UDP-glucose 4-epimerase

UDP-glucose 4-epimerase
Identifiers
AliasesUDPgalactose 4-epimerase4-epimeraseuridine diphosphate glucose 4-epimeraseUDPG-4-epimeraseUDP-galactose 4-epimeraseuridine diphosphoglucose epimeraseuridine diphospho-galactose-4-epimeraseUDP-D-galactose 4-epimeraseUDP-glucose epimeraseuridine diphosphoglucose 4-epimeraseuridine diphosphate galactose 4-epimerase
External IDsGeneCards: ; OMA:- orthologs
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human
UDP-glucose 4-epimerase
H. sapiens UDP-glucose 4-epimerase homodimer bound to NADH and UDP-glucose. Domains: N-terminal and C-terminal.
Identifiers
EC no.5.1.3.2
CAS no.9032-89-7
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins
UDP-galactose-4-epimerase
Human GALE bound to NAD+ and UDP-GlcNAc, with N- and C-terminal domains highlighted. Asn 207 contorts to accommodate UDP-GlcNAc within the active site.
Identifiers
SymbolGALE
NCBI gene2582
HGNC4116
OMIM606953
RefSeqNM_000403
UniProtQ14376
Other data
EC number5.1.3.2
LocusChr. 1 p36-p35
Search for
StructuresSwiss-model
DomainsInterPro
NAD-dependent epimerase/dehydratase
Identifiers
Symbol?
PfamPF01370
InterProIPR001509
Membranome330
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary

The enzyme UDP-glucose 4-epimerase (EC 5.1.3.2), also known as UDP-galactose 4-epimerase or GALE, is a homodimeric epimerase found in bacterial, fungal, plant, and mammalian cells. This enzyme performs the final step in the Leloir pathway of galactose metabolism, catalyzing the reversible conversion of UDP-galactose to UDP-glucose. GALE tightly binds nicotinamide adenine dinucleotide (NAD+), a co-factor required for catalytic activity.

Additionally, human and some bacterial GALE isoforms reversibly catalyze the formation of UDP-N-acetylgalactosamine (UDP-GalNAc) from UDP-N-acetylglucosamine (UDP-GlcNAc) in the presence of NAD+, an initial step in glycoprotein or glycolipid synthesis.