Summary: UDP-N-acetylglucosamine 2-epimerase
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This is the Wikipedia entry entitled "UDP-N-acetylglucosamine 2-epimerase". More...
UDP-N-acetylglucosamine 2-epimerase Edit Wikipedia article
| UDP-N-acetylglucosamine 2-epimerase | |||||||||
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| Identifiers | |||||||||
| EC number | 5.1.3.14 | ||||||||
| CAS number | 9037-71-2 | ||||||||
| 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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| UDP-N-acetylglucosamine 2-epimerase | |||||||||
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| crystal structure of udp-n-acetylglucosamine_2 epimerase | |||||||||
| Identifiers | |||||||||
| Symbol | Epimerase_2 | ||||||||
| Pfam | PF02350 | ||||||||
| Pfam clan | CL0113 | ||||||||
| InterPro | IPR003331 | ||||||||
| SCOP | 1f6d | ||||||||
| SUPERFAMILY | 1f6d | ||||||||
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In enzymology, an UDP-N-acetylglucosamine 2-epimerase (EC 5.1.3.14) is an enzyme that catalyzes the chemical reaction
- UDP-N-acetyl-D-glucosamine
UDP-N-acetyl-D-mannosamine
Hence, this enzyme has one substrate, UDP-N-acetyl-D-glucosamine, and one product, UDP-N-acetyl-D-mannosamine.
This enzyme belongs to the family of isomerases, specifically those racemases and epimerases acting on carbohydrates and derivatives. The systematic name of this enzyme class is UDP-N-acetyl-D-glucosamine 2-epimerase. Other names in common use include UDP-N-acetylglucosamine 2'-epimerase, uridine diphosphoacetylglucosamine 2'-epimerase, uridine diphospho-N-acetylglucosamine 2'-epimerase, and uridine diphosphate-N-acetylglucosamine-2'-epimerase. This enzyme participates in aminosugars metabolism.
In microorganisms this epimerase is involved in the synthesis of the capsule precursor UDP-ManNAcA.[1][2] Some of these enzymes are bifunctional. The UDP-N-acetylglucosamine 2-epimerase from rat liver displays both epimerase and kinase activity.[3]
[edit] Structural studies
As of late 2007, 4 structures have been solved for this class of enzymes, with PDB accession codes 1F6D, 1O6C, 1V4V, and 1VGV.
[edit] References
- ^ Swartley JS, Liu LJ, Miller YK, Martin LE, Edupuganti S, Stephens DS (March 1998). "Characterization of the Gene Cassette Required for Biosynthesis of the (α1→6)-Linked N-Acetyl-d-Mannosamine-1-Phosphate Capsule of Serogroup A Neisseria meningitidis". J. Bacteriol. 180 (6): 1533–9. PMC 107054. PMID 9515923. //www.ncbi.nlm.nih.gov/pmc/articles/PMC107054/.
- ^ Kiser KB, Lee JC (January 1998). "Staphylococcus aureus cap5O and cap5P Genes Functionally Complement Mutations Affecting Enterobacterial Common-Antigen Biosynthesis in Escherichia coli". J. Bacteriol. 180 (2): 403–6. PMC 106897. PMID 9440531. //www.ncbi.nlm.nih.gov/pmc/articles/PMC106897/.
- ^ Stasche R, Hinderlich S, Weise C, Effertz K, Lucka L, Moormann P, Reutter W (September 1997). "A bifunctional enzyme catalyzes the first two steps in N-acetylneuraminic acid biosynthesis of rat liver. Molecular cloning and functional expression of UDP-N-acetyl-glucosamine 2-epimerase/N-acetylmannosamine kinase". J. Biol. Chem. 272 (39): 24319–24. doi:10.1074/jbc.272.39.24319. PMID 9305888.
[edit] Further reading
- Kikuchi K, Tsuiki S (1973). "Purification and properties of UDP-N-acetylglucosamine 2'-epimerase from rat liver". Biochim. Biophys. Acta. 327 (1): 193–206. PMID 4770741.
This article incorporates text from the public domain Pfam and InterPro IPR003331
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UDP-N-acetylglucosamine 2-epimerase Provide feedback
This family consists of UDP-N-acetylglucosamine 2-epimerases EC:5.1.3.14 this enzyme catalyses the production of UDP-ManNAc from UDP-GlcNAc. Note that some of the enzymes is this family are bifunctional such as O35826 and Q9Z0P6 in this instance Pfam matches only the N-terminal half of the protein suggesting that the additional C-terminal part (when compared to mono-functional members of this family) is responsible for the UPD-N-acetylmannosamine kinase activity of these enzymes. This hypothesis is further supported by the assumption that the C-terminal part of O35826 is the kinase domain [3].
