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Protein

UDP-glucose 4-epimerase

Gene

GALE

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes two distinct but analogous reactions: the reversible epimerization of UDP-glucose to UDP-galactose and the reversible epimerization of UDP-N-acetylglucosamine to UDP-N-acetylgalactosamine. The reaction with UDP-Gal plays a critical role in the Leloir pathway of galactose catabolism in which galactose is converted to the glycolytic intermediate glucose 6-phosphate. It contributes to the catabolism of dietary galactose and enables the endogenous biosynthesis of both UDP-Gal and UDP-GalNAc when exogenous sources are limited. Both UDP-sugar interconversions are important in the synthesis of glycoproteins and glycolipids.1 Publication1 Publication

Catalytic activityi

UDP-alpha-D-glucose = UDP-alpha-D-galactose.1 Publication
UDP-N-acetyl-alpha-D-glucosamine = UDP-N-acetyl-alpha-D-galactosamine.1 Publication

Cofactori

NAD+2 Publications2 Publications

Kineticsi

  1. KM=69 µM for UDP-galactose (at 37 degrees Celsius and pH 8.8)2 Publications
  1. Vmax=1.22 mmol/min/mg enzyme with UDP-galactose as substrate2 Publications

Pathwayi: galactose metabolism

This protein is involved in the pathway galactose metabolism, which is part of Carbohydrate metabolism.
View all proteins of this organism that are known to be involved in the pathway galactose metabolism and in Carbohydrate metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei88NAD; via carbonyl oxygen3 Publications1
Binding sitei92NAD3 Publications1
Active sitei157Proton acceptor1 Publication3 Publications1
Binding sitei161NAD3 Publications1
Binding sitei185NAD1 Publication1
Binding sitei239Substrate3 Publications1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi12 – 14NAD3 Publications3
Nucleotide bindingi33 – 37NAD3 Publications5
Nucleotide bindingi66 – 67NAD3 Publications2

GO - Molecular functioni

  • protein homodimerization activity Source: UniProtKB
  • UDP-glucose 4-epimerase activity Source: UniProtKB
  • UDP-N-acetylglucosamine 4-epimerase activity Source: UniProtKB-EC

GO - Biological processi

  • galactose catabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Biological processi

Carbohydrate metabolism, Galactose metabolism

Keywords - Ligandi

NAD

Enzyme and pathway databases

BioCyciMetaCyc:HS04117-MONOMER.
ZFISH:HS04117-MONOMER.
BRENDAi5.1.3.2. 2681.
ReactomeiR-HSA-70370. Galactose catabolism.
SABIO-RKQ14376.
UniPathwayiUPA00214.

Names & Taxonomyi

Protein namesi
Recommended name:
UDP-glucose 4-epimerase1 Publication (EC:5.1.3.21 Publication)
Alternative name(s):
Galactowaldenase
UDP-N-acetylgalactosamine 4-epimerase1 Publication
Short name:
UDP-GalNAc 4-epimerase1 Publication
UDP-N-acetylglucosamine 4-epimerase1 Publication (EC:5.1.3.71 Publication)
Short name:
UDP-GlcNAc 4-epimerase1 Publication
UDP-galactose 4-epimerase1 Publication
Gene namesi
Name:GALEImported
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:4116. GALE.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: Reactome
  • extracellular exosome Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Involvement in diseasei

