A0A0P0UPQ9 · A0A0P0UPQ9_9GAMM

Function

function

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.

Catalytic activity

Cofactor

Fe2+ (UniProtKB | Rhea| CHEBI:29033 )

Note: Binds 1 Fe2+ ion.

Features

Showing features for binding site, active site.

118220406080100120140160180
TypeIDPosition(s)Description
Binding site110Fe cation (UniProtKB | ChEBI)
Binding site152Fe cation (UniProtKB | ChEBI)
Active site153
Binding site156Fe cation (UniProtKB | ChEBI)

GO annotations

AspectTerm
Molecular Functionmetal ion binding
Molecular Functionpeptide deformylase activity
Biological Processpeptidyl-methionine modification
Biological Processtranslation

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Peptide deformylase
  • EC number
  • Short names
    PDF
  • Alternative names
    • Polypeptide deformylase

Gene names

    • Name
      def
    • ORF names
      BSEPE_0154

Organism names

Accessions

  • Primary accession
    A0A0P0UPQ9

Proteomes

Interaction

Protein-protein interaction databases

Family & Domains

Sequence similarities

Belongs to the polypeptide deformylase family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    182
  • Mass (Da)
    20,767
  • Last updated
    2016-01-20 v1
  • Checksum
    FE3DDEE3A76D793B
MILPILKFPDKRLRTKAIKVETVNASIKALVADMFETMYAEDGIGLAATQVDRHMQIVVMDVPDSGEDYQLLLKKRESKTKKPLEAKHPLCFINPKIIEKGGKETHSEGCLSIPSYYADVERFNHVVVEALNENGESFTLEARNLLAVCIQHELDHLKGILFVDYLSKLKQQRLKEKFRKSK

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AP013042
EMBL· GenBank· DDBJ
BAS67178.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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