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20  structures 3029  species 1  interaction 4483  sequences 13  architectures

Family: Epimerase_2 (PF02350)

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
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
UDP-N-acetylglucosamine 2-epimerase
PDB 1vgv EBI.jpg
crystal structure of udp-n-acetylglucosamine_2 epimerase
Identifiers
Symbol Epimerase_2
Pfam PF02350
Pfam clan CL0113
InterPro IPR003331
SCOP 1f6d
SUPERFAMILY 1f6d

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 \rightleftharpoons 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] An inhibitor of the bacterial 2-epimerase, epimerox, has been described. Some of these enzymes are bifunctional. The UDP-N-acetylglucosamine 2-epimerase from rat liver displays both epimerase and kinase activity.[3]

Structural studies[edit]

As of late 2007, 4 structures have been solved for this class of enzymes, with PDB accession codes 1F6D, 1O6C, 1V4V, and 1VGV.

References[edit]

  1. ^ 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. 
  2. ^ 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. 
  3. ^ 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. 

Further reading[edit]

  • 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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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.

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

  1. 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

  2. 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

  3. 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

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

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Domain organisation

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Alignments

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Full
(4483)
Representative proteomes NCBI
(3343)
Meta
(2891)
RP15
(306)
RP35
(604)
RP55
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RP75
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  Seed
(187)
Full
(4483)
Representative proteomes NCBI
(3343)
Meta
(2891)
RP15
(306)
RP35
(604)
RP55
(780)
RP75
(922)
Alignment:
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  Seed
(187)
Full
(4483)
Representative proteomes NCBI
(3343)
Meta
(2891)
RP15
(306)
RP35
(604)
RP55
(780)
RP75
(922)
Raw Stockholm Download   Download   Download   Download   Download   Download   Download   Download  
Gzipped Download   Download   Download   Download   Download   Download   Download   Download  

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.

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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.

Curation View help on the curation process

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 View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 22.8 22.8
Trusted cut-off 22.8 22.8
Noise cut-off 22.7 22.7
Model length: 346
Family (HMM) version: 14
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Species distribution

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Interactions

There is 1 interaction for this family. More...

Epimerase_2

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 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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