DB code: T00100
CATH domain | 3.40.50.1070 : Rossmann fold | |
---|---|---|
3.40.275.10 : L-fucose Isomerase; Chain A, domain 2 | Catalytic domain | |
3.20.14.10 : L-fucose Isomerase; Chain A, domain 3 | Catalytic domain | |
E.C. | 5.3.1.25 | |
CSA | 1fui | |
M-CSA | 1fui | |
MACiE | M0095 |
CATH domain | Related DB codes (homologues) |
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Uniprot Enzyme Name | UniprotKB | Protein name | Synonyms | RefSeq | Pfam |
---|---|---|---|---|
P69922 |
L-fucose isomerase
|
EC
5.3.1.25
6-deoxy-L-galactose isomerase FucIase |
NP_417282.1
(Protein)
NC_000913.2 (DNA/RNA sequence) YP_491010.1 (Protein) NC_007779.1 (DNA/RNA sequence) |
PF02952
(Fucose_iso_C)
PF07881 (Fucose_iso_N1) PF07882 (Fucose_iso_N2) [Graphical View] |
KEGG enzyme name |
---|
L-fucose isomerase
|
UniprotKB: Accession Number | Entry name | Activity | Subunit | Subcellular location | Cofactor |
---|---|---|---|---|---|
P69922 | FUCI_ECOLI | L-fucose = L-fuculose. | Homohexamer. | Cytoplasm. | Manganese. |
KEGG Pathways | Map code | Pathways | E.C. |
---|---|---|
MAP00051 | Fructose and mannose metabolism |
Compound table | |||||||||
---|---|---|---|---|---|---|---|---|---|
Cofactors | Substrates | Products | Intermediates | ||||||
KEGG-id | C00034 | C01019 | C01721 | ||||||
E.C. | |||||||||
Compound | Manganese | L-Fucose | L-Fuculose | ||||||
Type | heavy metal | carbohydrate | carbohydrate | ||||||
ChEBI |
18291 35154 18291 35154 |
2181 2181 |
17617 17617 |
||||||
PubChem |
23930 23930 |
17106 17106 |
6857362 6857362 |
||||||
1fuiA01 | Unbound | Unbound | Unbound | ||||||
1fuiB01 | Unbound | Unbound | Unbound | ||||||
1fuiC01 | Unbound | Unbound | Unbound | ||||||
1fuiD01 | Unbound | Unbound | Unbound | ||||||
1fuiE01 | Unbound | Unbound | Unbound | ||||||
1fuiF01 | Unbound | Unbound | Unbound | ||||||
1fuiA02 | Unbound | Unbound | Unbound | ||||||
1fuiB02 | Unbound | Unbound | Unbound | ||||||
1fuiC02 | Unbound | Unbound | Unbound | ||||||
1fuiD02 | Unbound | Unbound | Unbound | ||||||
1fuiE02 | Unbound | Unbound | Unbound | ||||||
1fuiF02 | Unbound | Unbound | Unbound | ||||||
1fuiA03 | Bound:_MN | Analogue:FOC | Unbound | ||||||
1fuiB03 | Bound:_MN | Analogue:FOC | Unbound | ||||||
1fuiC03 | Bound:_MN | Analogue:FOC | Unbound | ||||||
1fuiD03 | Bound:_MN | Analogue:FOC | Unbound | ||||||
1fuiE03 | Bound:_MN | Analogue:FOC | Unbound | ||||||
1fuiF03 | Unbound | Analogue:FOC | Unbound |
Reference for Active-site residues | ||
---|---|---|
resource | references | E.C. |
Swiss-prot;P69922 & literature [7] |
Active-site residues | ||||||||||
---|---|---|---|---|---|---|---|---|---|---|
PDB | Catalytic residues | Cofactor-binding residues | Modified residues | Main-chain involved in catalysis | Comment | |||||
1fuiA01 | ||||||||||
1fuiB01 | ||||||||||
1fuiC01 | ||||||||||
1fuiD01 | ||||||||||
1fuiE01 | ||||||||||
1fuiF01 | ||||||||||
1fuiA02 | GLU 337 | GLU 337(Manganese binding) | ||||||||
1fuiB02 | GLU 337 | GLU 337(Manganese binding) | ||||||||
1fuiC02 | GLU 337 | GLU 337(Manganese binding) | ||||||||
1fuiD02 | GLU 337 | GLU 337(Manganese binding) | ||||||||
1fuiE02 | GLU 337 | GLU 337(Manganese binding) | ||||||||
1fuiF02 | GLU 337 | GLU 337(Manganese binding) | ||||||||
1fuiA03 | ASP 361 | ASP 361;HIS 528(Manganese binding) | ||||||||
1fuiB03 | ASP 361 | ASP 361;HIS 528(Manganese binding) | ||||||||
1fuiC03 | ASP 361 | ASP 361;HIS 528(Manganese binding) | ||||||||
1fuiD03 | ASP 361 | ASP 361;HIS 528(Manganese binding) | ||||||||
1fuiE03 | ASP 361 | ASP 361;HIS 528(Manganese binding) | ||||||||
1fuiF03 | ASP 361 | ASP 361;HIS 528(Manganese binding) |
References for Catalytic Mechanism | ||
---|---|---|
References | Sections | No. of steps in catalysis |
[7]
|
Fig.11, p.260-262, p.264-266 | |
[10]
|
Scheme 16, p.9-10 | |
[11]
|
p.101 |
References | |
---|---|
