|Gene:||yggF||Accession Numbers: EG11245 (MetaCyc), b2930, ECK2926|
Species: Escherichia coli K-12 substr. MG1655
Genomic SELEX screening predicted a number of novel target genes, including yggF, to be under the control of transcriptional activator cAMP-CRP. The data suggested that CRP has a major role in control of the switch between glycolysis and gluconeogenesis [Shimada11]. Genomic SELEX screening is described in [Gold95].
|Map Position: [3,073,239 <- 3,074,204]|
Molecular Weight of Polypeptide: 34.323 kD (from nucleotide sequence)
Molecular Weight of Multimer: 76.0 kD (experimental) [Brown09]
Unification Links: ASAP:ABE-0009615 , EchoBASE:EB1226 , EcoGene:EG11245 , EcoliWiki:b2930 , ModBase:P21437 , OU-Microarray:b2930 , PortEco:yggF , Protein Model Portal:P21437 , RefSeq:NP_417405 , RegulonDB:EG11245 , SMR:P21437 , String:511145.b2930 , Swiss-Model:P21437 , UniProt:P21437
|Biological Process:||GO:0016311 - dephosphorylation
[GOA01, GOA01a, Brown09]
GO:0005975 - carbohydrate metabolic process [UniProtGOA11a]
GO:0006071 - glycerol metabolic process [GOA01a]
GO:0006094 - gluconeogenesis [GOA01a]
|Molecular Function:||GO:0030145 - manganese ion binding
GO:0042132 - fructose 1,6-bisphosphate 1-phosphatase activity [GOA01, GOA01a, Brown09]
GO:0042803 - protein homodimerization activity [Brown09]
GO:0016787 - hydrolase activity [UniProtGOA11a]
GO:0046872 - metal ion binding [UniProtGOA11a]
|Cellular Component:||GO:0005829 - cytosol [DiazMejia09]|
|MultiFun Terms:||metabolism → central intermediary metabolism|
Enzymatic reaction of: fructose-1,6-bisphosphatase
EC Number: 188.8.131.52
The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction in which it was curated.
The reaction is physiologically favored in the direction shown.
In Pathways: photosynthetic 3-hydroxybutanoate biosynthesis (engineered) , superpathway of hexitol degradation (bacteria) , superpathway of N-acetylneuraminate degradation , superpathway of glycolysis and Entner-Doudoroff , superpathway of glycolysis, pyruvate dehydrogenase, TCA, and glyoxylate bypass , gluconeogenesis I , glycolysis II (from fructose 6-phosphate) , glycolysis I (from glucose 6-phosphate)
Substrate binding shows positive cooperativity, with a Hill coefficient of ~2.0 [Brown09].
The enzyme had low activity toward glucose 1,6-bisphosphate. Non-substrates included ribulose 1,5-bisphosphate, fructose 2,6-bisphosphate, and fructose 1-phosphate. Of several divalent ions tested, only Mn2+ served as cofactor [Brown09].
Addition of 1 mM dithiothreitol increased the activity 40-50%, whereas 1 mM ATP reduced the activity by 40%. Addition of 1 mM AMP, ADP, PEP, and glycerol 3-phosphate had no significant effect on activity [Brown09].
pH(opt): 7.5-8 [Brown09]
|Protein-Segment||87 -> 89|
|Protein-Segment||163 -> 165|
|Sequence-Conflict||182 -> 186|
|Protein-Segment||185 -> 187|
Peter D. Karp on Thu Jan 16, 2003:
Predicted gene function revised as a result of E. coli genome reannotation by Serres et al. [Serres01 ].
10/20/97 Gene b2930 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG11245; confirmed by SwissProt match.
Alefounder89: Alefounder PR, Perham RN (1989). "Identification, molecular cloning and sequence analysis of a gene cluster encoding the class II fructose 1,6-bisphosphate aldolase, 3-phosphoglycerate kinase and a putative second glyceraldehyde 3-phosphate dehydrogenase of Escherichia coli." Mol Microbiol 3(6);723-32. PMID: 2546007
Brown09: Brown G, Singer A, Lunin VV, Proudfoot M, Skarina T, Flick R, Kochinyan S, Sanishvili R, Joachimiak A, Edwards AM, Savchenko A, Yakunin AF (2009). "Structural and biochemical characterization of the type II fructose-1,6-bisphosphatase GlpX from Escherichia coli." J Biol Chem 284(6);3784-92. PMID: 19073594
DiazMejia09: Diaz-Mejia JJ, Babu M, Emili A (2009). "Computational and experimental approaches to chart the Escherichia coli cell-envelope-associated proteome and interactome." FEMS Microbiol Rev 33(1);66-97. PMID: 19054114
Shimada11: Shimada T, Fujita N, Yamamoto K, Ishihama A (2011). "Novel roles of cAMP receptor protein (CRP) in regulation of transport and metabolism of carbon sources." PLoS One 6(6);e20081. PMID: 21673794
©2015 SRI International, 333 Ravenswood Avenue, Menlo Park, CA 94025-3493