Q89AP3 (AMPM_BUCBP) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 65.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Methionine aminopeptidase Short name=MAP EC=3.4.11.18 Alternative name(s): Peptidase M | ||||
| Gene names |
| ||||
| Organism | Buchnera aphidicola subsp. Baizongia pistaciae (strain Bp) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 224915 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Buchnera |
Protein attributes
| Sequence length | 266 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Removes the amino-terminal methionine from nascent proteins By similarity. |
| Catalytic activity | Release of N-terminal amino acids, preferentially methionine, from peptides and arylamides. |
| Cofactor | Binds 2 cobalt ions per subunit. The true nature of the physiological cofactor is under debate. The enzyme is also active with zinc, manganese or divalent iron ions By similarity. Binds 1 sodium ion per subunit. The sodium ion has a structural role By similarity. |
| Sequence similarities | Belongs to the peptidase M24A family. |
Ontologies
| Keywords | |
|---|---|
| Ligand | Cobalt Metal-binding |
| Molecular function | Aminopeptidase Hydrolase Protease |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | cellular process Inferred from electronic annotation. Source: InterPro proteolysisInferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | aminopeptidase activity Inferred from electronic annotation. Source: UniProtKB-KW metal ion bindingInferred from electronic annotation. Source: UniProtKB-KW metalloexopeptidase activityInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 266 | 266 | Methionine aminopeptidase | PRO_0000148931 | |||||
Sites | |||||||||
| Metal binding | 98 | 1 | Cobalt 1 By similarity | ||||||
| Metal binding | 109 | 1 | Cobalt 1 By similarity | ||||||
| Metal binding | 109 | 1 | Cobalt 2 By similarity | ||||||
| Metal binding | 172 | 1 | Cobalt 2 By similarity | ||||||
| Metal binding | 206 | 1 | Cobalt 2 By similarity | ||||||
| Metal binding | 237 | 1 | Cobalt 1 By similarity | ||||||
| Metal binding | 237 | 1 | Cobalt 2 By similarity | ||||||
| Binding site | 80 | 1 | Substrate By similarity | ||||||
| Binding site | 179 | 1 | Substrate By similarity | ||||||
Sequences
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References
| [1] | "Reductive genome evolution in Buchnera aphidicola." van Ham R.C.H.J., Kamerbeek J., Palacios C., Rausell C., Abascal F., Bastolla U., Fernandez J.M., Jimenez L., Postigo M., Silva F.J., Tamames J., Viguera E., Latorre A., Valencia A., Moran F., Moya A. Proc. Natl. Acad. Sci. U.S.A. 100:581-586(2003) [PubMed: 12522265] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Bp. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AE016826 Genomic DNA. Translation: AAO26944.1. |
| RefSeq | NP_777839.1. NC_004545.1. |
3D structure databases | |
| ProteinModelPortal | Q89AP3. |
| ModBase | Search... |
Protein family/group databases | |
| MEROPS | M24.001. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | EBBUCT00000002208; EBBUCP00000002032; EBBUCG00000002208. |
| GeneID | 1058483. |
| GenomeReviews | Gene locus bbp_212 in contig AE016826_GR. |
| KEGG | bab:bbp212. |
| PATRIC | 21245199. VBIBucAph80364_0206. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| GeneTree | EBGT00050000008074. |
| HOGENOM | HBG299384. |
| OMA | HYGTRGK. |
Enzyme and pathway databases | |
| BioCyc | BAPH224915:BBP_212-MONOMER. |
Family and domain databases | |
| InterPro | IPR001714. Pept_M24_MAP. IPR000994. Pept_M24_structural-domain. IPR002467. Pept_M24A_MAP1. [Graphical view] |
| Gene3D | G3DSA:3.90.230.10. Peptidase_M24_cat_core. 1 hit. |
| KO | K01265. |
| Pfam | PF00557. Peptidase_M24. 1 hit. [Graphical view] |
| PRINTS | PR00599. MAPEPTIDASE. |
| SUPFAM | SSF55920. Peptidase_M24_cat_core. 1 hit. |
| TIGRFAMs | TIGR00500. Met_pdase_I. 1 hit. |
| PROSITE | PS00680. MAP_1. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | AMPM_BUCBP | ||||||||
| Accession | Primary (citable) accession number: Q89AP3 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| Peptidase families Classification of peptidase families and list of entries |
| SIMILARITY comments Index of protein domains and families |

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