Fructose-bisphosphate aldolase class 2 (P0AB71)

Identification
Name:Fructose-bisphosphate aldolase class 2
Synonyms:
  • FBP aldolase
  • FBPA
  • Fructose-1,6-bisphosphate aldolase
  • Fructose-bisphosphate aldolase class II
Gene Name:fbaA
Enzyme Class:
Biological Properties
General Function:Involved in catalytic activity
Specific Function:Catalyzes the aldol condensation of dihydroxyacetone phosphate (DHAP or glycerone-phosphate) with glyceraldehyde 3- phosphate (G3P) to form fructose 1,6-bisphosphate (FBP) in gluconeogenesis and the reverse reaction in glycolysis
Cellular Location:Not Available
SMPDB Pathways:
KEGG Pathways:
KEGG Reactions:
1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0Fructose 1,6-bisphosphate ↔ 1.0Dihydroxyacetone phosphate + 1.0D-Glyceraldehyde 3-phosphate
ReactionCard
1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0Sedoheptulose 1,7-bisphosphate ↔ 1.0Dihydroxyacetone phosphate + 1.0D-Erythrose 4-phosphate
ReactionCard
1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0beta-D-Fructose 1,6-bisphosphate ↔ 1.0Dihydroxyacetone phosphate + 1.0D-Glyceraldehyde 3-phosphate
ReactionCard
1.0Thumb ↔ 1.0Thumb+1.0D-Glyceraldehyde
1.0Fructose 1-phosphate ↔ 1.0Dihydroxyacetone phosphate + 1.0D-Glyceraldehyde
ReactionCard
SMPDB Reactions:
1.0Fructose 1,6-bisphosphate+1.0Thumb ↔ 1.0D-Glyceraldehyde 3-phosphate+1.0Thumb+1.0Thumb
1.0Fructose 1,6-bisphosphate + 1.0Fructose 1,6-bisphosphate ↔ 1.0D-Glyceraldehyde 3-phosphate + 1.0Dihydroxyacetone phosphate + 1.0D-Glyceraldehyde 3-phosphate
ReactionCard
1.0D-Glyceraldehyde 3-phosphate+1.0Thumb+1.0Thumb → 1.0Fructose 1,6-bisphosphate+1.0Thumb
1.0D-Glyceraldehyde 3-phosphate + 1.0Dihydroxyacetone phosphate + 1.0D-Glyceraldehyde 3-phosphate → 1.0Fructose 1,6-bisphosphate + 1.0Fructose 1,6-bisphosphate
ReactionCard
1.0Fructose 1,6-bisphosphate+1.0Thumb → 1.0Thumb+1.0D-Glyceraldehyde 3-phosphate+1.0Thumb
1.0Fructose 1,6-bisphosphate + 1.0Fructose 1,6-bisphosphate → 1.0Dihydroxyacetone phosphate + 1.0D-Glyceraldehyde 3-phosphate + 1.0D-Glyceraldehyde 3-phosphate
ReactionCard
1.0Sedoheptulose 1,7-bisphosphate → 1.0Thumb+1.0Glycerone phosphate
1.0Sedoheptulose 1,7-bisphosphate → 1.0D-Erythrose 4-phosphate + 1.0Glycerone phosphate
ReactionCard
EcoCyc Reactions:
1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0Fructose 1,6-bisphosphate ↔ 1.0Dihydroxyacetone phosphate + 1.0D-Glyceraldehyde 3-phosphate
ReactionCard
1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0Sedoheptulose 1,7-bisphosphate ↔ 1.0Dihydroxyacetone phosphate + 1.0D-Erythrose 4-phosphate
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB20123beta-D-Fructose 1,6-bisphosphateMetaboCard
ECMDB02649D-Erythrose 4-phosphateMetaboCard
ECMDB01051D-GlyceraldehydeMetaboCard
ECMDB01112D-Glyceraldehyde 3-phosphateMetaboCard
ECMDB01473Dihydroxyacetone phosphateMetaboCard
