GALE_ECOLI
ID GALE_ECOLI Reviewed; 338 AA.
AC P09147; Q47493;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 190.
DE RecName: Full=UDP-glucose 4-epimerase;
DE EC=5.1.3.2;
DE AltName: Full=Galactowaldenase;
DE AltName: Full=UDP-galactose 4-epimerase;
GN Name=galE; Synonyms=galD; OrderedLocusNames=b0759, JW0742;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3022232; DOI=10.1093/nar/14.19.7705;
RA Lemaire H.-G., Mueller-Hill B.;
RT "Nucleotide sequences of the gal E gene and the gal T gene of E. coli.";
RL Nucleic Acids Res. 14:7705-7711(1986).
RN [2]
RP SEQUENCE REVISION.
RA Lemaire H.-G.;
RL Submitted (APR-1988) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-146.
RX PubMed=2134186; DOI=10.3109/10425179009016043;
RA Bernardi F., Bernardi A.;
RT "Completed sequence of pKG1800, a vector for determination of transcription
RT terminators.";
RL DNA Seq. 1:147-150(1990).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-31.
RC STRAIN=K12;
RX PubMed=8564363; DOI=10.1016/s0944-5013(11)80016-9;
RA Walkenhorst H.M., Hemschemeier S.K., Eichenlaub R.;
RT "Molecular analysis of the molybdate uptake operon, modABCD, of Escherichia
RT coli and modR, a regulatory gene.";
RL Microbiol. Res. 150:347-361(1995).
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-6.
RX PubMed=6301942; DOI=10.1016/0378-1119(83)90154-3;
RA Busby S., Dreyfus M.;
RT "Segment-specific mutagenesis of the regulatory region in the Escherichia
RT coli galactose operon: isolation of mutations reducing the initiation of
RT transcription and translation.";
RL Gene 21:121-131(1983).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND INDUCTION.
RX PubMed=14235524;
RA Wilson D.B., Hogness D.S.;
RT "The enzymes of the galactose operon in Escherichia coli. I. Purification
RT and characterization of uridine diphosphogalactose 4-epimerase.";
RL J. Biol. Chem. 239:2469-2481(1964).
RN [10]
RP SUBUNIT.
RX PubMed=4305667; DOI=10.1016/s0021-9258(18)94376-0;
RA Wilson D.B., Hogness D.S.;
RT "The enzymes of the galactose operon in Escherichia coli. II. The subunits
RT of uridine diphosphogalactose 4-epimerase.";
RL J. Biol. Chem. 244:2132-2136(1969).
RN [11]
RP MUTAGENESIS OF LYS-153, BIOPHYSICOCHEMICAL PROPERTIES, AND COFACTOR.
RX PubMed=8241178; DOI=10.1021/bi00211a035;
RA Swanson B.A., Frey P.A.;
RT "Identification of lysine 153 as a functionally important residue in UDP-
RT galactose 4-epimerase from Escherichia coli.";
RL Biochemistry 32:13231-13236(1993).
RN [12]
RP COFACTOR, AND SUBUNIT.
RX PubMed=8652544; DOI=10.1021/bi960102v;
RA Liu Y., Vanhooke J.L., Frey P.A.;
RT "UDP-galactose 4-epimerase: NAD+ content and a charge-transfer band
RT associated with the substrate-induced conformational transition.";
RL Biochemistry 35:7615-7620(1996).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH NAD AND SUBSTRATE
RP ANALOGS, ACTIVITY REGULATION, AND SUBUNIT.
RX PubMed=1579570; DOI=10.1002/prot.340120409;
RA Bauer A.J., Rayment I., Frey P.A., Holden H.M.;
RT "The molecular structure of UDP-galactose 4-epimerase from Escherichia coli
RT determined at 2.5-A resolution.";
RL Proteins 12:372-381(1992).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH NAD AND SUBSTRATE
RP ANALOGS, AND COFACTOR.
