B2HDU8 (ADD_MYCMM) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 29.
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: Adenosine deaminase EC=3.5.4.4 Alternative name(s): Adenosine aminohydrolase | ||||
| Gene names |
| ||||
| Organism | Mycobacterium marinum (strain ATCC BAA-535 / M) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 216594 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium |
Protein attributes
| Sequence length | 362 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Catalytic activity | Adenosine + H2O = inosine + NH3. HAMAP MF_00540 |
| Cofactor | Binds 1 zinc ion per subunit By similarity. HAMAP MF_00540 |
| Sequence similarities | Belongs to the adenosine and AMP deaminases family. Adenosine deaminase subfamily. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Nucleotide metabolism |
| Ligand | Metal-binding Zinc |
| Molecular function | Hydrolase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | purine ribonucleoside monophosphate biosynthetic process Inferred from electronic annotation. Source: InterPro |
| Molecular function | adenosine deaminase activity Inferred from electronic annotation. Source: EC metal ion bindingInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 362 | 362 | Adenosine deaminase HAMAP MF_00540 | PRO_1000128852 | |||||
Sites | |||||||||
| Active site | 211 | 1 | Proton donor By similarity | ||||||
| Metal binding | 19 | 1 | Zinc; catalytic By similarity | ||||||
| Metal binding | 21 | 1 | Zinc; catalytic By similarity | ||||||
| Metal binding | 208 | 1 | Zinc; catalytic By similarity | ||||||
| Metal binding | 300 | 1 | Zinc; catalytic By similarity | ||||||
| Binding site | 21 | 1 | Substrate By similarity | ||||||
| Binding site | 23 | 1 | Substrate By similarity | ||||||
| Binding site | 181 | 1 | Substrate; via amide nitrogen and carbonyl oxygen By similarity | ||||||
| Site | 232 | 1 | Important for catalytic activity By similarity | ||||||
Sequences
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References
| [1] | "Insights from the complete genome sequence of Mycobacterium marinum on the evolution of Mycobacterium tuberculosis." Stinear T.P., Seemann T., Harrison P.F., Jenkin G.A., Davies J.K., Johnson P.D., Abdellah Z., Arrowsmith C., Chillingworth T., Churcher C., Clarke K., Cronin A., Davis P., Goodhead I., Holroyd N., Jagels K., Lord A., Moule S. Cole S.T.Genome Res. 18:729-741(2008) [PubMed: 18403782] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-535 / M. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CP000854 Genomic DNA. Translation: ACC39664.1. |
| RefSeq | YP_001849519.1. NC_010612.1. |
3D structure databases | |
| ProteinModelPortal | B2HDU8. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | B2HDU8. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | EBMYCT00000035943; EBMYCP00000034383; EBMYCG00000035938. |
| GeneID | 6225461. |
| GenomeReviews | Gene locus MMAR_1206 in contig CP000854_GR. |
| KEGG | mmi:MMAR_1206. |
| PATRIC | 18063201. VBIMycMar75906_1289. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| GeneTree | EBGT00050000016615. |
| HOGENOM | HBG630382. |
| OMA | PYYMAMN. |
| ProtClustDB | PRK09358. |
Family and domain databases | |
| HAMAP | MF_00540. A_deaminase. [Tree] |
| InterPro | IPR001365. A/AMP_deaminase_dom. IPR006330. A_deaminase. [Graphical view] |
| KO | K01488. |
| PANTHER | PTHR11409:SF21. PTHR11409:SF21. 1 hit. |
| Pfam | PF00962. A_deaminase. 1 hit. [Graphical view] |
| TIGRFAMs | TIGR01430. Aden_deam. 1 hit. |
| PROSITE | PS00485. A_DEAMINASE. False negative. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | ADD_MYCMM | ||||||||
| Accession | Primary (citable) accession number: B2HDU8 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

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