ECMDB01058Fructose 1,6-bisphosphateMetaboCard
ECMDB01076Fructose 1-phosphateMetaboCard
ECMDB20192Sedoheptulose 1,7-bisphosphateMetaboCard
GO Classification:
Function
aldehyde-lyase activity
binding
carbon-carbon lyase activity
catalytic activity
cation binding
fructose-bisphosphate aldolase activity
ion binding
lyase activity
metal ion binding
transition metal ion binding
zinc ion binding
Process
alcohol metabolic process
glucose catabolic process
glucose metabolic process
glycolysis
hexose metabolic process
metabolic process
monosaccharide metabolic process
small molecule metabolic process
Gene Properties
Blattner:b2925
Gene OrientationCounterclockwise
Centisome Percentage:66.13
Left Sequence End3068187
Right Sequence End3069266
Gene Sequence:
>1080 bp
ATGTCTAAGATTTTTGATTTCGTAAAACCTGGCGTAATCACTGGTGATGACGTACAGAAA
GTTTTCCAGGTAGCAAAAGAAAACAACTTCGCACTGCCAGCAGTAAACTGCGTCGGTACT
GACTCCATCAACGCCGTACTGGAAACCGCTGCTAAAGTTAAAGCGCCGGTTATCGTTCAG
TTCTCCAACGGTGGTGCTTCCTTTATCGCTGGTAAAGGCGTGAAATCTGACGTTCCGCAG
GGTGCTGCTATCCTGGGCGCGATCTCTGGTGCGCATCACGTTCACCAGATGGCTGAACAT
TATGGTGTTCCGGTTATCCTGCACACTGACCACTGCGCGAAGAAACTGCTGCCGTGGATC
GACGGTCTGTTGGACGCGGGTGAAAAACACTTCGCAGCTACCGGTAAGCCGCTGTTCTCT
TCTCACATGATCGACCTGTCTGAAGAATCTCTGCAAGAGAACATCGAAATCTGCTCTAAA
TACCTGGAGCGCATGTCCAAAATCGGCATGACTCTGGAAATCGAACTGGGTTGCACCGGT
GGTGAAGAAGACGGCGTGGACAACAGCCACATGGACGCTTCTGCACTGTACACCCAGCCG
GAAGACGTTGATTACGCATACACCGAACTGAGCAAAATCAGCCCGCGTTTCACCATCGCA
GCGTCCTTCGGTAACGTACACGGTGTTTACAAGCCGGGTAACGTGGTTCTGACTCCGACC
ATCCTGCGTGATTCTCAGGAATATGTTTCCAAGAAACACAACCTGCCGCACAACAGCCTG
AACTTCGTATTCCACGGTGGTTCCGGTTCTACTGCTCAGGAAATCAAAGACTCCGTAAGC
TACGGCGTAGTAAAAATGAACATCGATACCGATACCCAATGGGCAACCTGGGAAGGCGTT
CTGAACTACTACAAAGCGAACGAAGCTTATCTGCAGGGTCAGCTGGGTAACCCGAAAGGC
GAAGATCAGCCGAACAAGAAATACTACGATCCGCGCGTATGGCTGCGTGCCGGTCAGACT
TCGATGATCGCTCGTCTGGAGAAAGCATTCCAGGAACTGAACGCGATCGACGTTCTGTAA
Protein Properties
Pfam Domain Function:
Protein Residues:359
Protein Molecular Weight:39147
Protein Theoretical pI:6
PDB File:1GYN
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Fructose-bisphosphate aldolase class 2
MSKIFDFVKPGVITGDDVQKVFQVAKENNFALPAVNCVGTDSINAVLETAAKVKAPVIVQ
FSNGGASFIAGKGVKSDVPQGAAILGAISGAHHVHQMAEHYGVPVILHTDHCAKKLLPWI
DGLLDAGEKHFAATGKPLFSSHMIDLSEESLQENIEICSKYLERMSKIGMTLEIELGCTG
GEEDGVDNSHMDASALYTQPEDVDYAYTELSKISPRFTIAASFGNVHGVYKPGNVVLTPT
ILRDSQEYVSKKHNLPHNSLNFVFHGGSGSTAQEIKDSVSYGVVKMNIDTDTQWATWEGV
LNYYKANEAYLQGQLGNPKGEDQPNKKYYDPRVWLRAGQTSMIARLEKAFQELNAIDVL
References
External Links:
ResourceLink
Uniprot ID:P0AB71
Uniprot Name:ALF_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85675736
PDB ID:1GYN
Ecogene ID:EG10282
Ecocyc:EG10282
ColiBase:b2925
Kegg Gene:b2925
EchoBASE ID:EB0278
CCDB:ALF_ECOLI
BacMap:16130826
General Reference:
  • Alefounder, P. R., Baldwin, S. A., Perham, R. N., Short, N. J. (1989). "Cloning, sequence analysis and over-expression of the gene for the class II fructose 1,6-bisphosphate aldolase of Escherichia coli." Biochem J 257:529-534. Pubmed: 2649077
  • Alefounder, P. R., Perham, R. N. (1989). "Identification, molecular cloning and sequence analysis of a gene cluster encoding the class II fructose 1,6-bisphosphate aldolase, 3-phosphoglycerate kinase and a putative second glyceraldehyde 3-phosphate dehydrogenase of Escherichia coli." Mol Microbiol 3:723-732. Pubmed: 2546007
  • Berry, A., Marshall, K. E. (1993). "Identification of zinc-binding ligands in the class II fructose-1,6-bisphosphate aldolase of Escherichia coli." FEBS Lett 318:11-16. Pubmed: 8436219
  • 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
  • Blom, N. S., Tetreault, S., Coulombe, R., Sygusch, J. (1996). "Novel active site in Escherichia coli fructose 1,6-bisphosphate aldolase." Nat Struct Biol 3:856-862. Pubmed: 8836102
  • Cooper, S. J., Leonard, G. A., McSweeney, S. M., Thompson, A. W., Naismith, J. H., Qamar, S., Plater, A., Berry, A., Hunter, W. N. (1996). "The crystal structure of a class II fructose-1,6-bisphosphate aldolase shows a novel binuclear metal-binding active site embedded in a familiar fold." Structure 4:1303-1315. Pubmed: 8939754
  • Hall, D. R., Kemp, L. E., Leonard, G. A., Marshall, K., Berry, A., Hunter, W. N. (2003). "The organization of divalent cations in the active site of cadmium Escherichia coli fructose-1,6-bisphosphate aldolase." Acta Crystallogr D Biol Crystallogr 59:611-614. Pubmed: 12595741
  • Hall, D. R., Leonard, G. A., Reed, C. D., Watt, C. I., Berry, A., Hunter, W. N. (1999). "The crystal structure of Escherichia coli class II fructose-1, 6-bisphosphate aldolase in complex with phosphoglycolohydroxamate reveals details of mechanism and specificity." J Mol Biol 287:383-394. Pubmed: 10080900
  • 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
  • Link, A. J., Robison, K., Church, G. M. (1997). "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12." Electrophoresis 18:1259-1313. Pubmed: 9298646
  • Wilkins, M. R., Gasteiger, E., Tonella, L., Ou, K., Tyler, M., Sanchez, J. C., Gooley, A. A., Walsh, B. J., Bairoch, A., Appel, R. D., Williams, K. L., Hochstrasser, D. F. (1998). "Protein identification with N and C-terminal sequence tags in proteome projects." J Mol Biol 278:599-608. Pubmed: 9600841
  • Zgiby, S. M., Thomson, G. J., Qamar, S., Berry, A. (2000). "Exploring substrate binding and discrimination in fructose1, 6-bisphosphate and tagatose 1,6-bisphosphate aldolases." Eur J Biochem 267:1858-1868. Pubmed: 10712619
  • Zhang, J., Sprung, R., Pei, J., Tan, X., Kim, S., Zhu, H., Liu, C. F., Grishin, N. V., Zhao, Y. (2009). "Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli." Mol Cell Proteomics 8:215-225. Pubmed: 18723842