Epimerase-deficiency galactosemia (EDG)5 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionClinical features include early-onset cataracts, liver damage, deafness and mental retardation. There are two clinically distinct forms of EDG. (1) A benign, or 'peripheral' form with no detectable GALE activity in red blood cells and characterized by mild symptoms. Some patients may suffer no symptoms beyond raised levels of galactose-1-phosphate in the blood. (2) A much rarer 'generalized' form with undetectable levels of GALE activity in all tissues and resulting in severe features such as restricted growth and mental development.
See also OMIM:230350
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_03773325A → V in EDG. 1 Publication1
Natural variantiVAR_00253934N → S in EDG; peripheral; nearly normal activity towards UDP-galactose. 3 PublicationsCorresponds to variant rs121908046dbSNPEnsembl.1
Natural variantiVAR_03773440R → C in EDG. 1 PublicationCorresponds to variant rs144492228dbSNPEnsembl.1
Natural variantiVAR_03773569D → E in EDG. 1 Publication1
Natural variantiVAR_00254090G → E in EDG; 800-fold decrease in UDP-galactose epimerization activity. 4 PublicationsCorresponds to variant rs28940882dbSNPEnsembl.1
Natural variantiVAR_01005894V → M in EDG; generalized; 30-fold decrease in UDP-galactose epimerization activity; 2-fold decrease in affinity for UDP-galactose; 24% of normal activity with respect to UDP-N-acetylgalactosamine. 4 PublicationsCorresponds to variant rs121908047dbSNPEnsembl.1
Natural variantiVAR_002541103D → G in EDG; 7-fold decrease in UDP-galactose epimerization activity; very mild decrease in activity towards UDP-N-acetylgalactosamine. 4 PublicationsCorresponds to variant rs28940883dbSNPEnsembl.1
Natural variantiVAR_037736165E → K in EDG. 1 PublicationCorresponds to variant rs528467258dbSNPEnsembl.1
Natural variantiVAR_037737169R → W in EDG. 1 PublicationCorresponds to variant rs137853859dbSNPEnsembl.1
Natural variantiVAR_002543183L → P in EDG; peripheral; 3-fold decrease in UDP-galactose epimerization activity. 3 PublicationsCorresponds to variant rs121908045dbSNPEnsembl.1
Natural variantiVAR_037738239R → W in EDG. 1 PublicationCorresponds to variant rs137853860dbSNPEnsembl.1
Natural variantiVAR_002544257K → R in EDG; 7-fold decrease in UDP-galactose epimerization activity; does not affect affinity for UDP-galactose. 4 PublicationsCorresponds to variant rs28940884dbSNPEnsembl.1
Natural variantiVAR_037739302G → D in EDG. 1 PublicationCorresponds to variant rs137853861dbSNPEnsembl.1
Natural variantiVAR_002545313L → M in EDG; 6-fold decrease in UDP-galactose epimerization activity; very mild decrease in activity towards UDP-N-acetylgalactosamine. 4 PublicationsCorresponds to variant rs3180383dbSNPEnsembl.1
Natural variantiVAR_002546319G → E in EDG; nearly normal activity towards UDP-galactose; mild impairment under conditions of substrate limitation. 4 PublicationsCorresponds to variant rs28940885dbSNPEnsembl.1
Natural variantiVAR_037740335R → H in EDG; 2-fold decrease in UDP-galactose epimerization activity. 3 PublicationsCorresponds to variant rs368637540dbSNPEnsembl.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi132S → A: Loss of activity. 1 Publication1
Mutagenesisi157Y → F: Loss of activity. 1 Publication1
Mutagenesisi307C → Y: No effect on activity towards UDP-galactose. Loss of activity towards UDP-N-acetylgalactosamine. 1 Publication1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNETi2582.
MalaCardsiGALE.
MIMi230350. phenotype.
OpenTargetsiENSG00000117308.
Orphaneti308473. Erythrocyte galactose epimerase deficiency.
308487. Generalized galactose epimerase deficiency.
PharmGKBiPA28531.

Chemistry databases

ChEMBLiCHEMBL5843.

Polymorphism and mutation databases

BioMutaiGALE.
DMDMi68056598.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001831891 – 348UDP-glucose 4-epimeraseAdd BLAST348

Proteomic databases

EPDiQ14376.
PaxDbiQ14376.
PeptideAtlasiQ14376.
PRIDEiQ14376.
TopDownProteomicsiQ14376-1. [Q14376-1]

PTM databases

iPTMnetiQ14376.
PhosphoSitePlusiQ14376.
SwissPalmiQ14376.

Expressioni

Gene expression databases

BgeeiENSG00000117308.
CleanExiHS_GALE.
ExpressionAtlasiQ14376. baseline and differential.
GenevisibleiQ14376. HS.

