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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)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei99 – 991NAD9 Publications
    Binding sitei124 – 1241NAD9 Publications
    Binding sitei124 – 1241Substrate
    Active sitei149 – 1491Proton acceptor1 Publication
    Binding sitei149 – 1491NAD9 Publications
    Binding sitei149 – 1491Substrate
    Binding sitei153 – 1531NAD9 Publications
    Binding sitei178 – 1781NAD; via carbonyl oxygen9 Publications
    Binding sitei179 – 1791Substrate
    Binding sitei231 – 2311Substrate
    Binding sitei299 – 2991Substrate

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi11 – 122NAD9 Publications
    Nucleotide bindingi31 – 366NAD9 Publications
    Nucleotide bindingi58 – 592NAD9 Publications
    Nucleotide bindingi80 – 845NAD9 Publications

    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
    Complete GO annotation...

    Keywords - Molecular functioni

    Isomerase

    Keywords - Biological processi

    Carbohydrate metabolism, Galactose metabolism

    Keywords - Ligandi

    NAD

    Enzyme and pathway databases

    BioCyciEcoCyc:UDPGLUCEPIM-MONOMER.
    ECOL316407:JW0742-MONOMER.
    MetaCyc:UDPGLUCEPIM-MONOMER.
    BRENDAi5.1.3.2. 2026.
    SABIO-RKP09147.
    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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    Proteomesi
    • UP000000318 Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG10362. galE.

    Subcellular locationi

    GO - Cellular componenti

    • cytoplasm Source: EcoliWiki
    • cytosol Source: UniProtKB
    Complete GO annotation...

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi124 – 1241S → A: No major structural changes. Catalytic efficiency is very low and affinity binding is 21% of the wild-type enzyme. 3 Publications
    Mutagenesisi124 – 1241S → 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 Publications
    Mutagenesisi149 – 1491Y → F: No major structural changes. Catalytic efficiency is very low and affinity binding is 12% of the wild-type enzyme. 2 Publications
    Mutagenesisi153 – 1531K → A: Decreases the catalytic activity. Not reduced by sugars in the presence or absence of UMP. It contains very little NADH. 1 Publication
    Mutagenesisi153 – 1531K → M: Decreases the catalytic activity. Not reduced by sugars in the presence or absence of UMP. It contains very little NADH. 1 Publication
    Mutagenesisi299 – 2991Y → 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 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 338338UDP-glucose 4-epimerasePRO_0000183203Add
    BLAST

    Proteomic databases

    EPDiP09147.
    PaxDbiP09147.
    PRIDEiP09147.

    2D gel databases

    SWISS-2DPAGEP09147.

    Expressioni

    Inductioni

    By D-galactose and D-fucose.1 Publication

    Interactioni

    Subunit structurei

    Homodimer.11 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself3EBI-909010,EBI-909010
    yjjWP394092EBI-909010,EBI-9132384

    GO - Molecular functioni

    • identical protein binding Source: IntAct

    Protein-protein interaction databases

    BioGridi4261900. 143 interactions.
    DIPiDIP-9728N.
    IntActiP09147. 15 interactions.
    STRINGi511145.b0759.

    Structurei

    Secondary structure

    1
    338
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi2 – 65Combined sources
    Turni7 – 93Combined sources
    Helixi11 – 2212Combined sources
    Beta strandi26 – 316Combined sources
    Beta strandi34 – 363Combined sources
    Helixi40 – 489Combined sources
    Beta strandi53 – 564Combined sources
    Helixi62 – 7110Combined sources
    Beta strandi75 – 795Combined sources
    Helixi86 – 916Combined sources
    Helixi93 – 11422Combined sources
    Beta strandi118 – 1247Combined sources
    Helixi125 – 1284Combined sources
    Beta strandi133 – 1364Combined sources
    Helixi148 – 16619Combined sources
    Beta strandi171 – 1777Combined sources
    Beta strandi179 – 1813Combined sources
    Beta strandi187 – 1893Combined sources
    Beta strandi194 – 1963Combined sources
    Helixi200 – 2089Combined sources
    Beta strandi211 – 2133Combined sources
    Beta strandi215 – 2184Combined sources
    Beta strandi222 – 2287Combined sources
    Beta strandi233 – 2353Combined sources
    Helixi236 – 25015Combined sources
    Beta strandi255 – 2628Combined sources
    Helixi269 – 28012Combined sources
    Beta strandi286 – 2894Combined sources
    Helixi304 – 3107Combined sources
    Helixi318 – 33114Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    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[»]
    ProteinModelPortaliP09147.
    SMRiP09147. Positions 1-338.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP09147.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni199 – 2002Substrate binding
    Regioni216 – 2183Substrate binding
    Regioni292 – 2954Substrate binding

