DB code: S00391

CATH domain 3.40.225.10 : L-fuculose-1-phosphate Aldolase Catalytic domain
E.C. 4.1.2.17
CSA 1fua
M-CSA 1fua
MACiE M0072

CATH domain Related DB codes (homologues)

Uniprot Enzyme Name
UniprotKB Protein name Synonyms RefSeq Pfam
P0AB87 L-fuculose phosphate aldolase
EC 4.1.2.17
L-fuculose-1-phosphate aldolase
NP_417280.1 (Protein)
NC_000913.2 (DNA/RNA sequence)
YP_491008.1 (Protein)
NC_007779.1 (DNA/RNA sequence)
PF00596 (Aldolase_II)
[Graphical View]

KEGG enzyme name
L-fuculose-phosphate aldolase
L-fuculose 1-phosphate aldolase
fuculose aldolase
L-fuculose-1-phosphate lactaldehyde-lyase

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
P0AB87 FUCA_ECOLI L-fuculose 1-phosphate = glycerone phosphate + (S)-lactaldehyde. Homotetramer. Binds 1 zinc ion per subunit.

KEGG Pathways
Map code Pathways E.C.
MAP00051 Fructose and mannose metabolism

Compound table
Cofactors Substrates Products Intermediates
KEGG-id C00038 C01099 C00111 C00424
E.C.
Compound Zinc L-Fuculose 1-phosphate Glycerone phosphate (S)-Lactaldehyde
Type heavy metal carbohydrate,phosphate group/phosphate ion carbohydrate,phosphate group/phosphate ion carbohydrate
ChEBI 29105
 29105
 		16647
 16647
 		16108
 16108
 		18041
 18041
PubChem 32051
 32051
 		6857415
 6857415
 		668
 668
 		439231
 439231
1dzuP Bound:_ZN Unbound Unbound Unbound
1dzvP Bound:_ZN Unbound Unbound Unbound
1dzwP Bound:_ZN Unbound Unbound Unbound
1dzxP Bound:_ZN Unbound Unbound Unbound
1dzyP Bound:_ZN Unbound Unbound Unbound
1dzzP Bound:_ZN Unbound Unbound Unbound
1e46P Bound:_ZN Unbound Unbound Unbound
1e47P Bound:_ZN Unbound Bound:13P Unbound
1e48P Bound:_ZN Unbound Bound:13P Unbound
1e49P Bound:_ZN Unbound Unbound Unbound
1e4aP Bound:_ZN Unbound Unbound Unbound
1e4bP Bound:_ZN Unbound Unbound Unbound
1e4cP Bound:_ZN Unbound Unbound Unbound
1fuaA Bound:_ZN Unbound Unbound Unbound
2fuaA Analogue:_CO Unbound Unbound Unbound
3fuaA Bound:_ZN Unbound Unbound Unbound
4fuaA Bound:_ZN Unbound Analogue:PGH Unbound

Reference for Active-site residues
resource references E.C.
Swiss-prot;P0AB87 & literature;[3],[5]

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1dzuP GLU 73;TYR 113 GLU 73;HIS 92;HIS 94;HIS 155(Zinc binding) mutant T26A
1dzvP GLU 73; GLU 73;HIS 92;HIS 94;HIS 155(Zinc binding) mutant Y113F;Y209F
1dzwP GLU 73;TYR 113 GLU 73;HIS 92;HIS 94;HIS 155(Zinc binding) mutant F131A
1dzxP GLU 73;TYR 113 GLU 73;HIS 92;HIS 94;HIS 155(Zinc binding) mutant R212A
1dzyP GLU 73;TYR 113 GLU 73;HIS 92;HIS 94;HIS 155(Zinc binding) mutant E214A
1dzzP GLU 73; GLU 73;HIS 92;HIS 94;HIS 155(Zinc binding) mutant Y113F
1e46P ;TYR 113 ;HIS 92;HIS 94;HIS 155(Zinc binding) mutant E73S
1e47P ;TYR 113 ;HIS 92;HIS 94;HIS 155(Zinc binding) mutant E73Q
1e48P ; ;HIS 92;HIS 94;HIS 155(Zinc binding) mutant E73Q;Y113F;Y209F
1e49P GLU 73;TYR 113 GLU 73;HIS 92;HIS 94;HIS 155(Zinc binding) mutant N29L;S71A
1e4aP GLU 73;TYR 113 GLU 73;HIS 92;HIS 94;HIS 155(Zinc binding) deletion A27
1e4bP GLU 73;TYR 113 GLU 73;HIS 92;HIS 94;HIS 155(Zinc binding) mutant N29Q
1e4cP GLU 73;TYR 113 GLU 73;HIS 92;HIS 94;HIS 155(Zinc binding) mutant S71Q
1fuaA GLU 73;TYR 113 GLU 73;HIS 92;HIS 94;HIS 155(Zinc binding)
2fuaA GLU 73;TYR 113 GLU 73;HIS 92;HIS 94;HIS 155(Zinc binding)
3fuaA GLU 73;TYR 113 GLU 73;HIS 92;HIS 94;HIS 155(Zinc binding)
4fuaA GLU 73;TYR 113 GLU 73;HIS 92;HIS 94;HIS 155(Zinc binding)