[1] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 13319278 |
Journal | J Biol Chem |
Year | 1956 |
Volume | 219 |
Pages | 557-68 |
Authors | GREEN M, COHEN SS |
Title | Enzymatic conversion of L-fucose to L-fuculose. |
Related PDB | |
Related UniProtKB | |
[2] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | |
Journal | Methods Enzymol |
Year | 1966 |
Volume | 9 |
Pages | 583-5 |
Authors | Mortlock RP |
Title | D-Arabinose isomerase. |
Related PDB | |
Related UniProtKB | |
[3] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 4632320 |
Journal | J Bacteriol |
Year | 1973 |
Volume | 113 |
Pages | 687-96 |
Authors | Boulter JR, Gielow WO |
Title | Properties of D-arabinose isomerase purified from two strains of Escherichia coli. |
Related PDB | |
Related UniProtKB | |
[4] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | |
Journal | Agric Biol Chem |
Year | 1974 |
Volume | 38 |
Pages | 267-73 |
Authors | Izumori K, Yamanaka K |
Title | Purification and crystallization of D-arabinose (L-fucose) isomerase from Aerobacter aerogenes by polyethylene glycol. |
Related PDB | |
Related UniProtKB | |
[5] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | |
Journal | Agric Biol Chem |
Year | 1976 |
Volume | 40 |
Pages | 439-440 |
Authors | Yamanaka K, Izumori K |
Title | Inhibition of D-arabinose (L-fucose) isomerase activity by Tris and its analogues. |
Related PDB | |
Related UniProtKB | |
[6] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | |
Journal | Agric Biol Chem |
Year | 1979 |
Volume | 43 |
Pages | 1993-4 |
Authors | Izumori K, Yamanaka K |
Title | Activation and inhibition of D-arabinose isomerase of Klebsiella aerogenes by L-histidine. |
Related PDB | |
Related UniProtKB | |
[7] | |
Resource | |
Comments | X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS). |
Medline ID | 98035055 |
PubMed ID | 9367760 |
Journal | J Mol Biol |
Year | 1997 |
Volume | 273 |
Pages | 256-68 |
Authors | Seemann JE, Schulz GE |
Title | Structure and mechanism of L-fucose isomerase from Escherichia coli. |
Related PDB | 1fui |
Related UniProtKB | P69922 |
[8] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 9485504 |
Journal | Proteins |
Year | 1997 |
Volume | Suppl 1 |
Pages | 129-33 |
Authors | Flockner H, Domingues FS, Sippl MJ |
Title | Protein folds from pair interactions: a blind test in fold recognition. |
Related PDB | |
Related UniProtKB | |
[9] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 10368289 |
Journal | Structure Fold Des |
Year | 1999 |
Volume | 7 |
Pages | 227-36 |
Authors | Castillo RM, Mizuguchi K, Dhanaraj V, Albert A, Blundell TL, Murzin AG |
Title | A six-stranded double-psi beta barrel is shared by several protein superfamilies. |
Related PDB | |
Related UniProtKB | |
[10] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 11368170 |
Journal | Arch Biochem Biophys |
Year | 2001 |
Volume | 387 |
Pages | 1-10 |
Authors | Creighton DJ, Hamilton DS |
Title |
Brief history of glyoxalase I and what we have learned about metal ion-dependent, |
Related PDB | |
Related UniProtKB | |
[11] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | |
Journal | Top Curr Chem |
Year | 2001 |
Volume | 215 |
Pages | 77-114 |
Authors | Hausler H, Stutz AE |
Title | D-xylose (D-glucose) isomerase and related enzymes in carbohydrate synthesis. |
Related PDB | |
Related UniProtKB | |
[12] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 12645017 |
Journal | Chemistry |
Year | 2003 |
Volume | 9 |
Pages | 1281-95 |
Authors | Casanova D, Alemany P, Bofill JM, Alvarez S |
Title | Shape and symmetry of heptacoordinate transition-metal complexes: structural trends. |
Related PDB | |
Related UniProtKB |
Comments |
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Created | Updated |
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2005-07-04 | 2009-02-26 |