HMM Summary Page: TIGR02477

AccessionTIGR02477
NamePFKA_PPi
Functiondiphosphate--fructose-6-phosphate 1-phosphotransferase
Trusted Cutoff587.95
Domain Trusted Cutoff587.95
Noise Cutoff197.90
Domain Noise Cutoff197.90
Isology Typeequivalog
EC Number2.7.1.90
HMM Length539
Mainrole CategoryEnergy metabolism
Subrole CategoryGlycolysis/gluconeogenesis
Gene Ontology TermGO:0006096: glycolysis biological_process
GO:0047334: diphosphate-fructose-6-phosphate 1-phosphotransferase activity molecular_function
AuthorRosovitz MJ, Haft DH
Entry DateFeb 18 2005 3:48PM
Last ModifiedFeb 14 2011 3:27PM
CommentDiphosphate--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.
ReferencesRN [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.