References for Catalytic Mechanism
References Sections No. of steps in catalysis
[3]
Fig.6, p.463-465 3
[4]
Fig.6, p.5752 2
[5]
Fig.3
[8]
Fig.2
[9]
Fig.1

References
[1]
Resource
Comments
Medline ID
PubMed ID 8515438
Journal J Mol Biol
Year 1993
Volume 231
Pages 549-53
Authors Dreyer MK, Schulz GE
Title The spatial structure of the class II L-fuculose-1-phosphate aldolase from Escherichia coli.
Related PDB
Related UniProtKB
[2]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
Medline ID
PubMed ID
Journal Acta Crystallogr D Biol Crystallogr
Year 1996
Volume 52
Pages 1082-91
Authors Dreyer MK, Schulz GE
Title Refined high-resolution structure of the metal-ion dependent L-fuculose-1-phosphate aldolase (class II) from Escherichia coli.
Related PDB 1fua 2fua
Related UniProtKB P0AB87
[3]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS), AND CATALYTIC MECHANISM.
Medline ID 96256522
PubMed ID 8676381
Journal J Mol Biol
Year 1996
Volume 259
Pages 458-66
Authors Dreyer MK, Schulz GE
Title Catalytic mechanism of the metal-dependent fuculose aldolase from Escherichia coli as derived from the structure.
Related PDB 3fua 4fua
Related UniProtKB P0AB87
[4]
Resource
Comments Homologous enzyme
Medline ID
PubMed ID 9548961
Journal Biochemistry
Year 1998
Volume 37
Pages 5746-54
Authors Johnson AE, Tanner ME
Title Epimerization via carbon-carbon bond cleavage. L-ribulose-5-phosphate 4-epimerase as a masked class II aldolase.
Related PDB
Related UniProtKB
[5]
Resource
Comments X-RAY CRYSTALLOGRAPHY (1.86 ANGSTROMS), AND MUTAGENESIS.
Medline ID 20281325
PubMed ID 10821675
Journal Biochemistry
Year 2000
Volume 39
Pages 6033-41
Authors Joerger AC, Gosse C, Fessner WD, Schulz GE
Title Catalytic action of fuculose 1-phosphate aldolase (class II) as derived from structure-directed mutagenesis.
Related PDB 1dzu 1dzv 1dzw 1dzx 1dzy 1dzz
Related UniProtKB P0AB87
[6]
Resource
Comments Homologous enzyme
Medline ID
PubMed ID 10769138
Journal Biochemistry
Year 2000
Volume 39
Pages 4808-20
Authors Lee LV, Vu MV, Cleland WW
Title 13C and deuterium isotope effects suggest an aldol cleavage mechanism for L-ribulose-5-phosphate 4-epimerase.
Related PDB
Related UniProtKB
[7]
Resource
Comments X-RAY CRYSTALLOGRAPHY OF MUTANTS.
Medline ID 20510153
PubMed ID 11054289
Journal J Mol Biol
Year 2000
Volume 303
Pages 531-43
Authors Joerger AC, Mueller-Dieckmann C, Schulz GE
Title Structures of l-fuculose-1-phosphate aldolase mutants outlining motions during catalysis.
Related PDB 1e46 1e47 1e48 1e49 1e4a 1e4b 1e4c
Related UniProtKB P0AB87
[8]
Resource
Comments Homologous enzyme
Medline ID
PubMed ID 11732895
Journal Biochemistry
Year 2001
Volume 40
Pages 14763-71
Authors Luo Y, Samuel J, Mosimann SC, Lee JE, Tanner ME, Strynadka NC
Title The structure of L-ribulose-5-phosphate 4-epimerase: an aldolase-like platform for epimerization.
Related PDB
Related UniProtKB
[9]
Resource
Comments Homologous enzyme
Medline ID
PubMed ID 11732896
Journal Biochemistry
Year 2001
Volume 40
Pages 14772-80
Authors Samuel J, Luo Y, Morgan PM, Strynadka NC, Tanner ME
Title Catalysis and binding in L-ribulose-5-phosphate 4-epimerase: a comparison with L-fuculose-1-phosphate aldolase.
Related PDB
Related UniProtKB

Comments
This enzyme belongs to the aldolase class II family, which utilizes the metal ion as cofactor.

Created Updated
2004-06-28 2009-02-26