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Information on EC 5.1.3.2 - UDP-glucose 4-epimerase and Organism(s) Drosophila melanogaster and UniProt Accession Q9W0P5

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EC Tree
     5 Isomerases
         5.1 Racemases and epimerases
             5.1.3 Acting on carbohydrates and derivatives
                5.1.3.2 UDP-glucose 4-epimerase
IUBMB Comments
Requires NAD+. Also acts on UDP-2-deoxyglucose.
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This record set is specific for:
Drosophila melanogaster
UNIPROT: Q9W0P5
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Word Map
The taxonomic range for the selected organisms is: Drosophila melanogaster
The enzyme appears in selected viruses and cellular organisms
Synonyms
gal10, udp-galactose 4-epimerase, 4-epimerase, udp-glucose 4-epimerase, udp-galactose-4-epimerase, udp-galactose 4'-epimerase, udp-glucose 4'-epimerase, udp-glucose-4-epimerase, udp-glucose epimerase, gal10p, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
UDP-Gal 4-epimerase
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UDP-hexose 4-epimerase
-
UDP-sugar 4-epimerase
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Uridine diphosphate galactose 4-epimerase
-
4-Epimerase
-
-
-
-
Epimerase, uridine diphosphoglucose
-
-
-
-
Galactowaldenase
-
-
-
-
UDP-D-galactose 4-epimerase
-
-
-
-
UDP-galactose 4-epimerase
-
-
-
-
UDP-glucose epimerase
-
-
-
-
UDPG-4-epimerase
-
-
-
-
UDPgalactose 4-epimerase
-
-
-
-
Uridine diphosphate galactose 4-epimerase
-
-
-
-
Uridine diphosphate glucose 4-epimerase
-
-
-
-
Uridine diphospho-galactose-4-epimerase
-
-
-
-
Uridine diphosphoglucose 4-epimerase
-
-
-
-
Uridine diphosphoglucose epimerase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
UDP-alpha-D-glucose = UDP-alpha-D-galactose
show the reaction diagram
reaction mechanism, overview
SYSTEMATIC NAME
IUBMB Comments
UDP-glucose 4-epimerase
Requires NAD+. Also acts on UDP-2-deoxyglucose.
CAS REGISTRY NUMBER
COMMENTARY hide
9032-89-7
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
UDP-alpha-D-glucose
UDP-alpha-D-galactose
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-alpha-D-glucose
UDP-alpha-D-galactose
show the reaction diagram
-
-
-
r
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)
metabolism
UDP-sugar 4-epimerase (GalE) is one of enzymes in the Leloir pathway
physiological function
UDP-galactose 4-epimerase plays an essential role in development and homeostasis of Drosophila that extends beyond the Leloir pathway. UDP-galactose 4-epimerase is important for the biosynthesis of polysaccharide structures
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
GALE_DROME
350
0
38697
Swiss-Prot
other Location (Reliability: 3)
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Beerens, K.; Soetaert, W.; Desmet, T.
UDP-hexose 4-epimerases a view on structure, mechanism and substrate specificity
Carbohydr. Res.
414
8-14
2015
Marinithermus hydrothermalis (F2NQX6), Thermus thermophilus (F6DEY6), Saccharomyces cerevisiae (P04397), Escherichia coli (P09147), Streptococcus thermophilus (P21977), Homo sapiens (Q14376), Homo sapiens, Drosophila melanogaster (Q9W0P5), Saccharomyces cerevisiae ATCC 204508 / S288c (P04397), Thermus thermophilus SG0.5JP17-16 (F6DEY6), Marinithermus hydrothermalis DSM 14884 / JCM 11576 / T1 (F2NQX6)
Manually annotated by BRENDA team