Fructose-1,6-bisphosphatase class 1 (P0A993)

Identification
Name:Fructose-1,6-bisphosphatase class 1
Synonyms:
  • FBPase class 1
  • D-fructose-1,6-bisphosphate 1-phosphohydrolase class 1
Gene Name:fbp
Enzyme Class:
Biological Properties
General Function:Involved in phosphoric ester hydrolase activity
Specific Function:D-fructose 1,6-bisphosphate + H(2)O = D- fructose 6-phosphate + phosphate
Cellular Location:Cytoplasm (Potential)
SMPDB Pathways:
  • Gluconeogenesis from L-malic acid PW000819
  • glycerol metabolism PW000914
  • glycerol metabolism II PW000915
  • glycerol metabolism III (sn-glycero-3-phosphoethanolamine) PW000916
  • glycerol metabolism IV (glycerophosphoglycerol) PW000917
  • glycerol metabolism V (glycerophosphoserine) PW000918
  • glycolysis and pyruvate dehydrogenase PW000785
KEGG Pathways:
KEGG Reactions:
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0Fructose 1,6-bisphosphate + 1.0Water ↔ 1.0Fructose 6-phosphate + 1.0Phosphate
ReactionCard
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0beta-D-Fructose 1,6-bisphosphate + 1.0Water ↔ 1.0beta-D-Fructose 6-phosphate + 1.0Phosphate
ReactionCard
SMPDB Reactions:
1.0Fructose 6-phosphate+1.0Thumb+1.0Thumb → 1.0Fructose 1,6-bisphosphate+1.0Thumb+1.0Thumb
1.0Fructose 6-phosphate + 1.0Phosphate + 1.0Fructose 6-phosphate → 1.0Fructose 1,6-bisphosphate + 1.0Water + 1.0Fructose 1,6-bisphosphate
ReactionCard
1.0Fructose 1,6-bisphosphate+1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb
1.0Fructose 1,6-bisphosphate + 1.0Water + 1.0Fructose 1,6-bisphosphate → 1.0Phosphate + 1.0D-tagatofuranose 6-phosphate
ReactionCard
EcoCyc Reactions:
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0Fructose 1,6-bisphosphate + 1.0Water ↔ 1.0Fructose 6-phosphate + 1.0Phosphate
ReactionCard
Complex Reactions:
1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb
1.0Fructose 1,6-bisphosphate + 1.0Water → 1.0Fructose 6-phosphate + 1.0Inorganic phosphate
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB20123beta-D-Fructose 1,6-bisphosphateMetaboCard
ECMDB03971beta-D-Fructose 6-phosphateMetaboCard
ECMDB24205D-tagatofuranose 6-phosphateMetaboCard
ECMDB01058Fructose 1,6-bisphosphateMetaboCard
ECMDB00124Fructose 6-phosphateMetaboCard
ECMDB21380Inorganic phosphateMetaboCard
ECMDB01429PhosphateMetaboCard
ECMDB00494WaterMetaboCard
GO Classification:
Function
catalytic activity
hydrolase activity
hydrolase activity, acting on ester bonds
phosphoric ester hydrolase activity
Process
carbohydrate metabolic process
metabolic process
primary metabolic process
Gene Properties
Blattner:b4232
Gene OrientationCounterclockwise
Centisome Percentage:95.97
Left Sequence End4452634
Right Sequence End4453632
Gene Sequence:
>999 bp
ATGAAACTTTTTCGTATCCTCGATCCTTTCACCTTAACCCTGATCACGGTGGTGTTGCTG
GCCTCTTTCTTTCCGGCCAGAGGCGATTTCGTCCCCTTCTTTGAAAATCTGACCACCGCA
GCTATTGCCCTGCTGTTCTTTATGCACGGCGCGAAGTTGTCGCGTGAGGCGATTATTGCT
GGCGGTGGTCACTGGCGACTGCATTTGTGGGTAATGTGCAGCACCTTCGTGCTGTTTCCG
ATTCTGGGTGTACTGTTTGCCTGGTGGAAACCGGTAAATGTCGACCCGATGCTCTACTCC
GGTTTTCTCTACTTGTGCATTCTCCCGGCTACCGTGCAGTCTGCAATCGCCTTCACGTCA
ATGGCGGGCGGTAACGTCGCGGCAGCGGTTTGTTCTGCGTCGGCATCCAGCCTGCTGGGG
