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Protein

UDP-glucose 4-epimerase

Gene

galE

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in the metabolism of galactose. Catalyzes the conversion of UDP-galactose (UDP-Gal) to UDP-glucose (UDP-Glc) through a mechanism involving the transient reduction of NAD. It is only active on UDP-galactose and UDP-glucose.1 Publication

Catalytic activityi

UDP-alpha-D-glucose = UDP-alpha-D-galactose.1 Publication

Cofactori

NAD+8 Publications

Enzyme regulationi

Inhibited by UDP-phenol and NaBH3CN.2 Publications

Kineticsi

Kcat is 760 sec(-1) for UDP-Glc (at pH 8.5 and 27 degrees Celsius) and 24 sec(-1) for UDP-Gal (at pH 8.5).
  1. KM=18 µM for UDP-Gal (at pH 8.5)3 Publications
  2. KM=160 µM for UDP-Gal (at pH 8.5 and 27 degrees Celsius)3 Publications
  3. KM=225 µM for UDP-Glc (at pH 8.5 and 27 degrees Celsius)3 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 sitei99NAD9 Publications1
    Binding sitei124NAD9 Publications1
    Binding sitei124Substrate1
    Active sitei149Proton acceptor1 Publication1
    Binding sitei149NAD9 Publications1
    Binding sitei149Substrate1
    Binding sitei153NAD9 Publications1
    Binding sitei178NAD; via carbonyl oxygen9 Publications1
    Binding sitei179Substrate1
    Binding sitei231Substrate1
    Binding sitei299Substrate1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Nucleotide bindingi11 – 12NAD9 Publications2
    Nucleotide bindingi31 – 36NAD9 Publications6
    Nucleotide bindingi58 – 59NAD9 Publications2
    Nucleotide bindingi80 – 84NAD9 Publications5

    GO - Molecular functioni

    • identical protein binding Source: IntAct
    • NAD+ binding Source: EcoCyc
    • racemase and epimerase activity, acting on carbohydrates and derivatives Source: EcoliWiki
    • UDP-glucose 4-epimerase activity Source: EcoCyc

    GO - Biological processi

    • carbohydrate metabolic process Source: EcoliWiki
    • colanic acid biosynthetic process Source: EcoCyc
    • galactose catabolic process via UDP-galactose Source: EcoCyc
    • galactose metabolic process Source: EcoliWiki

    Keywordsi

    Molecular functionIsomerase
    Biological processCarbohydrate metabolism, Galactose metabolism
    LigandNAD

    Enzyme and pathway databases

    BioCyciEcoCyc:UDPGLUCEPIM-MONOMER.
    MetaCyc:UDPGLUCEPIM-MONOMER.
    BRENDAi5.1.3.2. 2026.
    SABIO-RKiP09147.
    UniPathwayiUPA00214.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    UDP-glucose 4-epimerase (EC:5.1.3.2)
    Alternative name(s):
    Galactowaldenase
    UDP-galactose 4-epimerase
    Gene namesi
    Name:galE
    Synonyms:galD
    Ordered Locus Names:b0759, JW0742
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
    Proteomesi
    • UP000000318 Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG10362. galE.

    Subcellular locationi

    GO - Cellular componenti

    • cytoplasm Source: EcoliWiki
    • cytosol Source: UniProtKB

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi124S → A: No major structural changes. Catalytic efficiency is very low and affinity binding is 21% of the wild-type enzyme. 3 Publications1
    Mutagenesisi124S → T: No major structural changes. Catalytic efficiency is about 30% of that of the wild-type enzyme, and affinity binding is similar to that of the native enzyme. 3 Publications1
    Mutagenesisi149Y → F: No major structural changes. Catalytic efficiency is very low and affinity binding is 12% of the wild-type enzyme. 2 Publications1
    Mutagenesisi153K → A: Decreases the catalytic activity. Not reduced by sugars in the presence or absence of UMP. It contains very little NADH. 1 Publication1
    Mutagenesisi153K → M: Decreases the catalytic activity. Not reduced by sugars in the presence or absence of UMP. It contains very little NADH. 1 Publication1
    Mutagenesisi299Y → C: Loss of epimerase activity with UDP-Gal by almost 5-fold, but it results in a gain of epimerase activity with uridine diphosphate N-acetylglucosamine (UDP-GlcNAc) by 230-fold with minimal changes in its three-dimensional structure. 1 Publication1

    Chemistry databases

    DrugBankiDB02790. Phenyl-Uridine-5'-Diphosphate.
    DB01861. Uridine diphosphate glucose.
    DB03435. Uridine-5'-Diphosphate.
    DB04097. Uridine-5'-Diphosphate-4-Deoxy-4-Fluoro-Alpha-D-Galactose.
    DB02421. Uridine-5'-Diphosphate-Mannose.
    DB03397. Uridine-Diphosphate-N-Acetylglucosamine.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00001832031 – 338UDP-glucose 4-epimeraseAdd BLAST338

    Proteomic databases

    PaxDbiP09147.
    PRIDEiP09147.

    2D gel databases

    SWISS-2DPAGEiP09147.

    Expressioni

    Inductioni

    By D-galactose and D-fucose.1 Publication

    Interactioni

    Subunit structurei

    Homodimer.11 Publications

    Binary interactionsi

    Show more details

    GO - Molecular functioni

    • identical protein binding Source: IntAct

    Protein-protein interaction databases

    BioGridi4261900. 143 interactors.
    DIPiDIP-9728N.
    IntActiP09147. 15 interactors.
    STRINGi316385.ECDH10B_0827.

