PROSITE documentation PDOC00894Glucosamine/galactosamine-6-phosphate isomerases signature
Glucosamine-6-phosphate isomerase (EC 3.5.99.6) (or Glc-6-P deaminase) is the enzyme responsible for the conversion of glucosamine 6-phosphate into fructose 6 phosphate [1]. It is the last specific step in the pathway for N-acetylglucosamine (GlcNAC) utilization in bacteria such as Escherichia coli (gene nagB) or in fungi such as Candida albicans (gene NAG1).
Glc-6-P isomerase is evolutionary related to:
- A putative Escherichia coli galactosamine-6-phosphate isomerase (gene agaI) [2].
- Escherichia coli hypothetical protein yieK.
- Bacillus subtilis hypothetical protein ybfT.
As a signature pattern we selected a conserved region located in the central part of these enzymes. This region contains a conserved histidine which has been shown [1], in nagB, to be important for the pyranose ring-opening step of the catalytic mechanism.
Last update:December 2004 / Pattern and text revised.
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PROSITE method (with tools and information) covered by this documentation:
| 1 | Authors | Oliva G. Fontes M.R.M. Garratt R.C. Altamirano M.M. Calcagno M.L. Horjales E. |
| Title | Structure and catalytic mechanism of glucosamine 6-phosphate deaminase from Escherichia coli at 2.1 A resolution. | |
| Source | Structure 3:1323-1332(1995). | |
| PubMed ID | 8747459 |
| 2 | Authors | Reizer J. Ramseier T.M. Reizer A. Charbit A. Saier M.H. Jr. |
| Title | Novel phosphotransferase genes revealed by bacterial genome sequencing: a gene cluster encoding a putative N-acetylgalactosamine metabolic pathway in Escherichia coli. | |
| Source | Microbiology 142:231-250(1996). | |
| PubMed ID | 8932697 |
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