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A0A087CSZ0 · A0A087CSZ0_9BIFI

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.

Caution

The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

Catalytic activity

Cofactor

Fe2+ (UniProtKB | Rhea| CHEBI:29033 )

Note: Binds 1 Fe2+ ion.

Features

Showing features for binding site, active site.

Type
IDPosition(s)Description
Binding site88Fe cation (UniProtKB | ChEBI)
Binding site130Fe cation (UniProtKB | ChEBI)
Active site131
Binding site134Fe 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
      BREU_1571

Organism names

Accessions

  • Primary accession
    A0A087CSZ0

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
    161
  • Mass (Da)
    18,292
  • Last updated
    2014-10-29 v1
  • MD5 Checksum
    5B6083BA83B968CC15EF5EAF064107E0
MAIREIRVVPDPVLRTPCDEIREITPAVRRLVQDLLDTVNDPGRAGLSANQIGVSLRAFSYNIDGHVGYILNPVLEETSGEQYGDEGCLSVPGLWYKTRRADHARVRGIDLDGKEVVLEGAGLMGRMLQHECDHLDGHVYLDRLEKDERREAMRYMRTHQR

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JGZK01000005
EMBL· GenBank· DDBJ
KFI86390.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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