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Information on EC 5.1.3.7 - UDP-N-acetylglucosamine 4-epimerase and Organism(s) Plesiomonas shigelloides and UniProt Accession Q7BJX9

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This record set is specific for:
Plesiomonas shigelloides
UNIPROT: Q7BJX9 not found.
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Word Map
The taxonomic range for the selected organisms is: Plesiomonas shigelloides
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
uae, udp-n-acetylglucosamine 4-epimerase, udp-n-acetylglucosamine 4'-epimerase, udp-galnac 4-epimerase, udp-glcnac epimerase, gne epimerase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
group 3 epimerase
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UDP-GalNAc 4-epimerase
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UDP-hexose 4-epimerase
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UDP-sugar 4-epimerase
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UDPGlcNAc 4-epimerase
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Epimerase, uridine diphosphoacetylglucosamine
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-
-
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UDP acetylglucosamine epimerase
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-
-
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Uridine 5'-diphospho-N-acetylglucosamine-4-epimerase
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-
-
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Uridine diphosphate N-acetylglucosamine-4-epimerase
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-
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Uridine diphosphoacetylglucosamine epimerase
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-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
epimerization
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
UDP-N-acetyl-D-glucosamine 4-epimerase
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CAS REGISTRY NUMBER
COMMENTARY hide
9024-16-2
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
UDP-GlcNAc
UDP-GalNAc
show the reaction diagram
-
-
-
r
UDP-N-acetyl-alpha-D-glucosamine
UDP-N-acetyl-alpha-D-galactosamine
show the reaction diagram
-
-
-
r
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
UDP-N-acetyl-alpha-D-glucosamine
UDP-N-acetyl-alpha-D-galactosamine
show the reaction diagram
-
-
-
r
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
UDP-Gal 4-epimerases and the other GalE-like UDP-sugar 4-epimerases belong to the short-chain dehydrogenase/reductase (SDR) superfamily of proteins. Classification of UDP-hexose 4-epimerases into three groups with distinct substrate promiscuity. Group 1 contains the 4-epimerases that exhibit a strong preference for non-acetylated substrates (such as Escherichia coli enzyme eGalE), group 2 members can epimerize both non-acetylated and N-acetylated substrates equally well (such as the human enzyme hGalE), and group 3 epimerases are very specific for N-acetylated substrates (like the WbpP from Pseudomonas aeruginosa). The enzyme from Pleisomonas shigelloides is a group 3 epimerase. The model of the '297-308 belt' is proposed to determine substrate specificity in group 3 members. The belts conformation supports (i) the formation of a hydrophobic cluster that interacts with the methyl group of the N-acetyl moiety, (ii) a correct positioning of the Asn195, and (iii) orients the substrate so the GlcNAc moiety will form hydrogen bonds with Ser143 and Ser144. Due to this belt and the resulting hydrogen bond network, the group 3 members have a distinct conformation at this region whereas the conformation of group 1 and group 2 enzymes is very similar
malfunction
the S306Y mutation allows a switch from group 2 to group 1 and forms steric clashes between the group 3 epimerases and their substrates, which results in the observed loss of activity
metabolism
the enzyme is involved in biosynthetic pathway of the glycan 2-deoxy-L-altruronic acid that is found in the lipopolysaccharide of Pleisomonas shigelloides
additional information
enzyme structure and substrate specificity, comparison of the hexagonal box model of sugar-binding pockeets of several UDP-sugar 4-epimerases. Importance and flexibility of the hydrogen bond network
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
GNE_PLESH
345
0
38949
Swiss-Prot
-
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
x-ray crystallography
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
microbatch under oil method, using 250 mM ammonium sulfate, 100 mM Bis-Tris pH 6.5, (25% w/v) PEG 3350
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
S306Y
site-directed mutagenesis, the mutation allows a switch from group 2 to group 1 and forms steric clashes between the group 3 epimerases and their substrates, which results in the observed loss of activity
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
nickel-Sepharose column chromatography
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Bhatt, V.S.; Guo, C.Y.; Guan, W.; Zhao, G.; Yi, W.; Liu, Z.J.; Wang, P.G.
Altered architecture of substrate binding region defines the unique specificity of UDP-GalNAc 4-epimerases
Protein Sci.
20
856-866
2011
Plesiomonas shigelloides (Q7BJX9), Plesiomonas shigelloides O17 (Q7BJX9)
Manually annotated by BRENDA team
Beerens, K.; Soetaert, W.; Desmet, T.
UDP-hexose 4-epimerases a view on structure, mechanism and substrate specificity
Carbohydr. Res.
414
8-14
2015
Plesiomonas shigelloides (Q7BJX9), Pseudomonas aeruginosa (Q8KN66)
Manually annotated by BRENDA team