Escherichia coli K-12 substr. MG1655 Enzyme: fructose-1-phosphatase

Gene: yqaB Accession Numbers: G7408 (EcoCyc), b2690, ECK2685

Regulation Summary Diagram: ?

Regulation summary diagram for yqaB

YqaB is a sugar phosphatase belonging to the superfamily of haloacid dehalogenase (HAD)-like hydrolases. In addition to its main fructose-1-phosphatase activity, YqaB has low β-phosphoglucomutase activity [Kuznetsova06]. The phosphatase activity of YqaB was first discovered in a high-throughput screen of purified proteins [Kuznetsova05].

Locations: cytosol

Map Position: [2,814,959 <- 2,815,525] (60.67 centisomes, 218°)
Length: 567 bp / 188 aa

Molecular Weight of Polypeptide: 20.78 kD (from nucleotide sequence)

Unification Links: ASAP:ABE-0008850 , DIP:DIP-12842N , EchoBASE:EB3301 , EcoGene:EG13530 , EcoliWiki:b2690 , Mint:MINT-1265616 , ModBase:P77475 , OU-Microarray:b2690 , PortEco:yqaB , Protein Model Portal:P77475 , RefSeq:NP_417175 , RegulonDB:G7408 , SMR:P77475 , String:511145.b2690 , UniProt:P77475

Relationship Links: InterPro:IN-FAMILY:IPR006439 , InterPro:IN-FAMILY:IPR010976 , InterPro:IN-FAMILY:IPR023214 , Pfam:IN-FAMILY:PF00702 , Prints:IN-FAMILY:PR00413

In Paralogous Gene Group: 276 (8 members)

Gene-Reaction Schematic: ?

Gene-Reaction Schematic

Instance reaction of [D-glucopyranose 6-phosphate[periplasmic space] + H2O[periplasmic space] → D-glucopyranose[periplasmic space] + phosphate[periplasmic space]] (
i1: α-D-glucose 6-phosphate + H2O → α-D-glucose + phosphate (

Instance reactions of [a sugar phosphate + H2O → a sugar + phosphate] (
i2: β-D-fructofuranose 1-phosphate + H2O → β-D-fructofuranose + phosphate (3.1.3.-)

i3: β-D-glucose 6-phosphate + H2O → β-D-glucopyranose + phosphate (

i4: D-glucopyranose 6-phosphate[periplasmic space] + H2O[periplasmic space] → D-glucopyranose[periplasmic space] + phosphate[periplasmic space] (

i5: α-D-glucopyranose 1-phosphate + H2O → D-glucopyranose + phosphate (

i6: D-ribose 5-phosphate[periplasmic space] + H2O[periplasmic space]aldehydo-D-ribose[periplasmic space] + phosphate[periplasmic space] (3.1.3.-)

i7: a hexose phosphate + H2O = a hexose + phosphate (3.1.3.-)

GO Terms:

Biological Process: GO:0016311 - dephosphorylation Inferred from experiment [Kuznetsova06]
GO:0008152 - metabolic process Inferred by computational analysis [GOA01a]
Molecular Function: GO:0000287 - magnesium ion binding Inferred from experiment [Kuznetsova06]
GO:0008801 - beta-phosphoglucomutase activity Inferred from experiment [Kuznetsova06]
GO:0016791 - phosphatase activity Inferred from experiment [Kuznetsova06]
GO:0016787 - hydrolase activity Inferred by computational analysis [UniProtGOA11a, GOA01a]
GO:0046872 - metal ion binding Inferred by computational analysis [UniProtGOA11a]
Cellular Component: GO:0005829 - cytosol Inferred by computational analysis [DiazMejia09]

MultiFun Terms: metabolism

Essentiality data for yqaB knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB enriched Yes 37 Aerobic 6.95   Yes [Gerdes03, Comment 1]
LB Lennox Yes 37 Aerobic 7   Yes [Baba06, Comment 2]
M9 medium with 1% glycerol Yes 37 Aerobic 7.2 0.35 Yes [Joyce06, Comment 3]
MOPS medium with 0.4% glucose Yes 37 Aerobic 7.2 0.22 Yes [Baba06, Comment 2]
Yes [Feist07, Comment 4]

Last-Curated ? 27-Sep-2006 by Keseler I , SRI International
Revised 23-May-2011 by Brito D

Enzymatic reaction of: fructose-1-phosphatase

Synonyms: HAD6

EC Number: 3.1.3.-

β-D-fructofuranose 1-phosphate + H2O <=> β-D-fructofuranose + phosphate

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.

