Q2RK25 · DEF_MOOTA
- ProteinPeptide deformylase
- Genedef
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids155 (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 > Bacillota > Clostridia > Moorellales > Moorellaceae > Moorella
Accessions
- Primary accessionQ2RK25
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000301056 | 1-155 | Peptide deformylase | |||
Sequence: MAIHKILTLGDPLLREKSQPVRKITSNVWKLLDNLADTMYDAPGVGLAAPQIGVLKRVIVVDVGEGLTELINPEVIAASGEEVGAEGCLSIPGAQGEVPRAAVVTVRGLDRHGRVREIRAEGLYARALQHEIDHLDGILFIDKVVRWLENQPGER |
Interaction
Protein-protein interaction databases
Structure
Sequence
- Sequence statusComplete
- Length155
- Mass (Da)16,851
- Last updated2006-01-24 v1
- Checksum9F0415CE4692EF7F
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP000232 EMBL· GenBank· DDBJ | ABC19214.1 EMBL· GenBank· DDBJ | Genomic DNA |