A0A447SNR5 · A0A447SNR5_AVIVO
- ProteinPeptide deformylase
- Genedef1
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids169 (go to sequence)
- Protein existenceInferred from homology
- Annotation score2/5
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
- N-terminal N-formyl-L-methionyl-[peptide] + H2O = N-terminal L-methionyl-[peptide] + formate
Cofactor
Note: Binds 1 Fe2+ ion.
Features
Showing features for binding site, active site.
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | metal ion binding | |
Molecular Function | peptide deformylase activity | |
Biological Process | peptidyl-methionine modification | |
Biological Process | translation |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePeptide deformylase
- EC number
- Short namesPDF
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Pasteurellales > Pasteurellaceae > Avibacterium
Accessions
- Primary accessionA0A447SNR5
Proteomes
Structure
Sequence
- Sequence statusComplete
- Length169
- Mass (Da)19,119
- Last updated2019-05-08 v1
- ChecksumCE12B68E9C59A697
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
LR134167 EMBL· GenBank· DDBJ | VEB22404.1 EMBL· GenBank· DDBJ | Genomic DNA |