Ribose-5-phosphate isomerase B
Details
- Name
- Ribose-5-phosphate isomerase B
- Synonyms
- 5.3.1.6
- Phosphoriboisomerase B
- Gene Name
- rpiB
- Organism
- Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
- Amino acid sequence
>lcl|BSEQ0051191|Ribose-5-phosphate isomerase B MSGMRVYLGADHAGYELKQRIIEHLKQTGHEPIDCGALRYDADDDYPAFCIAAATRTVAD PGSLGIVLGGSGNGEQIAANKVPGARCALAWSVQTAALAREHNNAQLIGIGGRMHTVAEA LAIVDAFVTTPWSKAQRHQRRIDILAEYERTHEAPPVPGAPA
- Number of residues
- 162
- Molecular Weight
- 17277.355
- Theoretical pI
- Not Available
- GO Classification
- Functionsribose-5-phosphate isomerase activityProcessescarbohydrate metabolic process / pentose-phosphate shunt, non-oxidative branchComponentsextracellular region
- General Function
- Catalyzes the interconversion of ribulose-5-P and ribose-5-P. It has not isomerase activity towards D-allose 6-phosphate.
- Specific Function
- Ribose-5-phosphate isomerase activity
- Pfam Domain Function
- LacAB_rpiB (PF02502)
- Transmembrane Regions
- Not Available
- Cellular Location
- Not Available
- Gene sequence
>lcl|BSEQ0051192|Ribose-5-phosphate isomerase B (rpiB) ATGTCGGGCATGCGCGTCTACCTGGGGGCCGACCACGCCGGATATGAGCTCAAGCAGCGG ATCATCGAGCACCTGAAGCAAACCGGCCACGAGCCGATCGACTGCGGCGCGTTGCGCTAC GACGCCGACGACGACTACCCGGCATTCTGCATTGCCGCAGCGACGCGCACTGTCGCCGAT CCGGGCAGCCTGGGCATCGTGCTGGGCGGATCGGGCAACGGGGAGCAGATCGCCGCCAAC AAGGTGCCCGGCGCTCGCTGCGCGCTGGCCTGGAGTGTGCAGACCGCGGCGCTGGCTCGC GAGCACAACAACGCCCAATTGATCGGCATCGGCGGCCGCATGCACACGGTGGCCGAGGCA CTGGCGATAGTCGACGCCTTCGTCACCACGCCGTGGTCGAAAGCGCAACGCCACCAACGG CGTATCGACATTCTCGCCGAGTACGAACGGACCCACGAAGCGCCGCCGGTGCCCGGCGCT CCGGCCTGA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID P9WKD7 UniProtKB Entry Name RPIB_MYCTU - General References
- Cole ST, Brosch R, Parkhill J, Garnier T, Churcher C, Harris D, Gordon SV, Eiglmeier K, Gas S, Barry CE 3rd, Tekaia F, Badcock K, Basham D, Brown D, Chillingworth T, Connor R, Davies R, Devlin K, Feltwell T, Gentles S, Hamlin N, Holroyd S, Hornsby T, Jagels K, Krogh A, McLean J, Moule S, Murphy L, Oliver K, Osborne J, Quail MA, Rajandream MA, Rogers J, Rutter S, Seeger K, Skelton J, Squares R, Squares S, Sulston JE, Taylor K, Whitehead S, Barrell BG: Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence. Nature. 1998 Jun 11;393(6685):537-44. [Article]
- Kelkar DS, Kumar D, Kumar P, Balakrishnan L, Muthusamy B, Yadav AK, Shrivastava P, Marimuthu A, Anand S, Sundaram H, Kingsbury R, Harsha HC, Nair B, Prasad TS, Chauhan DS, Katoch K, Katoch VM, Kumar P, Chaerkady R, Ramachandran S, Dash D, Pandey A: Proteogenomic analysis of Mycobacterium tuberculosis by high resolution mass spectrometry. Mol Cell Proteomics. 2011 Dec;10(12):M111.011627. doi: 10.1074/mcp.M111.011445. Epub 2011 Oct 3. [Article]
- Roos AK, Andersson CE, Bergfors T, Jacobsson M, Karlen A, Unge T, Jones TA, Mowbray SL: Mycobacterium tuberculosis ribose-5-phosphate isomerase has a known fold, but a novel active site. J Mol Biol. 2004 Jan 16;335(3):799-809. [Article]
- Roos AK, Burgos E, Ericsson DJ, Salmon L, Mowbray SL: Competitive inhibitors of Mycobacterium tuberculosis ribose-5-phosphate isomerase B reveal new information about the reaction mechanism. J Biol Chem. 2005 Feb 25;280(8):6416-22. Epub 2004 Dec 7. [Article]
- Roos AK, Mariano S, Kowalinski E, Salmon L, Mowbray SL: D-ribose-5-phosphate isomerase B from Escherichia coli is also a functional D-allose-6-phosphate isomerase, while the Mycobacterium tuberculosis enzyme is not. J Mol Biol. 2008 Oct 10;382(3):667-79. doi: 10.1016/j.jmb.2008.06.090. Epub 2008 Jul 9. [Article]