Organism-specific databases

HPAiHPA007340.

Interactioni

Subunit structurei

Homodimer.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself4EBI-750057,EBI-750057

GO - Molecular functioni

  • protein homodimerization activity Source: UniProtKB

Protein-protein interaction databases

BioGridi108855. 21 interactors.
IntActiQ14376. 2 interactors.
MINTiMINT-5001272.
STRINGi9606.ENSP00000363621.

Chemistry databases

BindingDBiQ14376.

Structurei

Secondary structure

1348
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi3 – 8Combined sources6
Turni9 – 11Combined sources3
Helixi13 – 24Combined sources12
Beta strandi29 – 33Combined sources5
Beta strandi35 – 38Combined sources4
Beta strandi42 – 46Combined sources5
Helixi47 – 56Combined sources10
Beta strandi61 – 64Combined sources4
Helixi70 – 79Combined sources10
Beta strandi82 – 87Combined sources6
Helixi94 – 99Combined sources6
Helixi101 – 121Combined sources21
Beta strandi126 – 132Combined sources7
Helixi133 – 136Combined sources4
Beta strandi140 – 144Combined sources5
Helixi156 – 174Combined sources19
Beta strandi179 – 185Combined sources7
Beta strandi187 – 189Combined sources3
Beta strandi195 – 197Combined sources3
Beta strandi202 – 204Combined sources3
Helixi208 – 216Combined sources9
Beta strandi219 – 221Combined sources3
Beta strandi223 – 226Combined sources4
Beta strandi230 – 236Combined sources7
Beta strandi241 – 243Combined sources3
Helixi244 – 258Combined sources15
Turni259 – 261Combined sources3
Beta strandi264 – 269Combined sources6
Helixi277 – 288Combined sources12
Beta strandi294 – 297Combined sources4
Beta strandi305 – 307Combined sources3
Helixi312 – 316Combined sources5
Helixi326 – 339Combined sources14

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1EK5X-ray1.80A1-348[»]
1EK6X-ray1.50A/B1-348[»]
1HZJX-ray1.50A/B1-348[»]
1I3KX-ray1.50A/B1-348[»]
1I3LX-ray1.50A/B1-348[»]
1I3MX-ray1.50A/B1-348[»]
1I3NX-ray1.50A/B1-348[»]
ProteinModelPortaliQ14376.
SMRiQ14376.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ14376.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni132 – 134Substrate binding1 Publication3 Publications3
Regioni185 – 187Substrate binding2 Publications3
Regioni206 – 208Substrate binding3 Publications3
Regioni224 – 226Substrate binding3 Publications3
Regioni300 – 303Substrate binding2 Publications4

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG1371. Eukaryota.
COG1087. LUCA.
GeneTreeiENSGT00530000063128.
HOGENOMiHOG000168001.
HOVERGENiHBG001396.
InParanoidiQ14376.
KOiK01784.
OMAiCGCKVYN.
OrthoDBiEOG091G0ACI.
PhylomeDBiQ14376.
TreeFamiTF105800.

Family and domain databases

Gene3Di3.40.50.720. 2 hits.
InterProiIPR005886. GalE.
IPR016040. NAD(P)-bd_dom.
IPR008089. Nuc_sugar_epim.
[Graphical view]
PfamiPF16363. GDP_Man_Dehyd. 1 hit.
[Graphical view]
PRINTSiPR01713. NUCEPIMERASE.
SUPFAMiSSF51735. SSF51735. 1 hit.
TIGRFAMsiTIGR01179. galE. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q14376-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MAEKVLVTGG AGYIGSHTVL ELLEAGYLPV VIDNFHNAFR GGGSLPESLR
60 70 80 90 100
RVQELTGRSV EFEEMDILDQ GALQRLFKKY SFMAVIHFAG LKAVGESVQK
110 120 130 140 150
PLDYYRVNLT GTIQLLEIMK AHGVKNLVFS SSATVYGNPQ YLPLDEAHPT
160 170 180 190 200
GGCTNPYGKS KFFIEEMIRD LCQADKTWNA VLLRYFNPTG AHASGCIGED
210 220 230 240 250
PQGIPNNLMP YVSQVAIGRR EALNVFGNDY DTEDGTGVRD YIHVVDLAKG
260 270 280 290 300
HIAALRKLKE QCGCRIYNLG TGTGYSVLQM VQAMEKASGK KIPYKVVARR
310 320 330 340
EGDVAACYAN PSLAQEELGW TAALGLDRMC EDLWRWQKQN PSGFGTQA
Length:348
Mass (Da):38,282
Last modified:May 10, 2005 - v2
Checksum:i06FDBF9B1943DF49
GO
Isoform 2 (identifier: Q14376-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-79: MAEKVLVTGG...QGALQRLFKK → MSPLQ

