O52353 (AMPM_MYCGA) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 88.
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 |
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| Organism | Mycoplasma gallisepticum (strain R(low / passage 15 / clone 2)) [Complete proteome] [HAMAP] | ||||||
| Taxonomic identifier | 710127 [NCBI] | ||||||
| Taxonomic lineage | Bacteria › Tenericutes › Mollicutes › Mycoplasmataceae › Mycoplasma |
Protein attributes
| Sequence length | 250 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Removes the amino-terminal methionine from nascent proteins. |
| 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. |
| 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 – 250 | 250 | Methionine aminopeptidase | PRO_0000148945 | |||||
Sites | |||||||||
| Metal binding | 94 | 1 | Cobalt 1 By similarity | ||||||
| Metal binding | 105 | 1 | Cobalt 1 By similarity | ||||||
| Metal binding | 105 | 1 | Cobalt 2 By similarity | ||||||
| Metal binding | 169 | 1 | Cobalt 2 By similarity | ||||||
| Metal binding | 202 | 1 | Cobalt 2 By similarity | ||||||
| Metal binding | 235 | 1 | Cobalt 1 By similarity | ||||||
| Metal binding | 235 | 1 | Cobalt 2 By similarity | ||||||
| Binding site | 77 | 1 | Substrate By similarity | ||||||
| Binding site | 176 | 1 | Substrate By similarity | ||||||
Experimental info | |||||||||
| Sequence conflict | 73 | 1 | Q → K in AAB95408. Ref.1 | ||||||
| Sequence conflict | 83 | 1 | E → D in AAB95408. Ref.1 | ||||||
| Sequence conflict | 117 | 1 | P → L in AAB95408. Ref.1 | ||||||
| Sequence conflict | 132 | 1 | E → D in AAB95408. Ref.1 | ||||||
| Sequence conflict | 158 | 1 | Y → H in AAB95408. Ref.1 | ||||||
| Sequence conflict | 161 | 1 | S → N in AAB95408. Ref.1 | ||||||
| Sequence conflict | 189 – 190 | 2 | SS → PG in AAB95408. Ref.1 | ||||||
| Sequence conflict | 217 | 1 | D → V in AAB95408. Ref.1 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Determination and analysis of the nucleotide sequence of a segment of a Mycoplasma gallisepticum strain A5969 chromosome, containing operons S10 and rrn23-5." Skamrov A.V., Gol'dman M.A., Feoktistova E.S., Bibilashvili R.S. Mol. Biol. (Mosk.) 34:390-396(2000) [PubMed: 10867916] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: A5969Var.B. |
| [2] | "The complete genome sequence of the avian pathogen Mycoplasma gallisepticum strain R(low)." Papazisi L., Gorton T.S., Kutish G., Markham P.F., Browning G.F., Nguyen D.K., Swartzell S., Madan A., Mahairas G., Geary S.J. Microbiology 149:2307-2316(2003) [PubMed: 12949158] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: R(low / passage 15 / clone 2). |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AF036708 Genomic DNA. Translation: AAB95408.1. AE015450 Genomic DNA. Translation: AAP56422.1. |
| RefSeq | NP_852854.1. NC_004829.2. |
3D structure databases | |
| ProteinModelPortal | O52353. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 1090121. |
| GenomeReviews | Gene locus MYCGA0720 in contig AE015450_GR. |
| KEGG | mga:MGA_0745. |
| PATRIC | 20007816. VBIMycGal115357_0076. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | HBG299384. |
| OMA | LCHAYMR. |
| PhylomeDB | O52353. |
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_MYCGA | ||||||||
| Accession | Primary (citable) accession number: O52353 | ||||||||
| 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 |

Clusters with