Escherichia coli K-12 substr. MG1655 Enzyme: L-fuculose-phosphate aldolase

Gene: fucA Accession Numbers: EG10348 (EcoCyc), b2800, ECK2795

Synonyms: fucC, prd

Regulation Summary Diagram: ?

Regulation summary diagram for fucA

Subunit composition of L-fuculose-phosphate aldolase = [FucA]4

FucA can function as both an L-fuculose-phosphate aldolase and a D-ribulose-phosphate aldolase, the third enzyme of the L-fucose and D-arabinose degradation pathways, respectively. However, production of FucA is only induced by L-fucose [LeBlanc71a, LeBlanc71].

The substrate specificity of the enzyme was tested with a partially purified preparation from an unnamed E. coli strain [Ozaki90].

Crystal structures of the enzyme and a number of point mutants have been solved. The combination of structural data and enzymatic activity of mutants allowed modelling and refinement of the catalytic mechanism of the enzyme. [Dreyer93, Dreyer96, Dreyer96a, Joerger00, Joerger00a]

The enantiomeric selectivity of the enzyme has been studied [Joerger00].

A fucAO deletion mutant colonizes the mouse intestine and maintains its population at a lower level than wild type; the accumulation of fuculose-1-phosphate appears to enable the mutant to switch to utilization of ribose for growth [Autieri07].

Gene Citations: [Chen89a, Conway89]

Locations: cytosol

Map Position: [2,931,063 <- 2,931,710] (63.17 centisomes, 227°)
Length: 648 bp / 215 aa

Molecular Weight of Polypeptide: 23.775 kD (from nucleotide sequence)

pI: 6.51

Unification Links: ASAP:ABE-0009179 , CGSC:17701 , DIP:DIP-9710N , EchoBASE:EB0344 , EcoGene:EG10348 , EcoliWiki:b2800 , ModBase:P0AB87 , OU-Microarray:b2800 , PortEco:fucA , PR:PRO_000022727 , Protein Model Portal:P0AB87 , RefSeq:NP_417280 , RegulonDB:EG10348 , SMR:P0AB87 , String:511145.b2800 , UniProt:P0AB87

Relationship Links: InterPro:IN-FAMILY:IPR001303 , InterPro:IN-FAMILY:IPR004782 , PDB:Structure:1DZU , PDB:Structure:1DZV , PDB:Structure:1DZW , PDB:Structure:1DZX , PDB:Structure:1DZY , PDB:Structure:1DZZ , PDB:Structure:1E46 , PDB:Structure:1E47 , PDB:Structure:1E48 , PDB:Structure:1E49 , PDB:Structure:1E4A , PDB:Structure:1E4B , PDB:Structure:1E4C , PDB:Structure:1FUA , PDB:Structure:2FUA , PDB:Structure:3FUA , PDB:Structure:4FUA , Pfam:IN-FAMILY:PF00596 , Smart:IN-FAMILY:SM01007

In Paralogous Gene Group: 450 (4 members)

Gene-Reaction Schematic: ?

Gene-Reaction Schematic

Genetic Regulation Schematic: ?

Genetic regulation schematic for fucA

GO Terms:

Biological Process: GO:0019571 - D-arabinose catabolic process Inferred from experiment [LeBlanc71]
GO:0042355 - L-fucose catabolic process Inferred from experiment [LeBlanc71]
GO:0005975 - carbohydrate metabolic process Inferred by computational analysis [UniProtGOA11]
GO:0006004 - fucose metabolic process Inferred by computational analysis [UniProtGOA11, GOA01]
GO:0019317 - fucose catabolic process Inferred by computational analysis [UniProtGOA12]
Molecular Function: GO:0008738 - L-fuculose-phosphate aldolase activity Inferred from experiment Inferred by computational analysis [GOA01a, GOA01, Joerger00]
GO:0016832 - aldehyde-lyase activity Inferred from experiment [LeBlanc71]
GO:0008270 - zinc ion binding Inferred by computational analysis [GOA01]
GO:0016829 - lyase activity Inferred by computational analysis [UniProtGOA11]
GO:0046872 - metal ion binding Inferred by computational analysis [UniProtGOA11]
Cellular Component: GO:0005829 - cytosol Inferred by computational analysis [DiazMejia09]

