A0AAE5CF30 · A0AAE5CF30_RHOHA
- ProteinMethionine aminopeptidase
- Genemap
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids256 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
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). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed.
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.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 83 | substrate | ||||
Sequence: H | ||||||
Binding site | 100 | a divalent metal cation 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 111 | a divalent metal cation 2 (UniProtKB | ChEBI); catalytic | ||||
Sequence: D | ||||||
Binding site | 111 | a divalent metal cation 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 174 | a divalent metal cation 2 (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Binding site | 181 | substrate | ||||
Sequence: H | ||||||
Binding site | 207 | a divalent metal cation 2 (UniProtKB | ChEBI); catalytic | ||||
Sequence: E | ||||||
Binding site | 239 | a divalent metal cation 1 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 239 | a divalent metal cation 2 (UniProtKB | ChEBI); catalytic | ||||
Sequence: E |
GO annotations
Aspect | Term | |
---|---|---|
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
Names & Taxonomy
Protein names
- Recommended nameMethionine aminopeptidase
- EC number
- Short namesMAP ; MetAP
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Actinomycetota > Actinomycetes > Mycobacteriales > Nocardiaceae > Prescottella
Accessions
- Primary accessionA0AAE5CF30
Proteomes
Interaction
Subunit
Monomer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 12-246 | Peptidase M24 | ||||
Sequence: GMRAAGRVVADALAAARAHAQVGVSLRELDAVAARVVADAGAEPLFLNYRPNWAATPFPGVLCTSVNDAVVHGIPSGYRLRDGDLVSIDGGARLNGWCGDSAISFVVGAANPADEALVAATDEALRRGIEAARVGNRLGDIGAAIGTFARSRGFGLLADHGGHGIGRVMHESPDVPNEARAGRGMRLRDGLVLAIEPMLIADGSDDYRHDADGWTLRTVTGARAAHSEHTVAITD |
Sequence similarities
Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily.
Family and domain databases
Sequence
- Sequence statusComplete
- Length256
- Mass (Da)26,663
- Last updated2024-05-29 v1
- Checksum1486C85B30ED31EE