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiENOG4105CMR. Bacteria.
    COG1087. LUCA.
    HOGENOMiHOG000168001.
    InParanoidiP09147.
    KOiK01784.
    OMAiCGCKVYN.
    OrthoDBiEOG6WHNS9.
    PhylomeDBiP09147.

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    InterProiIPR005886. GalE.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view]
    PfamiPF16363. GDP_Man_Dehyd. 1 hit.
    [Graphical view]
    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)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti140 – 1456FPTGTP → LLPIPG in CAA35813 (PubMed:2134186).Curated

    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.
    PATRICi32116719. VBIEscCol129921_0785.

    Cross-referencesi

    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.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    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[»]
    ProteinModelPortaliP09147.
    SMRiP09147. Positions 1-338.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi4261900. 143 interactions.
    DIPiDIP-9728N.
    IntActiP09147. 15 interactions.
    STRINGi511145.b0759.

    2D gel databases

    SWISS-2DPAGEP09147.

    Proteomic databases

    EPDiP09147.
    PaxDbiP09147.
    PRIDEiP09147.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC73846; AAC73846; b0759.
    BAA35421; BAA35421; BAA35421.
    GeneIDi945354.
    KEGGiecj:JW0742.
    eco:b0759.
    PATRICi32116719. VBIEscCol129921_0785.

    Organism-specific databases

    EchoBASEiEB0357.
    EcoGeneiEG10362. galE.

    Phylogenomic databases

    eggNOGiENOG4105CMR. Bacteria.
    COG1087. LUCA.
    HOGENOMiHOG000168001.
    InParanoidiP09147.
    KOiK01784.
    OMAiCGCKVYN.
    OrthoDBiEOG6WHNS9.
    PhylomeDBiP09147.

    Enzyme and pathway databases

    UniPathwayiUPA00214.
    BioCyciEcoCyc:UDPGLUCEPIM-MONOMER.
    ECOL316407:JW0742-MONOMER.
    MetaCyc:UDPGLUCEPIM-MONOMER.
    BRENDAi5.1.3.2. 2026.
    SABIO-RKP09147.

    Miscellaneous databases

    EvolutionaryTraceiP09147.
    PROiP09147.

