A0A7L5ZF91 · A0A7L5ZF91_9ACTN
- ProteinMultifunctional fusion protein
- Genemap
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids472 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
Function
function
Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism.
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
- AMP + ATP = 2 ADP
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.
Pathway
Purine metabolism; AMP biosynthesis via salvage pathway; AMP from ADP: step 1/1.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 10-15 | ATP (UniProtKB | ChEBI) | |||
Binding site | 31 | AMP (UniProtKB | ChEBI) | |||
Binding site | 36 | AMP (UniProtKB | ChEBI) | |||
Binding site | 57-59 | AMP (UniProtKB | ChEBI) | |||
Binding site | 92 | AMP (UniProtKB | ChEBI) | |||
Binding site | 127 | ATP (UniProtKB | ChEBI) | |||
Binding site | 133 | AMP (UniProtKB | ChEBI) | |||
Binding site | 144 | AMP (UniProtKB | ChEBI) | |||
Binding site | 163 | ATP (UniProtKB | ChEBI) | |||
Binding site | 280 | substrate | |||
Binding site | 297 | a divalent metal cation 1 (UniProtKB | ChEBI) | |||
Binding site | 308 | a divalent metal cation 2 (UniProtKB | ChEBI); catalytic | |||
Binding site | 308 | a divalent metal cation 1 (UniProtKB | ChEBI) | |||
Binding site | 373 | a divalent metal cation 2 (UniProtKB | ChEBI); catalytic | |||
Binding site | 380 | substrate | |||
Binding site | 406 | a divalent metal cation 2 (UniProtKB | ChEBI); catalytic | |||
Binding site | 437 | a divalent metal cation 1 (UniProtKB | ChEBI) | |||
Binding site | 437 | a divalent metal cation 2 (UniProtKB | ChEBI); catalytic | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Molecular Function | adenylate kinase activity | |
Molecular Function | ATP binding | |
Molecular Function | initiator methionyl aminopeptidase activity | |
Molecular Function | metal ion binding | |
Molecular Function | metalloaminopeptidase activity | |
Biological Process | AMP salvage | |
Biological Process | phosphorylation | |
Biological Process | proteolysis |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameMultifunctional fusion protein
Including 2 domains:
- Recommended nameAdenylate kinase
- EC number
- Short namesAK
- Alternative names
- Recommended nameMethionine aminopeptidase
- EC number
- Short namesMAP ; MetAP
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Actinomycetota > Actinomycetes > Propionibacteriales > Nocardioidaceae > Micropruina
Accessions
- Primary accessionA0A7L5ZF91
Proteomes
Subcellular Location
Interaction
Subunit
Monomer.
Structure
Family & Domains
Features
Showing features for region, domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Region | 30-59 | NMP | |||
Domain | 209-443 | Peptidase M24 | |||
Domain
Consists of three domains, a large central CORE domain and two small peripheral domains, NMPbind and LID, which undergo movements during catalysis. The LID domain closes over the site of phosphoryl transfer upon ATP binding. Assembling and dissambling the active center during each catalytic cycle provides an effective means to prevent ATP hydrolysis.
Sequence similarities
Belongs to the adenylate kinase family.
Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily.
Family and domain databases
Sequence
- Sequence statusComplete
- Length472
- Mass (Da)50,633
- Last updated2021-04-07 v1
- MD5 ChecksumF2C881F9EB4E6EDDACA16025A29A28FF
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP059261 EMBL· GenBank· DDBJ | QLQ15268.1 EMBL· GenBank· DDBJ | Genomic DNA |