Summary: L-fucose isomerase, C-terminal domain
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L-fucose isomerase Edit Wikipedia article
| L-fucose isomerase | |||||||
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| 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): 48834. 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, C-terminal domain Provide feedback
No Pfam abstract.
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 EPMC:9367760
External database links
| PANDIT: | PF02952 |
| Pseudofam: | PF02952 |
| SCOP: | 1fui |
| SYSTERS: | Fucose_iso_C |
This tab holds annotation information from the InterPro database.
InterPro entry IPR015888
L-fucose isomerase (EC) converts the aldose L-fucose into the corresponding ketose L-fuculose during the first step in fucose metabolism using Mn2+ as a cofactor. 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 A resolution [PUBMED:9367760].
This entry represents the C-terminal domain of L-fucose isomerase.
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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Pfam Clan
This family is a member of clan FucI-AraA_C (CL0393), which contains the following 2 members:
Arabinose_Iso_C Fucose_iso_CAlignments
We store a range of different sequence alignments for families. As well as the seed alignment from which the family is built, we provide the full alignment, generated by searching the sequence database using the family HMM. We also generate alignments using four representative proteomes (RP) sets, the NCBI sequence database, and our metagenomics sequence database. More...
View options
We make a range of alignments for each Pfam-A family. You can see a description of each above. You can view these alignments in various ways but please note that some types of alignment are never generated while others may not be available for all families, most commonly because the alignments are too large to handle.
| Seed (45) |
Full (1454) |
Representative proteomes | NCBI (864) |
Meta (123) |
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| RP15 (82) |
RP35 (141) |
RP55 (159) |
RP75 (185) |
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| Jalview | ||||||||
| HTML | ||||||||
| PP/heatmap | 1 | |||||||
| Pfam viewer | ||||||||
1Cannot generate PP/Heatmap alignments for seeds; no PP data available
Key:
available,
not generated,
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Format an alignment
Download options
We make all of our alignments available in Stockholm format. You can download them here as raw, plain text files or as gzip-compressed files.
| Seed (45) |
Full (1454) |
Representative proteomes | NCBI (864) |
Meta (123) |
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|---|---|---|---|---|---|---|---|---|
| RP15 (82) |
RP35 (141) |
RP55 (159) |
RP75 (185) |
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| Raw Stockholm | ||||||||
| Gzipped | ||||||||
You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.
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's seed alignment. 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 alignment.
Note: You can also download the data file for the tree.
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_9303 (Release 8.0) |
| Previous IDs: | fucose_iso_C; |
| Type: | Domain |
| Author: | Griffiths-Jones SR |
| Number in seed: | 45 |
| Number in full: | 1454 |
| Average length of the domain: | 155.10 aa |
| Average identity of full alignment: | 38 % |
| Average coverage of the sequence by the domain: | 29.63 % |
HMM information
| HMM build commands: |
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
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| Model details: |
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| Model length: | 142 | ||||||||||||
| Family (HMM) version: | 12 | ||||||||||||
| Download: | download the raw HMM for this family |
Species distribution
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Structures
For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the Fucose_iso_C domain has been found. There are 15 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.
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L-fuculose
Archea
Eukaryota
Bacteria
Other sequences
Viruses
Unclassified
Viroids
Unclassified sequence