| Identification |
|---|
| HMDB Protein ID
| HMDBP13339 |
| Secondary Accession Numbers
| None |
| Name
| D-ribitol-5-phosphate phosphatase |
| Synonyms
|
- 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase
|
| Gene Name
| (GENBANK) HALOACID DEHALOGENASE-LIKE HYDROLASE |
| Protein Type
| Unknown |
| Biological Properties |
|---|
| General Function
| Not Available |
| Specific Function
| Catalyzes the dephosphorylation of D-ribitol-5-phosphate and D-ribitol-1-phosphate. Is also able to dephosphorylate 5-amino-6-(5-phospho-D-ribitylamino)uracil, and thus could be involved in the riboflavin biosynthesis pathway. |
| Pathways
|
- Biosynthesis of cofactors
- Biosynthesis of secondary metabolites
- riboflavin biosynthesis
- Riboflavin metabolism
|
| Reactions
| Not Available |
| GO Classification
|
| Biological Process |
| dephosphorylation |
| riboflavin biosynthetic process |
| Molecular Function |
| metal ion binding |
| 5-amino-6-(5-phosphoribitylamino)uracil phosphatase activity |
| ribitol-5-phosphatase activity |
|
| Cellular Location
|
Not Available
|
| Gene Properties |
|---|
| Chromosome Location
| Not Available |
| Locus
| Not Available |
| SNPs
| Not Available |
| Gene Sequence
|
Not Available
|
| Protein Properties |
|---|
| Number of Residues
| 206 |
| Molecular Weight
| 23544.435 |
| Theoretical pI
| 4.904 |
| Pfam Domain Function
|
|
| Signals
|
Not Available
|
|
Transmembrane Regions
|
Not Available
|
| Protein Sequence
|
Not Available
|
| External Links |
|---|
| GenBank ID Protein
| Not Available |
| UniProtKB/Swiss-Prot ID
| Q8A947 |
| UniProtKB/Swiss-Prot Entry Name
| RIBX_BACTN |
| PDB IDs
|
|
| GenBank Gene ID
| Not Available |
| GeneCard ID
| Not Available |
| GenAtlas ID
| Not Available |
| HGNC ID
| Not Available |
| References |
|---|
| General References
| - Xu J, Bjursell MK, Himrod J, Deng S, Carmichael LK, Chiang HC, Hooper LV, Gordon JI: A genomic view of the human-Bacteroides thetaiotaomicron symbiosis. Science. 2003 Mar 28;299(5615):2074-6. doi: 10.1126/science.1080029. [PubMed:12663928 ]
- London N, Farelli JD, Brown SD, Liu C, Huang H, Korczynska M, Al-Obaidi NF, Babbitt PC, Almo SC, Allen KN, Shoichet BK: Covalent docking predicts substrates for haloalkanoate dehalogenase superfamily phosphatases. Biochemistry. 2015 Jan 20;54(2):528-37. doi: 10.1021/bi501140k. Epub 2015 Jan 5. [PubMed:25513739 ]
|