Literature references
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Swartley JS, Liu LJ, Miller YK, Martin LE, Edupuganti S, Stephens DS; , J Bacteriol. 1998;180:1533-1539.: Characterization of the gene cassette required for biosynthesis of the (alpha1-->6)-linked N-acetyl-D-mannosamine-1-phosphate capsule of serogroup A Neisseria meningitidis. PUBMED:9515923 EPMC:9515923
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Kiser KB, Lee JC; , J Bacteriol 1998;180:403-406.: Staphylococcus aureus cap5O and cap5P genes functionally complement mutations affecting enterobacterial common-antigen biosynthesis in Escherichia coli. PUBMED:9440531 EPMC:9440531
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Stasche R, Hinderlich S, Weise C, Effertz K, Lucka L, Moormann P, Reutter W; , J Biol Chem 1997;272:24319-24324.: A bifunctional enzyme catalyzes the first two steps in N-acetylneuraminic acid biosynthesis of rat liver. Molecular cloning and functional expression of UDP-N-acetyl-glucosamine 2-epimerase/N-acetylmannosamine kinase. PUBMED:9305888 EPMC:9305888
External database links
| PANDIT: | PF02350 |
| Pseudofam: | PF02350 |
| SCOP: | 1f6d |
| SYSTERS: | Epimerase_2 |
This tab holds annotation information from the InterPro database.
InterPro entry IPR003331
UDP-N-acetylglucosamine 2-epimerase EC catalyses the production of UDP-ManNAc from UDP-GlcNAc. Some of the enzymes is this family are bifunctional. In microorganisms the epimerase is involved in in the synthesis of the capsule precursor UDP-ManNAcA [PUBMED:9515923, PUBMED:9440531]. The protein from rat liver displays both epimerase and kinase activity [PUBMED:9305888].Gene Ontology
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
| Molecular function | UDP-N-acetylglucosamine 2-epimerase activity (GO:0008761) |
| Biological process | lipopolysaccharide biosynthetic process (GO:0009103) |
| UDP-N-acetylglucosamine metabolic process (GO:0006047) |
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 GT-B (CL0113), which contains the following 35 members:
Alg14 Capsule_synth DUF1205 DUF1972 DUF3492 DUF354 Epimerase_2 Glyco_tran_28_C Glyco_trans_1_2 Glyco_trans_1_3 Glyco_trans_1_4 Glyco_trans_4_2 Glyco_trans_4_3 Glyco_trans_4_4 Glyco_transf_20 Glyco_transf_28 Glyco_transf_4 Glyco_transf_41 Glyco_transf_5 Glyco_transf_56 Glyco_transf_9 Glyco_transf_90 Glycogen_syn Glycos_transf_1 Glycos_transf_N Glyphos_transf LpxB MGDG_synth Mito_fiss_Elm1 Phosphorylase PIGA PS_pyruv_trans SUA5 Sucrose_synth UDPGTAlignments
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...
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| Seed (187) |
Full (4483) |
Representative proteomes | NCBI (3343) |
Meta (2891) |
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| RP15 (306) |
RP35 (604) |
RP55 (780) |
RP75 (922) |
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| Jalview | ||||||||
| HTML | ||||||||
| PP/heatmap | 1 | |||||||
| Pfam viewer | ||||||||
1Cannot generate PP/Heatmap alignments for seeds; no PP data available
Key:
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not generated,
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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 (187) |
Full (4483) |
Representative proteomes | NCBI (3343) |
Meta (2891) |
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|---|---|---|---|---|---|---|---|---|
| RP15 (306) |
RP35 (604) |
RP55 (780) |
RP75 (922) |
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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_888 (release 5.2) & Pfam-B_4862 (Release 7.5) |
| Previous IDs: | none |
| Type: | Family |
| Author: | Bashton M, Bateman A |
| Number in seed: | 187 |
| Number in full: | 4483 |
| Average length of the domain: | 333.90 aa |
| Average identity of full alignment: | 34 % |
| Average coverage of the sequence by the domain: | 89.01 % |
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: | 346 | ||||||||||||
| Family (HMM) version: | 14 | ||||||||||||
| Download: | download the raw HMM for this family |
Species distribution
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Interactions
There is 1 interaction for this family. More...
Epimerase_2Structures
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 Epimerase_2 domain has been found. There are 20 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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UDP-N-acetyl-D-mannosamine
Archea
Eukaryota
Bacteria
Other sequences
Viruses
Unclassified
Viroids
Unclassified sequence