RX PubMed=8611559; DOI=10.1021/bi952715y;
RA Thoden J.B., Frey P.A., Holden H.M.;
RT "Crystal structures of the oxidized and reduced forms of UDP-galactose 4-
RT epimerase isolated from Escherichia coli.";
RL Biochemistry 35:2557-2566(1996).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH NAD AND SUBSTRATE
RP ANALOGS, ACTIVE SITE, AND COFACTOR.
RX PubMed=8611497; DOI=10.1021/bi9601114;
RA Thoden J.B., Frey P.A., Holden H.M.;
RT "Molecular structure of the NADH/UDP-glucose abortive complex of UDP-
RT galactose 4-epimerase from Escherichia coli: implications for the catalytic
RT mechanism.";
RL Biochemistry 35:5137-5144(1996).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH NAD AND SUBSTRATE
RP ANALOGS, COFACTOR, AND SUBUNIT.
RX PubMed=8931134; DOI=10.1002/pro.5560051102;
RA Thoden J.B., Frey P.A., Holden H.M.;
RT "High-resolution X-ray structure of UDP-galactose 4-epimerase complexed
RT with UDP-phenol.";
RL Protein Sci. 5:2149-2161(1996).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) IN COMPLEX WITH NAD AND SUBSTRATE
RP ANALOGS, AND COFACTOR.
RX PubMed=9174344; DOI=10.1021/bi970025j;
RA Thoden J.B., Hegeman A.D., Wesenberg G., Chapeau M.C., Frey P.A.,
RA Holden H.M.;
RT "Structural analysis of UDP-sugar binding to UDP-galactose 4-epimerase from
RT Escherichia coli.";
RL Biochemistry 36:6294-6304(1997).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF MUTANT PHE-149 IN COMPLEX WITH
RP SUBSTRATE ANALOGS AND NAD, MUTAGENESIS OF SER-124 AND TYR-149,
RP BIOPHYSICOCHEMICAL PROPERTIES, REACTION MECHANISM, AND ACTIVITY REGULATION.
RX PubMed=9271498; DOI=10.1021/bi970430a;
RA Liu Y., Thoden J.B., Kim J., Berger E., Gulick A.M., Ruzicka F.J.,
RA Holden H.M., Frey P.A.;
RT "Mechanistic roles of tyrosine 149 and serine 124 in UDP-galactose 4-
RT epimerase from Escherichia coli.";
RL Biochemistry 36:10675-10684(1997).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF MUTANTS ALA-124; THR-124 AND
RP VAL-124 IN COMPLEX WITH SUBSTRATE ANALOGS AND NAD, AND MUTAGENESIS OF
RP SER-124.
RX PubMed=9271499; DOI=10.1021/bi9704313;
RA Thoden J.B., Gulick A.M., Holden H.M.;
RT "Molecular structures of the S124A, S124T, and S124V site-directed mutants
RT of UDP-galactose 4-epimerase from Escherichia coli.";
RL Biochemistry 36:10685-10695(1997).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF DOUBLE MUTANT ALA-124/PHE-149 IN
RP COMPLEX WITH SUBSTRATE ANALOGS AND NAD, MUTAGENESIS OF SER-124 AND TYR-149,
RP REACTION MECHANISM, AND COFACTOR.
RX PubMed=9708982; DOI=10.1021/bi9808969;
RA Thoden J.B., Holden H.M.;
RT "Dramatic differences in the binding of UDP-galactose and UDP-glucose to
RT UDP-galactose 4-epimerase from Escherichia coli.";
RL Biochemistry 37:11469-11477(1998).
RN [21]
RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF MUTANT CYS-299 IN COMPLEX WITH
RP SUBSTRATE ANALOGS AND NAD, MUTAGENESIS OF TYR-299, SUBSTRATE SPECIFICITY,
RP AND COFACTOR.
