Summary: L-fucose isomerase, second N-terminal domain
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This is the Wikipedia entry entitled "L-fucose isomerase". More...
L-fucose isomerase
| L-fucose isomerase | |||||||
|---|---|---|---|---|---|---|---|
| Identifiers | |||||||
| EC number | 5.3.1.25 | ||||||
| CAS number | 60063-83-4 | ||||||
| Databases | |||||||
| IntEnz | IntEnz view | ||||||
| BRENDA | BRENDA entry | ||||||
| ExPASy | NiceZyme view | ||||||
| KEGG | KEGG entry | ||||||
| MetaCyc | metabolic pathway | ||||||
| PRIAM | profile | ||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||
| Gene Ontology | AmiGO / EGO | ||||||
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| l-fucose isomerase from escherichia coli | |||||||||
| Identifiers | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Symbol | Fucose_iso_N1 | ||||||||
| Pfam | PF07881 | ||||||||
| InterPro | IPR012888 | ||||||||
| SCOP | 1fui | ||||||||
| SUPERFAMILY | 1fui | ||||||||
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| l-fucose isomerase from escherichia coli | |||||||||
| Identifiers | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Symbol | Fucose_iso_N2 | ||||||||
| Pfam | PF07882 | ||||||||
| InterPro | IPR012889 | ||||||||
| SCOP | 1fui | ||||||||
| SUPERFAMILY | 1fui | ||||||||
|
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| l-fucose isomerase from escherichia coli | |||||||||
| Identifiers | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Symbol | Fucose_iso_C | ||||||||
| Pfam | PF02952 | ||||||||
| Pfam clan | CL0393 | ||||||||
| InterPro | IPR015888 | ||||||||
| SCOP | 1fui | ||||||||
| SUPERFAMILY | 1fui | ||||||||
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In enzymology, a L-fucose isomerase (EC 5.3.1.25) is an enzyme that catalyzes the chemical reaction
- L-fucose
L-fuculose
Hence, this enzyme has one substrate, L-fucose, and one product, L-fuculose.
This enzyme belongs to the family of isomerases, specifically those intramolecular oxidoreductases interconverting aldoses and ketoses. The systematic name of this enzyme class is L-fucose aldose-ketose-isomerase. This enzyme participates in fructose and mannose metabolism.
The enzyme is a hexamer, forming the largest structurally known ketol isomerase, and has no sequence or structural similarity with other ketol isomerases. The structure was determined by X-ray crystallography at 2.5 Angstrom resolution.[1] Each subunit of the hexameric enzyme is wedge-shaped and composed of three domains. Both domains 1 and 2 contain central parallel beta- sheets with surrounding alpha helices. The active centre is shared between pairs of subunits related along the molecular three-fold axis, with domains 2 and 3 from one subunit providing most of the substrate-contacting residues.[1]
[edit] References
[edit] Further reading
- Lu Z, Lin EC (1989). "The nucleotide sequence of Escherichia coli genes for L-fucose dissimilation". Nucleic. Acids. Res. 17 (12): 4883–4. doi:10.1093/nar/17.12.4883. PMC 318048. PMID 2664711. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=318048.
| This isomerase article is a stub. You can help Wikipedia by expanding it. |
This article incorporates text from the public domain Pfam and InterPro IPR015888
This article incorporates text from the public domain Pfam and InterPro IPR012889
This article incorporates text from the public domain Pfam and InterPro IPR012888
This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.
This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.
L-fucose isomerase, second N-terminal domain
The members of this family are similar to L-fucose isomerase expressed by E. coli (P11552 EC:5.3.1.3). This enzyme corresponds to glucose-6-phosphate isomerase in glycolysis, and converts an aldo-hexose to a ketose to prepare it for aldol cleavage. The enzyme is a hexamer, with each subunit being wedge-shaped and composed of three domains. Both domains 1 and 2 contain central parallel beta- sheets with surrounding alpha helices. The active centre is shared between pairs of subunits related along the molecular three-fold axis, with domains 2 and 3 from one subunit providing most of the substrate-contacting residues [1].
Literature references
-
Seemann JE, Schulz GE; , J Mol Biol 1997;273:256-268.: Structure and mechanism of L-fucose isomerase from Escherichia coli. PUBMED:9367760
External database links
| PANDIT: | PF07882 |
| Pseudofam: | PF07882 |
| SCOP: | 1fui |
| SYSTERS: | Fucose_iso_N2 |
This tab holds annotation information from the InterPro database.
InterPro entry IPR012889
Proteins containing this domain are similar to L-fucose isomerase expressed by Escherichia coli (SWISSPROT, EC). This enzyme corresponds to glucose-6-phosphate isomerase in glycolysis, and converts an aldo-hexose to a ketose to prepare it for aldol cleavage. The enzyme is a hexamer, with each subunit being wedge-shaped and composed of three domains. Both domains 1 and 2 contain central parallel beta- sheets with surrounding alpha helices. The active centre is shared between pairs of subunits related along the molecular three-fold axis, with domains 2 and 3 from one subunit providing most of the substrate-contacting residues [PUBMED:9367760].
Gene Ontology
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
| Cellular component | cytoplasm (GO:0005737) |
| Molecular function | L-fucose isomerase activity (GO:0008736) |
| Biological process | fucose metabolic process (GO:0006004) |
Domain organisation
Below is a listing of the unique domain organisations or architectures in which this domain is found. More...
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Alignments
There are various ways to view or download the sequence alignments that we store. You can use a sequence viewer to look at either the seed or full alignment for the family, or you can look at a plain text version of the sequence in a variety of different formats. More...
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Very large alignments can often cause problems for the formatting tool above. If you find that downloading or viewing a large alignment is problematic, you can also download a gzip-compressed, Stockholm-format file containing the seed or full alignment for this family.
You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.
The main seed and full alignments are generated using sequences from the UniProt sequence database. However, we also generate alignments using sequences from the NCBI sequence database and the "metaseq" metagenomics dataset.
You can view alignments from these two additional datasets using the form above, or you can download alignments of NCBI or metagenomics sequences, as gzip-compressed files.
External links
MyHits provides a collection of tools to handle multiple sequence alignments. For example, one can refine a seed alignment (sequence addition or removal, re-alignment or manual edition) and then search databases for remote homologs using HMMER3.
HMM logo
HMM logos is one way of visualising profile HMMs. Logos provide a quick overview of the properties of an HMM in a graphical form. You can see a more detailed description of HMM logos and find out how you can interpret them here. More...
Trees
This page displays the phylogenetic tree for this family. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed or full alignments.
Note: You can also download the data files for the seed, full, NCBI or metagenomics trees.
Curation and family details
This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.
Curation
| Seed source: | Pfam-B_11456 (release 14.0) |
| Previous IDs: | none |
| Type: | Family |
| Author: | Fenech M |
| Number in seed: | 21 |
| Number in full: | 595 |
| Average length of the domain: | 162.40 aa |
| Average identity of full alignment: | 56 % |
| Average coverage of the sequence by the domain: | 30.98 % |
HMM information
| HMM build commands: |
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 15929002 -E 1000 --cpu 4 HMM pfamseq
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| Model details: |
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| Model length: | 181 | ||||||||||||
| Family (HMM) version: | 7 | ||||||||||||
| Download: | download the raw HMM for this family |
Species distribution
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L-fuculose
Archea
Eukaryota
Bacteria
Other sequences
Viruses
Unclassified
Viroids
Unclassified sequence