Note: No experimental confirmation available.Curated
Show »
Length:274
Mass (Da):30,180
Checksum:i1410C9CCFBC96D9E
GO

Sequence cautioni

The sequence EAW95083 differs from that shown. Reason: Erroneous gene model prediction.Curated
The sequence EAW95084 differs from that shown. Reason: Erroneous gene model prediction.Curated
The sequence EAW95086 differs from that shown. Reason: Erroneous gene model prediction.Curated
The sequence EAW95090 differs from that shown. Reason: Erroneous gene model prediction.Curated
The sequence EAW95091 differs from that shown. Reason: Erroneous gene model prediction.Curated
The sequence EAW95092 differs from that shown. Reason: Erroneous gene model prediction.Curated
The sequence EAW95093 differs from that shown. Reason: Erroneous gene model prediction.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti293P → S in BAG51901 (PubMed:14702039).1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_03773325A → V in EDG. 1 Publication1
Natural variantiVAR_00253934N → S in EDG; peripheral; nearly normal activity towards UDP-galactose. 3 PublicationsCorresponds to variant rs121908046dbSNPEnsembl.1
Natural variantiVAR_03773440R → C in EDG. 1 PublicationCorresponds to variant rs144492228dbSNPEnsembl.1
Natural variantiVAR_03773569D → E in EDG. 1 Publication1
Natural variantiVAR_00254090G → E in EDG; 800-fold decrease in UDP-galactose epimerization activity. 4 PublicationsCorresponds to variant rs28940882dbSNPEnsembl.1
Natural variantiVAR_01005894V → M in EDG; generalized; 30-fold decrease in UDP-galactose epimerization activity; 2-fold decrease in affinity for UDP-galactose; 24% of normal activity with respect to UDP-N-acetylgalactosamine. 4 PublicationsCorresponds to variant rs121908047dbSNPEnsembl.1
Natural variantiVAR_002541103D → G in EDG; 7-fold decrease in UDP-galactose epimerization activity; very mild decrease in activity towards UDP-N-acetylgalactosamine. 4 PublicationsCorresponds to variant rs28940883dbSNPEnsembl.1
Natural variantiVAR_037736165E → K in EDG. 1 PublicationCorresponds to variant rs528467258dbSNPEnsembl.1
Natural variantiVAR_037737169R → W in EDG. 1 PublicationCorresponds to variant rs137853859dbSNPEnsembl.1
Natural variantiVAR_002542180A → V.2 PublicationsCorresponds to variant rs3204468dbSNPEnsembl.1
Natural variantiVAR_002543183L → P in EDG; peripheral; 3-fold decrease in UDP-galactose epimerization activity. 3 PublicationsCorresponds to variant rs121908045dbSNPEnsembl.1
Natural variantiVAR_037738239R → W in EDG. 1 PublicationCorresponds to variant rs137853860dbSNPEnsembl.1
Natural variantiVAR_002544257K → R in EDG; 7-fold decrease in UDP-galactose epimerization activity; does not affect affinity for UDP-galactose. 4 PublicationsCorresponds to variant rs28940884dbSNPEnsembl.1
Natural variantiVAR_037739302G → D in EDG. 1 PublicationCorresponds to variant rs137853861dbSNPEnsembl.1
Natural variantiVAR_002545313L → M in EDG; 6-fold decrease in UDP-galactose epimerization activity; very mild decrease in activity towards UDP-N-acetylgalactosamine. 4 PublicationsCorresponds to variant rs3180383dbSNPEnsembl.1
Natural variantiVAR_002546319G → E in EDG; nearly normal activity towards UDP-galactose; mild impairment under conditions of substrate limitation. 4 PublicationsCorresponds to variant rs28940885dbSNPEnsembl.1
Natural variantiVAR_037740335R → H in EDG; 2-fold decrease in UDP-galactose epimerization activity. 3 PublicationsCorresponds to variant rs368637540dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0568221 – 79MAEKV…RLFKK → MSPLQ in isoform 2. Add BLAST79