    Structurei

    Secondary structure

    1338
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi2 – 6Combined sources5
    Turni7 – 9Combined sources3
    Helixi11 – 22Combined sources12
    Beta strandi26 – 31Combined sources6
    Beta strandi34 – 36Combined sources3
    Helixi38 – 40Combined sources3
    Helixi41 – 48Combined sources8
    Beta strandi53 – 56Combined sources4
    Helixi62 – 71Combined sources10
    Beta strandi75 – 79Combined sources5
    Helixi86 – 91Combined sources6
    Helixi93 – 114Combined sources22
    Beta strandi118 – 124Combined sources7
    Helixi125 – 128Combined sources4
    Beta strandi134 – 136Combined sources3
    Helixi148 – 166Combined sources19
    Beta strandi171 – 177Combined sources7
    Beta strandi179 – 181Combined sources3
    Beta strandi187 – 189Combined sources3
    Beta strandi194 – 196Combined sources3
    Helixi200 – 208Combined sources9
    Beta strandi211 – 213Combined sources3
    Beta strandi215 – 218Combined sources4
    Beta strandi222 – 224Combined sources3
    Beta strandi233 – 235Combined sources3
    Helixi236 – 250Combined sources15
    Beta strandi255 – 262Combined sources8
    Helixi269 – 280Combined sources12
    Beta strandi286 – 289Combined sources4
    Helixi304 – 310Combined sources7
    Helixi318 – 331Combined sources14

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1A9YX-ray1.80A1-338[»]
    1A9ZX-ray1.90A1-338[»]
    1KVQX-ray2.15A1-338[»]
    1KVRX-ray1.90A1-338[»]
    1KVSX-ray2.15A1-338[»]
    1KVTX-ray2.15A1-338[»]
    1KVUX-ray1.90A1-338[»]
    1LRJX-ray1.90A1-338[»]
    1LRKX-ray1.75A1-338[»]
    1LRLX-ray1.80A1-338[»]
    1NAHX-ray1.80A1-338[»]
    1NAIX-ray2.00A1-338[»]
    1UDAX-ray1.80A1-338[»]
    1UDBX-ray1.65A1-338[»]
    1UDCX-ray1.65A1-338[»]
    1XELX-ray1.80A1-338[»]
    2UDPX-ray1.80A/B1-338[»]
    5GY7X-ray1.43A/B1-338[»]
    ProteinModelPortaliP09147.
    SMRiP09147.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP09147.

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni199 – 200Substrate binding2
    Regioni216 – 218Substrate binding3
    Regioni292 – 295Substrate binding4

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiENOG4105CMR. Bacteria.
    COG1087. LUCA.
    HOGENOMiHOG000168001.
    InParanoidiP09147.
    KOiK01784.
    PhylomeDBiP09147.

    Family and domain databases

    CDDicd05247. UDP_G4E_1_SDR_e. 1 hit.
    InterProiView protein in InterPro
    IPR016040. NAD(P)-bd_dom.
    IPR005886. UDP_G4E.
    PfamiView protein in Pfam
    PF16363. GDP_Man_Dehyd. 1 hit.
    SUPFAMiSSF51735. SSF51735. 1 hit.
    TIGRFAMsiTIGR01179. galE. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P09147-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MRVLVTGGSG YIGSHTCVQL LQNGHDVIIL DNLCNSKRSV LPVIERLGGK
    60 70 80 90 100
    HPTFVEGDIR NEALMTEILH DHAIDTVIHF AGLKAVGESV QKPLEYYDNN
    110 120 130 140 150
    VNGTLRLISA MRAANVKNFI FSSSATVYGD QPKIPYVESF PTGTPQSPYG
    160 170 180 190 200
    KSKLMVEQIL TDLQKAQPDW SIALLRYFNP VGAHPSGDMG EDPQGIPNNL
    210 220 230 240 250
    MPYIAQVAVG RRDSLAIFGN DYPTEDGTGV RDYIHVMDLA DGHVVAMEKL
    260 270 280 290 300
    ANKPGVHIYN LGAGVGNSVL DVVNAFSKAC GKPVNYHFAP RREGDLPAYW
    310 320 330
    ADASKADREL NWRVTRTLDE MAQDTWHWQS RHPQGYPD
    Length:338
    Mass (Da):37,265
    Last modified:July 1, 1989 - v1
    Checksum:i5CA8B4F7903F7792
    GO

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Sequence conflicti140 – 145FPTGTP → LLPIPG in CAA35813 (PubMed:2134186).Curated6

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    X06226 Genomic DNA. Translation: CAA29573.1.
    U00096 Genomic DNA. Translation: AAC73846.1.
    AP009048 Genomic DNA. Translation: BAA35421.1.
    X51449 Genomic DNA. Translation: CAA35813.1.
    U07867 Genomic DNA. Translation: AAB06890.1.
    J01613 Genomic DNA. Translation: AAA87978.1.
    PIRiS02089. XUECUG.
    RefSeqiNP_415280.3. NC_000913.3.
    WP_001265438.1. NZ_LN832404.1.

    Genome annotation databases

    EnsemblBacteriaiAAC73846; AAC73846; b0759.
    BAA35421; BAA35421; BAA35421.
    GeneIDi945354.
    KEGGiecj:JW0742.
    eco:b0759.
    PATRICifig|1411691.4.peg.1519.

    Similar proteinsi

    Entry informationi

    Entry nameiGALE_ECOLI
    AccessioniPrimary (citable) accession number: P09147
    Secondary accession number(s): Q47493
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 1, 1989
    Last sequence update: July 1, 1989
    Last modified: August 30, 2017
    This is version 161 of the entry and version 1 of the sequence. See complete history.
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families