RX PubMed=12019271; DOI=10.1074/jbc.m204413200;
RA Thoden J.B., Henderson J.M., Fridovich-Keil J.L., Holden H.M.;
RT "Structural analysis of the Y299C mutant of Escherichia coli UDP-galactose
RT 4-epimerase. Teaching an old dog new tricks.";
RL J. Biol. Chem. 277:27528-27534(2002).
CC -!- FUNCTION: Involved in the metabolism of galactose. Catalyzes the
CC conversion of UDP-galactose (UDP-Gal) to UDP-glucose (UDP-Glc) through
CC a mechanism involving the transient reduction of NAD. It is only active
CC on UDP-galactose and UDP-glucose. {ECO:0000269|PubMed:14235524}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=UDP-alpha-D-glucose = UDP-alpha-D-galactose;
CC Xref=Rhea:RHEA:22168, ChEBI:CHEBI:58885, ChEBI:CHEBI:66914;
CC EC=5.1.3.2; Evidence={ECO:0000269|PubMed:14235524};
CC -!- COFACTOR:
CC Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC Evidence={ECO:0000269|PubMed:12019271, ECO:0000269|PubMed:8241178,
CC ECO:0000269|PubMed:8611497, ECO:0000269|PubMed:8611559,
CC ECO:0000269|PubMed:8652544, ECO:0000269|PubMed:8931134,
CC ECO:0000269|PubMed:9174344, ECO:0000269|PubMed:9708982};
CC -!- ACTIVITY REGULATION: Inhibited by UDP-phenol and NaBH3CN.
CC {ECO:0000269|PubMed:1579570, ECO:0000269|PubMed:9271498}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=18 uM for UDP-Gal (at pH 8.5) {ECO:0000269|PubMed:14235524,
CC ECO:0000269|PubMed:8241178, ECO:0000269|PubMed:9271498};
CC KM=160 uM for UDP-Gal (at pH 8.5 and 27 degrees Celsius)
CC {ECO:0000269|PubMed:14235524, ECO:0000269|PubMed:8241178,
CC ECO:0000269|PubMed:9271498};
CC KM=225 uM for UDP-Glc (at pH 8.5 and 27 degrees Celsius)
CC {ECO:0000269|PubMed:14235524, ECO:0000269|PubMed:8241178,
CC ECO:0000269|PubMed:9271498};
CC Note=kcat is 760 sec(-1) for UDP-Glc (at pH 8.5 and 27 degrees
CC Celsius) and 24 sec(-1) for UDP-Gal (at pH 8.5).;
CC -!- PATHWAY: Carbohydrate metabolism; galactose metabolism.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:12019271,
CC ECO:0000269|PubMed:1579570, ECO:0000269|PubMed:4305667,
CC ECO:0000269|PubMed:8611497, ECO:0000269|PubMed:8611559,
CC ECO:0000269|PubMed:8652544, ECO:0000269|PubMed:8931134,
CC ECO:0000269|PubMed:9174344, ECO:0000269|PubMed:9271498,
CC ECO:0000269|PubMed:9271499, ECO:0000269|PubMed:9708982}.
CC -!- INTERACTION:
CC P09147; P09147: galE; NbExp=3; IntAct=EBI-909010, EBI-909010;
CC P09147; P39409: yjjW; NbExp=2; IntAct=EBI-909010, EBI-9132384;
CC -!- INDUCTION: By D-galactose and D-fucose. {ECO:0000269|PubMed:14235524}.
CC -!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase
CC family. {ECO:0000305}.
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DR EMBL; X06226; CAA29573.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73846.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35421.1; -; Genomic_DNA.
DR EMBL; X51449; CAA35813.1; -; Genomic_DNA.
DR EMBL; U07867; AAB06890.1; -; Genomic_DNA.
DR EMBL; J01613; AAA87978.1; -; Genomic_DNA.
DR PIR; S02089; XUECUG.
DR RefSeq; NP_415280.3; NC_000913.3.
