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0  structures 442  species 0  interactions 595  sequences 4  architectures

Family: Fucose_iso_N2 (PF07882)

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 Edit Wikipedia article

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
L-fucose isomerase, first N-terminal domain
PDB 1fui EBI.jpg
l-fucose isomerase from escherichia coli
Identifiers
Symbol Fucose_iso_N1
Pfam PF07881
InterPro IPR012888
SCOP 1fui
SUPERFAMILY 1fui
L-fucose isomerase, second N-terminal domain
PDB 1fui EBI.jpg
l-fucose isomerase from escherichia coli
Identifiers
Symbol Fucose_iso_N2
Pfam PF07882
InterPro IPR012889
SCOP 1fui
SUPERFAMILY 1fui
L-fucose isomerase, C-terminal domain
PDB 1fui EBI.jpg
l-fucose isomerase from escherichia coli
Identifiers
Symbol Fucose_iso_C
Pfam PF02952
Pfam clan CL0393
InterPro IPR015888
SCOP 1fui
SUPERFAMILY 1fui

In enzymology, a L-fucose isomerase (EC 5.3.1.25) is an enzyme that catalyzes the chemical reaction

L-fucose \rightleftharpoons 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

  1. ^ a b Seemann JE, Schulz GE (October 1997). "Structure and mechanism of L-fucose isomerase from Escherichia coli". J. Mol. Biol. 273 (1): 256–68. doi:10.1006/jmbi.1997.1280. PMID 9367760. 

[edit] Further reading

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

  1. 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

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

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Domain organisation

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Alignments

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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.

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Full length sequences

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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.

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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 View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 15929002 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 21.3 21.3
Trusted cut-off 21.7 21.4
Noise cut-off 20.9 21.2
Model length: 181
Family (HMM) version: 7
Download: download the raw HMM for this family

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