A0A292ZJK0 · A0A292ZJK0_SPHSA
- ProteinPeptide deformylase
- Genedef
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids192 (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.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 117 | Fe cation (UniProtKB | ChEBI) | |||
Binding site | 159 | Fe cation (UniProtKB | ChEBI) | |||
Active site | 160 | ||||
Binding site | 163 | Fe cation (UniProtKB | ChEBI) | |||
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 > Alphaproteobacteria > Sphingomonadales > Sphingomonadaceae > Sphingobium
Accessions
- Primary accessionA0A292ZJK0
Proteomes
Structure
Sequence
- Sequence statusComplete
- Length192
- Mass (Da)21,769
- Last updated2017-12-20 v1
- MD5 ChecksumBF779524B2D7EBB9D56F91B9CFCE36B4
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
BEWI01000032 EMBL· GenBank· DDBJ | GAY23104.1 EMBL· GenBank· DDBJ | Genomic DNA |