Summary: L-fucose isomerase, C-terminal domain
This is the Wikipedia entry entitled "L-fucose isomerase". More...
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L-fucose isomerase Edit Wikipedia article
|PDB structures||RCSB PDB PDBe PDBsum|
|Gene Ontology||AmiGO / EGO|
|L-fucose isomerase, first N-terminal domain|
l-fucose isomerase from escherichia coli
|L-fucose isomerase, second N-terminal domain|
l-fucose isomerase from escherichia coli
|L-fucose isomerase, C-terminal domain|
l-fucose isomerase from escherichia coli
- L-fucose 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. 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.
- 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.
|This isomerase article is a stub. You can help Wikipedia by expanding it.|
L-fucose isomerase, C-terminal domain Provide feedback
No Pfam abstract.
Internal database links
|Similarity to PfamA using HHSearch:||Arabinose_Iso_C|
External database links
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.
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)|
- the number of sequences which exhibit this architecture
a textual description of the architecture, e.g. Gla, EGF x 2, Trypsin.
This example describes an architecture with one
Gladomain, followed by two consecutive
EGFdomains, and finally a single
- the UniProt description of the protein sequence
- the number of residues in the sequence
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The enzymes in this superfamily function as a hexamer, which is the largest structurally known ketol isomerase, that has no sequence or structural similarity to other ketol isomerases.
The clan contains the following 2 members:Arabinose_Iso_C Fucose_iso_C
We make a range of alignments for each Pfam-A family:
- the curated alignment from which the HMM for the family is built
- the alignment generated by searching the sequence database using the HMM
- Representative Proteomes (RPs) at 15%, 35%, 55% and 75% co-membership thresholds
- alignment generated by searching the UniProtKB sequence database using the family HMM
- alignment generated by searching the NCBI sequence database using the family HMM
- alignment generated by searching the metagenomics sequence database using the family HMM
You can see the alignments as HTML or in three different sequence viewers:
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Curation and family details
|Seed source:||Pfam-B_9303 (Release 8.0)|
|Number in seed:||29|
|Number in full:||385|
|Average length of the domain:||140.90 aa|
|Average identity of full alignment:||27 %|
|Average coverage of the sequence by the domain:||27.65 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 11927849 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||14|
|Download:||download the raw HMM for this family|
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There are 4 interactions for this family. More...
We determine these interactions using iPfam, which considers the interactions between residues in three-dimensional protein structures and maps those interactions back to Pfam families. You can find more information about the iPfam algorithm in the journal article that accompanies the website.
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 21 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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