Accession | TIGR00330 |
Name | glpX |
Function | fructose-1,6-bisphosphatase, class II |
Gene Symbol | glpX |
Trusted Cutoff | 259.30 |
Domain Trusted Cutoff | 259.30 |
Noise Cutoff | 213.35 |
Domain Noise Cutoff | 213.35 |
Isology Type | equivalog |
EC Number | 3.1.3.11 |
HMM Length | 334 |
Mainrole Category | Energy metabolism |
Subrole Category | Pentose phosphate pathway |
Gene Ontology Term | GO:0006094: gluconeogenesis biological_process |
| GO:0042132: fructose 1,6-bisphosphate 1-phosphatase activity molecular_function |
Author | Haft DH, Loftus BJ |
Entry Date | Apr 20 1999 2:07PM |
Last Modified | Feb 14 2011 3:27PM |
Comment | This model represents GlpX, one of three classes of bacterial fructose-1,6-bisphosphatases. This form is homodimeric and Mn2+-dependent, and only very distantly related to the class I fructose-1,6-bisphosphatase, the product of the fbp gene, which is homotetrameric and Mg2+-dependent. A third class is found as one of two types in Bacillus subtilis.
In E. coli, GlpX is found in the glpFKX operon together with a glycerol update protein and glycerol kinase. |
References | DR ECOGENE; EG11517; glpX;
RM 10986273
RT Purification and characterization of glpX-encoded fructose 1, 6-bisphosphatase, a new enzyme of the glycerol 3-phosphate regulon of Escherichia coli.
RA Donahue JL, Bownas JL, Niehaus WG, Larson TJ.
RL J Bacteriol 2000 Oct;182(19):5624-7
SE TIGR
GA hmmls
DR EXPERIMENTAL; OMNI|NTL01EC03831; Escherichia coli
DR EXPERIMENTAL; GP|1753218; Synechocystis sp. PCC 6803 |
Genome Property | GenProp0120: pentose phosphate cycle (HMM) |