in entry P25924 (individually applies "Proton donor")
    • Subsequence at position 331 - 332 aligns to "[TS]-A" in entry P25924 (individually applies "S-adenosyl-L-methionine binding")
    • Subsequence at position 22 - 23 aligns to entry P25924 (individually applies "NAD")
    • Subsequence at position 382 - 382 aligns to "M" in entry P25924 (individually applies "S-adenosyl-L-methionine; via amide nitrogen")
    • Subsequence at position 216 - @CTER@ aligns to entry P25924 (individually applies "Uroporphyrinogen-III C-methyltransferase")
    • Subsequence at position 248 - 248 aligns to "D" in entry P25924 (individually applies "Proton acceptor")
    • Subsequence at position 301 - 303 aligns to "G-G-D" in entry P25924 (individually applies "S-adenosyl-L-methionine binding")
    • Subsequence at position 411 - 411 aligns to "[GA]" in entry P25924 (individually applies "S-adenosyl-L-methionine; via amide nitrogen and carbonyl oxygen")
    • Subsequence at position @NTER@ - 204 aligns to entry P25924 (individually applies "Precorrin-2 dehydrogenase / sirohydrochlorin ferrochelatase")

... 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:
    Siroheme synthase

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:cysG

<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: adenosylcobalamin biosynthesis

    This protein is involved in step 1 of the subpathway that synthesizes precorrin-2 from uroporphyrinogen III. This subpathway is part of the pathway adenosylcobalamin biosynthesis, which is itself part of Cofactor biosynthesis.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes precorrin-2 from uroporphyrinogen III, the pathway adenosylcobalamin biosynthesis and in Cofactor biosynthesis.
  • Pathwayi: adenosylcobalamin biosynthesis

    This protein is involved in step 1 of the subpathway that synthesizes sirohydrochlorin from precorrin-2. This subpathway is part of the pathway adenosylcobalamin biosynthesis, which is itself part of Cofactor biosynthesis.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes sirohydrochlorin from precorrin-2, the pathway adenosylcobalamin biosynthesis and in Cofactor biosynthesis.
  • Pathwayi: siroheme biosynthesis

    This protein is involved in step 1 of the subpathway that synthesizes precorrin-2 from uroporphyrinogen III. This subpathway is part of the pathway siroheme biosynthesis, which is itself part of Porphyrin-containing compound metabolism.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes precorrin-2 from uroporphyrinogen III, the pathway siroheme biosynthesis and in Porphyrin-containing compound metabolism.
  • Pathwayi: siroheme biosynthesis

    This protein is involved in step 1 of the subpathway that synthesizes siroheme from sirohydrochlorin. This subpathway is part of the pathway siroheme biosynthesis, which is itself part of Porphyrin-containing compound metabolism.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes siroheme from sirohydrochlorin, the pathway siroheme biosynthesis and in Porphyrin-containing compound metabolism.
  • Pathwayi: siroheme biosynthesis

    This protein is involved in step 1 of the subpathway that synthesizes sirohydrochlorin from precorrin-2. This subpathway is part of the pathway siroheme biosynthesis, which is itself part of Porphyrin-containing compound metabolism.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes sirohydrochlorin from precorrin-2, the pathway siroheme biosynthesis and in Porphyrin-containing compound metabolism.

<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

  • Multifunctional enzyme that catalyzes the SAM-dependent methylations of uroporphyrinogen III at position C-2 and C-7 to form precorrin-2 via precorrin-1. Then it catalyzes the NAD-dependent ring dehydrogenation of precorrin-2 to yield sirohydrochlorin. Finally, it catalyzes the ferrochelation of sirohydrochlorin to yield siroheme.

<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 ‘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

  • S-adenosyl-L-methionine binding (to residues corresponding to positions 331 - 332)
  • Uroporphyrinogen-III C-methyltransferase (to residues corresponding to positions 216 - @CTER@i)
  • S-adenosyl-L-methionine binding (to residues corresponding to positions 301 - 303)
  • Precorrin-2 dehydrogenase / sirohydrochlorin ferrochelatase (to residues corresponding to positions @NTER@i - 204)

<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

  • S-adenosyl-L-methionine; via carbonyl oxygen (to residues corresponding to position 306)
  • S-adenosyl-L-methionine; via carbonyl oxygen (to residues corresponding to position 225)
  • S-adenosyl-L-methionine; via amide nitrogen (to residues corresponding to position 382)
  • S-adenosyl-L-methionine; via amide nitrogen and carbonyl oxygen (to residues corresponding to position 411)

<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 43 - 44)
  • NAD (to residues corresponding to positions 22 - 23)

<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

  • Proton donor (to residues corresponding to position 270)
  • Proton acceptor (to residues corresponding to position 248)

<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei

  • Phosphoserine (to residues corresponding to position 128)

<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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