    Family and domain databases

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

    Publicationsi

    « Hide 'large scale' publications
    1. "Nucleotide sequences of the gal E gene and the gal T gene of E. coli."
      Lemaire H.-G., Mueller-Hill B.
      Nucleic Acids Res. 14:7705-7711(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. Lemaire H.-G.
      Submitted (APR-1988) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    5. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
      Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
      Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    6. "Completed sequence of pKG1800, a vector for determination of transcription terminators."
      Bernardi F., Bernardi A.
      DNA Seq. 1:147-150(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-146.
    7. "Molecular analysis of the molybdate uptake operon, modABCD, of Escherichia coli and modR, a regulatory gene."
      Walkenhorst H.M., Hemschemeier S.K., Eichenlaub R.
      Microbiol. Res. 150:347-361(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-31.
      Strain: K12.
    8. "Segment-specific mutagenesis of the regulatory region in the Escherichia coli galactose operon: isolation of mutations reducing the initiation of transcription and translation."
      Busby S., Dreyfus M.
      Gene 21:121-131(1983) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-6.
    9. "The enzymes of the galactose operon in Escherichia coli. I. Purification and characterization of uridine diphosphogalactose 4-epimerase."
      Wilson D.B., Hogness D.S.
      J. Biol. Chem. 239:2469-2481(1964) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, INDUCTION.
    10. "The enzymes of the galactose operon in Escherichia coli. II. The subunits of uridine diphosphogalactose 4-epimerase."
      Wilson D.B., Hogness D.S.
      J. Biol. Chem. 244:2132-2136(1969) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT.
    11. "Identification of lysine 153 as a functionally important residue in UDP-galactose 4-epimerase from Escherichia coli."
      Swanson B.A., Frey P.A.
      Biochemistry 32:13231-13236(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF LYS-153, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR.
    12. "UDP-galactose 4-epimerase: NAD+ content and a charge-transfer band associated with the substrate-induced conformational transition."
      Liu Y., Vanhooke J.L., Frey P.A.
      Biochemistry 35:7615-7620(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: COFACTOR, SUBUNIT.
    13. "The molecular structure of UDP-galactose 4-epimerase from Escherichia coli determined at 2.5-A resolution."
      Bauer A.J., Rayment I., Frey P.A., Holden H.M.
      Proteins 12:372-381(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH NAD AND SUSBTRATE ANALOGS, ENZYME REGULATION, SUBUNIT.
    14. "Crystal structures of the oxidized and reduced forms of UDP-galactose 4-epimerase isolated from Escherichia coli."
      Thoden J.B., Frey P.A., Holden H.M.
      Biochemistry 35:2557-2566(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH NAD AND SUBSTRATE ANALOGS, COFACTOR.
    15. "Molecular structure of the NADH/UDP-glucose abortive complex of UDP-galactose 4-epimerase from Escherichia coli: implications for the catalytic mechanism."
      Thoden J.B., Frey P.A., Holden H.M.
      Biochemistry 35:5137-5144(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH NAD AND SUBSTRATE ANALOGS, ACTIVE SITE, COFACTOR.
    16. "High-resolution X-ray structure of UDP-galactose 4-epimerase complexed with UDP-phenol."
      Thoden J.B., Frey P.A., Holden H.M.
      Protein Sci. 5:2149-2161(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH NAD AND SUBSTRATE ANALOGS, COFACTOR, SUBUNIT.
    17. "Structural analysis of UDP-sugar binding to UDP-galactose 4-epimerase from Escherichia coli."
      Thoden J.B., Hegeman A.D., Wesenberg G., Chapeau M.C., Frey P.A., Holden H.M.
      Biochemistry 36:6294-6304(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) IN COMPLEX WITH NAD AND SUBSTRATE ANALOGS, COFACTOR.
    18. "Mechanistic roles of tyrosine 149 and serine 124 in UDP-galactose 4-epimerase from Escherichia coli."
      Liu Y., Thoden J.B., Kim J., Berger E., Gulick A.M., Ruzicka F.J., Holden H.M., Frey P.A.
      Biochemistry 36:10675-10684(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF MUTANT PHE-149 IN COMPLEX WITH SUBSTRATE ANALOGS AND NAD, MUTAGENESIS OF SER-124 AND TYR-149, BIOPHYSICOCHEMICAL PROPERTIES, REACTION MECHANISM, ENZYME REGULATION.
    19. "Molecular structures of the S124A, S124T, and S124V site-directed mutants of UDP-galactose 4-epimerase from Escherichia coli."
      Thoden J.B., Gulick A.M., Holden H.M.
      Biochemistry 36:10685-10695(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF MUTANTS ALA-124; THR-124 AND VAL-124 IN COMPLEX WITH SUBSTRATE ANALOGS AND NAD, MUTAGENESIS OF SER-124.
    20. "Dramatic differences in the binding of UDP-galactose and UDP-glucose to UDP-galactose 4-epimerase from Escherichia coli."
      Thoden J.B., Holden H.M.
      Biochemistry 37:11469-11477(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF DOUBLE MUTANT ALA-124/PHE-149 IN COMPLEX WITH SUBSTRATE ANALOGS AND NAD, MUTAGENESIS OF SER-124 AND TYR-149, REACTION MECHANISM, COFACTOR.
    21. "Structural analysis of the Y299C mutant of Escherichia coli UDP-galactose 4-epimerase. Teaching an old dog new tricks."
      Thoden J.B., Henderson J.M., Fridovich-Keil J.L., Holden H.M.
      J. Biol. Chem. 277:27528-27534(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF MUTANT CYS-299 IN COMPLEX WITH SUBSTRATE ANALOGS AND NAD, MUTAGENESIS OF TYR-299, SUBSTRATE SPECIFICITY, COFACTOR.

    Entry informationi

    Entry nameiGALE_ECOLI
    AccessioniPrimary (citable) accession number: P09147
    Secondary accession number(s): Q47493
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1989
    Last sequence update: July 1, 1989
    Last modified: March 16, 2016
    This is version 152 of the entry and version 1 of the sequence. [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

    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.