Alternative Substrates for β-D-fructofuranose 1-phosphate: D-gluconate 6-phosphate [Kuznetsova06 ]

Cofactors or Prosthetic Groups: Mg2+ [Kuznetsova06]

Kinetic Parameters:

Km (μM)
β-D-fructofuranose 1-phosphate

Sequence Features

Protein sequence of fructose-1-phosphatase with features indicated

Feature Class Location Citations Comment
Metal-Binding-Site 11
UniProt: Magnesium; Non-Experimental Qualifier: by similarity.
Protein-Segment 11 -> 13
UniProt: Substrate; Sequence Annotation Type: region of interest; Non-Experimental Qualifier: by similarity.
Active-Site 11
UniProt: Nucleophile; Non-Experimental Qualifier: by similarity;
Metal-Binding-Site 13
UniProt: Magnesium; Non-Experimental Qualifier: by similarity.
Metal-Binding-Site 167
UniProt: Magnesium; Non-Experimental Qualifier: by similarity.

Gene Local Context (not to scale): ?

Gene local context diagram

Transcription Unit:

Transcription-unit diagram


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 ].
Markus Krummenacker on Tue Oct 14, 1997:
Gene object created from Blattner lab Genbank (v. M52) entry.


Baba06: Baba T, Ara T, Hasegawa M, Takai Y, Okumura Y, Baba M, Datsenko KA, Tomita M, Wanner BL, Mori H (2006). "Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: the Keio collection." Mol Syst Biol 2;2006.0008. PMID: 16738554

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

Feist07: Feist AM, Henry CS, Reed JL, Krummenacker M, Joyce AR, Karp PD, Broadbelt LJ, Hatzimanikatis V, Palsson BO (2007). "A genome-scale metabolic reconstruction for Escherichia coli K-12 MG1655 that accounts for 1260 ORFs and thermodynamic information." Mol Syst Biol 3;121. PMID: 17593909

Gerdes03: Gerdes SY, Scholle MD, Campbell JW, Balazsi G, Ravasz E, Daugherty MD, Somera AL, Kyrpides NC, Anderson I, Gelfand MS, Bhattacharya A, Kapatral V, D'Souza M, Baev MV, Grechkin Y, Mseeh F, Fonstein MY, Overbeek R, Barabasi AL, Oltvai ZN, Osterman AL (2003). "Experimental determination and system level analysis of essential genes in Escherichia coli MG1655." J Bacteriol 185(19);5673-84. PMID: 13129938

GOA01a: GOA, DDB, FB, MGI, ZFIN (2001). "Gene Ontology annotation through association of InterPro records with GO terms."

Joyce06: Joyce AR, Reed JL, White A, Edwards R, Osterman A, Baba T, Mori H, Lesely SA, Palsson BO, Agarwalla S (2006). "Experimental and computational assessment of conditionally essential genes in Escherichia coli." J Bacteriol 188(23);8259-71. PMID: 17012394

Kuznetsova05: Kuznetsova E, Proudfoot M, Sanders SA, Reinking J, Savchenko A, Arrowsmith CH, Edwards AM, Yakunin AF (2005). "Enzyme genomics: Application of general enzymatic screens to discover new enzymes." FEMS Microbiol Rev 29(2);263-79. PMID: 15808744

Kuznetsova06: Kuznetsova E, Proudfoot M, Gonzalez CF, Brown G, Omelchenko MV, Borozan I, Carmel L, Wolf YI, Mori H, Savchenko AV, Arrowsmith CH, Koonin EV, Edwards AM, Yakunin AF (2006). "Genome-wide analysis of substrate specificities of the Escherichia coli haloacid dehalogenase-like phosphatase family." J Biol Chem 281(47):36149-61. PMID: 16990279

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

UniProt10: UniProt Consortium (2010). "UniProt version 2010-07 released on 2010-06-15 00:00:00." Database.

UniProt12a: UniProt Consortium (2012). "UniProt version 2012-09 released on 2012-09-12 00:00:00." Database.

UniProtGOA11a: 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 EcoCyc: Nucleic Acids Research 41:D605-12 2013
Page generated by SRI International Pathway Tools version 19.0 on Fri Oct 9, 2015, BIOCYC14B.