3,4-dihydroxy-2-butanone 4-phosphate synthase (P0A7J0)

Identification
Name:3,4-dihydroxy-2-butanone 4-phosphate synthase
Synonyms:
  • DHBP synthase
Gene Name:ribB
Enzyme Class:
Biological Properties
General Function:Involved in 3,4-dihydroxy-2-butanone-4-phosphate synthase activity
Specific Function:Catalyzes the conversion of D-ribulose 5-phosphate to formate and 3,4-dihydroxy-2-butanone 4-phosphate
Cellular Location:Cell membrane; Peripheral membrane protein (Potential)
SMPDB Pathways:
KEGG Pathways:
KEGG Reactions:
1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb
1.0D-Ribulose 5-phosphate ↔ 1.03,4-Dihydroxy-2-butanone-4-P + 1.0Formic acid + 1.0Hydrogen ion
ReactionCard
1.0D-Ribulose 5-phosphate ↔ 1.0Thumb+1.0Thumb
1.0D-Ribulose 5-phosphate ↔ 1.03,4-Dihydroxy-2-butanone-4-P + 1.0Formic acid
ReactionCard
EcoCyc Reactions:
1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb
1.0D-Ribulose 5-phosphate ↔ 1.03,4-Dihydroxy-2-butanone-4-P + 1.0Formic acid + 1.0Hydrogen ion
ReactionCard
Complex Reactions:
1.0Thumb → 1.0Thumb+1.0Thumb
1.0D-Ribulose 5-phosphate → 1.0Formic acid + 1.01-Deoxy-L-glycero-tetrulose 4-phosphate
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB231221-Deoxy-L-glycero-tetrulose 4-phosphateMetaboCard
ECMDB040603,4-Dihydroxy-2-butanone-4-PMetaboCard
ECMDB04148D-Ribulose 5-phosphateMetaboCard
ECMDB00142Formic acidMetaboCard
ECMDB21225Hydrogen ionMetaboCard
GO Classification:
Function
3,4-dihydroxy-2-butanone-4-phosphate synthase activity
carbon-carbon lyase activity
catalytic activity
lyase activity
Process
metabolic process
nitrogen compound metabolic process
riboflavin biosynthetic process
riboflavin metabolic process
Gene Properties
Blattner:b3041
Gene OrientationCounterclockwise
Centisome Percentage:68.58
Left Sequence End3181835
Right Sequence End3182488
Gene Sequence:
>654 bp
ATGAGTAAGTCGAAAATGATTGTGCGCACCAAATTTATTGATCGCGCCTGTCACTGGACC
GTGGTGATTTGCTTCTTCCTGGTGGCGCTGTCCGGGATTTCGTTCTTCTTCCCGACGCTG
CAATGGCTGACGCAAACCTTCGGTACGCCGCAGATGGGACGCATTTTGCACCCGTTCTTC
GGCATTGCGATTTTCGTCGCACTGATGTTTATGTTTGTGCGTTTTGTGCATCACAACATC
CCGGATAAGAAAGATATTCCGTGGCTGTTGAACATTGTCGAAGTATTGAAAGGCAATGAG
CATAAAGTGGCGGATGTCGGTAAGTACAACGCCGGGCAAAAGATGATGTTCTGGTCGATC
ATGAGCATGATTTTCGTGCTGCTGGTGACCGGGGTGATTATCTGGCGTCCGTACTTTGCG
CAGTACTTCCCGATGCAGGTTGTTCGCTACAGCCTGCTGATCCACGCGGCTGCGGGTATC
ATCCTGATCCACGCCATCCTGATCCATATGTATATGGCATTTTGGGTGAAAGGATCGATT
AAAGGGATGATCGAAGGGAAGGTAAGTCGTCGCTGGGCGAAGAAACACCATCCGCGCTGG
TATCGTGAAATCGAGAAGGCAGAAGCGAAAAAAGAGAGTGAAGAAGGGATATAA
Protein Properties
Pfam Domain Function:
Protein Residues:217
Protein Molecular Weight:23353
Protein Theoretical pI:5
PDB File:1IEZ
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>3,4-dihydroxy-2-butanone 4-phosphate synthase
MNQTLLSSFGTPFERVENALAALREGRGVMVLDDEDRENEGDMIFPAETMTVEQMALTIR
HGSGIVCLCITEDRRKQLDLPMMVENNTSAYGTGFTVTIEAAEGVTTGVSAADRITTVRA
AIADGAKPSDLNRPGHVFPLRAQAGGVLTRGGHTEATIDLMTLAGFKPAGVLCELTNDDG
TMARAPECIEFANKHNMALVTIEDLVAYRQAHERKAS
References
External Links:
ResourceLink
Uniprot ID:P0A7J0
Uniprot Name:RIBB_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:1742409
PDB ID:1IEZ
Ecogene ID:EG10465
Ecocyc:EG10465
ColiBase:b3041
Kegg Gene:b3041
EchoBASE ID:EB0460
CCDB:RIBB_ECOLI
BacMap:16130937
General Reference:
  • 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
  • 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
  • Kelly, M. J., Ball, L. J., Krieger, C., Yu, Y., Fischer, M., Schiffmann, S., Schmieder, P., Kuhne, R., Bermel, W., Bacher, A., Richter, G., Oschkinat, H. (2001). "The NMR structure of the 47-kDa dimeric enzyme 3,4-dihydroxy-2-butanone-4-phosphate synthase and ligand binding studies reveal the location of the active site." Proc Natl Acad Sci U S A 98:13025-13030. Pubmed: 11687623
  • Liao, D. I., Calabrese, J. C., Wawrzak, Z., Viitanen, P. V., Jordan, D. B. (2001). "Crystal structure of 3,4-dihydroxy-2-butanone 4-phosphate synthase of riboflavin biosynthesis." Structure 9:11-18. Pubmed: 11342130
  • Raina, S., Mabey, L., Georgopoulos, C. (1991). "The Escherichia coli htrP gene product is essential for bacterial growth at high temperatures: mapping, cloning, sequencing, and transcriptional regulation of htrP." J Bacteriol 173:5999-6008. Pubmed: 1917833
  • Richter, G., Volk, R., Krieger, C., Lahm, H. W., Rothlisberger, U., Bacher, A. (1992). "Biosynthesis of riboflavin: cloning, sequencing, and expression of the gene coding for 3,4-dihydroxy-2-butanone 4-phosphate synthase of Escherichia coli." J Bacteriol 174:4050-4056. Pubmed: 1597419
  • Yang, T. P., Depew, R. E. (1992). "Nucleotide sequence of a region duplicated in Escherichia coli toc mutants." Biochim Biophys Acta 1130:227-228. Pubmed: 1314093