P56218 · MAP2_PYRFU
- ProteinMethionine aminopeptidase
- Genemap
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids295 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val).
Catalytic activity
Cofactor
Zn2+ (UniProtKB | Rhea| CHEBI:29105 )
Mn2+ (UniProtKB | Rhea| CHEBI:29035 )
Fe2+ (UniProtKB | Rhea| CHEBI:29033 )
Note: Binds 2 divalent metal cations per subunit. Has a high-affinity and a low affinity metal-binding site. The true nature of the physiological cofactor is under debate. The enzyme is active with cobalt, zinc, manganese or divalent iron ions. Most likely, methionine aminopeptidases function as mononuclear Fe2+-metalloproteases under physiological conditions, and the catalytically relevant metal-binding site has been assigned to the histidine-containing high-affinity site.
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
9.2 mM | a Met-Ala-Ser peptide (for the Fe2+-complexed enzyme) | |||||
11.8 mM | a Met-Ala-Ser peptide (for the Co2+-complexed enzyme) | |||||
5 mM | a Met-Gly-Met-Met peptide (for the Fe2+-complexed enzyme) | |||||
5.1 mM | a Met-Gly-Met-Met peptide (for the Co2+-complexed enzyme) | |||||
1.3 mM | a Met-Ser-Ser-His-Arg-Trp-Asp-Trp peptide (for the Fe2+-complexed enzyme) | |||||
2 mM | a Met-Ser-Ser-His-Arg-Trp-Asp-Trp peptide (for the Co2+-complexed enzyme) |
pH Dependence
Optimum pH is 7-8.
Temperature Dependence
Optimum temperature is about 90 degrees Celsius.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 62 | substrate | |||
Binding site | 82 | a divalent metal cation 1 (UniProtKB | ChEBI) | |||
Binding site | 93 | a divalent metal cation 1 (UniProtKB | ChEBI) | |||
Binding site | 93 | a divalent metal cation 2 (UniProtKB | ChEBI); catalytic | |||
Binding site | 153 | a divalent metal cation 2 (UniProtKB | ChEBI); catalytic | |||
Binding site | 161 | substrate | |||
Binding site | 187 | a divalent metal cation 2 (UniProtKB | ChEBI); catalytic | |||
Binding site | 280 | a divalent metal cation 1 (UniProtKB | ChEBI) | |||
Binding site | 280 | a divalent metal cation 2 (UniProtKB | ChEBI); catalytic | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | initiator methionyl aminopeptidase activity | |
Molecular Function | metal ion binding | |
Molecular Function | metalloaminopeptidase activity | |
Biological Process | proteolysis |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameMethionine aminopeptidase
- EC number
- Short namesMAP ; MetAP
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageArchaea > Methanobacteriati > Methanobacteriota > Thermococci > Thermococcales > Thermococcaceae > Pyrococcus
Accessions
- Primary accessionP56218
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Mutagenesis | 161 | Reduces enzymatic activity by 96% at 37 degrees Celsius and by 88% at 87 degrees Celsius; when associated with A-173. | |||
Mutagenesis | 173 | Reduces enzymatic activity by 96% at 37 degrees Celsius and by 88% at 87 degrees Celsius; when associated with A-161. | |||
Chemistry
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Chain | PRO_0000148978 | 1-295 | Methionine aminopeptidase | ||
Proteomic databases
Interaction
Structure
Sequence
- Sequence statusComplete
- Length295
- Mass (Da)32,842
- Last updated1998-07-15 v1
- MD5 ChecksumA3D0BCB6FD56AEBE03F62F526AEE7CEC
Mass Spectrometry
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AE009950 EMBL· GenBank· DDBJ | AAL80665.1 EMBL· GenBank· DDBJ | Genomic DNA |