DR RefSeq; WP_001265438.1; NZ_STEB01000028.1.
DR PDB; 1A9Y; X-ray; 1.80 A; A=1-338.
DR PDB; 1A9Z; X-ray; 1.90 A; A=1-338.
DR PDB; 1KVQ; X-ray; 2.15 A; A=1-338.
DR PDB; 1KVR; X-ray; 1.90 A; A=1-338.
DR PDB; 1KVS; X-ray; 2.15 A; A=1-338.
DR PDB; 1KVT; X-ray; 2.15 A; A=1-338.
DR PDB; 1KVU; X-ray; 1.90 A; A=1-338.
DR PDB; 1LRJ; X-ray; 1.90 A; A=1-338.
DR PDB; 1LRK; X-ray; 1.75 A; A=1-338.
DR PDB; 1LRL; X-ray; 1.80 A; A=1-338.
DR PDB; 1NAH; X-ray; 1.80 A; A=1-338.
DR PDB; 1NAI; X-ray; 2.00 A; A=1-338.
DR PDB; 1UDA; X-ray; 1.80 A; A=1-338.
DR PDB; 1UDB; X-ray; 1.65 A; A=1-338.
DR PDB; 1UDC; X-ray; 1.65 A; A=1-338.
DR PDB; 1XEL; X-ray; 1.80 A; A=1-338.
DR PDB; 2UDP; X-ray; 1.80 A; A/B=1-338.
DR PDB; 5GY7; X-ray; 1.43 A; A/B=1-338.
DR PDBsum; 1A9Y; -.
DR PDBsum; 1A9Z; -.
DR PDBsum; 1KVQ; -.
DR PDBsum; 1KVR; -.
DR PDBsum; 1KVS; -.
DR PDBsum; 1KVT; -.
DR PDBsum; 1KVU; -.
DR PDBsum; 1LRJ; -.
DR PDBsum; 1LRK; -.
DR PDBsum; 1LRL; -.
DR PDBsum; 1NAH; -.
DR PDBsum; 1NAI; -.
DR PDBsum; 1UDA; -.
DR PDBsum; 1UDB; -.
DR PDBsum; 1UDC; -.
DR PDBsum; 1XEL; -.
DR PDBsum; 2UDP; -.
DR PDBsum; 5GY7; -.
DR AlphaFoldDB; P09147; -.
DR SMR; P09147; -.
DR BioGRID; 4261900; 143.
DR BioGRID; 849730; 12.
DR DIP; DIP-9728N; -.
DR IntAct; P09147; 15.
DR STRING; 511145.b0759; -.
DR DrugBank; DB02790; Phenyl-uridine-5'-diphosphate.
DR DrugBank; DB01861; Uridine diphosphate glucose.
DR DrugBank; DB03435; Uridine-5'-Diphosphate.
DR DrugBank; DB04097; Uridine-5'-diphosphate-4-deoxy-4-fluoro-alpha-D-galactose.
DR DrugBank; DB02421; Uridine-5'-diphosphate-mannose.
DR DrugBank; DB03397; Uridine-Diphosphate-N-Acetylglucosamine.
DR SWISS-2DPAGE; P09147; -.
DR jPOST; P09147; -.
DR PaxDb; P09147; -.
DR PRIDE; P09147; -.
DR EnsemblBacteria; AAC73846; AAC73846; b0759.
DR EnsemblBacteria; BAA35421; BAA35421; BAA35421.
DR GeneID; 66670970; -.
DR GeneID; 945354; -.
DR KEGG; ecj:JW0742; -.
DR KEGG; eco:b0759; -.
DR PATRIC; fig|1411691.4.peg.1519; -.
DR EchoBASE; EB0357; -.
DR eggNOG; COG1087; Bacteria.
DR HOGENOM; CLU_007383_1_10_6; -.
DR InParanoid; P09147; -.
DR OMA; GEHLICN; -.
DR PhylomeDB; P09147; -.
