| Accession | TIGR01546 |
| Name | GAPDH-II_archae |
| Function | glyceraldehyde-3-phosphate dehydrogenase, type II |
| Trusted Cutoff | 232.90 |
| Domain Trusted Cutoff | 232.90 |
| Noise Cutoff | 56.25 |
| Domain Noise Cutoff | 56.25 |
| Isology Type | equivalog |
| EC Number | 1.2.1.59 |
| HMM Length | 333 |
| Author | Selengut J |
| Entry Date | Jun 12 2002 11:36AM |
| Last Modified | Feb 14 2011 3:27PM |
| Comment | This HMM describes the type II glyceraldehyde-3-phosphate dehydrogenases which are limited to archaea. These enzymes catalyze the interconversion of 1,3-diphosphoglycerate and glyceraldehyde-3-phosphate, a central step in glycolysis and gluconeogenesis. In archaea, either NAD or NADP may be utilized as the cofactor.
The class I GAPDH's from bacteria and eukaryotes are covered by TIGR01534.
All of the members of the seed are characterized. See, for instance [1]. This model is very solid, there are no species falling between trusted and noise at this time. The closest relatives scoring in the noise are the class I GAPDH's. |
| References | RN [1]
RM PMID: 2165475
RT Glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic archaebacterium Pyrococcus woesei: characterization of the enzyme, cloning and sequencing of the gene, and expression in Escherichia coli.
RA Zwickl P, Fabry S, Bogedain C, Haas A, Hensel R.
RL J Bacteriol 1990 Aug;172(8):4329-38.
DR HAMAP; MF_00559; 43 of 43 |
| Genome Property | GenProp0691: glycolysis (HMM) |
