A0A292ZJK0 · A0A292ZJK0_SPHSA

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 site117Fe cation (UniProtKB | ChEBI)
Binding site159Fe cation (UniProtKB | ChEBI)
Active site160
Binding site163Fe 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
      SFOMI_3668

Organism names

Accessions

  • Primary accession
    A0A292ZJK0

Proteomes

Family & Domains

Sequence similarities

Belongs to the polypeptide deformylase family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    192
  • Mass (Da)
    21,769
  • Last updated
    2017-12-20 v1
  • MD5 Checksum
    BF779524B2D7EBB9D56F91B9CFCE36B4
MWRSLEIFRPSDYFGSMAILPILEAPDPRLRTISSPVEAIDEDLQRLIDDMFETMYDAPGIGLAAIQVGVPKRVLVIDLQEPESDEEGAPPVRKPMVFINPEILEGSEDLSVYNEGCLSVPDQFAEVERPASIRASWMDRDGRIHEERLEGLLATCLQHEMDHLQGVLFIDHLSRLKRDMLMKKLTKARKAA

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
BEWI01000032
EMBL· GenBank· DDBJ
GAY23104.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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