DR BioCyc; EcoCyc:UDPGLUCEPIM-MON; -.
DR BioCyc; MetaCyc:UDPGLUCEPIM-MON; -.
DR BRENDA; 5.1.3.2; 2026.
DR SABIO-RK; P09147; -.
DR UniPathway; UPA00214; -.
DR EvolutionaryTrace; P09147; -.
DR PRO; PR:P09147; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IDA:EcoliWiki.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0070403; F:NAD+ binding; IDA:EcoCyc.
DR GO; GO:0016857; F:racemase and epimerase activity, acting on carbohydrates and derivatives; IDA:EcoliWiki.
DR GO; GO:0003978; F:UDP-glucose 4-epimerase activity; IDA:EcoCyc.
DR GO; GO:0005975; P:carbohydrate metabolic process; IMP:EcoliWiki.
DR GO; GO:0009242; P:colanic acid biosynthetic process; IMP:EcoCyc.
DR GO; GO:0033499; P:galactose catabolic process via UDP-galactose; IMP:EcoCyc.
DR GO; GO:0006012; P:galactose metabolic process; IDA:EcoliWiki.
DR CDD; cd05247; UDP_G4E_1_SDR_e; 1.
DR InterPro; IPR016040; NAD(P)-bd_dom.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR005886; UDP_G4E.
DR Pfam; PF16363; GDP_Man_Dehyd; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR TIGRFAMs; TIGR01179; galE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Galactose metabolism; Isomerase;
KW NAD; Reference proteome.
FT CHAIN 1..338
FT /note="UDP-glucose 4-epimerase"
FT /id="PRO_0000183203"
FT ACT_SITE 149
FT /note="Proton acceptor"
FT /evidence="ECO:0000269|PubMed:8611497"
FT BINDING 11..12
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:12019271,
FT ECO:0000269|PubMed:1579570, ECO:0000269|PubMed:8611497,
FT ECO:0000269|PubMed:8611559, ECO:0000269|PubMed:8931134,
FT ECO:0000269|PubMed:9174344, ECO:0000269|PubMed:9271498,
FT ECO:0000269|PubMed:9271499, ECO:0000269|PubMed:9708982"
FT BINDING 31..36
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:12019271,
FT ECO:0000269|PubMed:1579570, ECO:0000269|PubMed:8611497,
FT ECO:0000269|PubMed:8611559, ECO:0000269|PubMed:8931134,
FT ECO:0000269|PubMed:9174344, ECO:0000269|PubMed:9271498,
FT ECO:0000269|PubMed:9271499, ECO:0000269|PubMed:9708982"
FT BINDING 58..59
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:12019271,
FT ECO:0000269|PubMed:1579570, ECO:0000269|PubMed:8611497,
FT ECO:0000269|PubMed:8611559, ECO:0000269|PubMed:8931134,
FT ECO:0000269|PubMed:9174344, ECO:0000269|PubMed:9271498,
FT ECO:0000269|PubMed:9271499, ECO:0000269|PubMed:9708982"
FT BINDING 80..84
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:12019271,
FT ECO:0000269|PubMed:1579570, ECO:0000269|PubMed:8611497,
FT ECO:0000269|PubMed:8611559, ECO:0000269|PubMed:8931134,
FT ECO:0000269|PubMed:9174344, ECO:0000269|PubMed:9271498,
FT ECO:0000269|PubMed:9271499, ECO:0000269|PubMed:9708982"
FT BINDING 99
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:12019271,
FT ECO:0000269|PubMed:1579570, ECO:0000269|PubMed:8611497,
FT ECO:0000269|PubMed:8611559, ECO:0000269|PubMed:8931134,
FT ECO:0000269|PubMed:9174344, ECO:0000269|PubMed:9271498,
FT ECO:0000269|PubMed:9271499, ECO:0000269|PubMed:9708982"
FT BINDING 124
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:12019271,
