GALE_STRLI
ID GALE_STRLI Reviewed; 329 AA.
AC P13226;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 2.
DT 03-AUG-2022, entry version 102.
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;
OS Streptomyces lividans.
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces.
OX NCBI_TaxID=1916;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3335481; DOI=10.1128/jb.170.1.203-212.1988;
RA Adams C.W., Fornwald J.A., Schmidt F.J., Rosenberg M., Brawner M.E.;
RT "Gene organization and structure of the Streptomyces lividans gal operon.";
RL J. Bacteriol. 170:203-212(1988).
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 (By similarity).
CC {ECO:0000250}.
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;
CC -!- COFACTOR:
CC Name=NAD(+); Xref=ChEBI:CHEBI:57540; Evidence={ECO:0000250};
CC -!- PATHWAY: Carbohydrate metabolism; galactose metabolism.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA26747.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; M18953; AAA26747.1; ALT_FRAME; Genomic_DNA.
DR PIR; B28669; XUSMUG.
DR AlphaFoldDB; P13226; -.
DR SMR; P13226; -.
DR UniPathway; UPA00214; -.
DR GO; GO:0003978; F:UDP-glucose 4-epimerase activity; IEA:UniProtKB-EC.
DR GO; GO:0006012; P:galactose metabolic process; IEA:UniProtKB-UniPathway.
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 3: Inferred from homology;
KW Carbohydrate metabolism; Galactose metabolism; Isomerase; NAD.
FT CHAIN 1..329
FT /note="UDP-glucose 4-epimerase"
FT /id="PRO_0000183219"
FT ACT_SITE 144
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 13..14
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 33..38
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 53..54
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 76..80
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 95
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 120
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 120
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 144
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 144
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 148
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 172
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 173
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 190..191
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 207..209
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 221
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 281..284
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 329 AA; 35453 MW; 7E520CB140EA9A21 CRC64;
MSGKYLVTGG AGYVGSVVAQ HLVEAGNEVV VLHNLSTGFR AGVPAGASFY RGDIRDQDFM
RKVFRGRLSF DGVLHFAAFS QVGESVVKPE KYWDNNVGGT MALLEAMRGA GVRRLVFSST
AATYGEPEQV PIVESAPTRP TNPYGASKLA VDHMITGEAA AHGLGAVSVP YFNVAGANRG
VRLVHDPESH LIPLVLQVAQ GRREAISVYG DDYPTPDTCV RDYIHVADLA EAHLLAVRRR
PGNEHLICNL GNGNGFSVRE VVETVRRVTG HPIPEIMAPR RGRDPAVLVA SAGTAREKLG
WNPSRADLAI VSDAWEWHSS HPKGYDDRG