MultiFun Terms: metabolism carbon utilization carbon compounds

Essentiality data for fucA 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]

Created 19-Oct-2007 by Keseler I , SRI International
Last-Curated ? 19-Oct-2007 by Keseler I , SRI International

Enzymatic reaction of: L-fuculose-phosphate aldolase

Synonyms: L-fuculose-1-phosphate aldolase, L-fuculose-1-phosphate lactaldehyde-lyase

EC Number:

L-fuculose 1-phosphate <=> (S)-lactaldehyde + glycerone phosphate

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction of enzyme catalysis.

This reaction is reversible.

Alternative Substrates for (S)-lactaldehyde [Ghalambor62 ]: L-glyceraldehyde [Ghalambor62 ] , glycolaldehyde [Ghalambor62 ]

In Pathways: superpathway of fucose and rhamnose degradation , fucose degradation

This enzyme was first purified from E. coli strain O-111 B4 [Ghalambor62].

The Ki for phosphoglycolohydroxamate is 3.1 µM [Fessner96].

Cofactors or Prosthetic Groups: Zn2+ [GarciaJunceda95]

Inhibitors (Competitive): phosphoglycolohydroxamate [Dreyer96a, Fessner96]

Kinetic Parameters:

Km (μM)
L-fuculose 1-phosphate

Enzymatic reaction of: D-ribulose-phosphate aldolase (L-fuculose-phosphate aldolase)

D-ribulose 1-phosphate <=> glycolaldehyde + glycerone phosphate

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction of enzyme catalysis.

This reaction is reversible.

In Pathways: D-arabinose degradation I

The relative rate of the enzymatic activity with glycolaldehyde as the substrate is 59% of that with lactaldehyde [Ozaki90].

Cofactors or Prosthetic Groups: Zn2+ [GarciaJunceda95]

Inhibitors (Unknown Mechanism): phosphoglycolohydroxamate [Dreyer96a, Fessner96]

Sequence Features

Protein sequence of FucA with features indicated

Feature Class Location Citations Comment
Metal-Binding-Site 73
[Joerger00, Dreyer96, Dreyer96a, UniProt15]
UniProt: Zinc.
Active-Site 73
[Dreyer96a, UniProt15]
UniProt: Proton acceptor.
Metal-Binding-Site 92
[Joerger00, Dreyer96, Dreyer96a, UniProt15]
UniProt: Zinc.
Metal-Binding-Site 94
[Joerger00, Dreyer96, Dreyer96a, UniProt15]
UniProt: Zinc.
Active-Site 113
[Dreyer96a, UniProt15]
UniProt: Proton donor.
Metal-Binding-Site 155
[Joerger00, Dreyer96, Dreyer96a, UniProt15]
UniProt: Zinc.

Gene Local Context (not to scale): ?

Gene local context diagram

Transcription Unit:

Transcription-unit diagram


10/20/97 Gene b2800 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG10348; confirmed by SwissProt match.


Autieri07: Autieri SM, Lins JJ, Leatham MP, Laux DC, Conway T, Cohen PS (2007). "L-fucose stimulates utilization of D-ribose by Escherichia coli MG1655 DeltafucAO and E. coli Nissle 1917 DeltafucAO mutants in the mouse intestine and in M9 minimal medium." Infect Immun 75(11);5465-75. PMID: 17709419

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

Chen89a: Chen YM, Lu Z, Lin EC (1989). "Constitutive activation of the fucAO operon and silencing of the divergently transcribed fucPIK operon by an IS5 element in Escherichia coli mutants selected for growth on L-1,2-propanediol." J Bacteriol 1989;171(11);6097-105. PMID: 2553671

Conway89: Conway T, Ingram LO (1989). "Similarity of Escherichia coli propanediol oxidoreductase (fucO product) and an unusual alcohol dehydrogenase from Zymomonas mobilis and Saccharomyces cerevisiae." J Bacteriol 171(7);3754-9. PMID: 2661535