FT ECO:0000269|PubMed:1579570, ECO:0000269|PubMed:8611497,
FT ECO:0000269|PubMed:8611559, ECO:0000269|PubMed:8931134,
FT ECO:0000269|PubMed:9174344, ECO:0000269|PubMed:9271498,
FT ECO:0000269|PubMed:9271499, ECO:0000269|PubMed:9708982"
FT BINDING 124
FT /ligand="substrate"
FT BINDING 149
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:12019271,
FT ECO:0000269|PubMed:1579570, ECO:0000269|PubMed:8611497,
FT ECO:0000269|PubMed:8611559, ECO:0000269|PubMed:8931134,
FT ECO:0000269|PubMed:9174344, ECO:0000269|PubMed:9271498,
FT ECO:0000269|PubMed:9271499, ECO:0000269|PubMed:9708982"
FT BINDING 149
FT /ligand="substrate"
FT BINDING 153
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:12019271,
FT ECO:0000269|PubMed:1579570, ECO:0000269|PubMed:8611497,
FT ECO:0000269|PubMed:8611559, ECO:0000269|PubMed:8931134,
FT ECO:0000269|PubMed:9174344, ECO:0000269|PubMed:9271498,
FT ECO:0000269|PubMed:9271499, ECO:0000269|PubMed:9708982"
FT BINDING 178
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:12019271,
FT ECO:0000269|PubMed:1579570, ECO:0000269|PubMed:8611497,
FT ECO:0000269|PubMed:8611559, ECO:0000269|PubMed:8931134,
FT ECO:0000269|PubMed:9174344, ECO:0000269|PubMed:9271498,
FT ECO:0000269|PubMed:9271499, ECO:0000269|PubMed:9708982"
FT BINDING 179
FT /ligand="substrate"
FT BINDING 199..200
FT /ligand="substrate"
FT BINDING 216..218
FT /ligand="substrate"
FT BINDING 231
FT /ligand="substrate"
FT BINDING 292..295
FT /ligand="substrate"
FT BINDING 299
FT /ligand="substrate"
FT MUTAGEN 124
FT /note="S->A: No major structural changes. Catalytic
FT efficiency is very low and affinity binding is 21% of the
FT wild-type enzyme."
FT /evidence="ECO:0000269|PubMed:9271498,
FT ECO:0000269|PubMed:9271499, ECO:0000269|PubMed:9708982"
FT MUTAGEN 124
FT /note="S->T: No major structural changes. Catalytic
FT efficiency is about 30% of that of the wild-type enzyme,
FT and affinity binding is similar to that of the native
FT enzyme."
FT /evidence="ECO:0000269|PubMed:9271498,
FT ECO:0000269|PubMed:9271499, ECO:0000269|PubMed:9708982"
FT MUTAGEN 149
FT /note="Y->F: No major structural changes. Catalytic
FT efficiency is very low and affinity binding is 12% of the
FT wild-type enzyme."
FT /evidence="ECO:0000269|PubMed:9271498,
FT ECO:0000269|PubMed:9708982"
FT MUTAGEN 153
FT /note="K->A: Decreases the catalytic activity. Not reduced
FT by sugars in the presence or absence of UMP. It contains
FT very little NADH."
FT /evidence="ECO:0000269|PubMed:8241178"
FT MUTAGEN 153
FT /note="K->M: Decreases the catalytic activity. Not reduced
FT by sugars in the presence or absence of UMP. It contains
FT very little NADH."
FT /evidence="ECO:0000269|PubMed:8241178"
FT MUTAGEN 299
FT /note="Y->C: Loss of epimerase activity with UDP-Gal by
FT almost 5-fold, but it results in a gain of epimerase
FT activity with uridine diphosphate N-acetylglucosamine (UDP-
FT GlcNAc) by 230-fold with minimal changes in its three-
FT dimensional structure."
