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) |
|---|
| 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 |
|---|
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L-fucose isomerase
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| 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 |
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| PubChem |
23930 23930 |
17106 17106 |
6857362 6857362 |
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| 1fuiA01 |
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Unbound | Unbound | Unbound | |
| 1fuiB01 |
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Unbound | Unbound | Unbound | |
| 1fuiC01 |
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Unbound | Unbound | Unbound | |
| 1fuiD01 |
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Unbound | Unbound | Unbound | |
| 1fuiE01 |
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Unbound | Unbound | Unbound | |
| 1fuiF01 |
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Unbound | Unbound | Unbound | |
| 1fuiA02 |
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Unbound | Unbound | Unbound | |
| 1fuiB02 |
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Unbound | Unbound | Unbound | |
| 1fuiC02 |
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Unbound | Unbound | Unbound | |
| 1fuiD02 |
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Unbound | Unbound | Unbound | |
| 1fuiE02 |
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Unbound | Unbound | Unbound | |
| 1fuiF02 |
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Unbound | Unbound | Unbound | |
| 1fuiA03 |
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Bound:_MN | Analogue:FOC | Unbound | |
| 1fuiB03 |
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Bound:_MN | Analogue:FOC | Unbound | |
| 1fuiC03 |
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Bound:_MN | Analogue:FOC | Unbound | |
| 1fuiD03 |
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Bound:_MN | Analogue:FOC | Unbound | |
| 1fuiE03 |
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Bound:_MN | Analogue:FOC | Unbound | |
| 1fuiF03 |
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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 |
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| 1fuiB01 |
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| 1fuiC01 |
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| 1fuiD01 |
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| 1fuiE01 |
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| 1fuiF01 |
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| 1fuiA02 |
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GLU 337 | GLU 337(Manganese binding) | |||
| 1fuiB02 |
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GLU 337 | GLU 337(Manganese binding) | |||
| 1fuiC02 |
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GLU 337 | GLU 337(Manganese binding) | |||
| 1fuiD02 |
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GLU 337 | GLU 337(Manganese binding) | |||
| 1fuiE02 |
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GLU 337 | GLU 337(Manganese binding) | |||
| 1fuiF02 |
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GLU 337 | GLU 337(Manganese binding) | |||
| 1fuiA03 |
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ASP 361 | ASP 361;HIS 528(Manganese binding) | |||
| 1fuiB03 |
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ASP 361 | ASP 361;HIS 528(Manganese binding) | |||
| 1fuiC03 |
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ASP 361 | ASP 361;HIS 528(Manganese binding) | |||
| 1fuiD03 |
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ASP 361 | ASP 361;HIS 528(Manganese binding) | |||
| 1fuiE03 |
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ASP 361 | ASP 361;HIS 528(Manganese binding) | |||
| 1fuiF03 |
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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 | |
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[10]
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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 |
|---|
| Created | Updated |
|---|---|
| 2005-07-04 | 2009-02-26 |