B9DKM0 (DEOB_STACT) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 34.
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: Phosphopentomutase EC=5.4.2.7 Alternative name(s): Phosphodeoxyribomutase | ||||
| Gene names |
| ||||
| Organism | Staphylococcus carnosus (strain TM300) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 396513 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacilli › Bacillales › Staphylococcus › ![]() |
Protein attributes
| Sequence length | 396 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Phosphotransfer between the C1 and C5 carbon atoms of pentose By similarity. HAMAP-Rule MF_00740 |
| Catalytic activity | Alpha-D-ribose 1-phosphate = D-ribose 5-phosphate. HAMAP-Rule MF_00740 2-deoxy-alpha-D-ribose 1-phosphate = 2-deoxy-alpha-D-ribose 5-phosphate. HAMAP-Rule MF_00740 |
| Cofactor | Binds 1 or 2 manganese ions Potential. |
| Pathway | Metabolic intermediate biosynthesis; 5-phospho-alpha-D-ribose 1-diphosphate biosynthesis; 5-phospho-alpha-D-ribose 1-diphosphate from D-ribose 5-phosphate (route II): step 1/3. HAMAP-Rule MF_00740 |
| Subcellular location | Cytoplasm By similarity. |
| Sequence similarities | Belongs to the phosphopentomutase family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Cytoplasm |
| Ligand | Manganese Metal-binding |
| Molecular function | Isomerase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological_process | 5-phosphoribose 1-diphosphate biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway cellular metabolic compound salvageInferred from electronic annotation. Source: InterPro deoxyribonucleotide catabolic processInferred from electronic annotation. Source: HAMAP |
| Cellular_component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular_function | magnesium ion binding Inferred from electronic annotation. Source: InterPro manganese ion bindingInferred from electronic annotation. Source: HAMAP phosphopentomutase activityInferred 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 – 396 | 396 | Phosphopentomutase HAMAP-Rule MF_00740 | PRO_1000148251 | |||||
Sites | |||||||||
| Metal binding | 14 | 1 | Manganese By similarity | ||||||
| Metal binding | 291 | 1 | Manganese By similarity | ||||||
| Metal binding | 327 | 1 | Manganese By similarity | ||||||
| Metal binding | 328 | 1 | Manganese By similarity | ||||||
| Metal binding | 339 | 1 | Manganese By similarity | ||||||
Sequences
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References
| [1] | "Genome analysis of the meat starter culture bacterium Staphylococcus carnosus TM300." Rosenstein R., Nerz C., Biswas L., Resch A., Raddatz G., Schuster S.C., Goetz F. Appl. Environ. Microbiol. 75:811-822(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: TM300. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AM295250 Genomic DNA. Translation: CAL28916.1. |
| RefSeq | YP_002635101.1. NC_012121.1. |
3D structure databases | |
| ProteinModelPortal | B9DKM0. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 396513.Sca_2011. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 7550983. |
| KEGG | sca:Sca_2011. |
| PATRIC | 19604894. VBIStaCar105558_2009. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG1015. |
| HOGENOM | HOG000008159. |
| KO | K01839. |
| OMA | PNMAKLG. |
| ProtClustDB | PRK05362. |
Enzyme and pathway databases | |
| BioCyc | SCAR396513:GJ9G-2072-MONOMER. |
| UniPathway | UPA00087; UER00173. |
Family and domain databases | |
| Gene3D | 3.30.70.1250. 1 hit. 3.40.720.10. 2 hits. |
| HAMAP | MF_00740. Phosphopentomut. |
| InterPro | IPR017849. Alkaline_Pase-like_a/b/a. IPR017850. Alkaline_phosphatase_core. IPR010045. DeoB. IPR006124. Metalloenzyme. IPR024052. Phosphopentomutase_DeoB_cap. [Graphical view] |
| Pfam | PF01676. Metalloenzyme. 1 hit. [Graphical view] |
| PIRSF | PIRSF001491. Ppentomutase. 1 hit. |
| SUPFAM | SSF53649. Alkaline_phosphatase_core. 1 hit. SSF143856. SSF143856. 1 hit. |
| TIGRFAMs | TIGR01696. deoB. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | DEOB_STACT | ||||||||
| Accession | Primary (citable) accession number: B9DKM0 | ||||||||
| 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
