M3EPL1 · M3EPL1_9ACTN

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.

116420406080100120140160
Type
IDPosition(s)Description
Binding site89Fe cation (UniProtKB | ChEBI)
Binding site131Fe cation (UniProtKB | ChEBI)
Active site132
Binding site135Fe 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
      SBD_1118

Organism names

Accessions

  • Primary accession
    M3EPL1

Proteomes

Family & Domains

Sequence similarities

Belongs to the polypeptide deformylase family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    164
  • Mass (Da)
    18,304
  • Last updated
    2013-05-01 v1
  • MD5 Checksum
    BDFD94DD679A5C313DDB59D9F5CD9447
MTLLGDPVLQAPCEEVTEFGPELARLVEDMFATMYDARGVGLAANQVGRSLRVFVYDCPDDEDVRHLGHVVNPRLVSTEGIVLRGPEGCLSLPGLEAGVERYDEAAVEGFTVDGDRVRVWGSGFFARCLQHECDHLEGRVYVDRLSGWRRRRVMRKAARAAWGR

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
KB405056
EMBL· GenBank· DDBJ
EMF58446.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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