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MetaCyc Enzyme: fructose-1,6-bisphosphatase

Gene: yggF Accession Numbers: EG11245 (MetaCyc), b2930, ECK2926

Synonyms: yggK

Species: Escherichia coli K-12 substr. MG1655

Subunit composition of fructose-1,6-bisphosphatase = [YggF]2
         fructose-1,6-bisphosphatase = YggF

Summary:
YggF is a type II fructose-1,6-bisphosphatase and shows 58% sequence identity to GlpX [Brown09].

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 [Shimada11a]. Genomic SELEX screening is described in [Gold95].

Locations: cytosol

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

Relationship Links: InterPro:IN-FAMILY:IPR004464, Pfam:IN-FAMILY:PF03320

Gene-Reaction Schematic

Gene-Reaction Schematic


GO Terms:
Biological Process:
Inferred from experimentInferred by computational analysisGO:0016311 - dephosphorylation [GOA01a, GOA01, Brown09]
Inferred by computational analysisGO:0005975 - carbohydrate metabolic process [UniProtGOA11]
Inferred by computational analysisGO:0006071 - glycerol metabolic process [GOA01]
Inferred by computational analysisGO:0006094 - gluconeogenesis [GOA01]
Molecular Function:
Inferred from experimentGO:0030145 - manganese ion binding [Brown09]
Inferred from experimentInferred by computational analysisGO:0042132 - fructose 1,6-bisphosphate 1-phosphatase activity [GOA01a, GOA01, Brown09]
Inferred from experimentGO:0042803 - protein homodimerization activity [Brown09]
Inferred by computational analysisGO:0016787 - hydrolase activity [UniProtGOA11]
Inferred by computational analysisGO:0046872 - metal ion binding [UniProtGOA11]
Cellular Component:
Inferred by computational analysisGO:0005829 - cytosol [DiazMejia09]

MultiFun Terms: metabolismcentral intermediary metabolism

Credits:
Created in EcoCyc 13-Mar-2009 by Keseler I, SRI International
Imported from EcoCyc 30-Sep-2015 by Paley S, SRI International


Enzymatic reaction of: fructose-1,6-bisphosphatase

Inferred from experiment

EC Number: 3.1.3.11

fructose 1,6-bisphosphate + H2O → β-D-fructofuranose 6-phosphate + phosphate

The direction shown, i.e. which substrates are on the left and right sides, 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, glycolysis II (from fructose 6-phosphate), glycolysis I (from glucose 6-phosphate), gluconeogenesis I

Credits:
Imported from EcoCyc 30-Sep-2015 by Paley S, SRI International

Summary:
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].

Cofactors or Prosthetic Groups: Mn2+ [Brown09]

Activators (Unknown Mechanism): L-dithiothreitol [Brown09] Inhibitors (Unknown Mechanism): ATP [Brown09], potassium chloride [Brown09], Li+ [Brown09], phosphate [Brown09]Kinetic Parameters:
Substrate Km (μM) kcat (sec-1) kcat/Km (sec-1 μM-1) Citations
fructose 1,6-bisphosphate 100.0 2.5 0.025 [Brown09, BRENDA14]

pH(opt): 7.5-8 [Brown09]


Sequence Features

Feature Class Location Citations Comment
Metal-Binding-Site 32
Inferred by computational analysis[UniProt15]
UniProt: Manganese 1.
Metal-Binding-Site 56
Inferred by computational analysis[UniProt15]
UniProt: Manganese 1.
Metal-Binding-Site 84
Inferred by computational analysis[UniProt15]
UniProt: Manganese 2.
Metal-Binding-Site 87
Inferred by computational analysis[UniProt15]
UniProt: Manganese 2.
Protein-Segment 87 -> 89
Inferred by computational analysis[UniProt15]
UniProt: Substrate binding; Sequence Annotation Type: region of interest.
Amino-Acid-Sites-That-Bind 118
Inferred by computational analysis[UniProt15]
UniProt: Substrate.
Protein-Segment 163 -> 165
Inferred by computational analysis[UniProt15]
UniProt: Substrate binding; Sequence Annotation Type: region of interest.
Sequence-Conflict 182 -> 186
Inferred by curator[Alefounder89, UniProt15]
UniProt: (in Ref. 3; CAA32600).
Protein-Segment 185 -> 187
Inferred by computational analysis[UniProt15]
UniProt: Substrate binding; Sequence Annotation Type: region of interest.
Amino-Acid-Sites-That-Bind 209
Inferred by computational analysis[UniProt15]
UniProt: Substrate; via amide nitrogen.
Metal-Binding-Site 212
Inferred by computational analysis[UniProt15]
UniProt: Manganese 2.

History:
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.


References

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

BRENDA14: BRENDA team (2014). Imported from BRENDA version existing on Aug 2014.

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

GOA01: GOA, DDB, FB, MGI, ZFIN (2001). "Gene Ontology annotation through association of InterPro records with GO terms."

GOA01a: GOA, MGI (2001). "Gene Ontology annotation based on Enzyme Commission mapping." Genomics 74;121-128.

Gold95: Gold L, Polisky B, Uhlenbeck O, Yarus M (1995). "Diversity of oligonucleotide functions." Annu Rev Biochem 64;763-97. PMID: 7574500

Serres01: Serres MH, Gopal S, Nahum LA, Liang P, Gaasterland T, Riley M (2001). "A functional update of the Escherichia coli K-12 genome." Genome Biol 2(9);RESEARCH0035. PMID: 11574054

Shimada11a: 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

UniProt15: UniProt Consortium (2015). "UniProt version 2015-08 released on 2015-07-22." Database.

UniProtGOA11: UniProt-GOA (2011). "Gene Ontology annotation based on manual assignment of UniProtKB keywords in UniProtKB/Swiss-Prot entries."


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
Page generated by Pathway Tools version 19.5 (software by SRI International) on Wed Feb 10, 2016, biocyc13.