Accession | TIGR02477 |
Name | PFKA_PPi |
Function | diphosphate--fructose-6-phosphate 1-phosphotransferase |
Trusted Cutoff | 587.95 |
Domain Trusted Cutoff | 587.95 |
Noise Cutoff | 197.90 |
Domain Noise Cutoff | 197.90 |
Isology Type | equivalog |
EC Number | 2.7.1.90 |
HMM Length | 539 |
Mainrole Category | Energy metabolism |
Subrole Category | Glycolysis/gluconeogenesis |
Gene Ontology Term | GO:0006096: glycolysis biological_process |
| GO:0047334: diphosphate-fructose-6-phosphate 1-phosphotransferase activity molecular_function |
Author | Rosovitz MJ, Haft DH |
Entry Date | Feb 18 2005 3:48PM |
Last Modified | Feb 14 2011 3:27PM |
Comment | Diphosphate--fructose-6-phosphate 1-phosphotransferase catalyzes the addition of phosphate from diphosphate (PPi) to fructose 6-phosphate to give fructose 1,6-bisphosphate (EC 2.7.1.90). The enzyme is also known as pyrophosphate-dependent phosphofructokinase. The usage of PPi-dependent enzymes in glycolysis presumably frees up ATP for other processes [1]. TIGR02482 represents the ATP-dependent 6-phosphofructokinase enzyme contained within Pfam PF00365: Phosphofructokinase. This model hits primarily bacterial, plant alpha, and plant beta sequences. |
References | RN [1]
RM 12015149
RT The structure of a pyrophosphate-dependent phosphofructokinase from the Lyme disease spirochete Borrelia burgdorferi.
RA Moore SA, Ronimus RS, Roberson RS, Morgan HW.
RL Structure (Camb). 2002 May;10(5):659-71.
RN [2]
RM 11382227
RT Sequencing, high-level expression and phylogeny of the pyrophosphate-dependent phosphofructokinase from the thermophilic spirochete Spirochaeta thermophila.
RA Ronimus R, de Heus E, Ruckert A, Morgan H.
RL Arch Microbiol. 2001 Apr;175(4):308-12. |