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The annotation and conditions in this rule are derived from the following entries: P0A6K3 (DEF_ECOLI), O31410 (DEF2_GEOSE), Q93LE9 (DEF_LEPIN), P68826 (DEF_STAAU), Q45495 (DEF2_BACSU), P43522 (DEF_THETH)

If a protein meets these conditions... i

Common conditions

    • Matches HAMAP signature MF_00163
    • taxon = Bacteria
    • fragment ≠ the sequence is fragmented

Special conditions

    • Subsequence at position 91 - 91 aligns to "C" in entry P0A6K3 Subsequence at position 133 - 133 aligns to "H" in entry P0A6K3 Subsequence at position 137 - 137 aligns to "H" in entry P0A6K3
    • Subsequence at position 134 - 134 aligns to "E" in entry P0A6K3
  • Subsequence at position 91 - 91 aligns to "C" in entry P0A6K3 (applies "Iron") Subsequence at position 133 - 133 aligns to "H" in entry P0A6K3 (applies "Iron") Subsequence at position 137 - 137 aligns to "H" in entry P0A6K3 (applies "Iron")

... then these annotations are applied i

Protein namei

  • Recommended name:
    Peptide deformylase (EC:3.5.1.88)
    Short name:
    PDF
    Alternative name(s):
    Polypeptide deformylase

Gene namei

  • Name:def

Catalytic activityi

  • Formyl-L-methionyl peptide + H2O = formate + methionyl peptide.

Cofactori

  • Fe2+Note: Binds 1 Fe2+ ion.

Functioni

  • Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions.

Sequence similaritiesi

Active sitei

  • (to residues corresponding to position 134)

Metal bindingi

  • Iron (to residues corresponding to position 91)
  • Iron (to residues corresponding to position 133)
  • Iron (to residues corresponding to position 137)

Keywordsi

GO (Gene Ontology) termsi

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