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L41668 mRNA. Translation: AAB86498.1.
AF022382 Genomic DNA. Translation: AAC39645.1.
DQ233667 Genomic DNA. Translation: ABB04109.1.
DQ233668 mRNA. Translation: ABB04110.1.
AK057302 mRNA. Translation: BAG51901.1.
AK314397 mRNA. Translation: BAG37021.1.
AL031295 Genomic DNA. Translation: CAB40159.1.
CH471134 Genomic DNA. Translation: EAW95083.1. Sequence problems.
CH471134 Genomic DNA. Translation: EAW95084.1. Sequence problems.
CH471134 Genomic DNA. Translation: EAW95086.1. Sequence problems.
CH471134 Genomic DNA. Translation: EAW95090.1. Sequence problems.
CH471134 Genomic DNA. Translation: EAW95091.1. Sequence problems.
CH471134 Genomic DNA. Translation: EAW95092.1. Sequence problems.
CH471134 Genomic DNA. Translation: EAW95093.1. Sequence problems.
BC001273 mRNA. Translation: AAH01273.1.
BC050685 mRNA. Translation: AAH50685.2.
CCDSiCCDS242.1. [Q14376-1]
RefSeqiNP_000394.2. NM_000403.3. [Q14376-1]
NP_001008217.1. NM_001008216.1. [Q14376-1]
NP_001121093.1. NM_001127621.1. [Q14376-1]
UniGeneiHs.632380.

Genome annotation databases

EnsembliENST00000374497; ENSP00000363621; ENSG00000117308. [Q14376-1]
ENST00000617979; ENSP00000483375; ENSG00000117308. [Q14376-1]
GeneIDi2582.
KEGGihsa:2582.
UCSCiuc001bhv.2. human. [Q14376-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L41668 mRNA. Translation: AAB86498.1.
AF022382 Genomic DNA. Translation: AAC39645.1.
DQ233667 Genomic DNA. Translation: ABB04109.1.
DQ233668 mRNA. Translation: ABB04110.1.
AK057302 mRNA. Translation: BAG51901.1.
AK314397 mRNA. Translation: BAG37021.1.
AL031295 Genomic DNA. Translation: CAB40159.1.
CH471134 Genomic DNA. Translation: EAW95083.1. Sequence problems.
CH471134 Genomic DNA. Translation: EAW95084.1. Sequence problems.
CH471134 Genomic DNA. Translation: EAW95086.1. Sequence problems.
CH471134 Genomic DNA. Translation: EAW95090.1. Sequence problems.
CH471134 Genomic DNA. Translation: EAW95091.1. Sequence problems.
CH471134 Genomic DNA. Translation: EAW95092.1. Sequence problems.
CH471134 Genomic DNA. Translation: EAW95093.1. Sequence problems.
BC001273 mRNA. Translation: AAH01273.1.
BC050685 mRNA. Translation: AAH50685.2.
CCDSiCCDS242.1. [Q14376-1]
RefSeqiNP_000394.2. NM_000403.3. [Q14376-1]
NP_001008217.1. NM_001008216.1. [Q14376-1]
NP_001121093.1. NM_001127621.1. [Q14376-1]
UniGeneiHs.632380.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1EK5X-ray1.80A1-348[»]
1EK6X-ray1.50A/B1-348[»]
1HZJX-ray1.50A/B1-348[»]
1I3KX-ray1.50A/B1-348[»]
1I3LX-ray1.50A/B1-348[»]
1I3MX-ray1.50A/B1-348[»]
1I3NX-ray1.50A/B1-348[»]
ProteinModelPortaliQ14376.
SMRiQ14376.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108855. 21 interactors.
IntActiQ14376. 2 interactors.
MINTiMINT-5001272.
STRINGi9606.ENSP00000363621.