ATTTTCCTTTCACCATTGCTGGTTGGTCTGGTGATGAATGTTCACGGTGCAGGGGGCAGC
CTTGAGCAGGTCGGTAAAATTATGCTGCAACTGCTGCTGCCGTTTGTGTTGGGGCATCTT
TCCCGGCCGTGGATTGGTGACTGGGTGTCGCGCAATAAAAAATGGATTGCGAAAACTGAC
CAGACGTCCATTCTGTTGGTGGTTTATACAGCGTTCAGCGAAGCCGTCGTTAATGGTATC
TGGCATAAAGTTGGCTGGGGATCATTGCTGTTTATCGTGGTGGTCAGCTGCGTTCTTCTG
GCTATCGTGATTGTAGTTAACGTCTTTATGGCACGCCGACTGAGCTTCAATAAGGCAGAT
GAAATTACTATCGTCTTTTGTGGTTCGAAAAAGAGTCTGGCAAATGGCATCCCGATGGCA
AACATTCTGTTCCCCACATCGGTGATCGGTATGATGGTGCTGCCCCTGATGATTTTCCAT
CAGATCCAATTGATGGTCTGTGCGGTGCTGGCGCGTCGATACAAACGCCAGACCGAACAG
TTACAGGCGCAGCAGGAAAGCAGCGCCGATAAAGCTTAA
Protein Properties
Pfam Domain Function:
Protein Residues:332
Protein Molecular Weight:36834
Protein Theoretical pI:6
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Fructose-1,6-bisphosphatase class 1
MKTLGEFIVEKQHEFSHATGELTALLSAIKLGAKIIHRDINKAGLVDILGASGAENVQGE
VQQKLDLFANEKLKAALKARDIVAGIASEEEDEIVVFEGCEHAKYVVLMDPLDGSSNIDV
NVSVGTIFSIYRRVTPVGTPVTEEDFLQPGNKQVAAGYVVYGSSTMLVYTTGCGVHAFTY
DPSLGVFCLCQERMRFPEKGKTYSINEGNYIKFPNGVKKYIKFCQEEDKSTNRPYTSRYI
GSLVADFHRNLLKGGIYLYPSTASHPDGKLRLLYECNPMAFLAEQAGGKASDGKERILDI
IPETLHQRRSFFVGNDHMVEDVERFIREFPDA
References
External Links:
ResourceLink
Uniprot ID:P0A993
Uniprot Name:F16PA_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85675394
Ecogene ID:EG10283
Ecocyc:EG10283
ColiBase:b4232
Kegg Gene:b4232
EchoBASE ID:EB0279
CCDB:F16PA_ECOLI
BacMap:16132054
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
  • Burland, V., Plunkett, G. 3rd, Sofia, H. J., Daniels, D. L., Blattner, F. R. (1995). "Analysis of the Escherichia coli genome VI: DNA sequence of the region from 92.8 through 100 minutes." Nucleic Acids Res 23:2105-2119. Pubmed: 7610040
  • Hamilton, W. D., Harrison, D. A., Dyer, T. A. (1988). "Sequence of the Escherichia coli fructose-1,6-bisphosphatase gene." Nucleic Acids Res 16:8707. Pubmed: 2843822
  • 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
  • Hines, J. K., Chen, X., Nix, J. C., Fromm, H. J., Honzatko, R. B. (2007). "Structures of mammalian and bacterial fructose-1,6-bisphosphatase reveal the basis for synergism in AMP/fructose 2,6-bisphosphate inhibition." J Biol Chem 282:36121-36131. Pubmed: 17933867
  • Hines, J. K., Fromm, H. J., Honzatko, R. B. (2006). "Novel allosteric activation site in Escherichia coli fructose-1,6-bisphosphatase." J Biol Chem 281:18386-18393. Pubmed: 16670087
  • Hines, J. K., Fromm, H. J., Honzatko, R. B. (2007). "Structures of activated fructose-1,6-bisphosphatase from Escherichia coli. Coordinate regulation of bacterial metabolism and the conservation of the R-state." J Biol Chem 282:11696-11704. Pubmed: 17314096
  • Hines, J. K., Kruesel, C. E., Fromm, H. J., Honzatko, R. B. (2007). "Structure of inhibited fructose-1,6-bisphosphatase from Escherichia coli: distinct allosteric inhibition sites for AMP and glucose 6-phosphate and the characterization of a gluconeogenic switch." J Biol Chem 282:24697-24706. Pubmed: 17567577
  • Marcus, F., Gontero, B., Harrsch, P. B., Rittenhouse, J. (1986). "Amino acid sequence homology among fructose-1,6-bisphosphatases." Biochem Biophys Res Commun 135:374-381. Pubmed: 3008716