A0A059ZMR7 · A0A059ZMR7_ACIBA
- ProteinMethionine aminopeptidase
- Genemap
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids264 (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 | 82 | substrate | |||
Binding site | 100 | a divalent metal cation 1 (UniProtKB | ChEBI) | |||
Binding site | 111 | a divalent metal cation 2 (UniProtKB | ChEBI); catalytic | |||
Binding site | 111 | a divalent metal cation 1 (UniProtKB | ChEBI) | |||
Binding site | 174 | a divalent metal cation 2 (UniProtKB | ChEBI); catalytic | |||
Binding site | 181 | substrate | |||
Binding site | 207 | a divalent metal cation 2 (UniProtKB | ChEBI); catalytic | |||
Binding site | 238 | a divalent metal cation 2 (UniProtKB | ChEBI); catalytic | |||
Binding site | 238 | a divalent metal cation 1 (UniProtKB | ChEBI) | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Molecular Function | initiator methionyl aminopeptidase activity | |
Molecular Function | metalloaminopeptidase activity | |
Molecular Function | transition metal ion binding | |
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
- Organism
- Strains
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Moraxellales > Moraxellaceae > Acinetobacter > Acinetobacter calcoaceticus/baumannii complex
Accessions
- Primary accessionA0A059ZMR7
- Secondary accessions
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Interaction
Subunit
Monomer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 15-245 | Peptidase M24 | |||
Sequence similarities
Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length264
- Mass (Da)29,092
- Last updated2014-09-03 v1
- ChecksumAD2322C55E84AC2D
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP008706 EMBL· GenBank· DDBJ | AKA31513.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
LN997846 EMBL· GenBank· DDBJ | CUW35480.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AAYLMQ010000055 EMBL· GenBank· DDBJ | EGY2378915.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
ABFEVW020000007 EMBL· GenBank· DDBJ | EKU3567916.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
ABFEVW030000007 EMBL· GenBank· DDBJ | EMN1071013.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
JACSVK010000004 EMBL· GenBank· DDBJ | MBD0218786.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
JARTMM010000054 EMBL· GenBank· DDBJ | MDK4882678.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
VMAW01000001 EMBL· GenBank· DDBJ | MDT1910157.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
JARTMM020000001 EMBL· GenBank· DDBJ | MEC5496873.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
WIOC01000010 EMBL· GenBank· DDBJ | MQR49752.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
WPIP01000042 EMBL· GenBank· DDBJ | MVM91401.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
WWCH01000001 EMBL· GenBank· DDBJ | MYM78551.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
JAAGTY010000004 EMBL· GenBank· DDBJ | NDW40444.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
LYKI01000012 EMBL· GenBank· DDBJ | OIG73491.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
NGEL01000114 EMBL· GenBank· DDBJ | OTM86556.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
NGKM01000002 EMBL· GenBank· DDBJ | OWK68137.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
NXDV01000003 EMBL· GenBank· DDBJ | PHQ03524.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
PHJU02000018 EMBL· GenBank· DDBJ | PQL84119.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
NEPB01000031 EMBL· GenBank· DDBJ | PRN33361.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
QKWF01000197 EMBL· GenBank· DDBJ | PZM11780.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP061525 EMBL· GenBank· DDBJ | QNV23380.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP059300 EMBL· GenBank· DDBJ | QOJ60769.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP072270 EMBL· GenBank· DDBJ | QTK45075.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
RFBY01000027 EMBL· GenBank· DDBJ | RSP75700.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
RFCO01000050 EMBL· GenBank· DDBJ | RSQ43370.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
RXLU01000082 EMBL· GenBank· DDBJ | RTQ74327.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
RXYO01000031 EMBL· GenBank· DDBJ | RTY11398.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
UFDJ01000006 EMBL· GenBank· DDBJ | SSI39501.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
UFMQ01000007 EMBL· GenBank· DDBJ | SST23006.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
UFNM01000010 EMBL· GenBank· DDBJ | SSU12229.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
VHEY01000073 EMBL· GenBank· DDBJ | TPS81387.1 EMBL· GenBank· DDBJ | Genomic DNA |