FT /evidence="ECO:0000269|PubMed:12019271"
FT CONFLICT 140..145
FT /note="FPTGTP -> LLPIPG (in Ref. 6; CAA35813)"
FT /evidence="ECO:0000305"
FT STRAND 2..6
FT /evidence="ECO:0007829|PDB:5GY7"
FT TURN 7..9
FT /evidence="ECO:0007829|PDB:5GY7"
FT HELIX 11..22
FT /evidence="ECO:0007829|PDB:5GY7"
FT STRAND 26..31
FT /evidence="ECO:0007829|PDB:5GY7"
FT STRAND 34..36
FT /evidence="ECO:0007829|PDB:5GY7"
FT HELIX 38..40
FT /evidence="ECO:0007829|PDB:5GY7"
FT HELIX 41..48
FT /evidence="ECO:0007829|PDB:5GY7"
FT STRAND 53..56
FT /evidence="ECO:0007829|PDB:5GY7"
FT HELIX 62..71
FT /evidence="ECO:0007829|PDB:5GY7"
FT STRAND 75..79
FT /evidence="ECO:0007829|PDB:5GY7"
FT HELIX 86..91
FT /evidence="ECO:0007829|PDB:5GY7"
FT HELIX 93..114
FT /evidence="ECO:0007829|PDB:5GY7"
FT STRAND 118..124
FT /evidence="ECO:0007829|PDB:5GY7"
FT HELIX 125..128
FT /evidence="ECO:0007829|PDB:5GY7"
FT STRAND 134..136
FT /evidence="ECO:0007829|PDB:5GY7"
FT HELIX 148..166
FT /evidence="ECO:0007829|PDB:5GY7"
FT STRAND 171..177
FT /evidence="ECO:0007829|PDB:5GY7"
FT STRAND 179..181
FT /evidence="ECO:0007829|PDB:5GY7"
FT STRAND 187..189
FT /evidence="ECO:0007829|PDB:5GY7"
FT STRAND 194..196
FT /evidence="ECO:0007829|PDB:5GY7"
FT HELIX 200..208
FT /evidence="ECO:0007829|PDB:5GY7"
FT STRAND 211..213
FT /evidence="ECO:0007829|PDB:5GY7"
FT STRAND 215..218
FT /evidence="ECO:0007829|PDB:5GY7"
FT STRAND 222..224
FT /evidence="ECO:0007829|PDB:5GY7"
FT STRAND 233..235
FT /evidence="ECO:0007829|PDB:5GY7"
FT HELIX 236..250
FT /evidence="ECO:0007829|PDB:5GY7"
FT STRAND 255..262
FT /evidence="ECO:0007829|PDB:5GY7"
FT HELIX 269..280
FT /evidence="ECO:0007829|PDB:5GY7"
FT STRAND 286..289
FT /evidence="ECO:0007829|PDB:5GY7"
FT HELIX 304..310
FT /evidence="ECO:0007829|PDB:5GY7"
FT HELIX 318..331
FT /evidence="ECO:0007829|PDB:5GY7"
SQ SEQUENCE 338 AA; 37265 MW; 5CA8B4F7903F7792 CRC64;
MRVLVTGGSG YIGSHTCVQL LQNGHDVIIL DNLCNSKRSV LPVIERLGGK HPTFVEGDIR
NEALMTEILH DHAIDTVIHF AGLKAVGESV QKPLEYYDNN VNGTLRLISA MRAANVKNFI
FSSSATVYGD QPKIPYVESF PTGTPQSPYG KSKLMVEQIL TDLQKAQPDW SIALLRYFNP
VGAHPSGDMG EDPQGIPNNL MPYIAQVAVG RRDSLAIFGN DYPTEDGTGV RDYIHVMDLA
DGHVVAMEKL ANKPGVHIYN LGAGVGNSVL DVVNAFSKAC GKPVNYHFAP RREGDLPAYW
ADASKADREL NWRVTRTLDE MAQDTWHWQS RHPQGYPD