Chemistry databases

BindingDBiQ14376.
ChEMBLiCHEMBL5843.

PTM databases

iPTMnetiQ14376.
PhosphoSitePlusiQ14376.
SwissPalmiQ14376.

Polymorphism and mutation databases

BioMutaiGALE.
DMDMi68056598.

Proteomic databases

EPDiQ14376.
PaxDbiQ14376.
PeptideAtlasiQ14376.
PRIDEiQ14376.
TopDownProteomicsiQ14376-1. [Q14376-1]

Protocols and materials databases

DNASUi2582.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000374497; ENSP00000363621; ENSG00000117308. [Q14376-1]
ENST00000617979; ENSP00000483375; ENSG00000117308. [Q14376-1]
GeneIDi2582.
KEGGihsa:2582.
UCSCiuc001bhv.2. human. [Q14376-1]

Organism-specific databases

CTDi2582.
DisGeNETi2582.
GeneCardsiGALE.
GeneReviewsiGALE.
HGNCiHGNC:4116. GALE.
HPAiHPA007340.
MalaCardsiGALE.
MIMi230350. phenotype.
606953. gene.
neXtProtiNX_Q14376.
OpenTargetsiENSG00000117308.
Orphaneti308473. Erythrocyte galactose epimerase deficiency.
308487. Generalized galactose epimerase deficiency.
PharmGKBiPA28531.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1371. Eukaryota.
COG1087. LUCA.
GeneTreeiENSGT00530000063128.
HOGENOMiHOG000168001.
HOVERGENiHBG001396.
InParanoidiQ14376.
KOiK01784.
OMAiCGCKVYN.
OrthoDBiEOG091G0ACI.
PhylomeDBiQ14376.
TreeFamiTF105800.

Enzyme and pathway databases

UniPathwayiUPA00214.
BioCyciMetaCyc:HS04117-MONOMER.
ZFISH:HS04117-MONOMER.
BRENDAi5.1.3.2. 2681.
ReactomeiR-HSA-70370. Galactose catabolism.
SABIO-RKQ14376.

Miscellaneous databases

EvolutionaryTraceiQ14376.
GenomeRNAii2582.
PROiQ14376.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000117308.
CleanExiHS_GALE.
ExpressionAtlasiQ14376. baseline and differential.
GenevisibleiQ14376. HS.

Family and domain databases

Gene3Di3.40.50.720. 2 hits.
InterProiIPR005886. GalE.
IPR016040. NAD(P)-bd_dom.
IPR008089. Nuc_sugar_epim.
[Graphical view]
PfamiPF16363. GDP_Man_Dehyd. 1 hit.
[Graphical view]
PRINTSiPR01713. NUCEPIMERASE.
SUPFAMiSSF51735. SSF51735. 1 hit.
TIGRFAMsiTIGR01179. galE. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiGALE_HUMAN
AccessioniPrimary (citable) accession number: Q14376
Secondary accession number(s): A0A024RAH5
, B3KQ39, Q38G75, Q86W41, Q9BVE3, Q9UJB4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: May 10, 2005
Last modified: November 30, 2016
This is version 176 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Miscellaneous

Contrary to the human enzyme, the E.coli ortholog (AC P09147) does not catalyze the epimerization of UDP-N-acetylglucosamine to UDP-N-acetylgalactosamine. Compared to the E.coli enzyme, the sugar-binding pocket of the active site is 15% larger for the human enzyme, making it possible to accommodate the acetyl group.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.