B0JGA5 · B0JGA5_MICAN

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.

118020406080100120140160180
Type
IDPosition(s)Description
Binding site101Fe cation (UniProtKB | ChEBI)
Binding site143Fe cation (UniProtKB | ChEBI)
Active site144
Binding site147Fe 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
    • Ordered locus names
      MAE_22880

Organism names

Accessions

  • Primary accession
    B0JGA5

Proteomes

PTM/Processing

Proteomic databases

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
    180
  • Mass (Da)
    20,408
  • Last updated
    2008-03-18 v1
  • MD5 Checksum
    50CEFE43E0E5FB77B0228A84E3855087
MTQVLTITQLGNPILQQKAAAIDNLLDADCQNLIDSLITTVQAAHGVGIAAPQVARSLRLFIVASHPNPRYPDAPMMPPTAVINPRILRVSEEMVKGWEGCLSVPNLRGFVPRHQWIEVAYCDRNGREIRQVFRDFVARIFQHEYDHLEGILFLDRLASPADLYSEEEYQKISNIAEYKR

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AP009552
EMBL· GenBank· DDBJ
BAG02110.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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