Identification
Name:D-ribose pyranase
Synonyms:Not Available
Gene Name:rbsD
Enzyme Class:
Biological Properties
General Function:Involved in intramolecular lyase activity
Specific Function:Catalyzes the interconversion of beta-pyran and beta- furan forms of D-ribose. It also catalyzes the conversion between beta-allofuranose and beta-allopyranose
Cellular Location:Cytoplasm (Potential)
SMPDB Pathways:
KEGG Pathways:
KEGG Reactions:
1.0Thumb1.0Thumb
EcoCyc Reactions:
1.0Thumb1.0Thumb
Complex Reactions:
1.0Thumb+1.0Thumb+1.0Thumb1.0Thumb+1.0Thumb+1.0Thumb+1.0Thumb
1.0Thumb1.0Thumb
Metabolites:
ECMDB IDNameView
ECMDB00538Adenosine triphosphateMetaboCard
ECMDB01341ADPMetaboCard
ECMDB23073beta-D-AllofuranoseMetaboCard
ECMDB20343beta-D-ribofuranoseMetaboCard
ECMDB20344beta-D-RibopyranoseMetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB01429PhosphateMetaboCard
ECMDB00283RiboseMetaboCard
ECMDB00494WaterMetaboCard
GO Classification:
Process
carbohydrate transport
establishment of localization
transport
Gene Properties
Blattner:b3748
Gene OrientationClockwise
Centisome Percentage:84.73
Left Sequence End3931374
Right Sequence End3931793
Gene Sequence:
>420 bp
GTGAAACCTGCTGCTCGTCGCCGCGCTCGTGAGTGTGCCGTCCAGGCGCTCTACTCCTGG
CAGTTGTCCCAGAACGACATCGCTGATGTTGAATACCAGTTCCTGGCTGAACAGGATGTA
AAAGACGTTGACGTCCTGTACTTCCGTGAGCTGCTGGCCGGGGTGGCGACTAATACCGCA
TACCTCGACGGACTGATGAAGCCATACCTGTCCCGCCTGCTGGAAGAACTGGGACAGGTA
GAAAAAGCAGTACTGCGCATTGCGCTGTACGAACTGTCTAAACGTAGCGATGTGCCATAC
AAAGTGGCCATTAACGAAGCGATCGAACTGGCGAAATCGTTCGGCGCAGAAGACAGCCAT
AAGTTCGTCAACGGCGTACTCGATAAAGCAGCACCTGTGATTCGCCCTAACAAAAAGTGA
Protein Properties
Pfam Domain Function:
Protein Residues:139
Protein Molecular Weight:15292
Protein Theoretical pI:6
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>D-ribose pyranase
MKKGTVLNSDISSVISRLGHTDTLVVCDAGLPIPKSTTRIDMALTQGVPSFMQVLGVVTN
EMQVEAAIIAEEIKHHNPQLHETLLTHLEQLQKHQGNTIEIRYTTHEQFKQQTAESQAVI
RSGECSPYANIILCAGVTF
References
External Links:
ResourceLink
Uniprot ID:P04982
Uniprot Name:RBSD_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85674556
Ecogene ID:EG10817
Ecocyc:EG10817
ColiBase:b3748
Kegg Gene:b3748
EchoBASE ID:EB0810
CCDB:RBSD_ECOLI
BacMap:90111647
General Reference:
  • Bell, A. W., Buckel, S. D., Groarke, J. M., Hope, J. N., Kingsley, D. H., Hermodson, M. A. (1986). "The nucleotide sequences of the rbsD, rbsA, and rbsC genes of Escherichia coli K12." J Biol Chem 261:7652-7658. Pubmed: 3011793
  • Blattner, F. R., Plunkett, G. 3rd, Bloch, C. A., Perna, N. T., Burland, V., Riley, M., Collado-Vides, J., Glasner, J. D., Rode, C. K., Mayhew, G. F., Gregor, J., Davis, N. W., Kirkpatrick, H. A., Goeden, M. A., Rose, D. J., Mau, B., Shao, Y. (1997). "The complete genome sequence of Escherichia coli K-12." Science 277:1453-1462. Pubmed: 9278503
  • Burland, V., Plunkett, G. 3rd, Daniels, D. L., Blattner, F. R. (1993). "DNA sequence and analysis of 136 kilobases of the Escherichia coli genome: organizational symmetry around the origin of replication." Genomics 16:551-561. Pubmed: 7686882
  • Feng, Y., Jiao, W., Fu, X., Chang, Z. (2006). "Stepwise disassembly and apparent nonstepwise reassembly for the oligomeric RbsD protein." Protein Sci 15:1441-1448. Pubmed: 16731978
  • Hayashi, K., Morooka, N., Yamamoto, Y., Fujita, K., Isono, K., Choi, S., Ohtsubo, E., Baba, T., Wanner, B. L., Mori, H., Horiuchi, T. (2006). "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Mol Syst Biol 2:2006.0007. Pubmed: 16738553
  • Kim, M. S., Oh, H., Park, C., Oh, B. H. (2001). "Crystallization and preliminary X-ray crystallographic analysis of Escherichia coli RbsD, a component of the ribose-transport system with unknown biochemical function." Acta Crystallogr D Biol Crystallogr 57:728-730. Pubmed: 11320319
  • Kim, M. S., Shin, J., Lee, W., Lee, H. S., Oh, B. H. (2003). "Crystal structures of RbsD leading to the identification of cytoplasmic sugar-binding proteins with a novel folding architecture." J Biol Chem 278:28173-28180. Pubmed: 12738765
  • Ryu, K. S., Kim, C., Kim, I., Yoo, S., Choi, B. S., Park, C. (2004). "NMR application probes a novel and ubiquitous family of enzymes that alter monosaccharide configuration." J Biol Chem 279:25544-25548. Pubmed: 15060078
  • Schleyer, M., Bakker, E. P. (1993). "Nucleotide sequence and 3'-end deletion studies indicate that the K(+)-uptake protein kup from Escherichia coli is composed of a hydrophobic core linked to a large and partially essential hydrophilic C terminus." J Bacteriol 175:6925-6931. Pubmed: 8226635