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

Dreyer93: Dreyer MK, Schulz GE (1993). "The spatial structure of the class II L-fuculose-1-phosphate aldolase from Escherichia coli." J Mol Biol 231(3);549-53. PMID: 8515438

Dreyer96: Dreyer MK, Schulz GE (1996). "Refined high-resolution structure of the metal-ion dependent L-fuculose-1-phosphate aldolase (class II) from Escherichia coli." Acta Crystallogr D Biol Crystallogr 52(Pt 6);1082-91. PMID: 15299567

Dreyer96a: Dreyer MK, Schulz GE (1996). "Catalytic mechanism of the metal-dependent fuculose aldolase from Escherichia coli as derived from the structure." J Mol Biol 259(3);458-66. PMID: 8676381

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

Fessner96: Fessner W-D, Schneider A, Held H, Sinerius G, Walter C, Hixon M, Schloss JV (1996). "The mechanism of Class II, metal-dependent aldolases." Angew Chem Int Ed Engl 35:2219-2221.

GarciaJunceda95: Garcia-Junceda E, Shen GJ, Sugai T, Wong CH (1995). "A new strategy for the cloning, overexpression and one step purification of three DHAP-dependent aldolases: rhamnulose-1-phosphate aldolase, fuculose-1-phosphate aldolase and tagatose-1,6-diphosphate aldolase." Bioorg Med Chem 3(7);945-53. PMID: 7582972

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

Ghalambor62: Ghalambor MA, Heath EC (1962). "The metabolism of L-fucose. II. The enzymatic cleavage of L-fuculose 1-phosphate." J Biol Chem 237;2427-33. PMID: 13898172

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.

Joerger00: Joerger AC, Gosse C, Fessner WD, Schulz GE (2000). "Catalytic action of fuculose 1-phosphate aldolase (class II) as derived from structure-directed mutagenesis." Biochemistry 39(20);6033-41. PMID: 10821675

Joerger00a: Joerger AC, Mueller-Dieckmann C, Schulz GE (2000). "Structures of l-fuculose-1-phosphate aldolase mutants outlining motions during catalysis." J Mol Biol 303(4);531-43. PMID: 11054289

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

LeBlanc71: LeBlanc DJ, Mortlock RP (1971). "Metabolism of D-arabinose: a new pathway in Escherichia coli." J Bacteriol 106(1);90-6. PMID: 4928018

LeBlanc71a: LeBlanc DJ, Mortlock RP (1971). "Metabolism of D-arabinose: origin of a D-ribulokinase activity in Escherichia coli." J Bacteriol 106(1);82-9. PMID: 4323967

Ozaki90: Ozaki A, Toone EJ, von der Osten CH, Sinskey AJ, Whitesides GM (1990). "Overproduction and substrate specificity of a bacterial fuculose-1-phosphate aldolase: A new enzymatic catalyst for stereocontrolled aldol condensation." J Am Chem Soc 112:4970-4971.

UniProt15: UniProt Consortium (2015). "UniProt version 2015-01 released on 2015-01-16 00:00:00." Database.

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

UniProtGOA12: UniProt-GOA (2012). "Gene Ontology annotation based on UniPathway vocabulary mapping."

Other References Related to Gene Regulation

Huerta03: Huerta AM, Collado-Vides J (2003). "Sigma70 promoters in Escherichia coli: specific transcription in dense regions of overlapping promoter-like signals." J Mol Biol 333(2);261-78. PMID: 14529615

Podolny99: Podolny V, Lin EC, Hochschild A (1999). "A cyclic AMP receptor protein mutant that constitutively activates an Escherichia coli promoter disrupted by an IS5 insertion." J Bacteriol 1999;181(24);7457-63. PMID: 10601201

Zheng04: Zheng D, Constantinidou C, Hobman JL, Minchin SD (2004). "Identification of the CRP regulon using in vitro and in vivo transcriptional profiling." Nucleic Acids Res 32(19);5874-93. PMID: 15520470

Zhu88: Zhu Y, Lin EC (1988). "A mutant crp allele that differentially activates the operons of the fuc regulon in Escherichia coli." J Bacteriol 1988;170(5);2352-8. PMID: 2834341

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Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
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