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

... then these annotations are applied i

Protein namei

  • Recommended name:
    Siroheme synthase

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

  • Includes domain:
    Recommended name:
    Uroporphyrinogen-III C-methyltransferase (EC:2.1.1.107)
    Short name:
    Urogen III methylase
    Alternative name(s):
    SUMT
    Uroporphyrinogen III methylase
    Short name:
    UROM
  • Includes domain:
    Recommended name:
    Precorrin-2 dehydrogenase (EC:1.3.1.76)
  • Includes domain:
    Recommended name:
    Sirohydrochlorin ferrochelatase (EC:4.99.1.4)

Gene namei

  • Name:cysG

Catalytic activityi

  • Precorrin-2 + NAD+ = sirohydrochlorin + NADH.
  • S-adenosyl-L-methionine + precorrin-1 = S-adenosyl-L-homocysteine + precorrin-2.
  • S-adenosyl-L-methionine + uroporphyrinogen III = S-adenosyl-L-homocysteine + precorrin-1.
  • Siroheme + 2 H+ = sirohydrochlorin + Fe2+.

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.

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.

Sequence similaritiesi

Modified residuei

  • Phosphoserine (to residues corresponding to position 128)

Regioni

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

Binding sitei

  • S-adenosyl-L-methionine; via carbonyl oxygen (to residues corresponding to position 225)
  • S-adenosyl-L-methionine; via carbonyl oxygen (to residues corresponding to position 306)
  • 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)

Nucleotide bindingi

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

Active sitei

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

Keywordsi

GO (Gene Ontology) termsi