A1KM35 (DUT_MYCBP) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 48.
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: Deoxyuridine 5'-triphosphate nucleotidohydrolase Short name=dUTPase EC=3.6.1.23 Alternative name(s): dUTP pyrophosphatase | ||||
| Gene names |
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| Organism | Mycobacterium bovis (strain BCG / Pasteur 1173P2) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 410289 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex › ![]() |
Protein attributes
| Sequence length | 154 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | This enzyme is involved in nucleotide metabolism: it produces dUMP, the immediate precursor of thymidine nucleotides and it decreases the intracellular concentration of dUTP so that uracil cannot be incorporated into DNA By similarity. HAMAP-Rule MF_00116 |
| Catalytic activity | dUTP + H2O = dUMP + diphosphate. HAMAP-Rule MF_00116 |
| Cofactor | Magnesium By similarity. |
| Pathway | Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP (dUTP route): step 2/2. HAMAP-Rule MF_00116 |
| Subunit structure | Homotrimer By similarity. |
| Miscellaneous | Each trimer binds three substrate molecules. The ligands are bound between subunits, and for each substrate molecule, residues from adjacent subunits contribute to the binding interactions By similarity. HAMAP-Rule MF_00116 |
| Sequence similarities | Belongs to the dUTPase family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Nucleotide metabolism |
| Ligand | Magnesium Metal-binding |
| Molecular function | Hydrolase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological_process | dUMP biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway dUTP metabolic processInferred from electronic annotation. Source: InterPro |
| Molecular_function | dUTP diphosphatase activity Inferred from electronic annotation. Source: HAMAP magnesium ion bindingInferred from electronic annotation. Source: HAMAP |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 154 | 154 | Deoxyuridine 5'-triphosphate nucleotidohydrolase HAMAP-Rule MF_00116 | PRO_1000015484 | |||||
Regions | |||||||||
| Region | 64 – 66 | 3 | Substrate binding By similarity | ||||||
| Region | 81 – 83 | 3 | Substrate binding By similarity | ||||||
Sites | |||||||||
| Binding site | 77 | 1 | Substrate By similarity | ||||||
| Binding site | 91 | 1 | Substrate; via amide nitrogen and carbonyl oxygen By similarity | ||||||
Sequences
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References
| [1] | "Genome plasticity of BCG and impact on vaccine efficacy." Brosch R., Gordon S.V., Garnier T., Eiglmeier K., Frigui W., Valenti P., Dos Santos S., Duthoy S., Lacroix C., Garcia-Pelayo C., Inwald J.K., Golby P., Garcia J.N., Hewinson R.G., Behr M.A., Quail M.A., Churcher C., Barrell B.G., Parkhill J., Cole S.T. Proc. Natl. Acad. Sci. U.S.A. 104:5596-5601(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: BCG / Pasteur 1173P2. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AM408590 Genomic DNA. Translation: CAL72698.1. |
| RefSeq | YP_978796.1. NC_008769.1. |
3D structure databases | |
| ProteinModelPortal | A1KM35. |
| SMR | A1KM35. Positions 1-138. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 410289.BCG_2710c. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | CAL72698; CAL72698; BCG_2710c. |
| GeneID | 4698537. |
| KEGG | mbb:BCG_2710c. |
| PATRIC | 18016416. VBIMycBov80988_2954. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG0756. |
| HOGENOM | HOG000028966. |
| KO | K01520. |
| OMA | KVCLINH. |
| ProtClustDB | PRK00601. |
Enzyme and pathway databases | |
| BioCyc | MBOV410289:GJW7-2750-MONOMER. |
| UniPathway | UPA00610; UER00666. |
Family and domain databases | |
| HAMAP | MF_00116. dUTPase_bact. |
| InterPro | IPR008180. dUTP_pyroPase. IPR008181. dUTP_pyroPase_sf. [Graphical view] |
| PANTHER | PTHR11241. PTHR11241. 1 hit. |
| Pfam | PF00692. dUTPase. 1 hit. [Graphical view] |
| TIGRFAMs | TIGR00576. dut. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | DUT_MYCBP | ||||||||
| Accession | Primary (citable) accession number: A1KM35 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with
