GALE_STRMU
ID GALE_STRMU Reviewed; 333 AA.
AC P96995;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2002, sequence version 2.
DT 03-AUG-2022, entry version 136.
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; OrderedLocusNames=SMU_888;
OS Streptococcus mutans serotype c (strain ATCC 700610 / UA159).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=210007;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Ingbritt;
RX PubMed=8973358; DOI=10.1016/s0378-1119(96)00434-9;
RA Ajdic D., Sutcliffe I.C., Russell R.R.B., Ferretti J.J.;
RT "Organization and nucleotide sequence of the Streptococcus mutans galactose
RT operon.";
RL Gene 180:137-144(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700610 / UA159;
RX PubMed=12397186; DOI=10.1073/pnas.172501299;
RA Ajdic D.J., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B.,
RA Primeaux C., Tian R., Kenton S., Jia H.G., Lin S.P., Qian Y., Li S.,
RA Zhu H., Najar F.Z., Lai H., White J., Roe B.A., Ferretti J.J.;
RT "Genome sequence of Streptococcus mutans UA159, a cariogenic dental
RT pathogen.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(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 (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=AAN58602.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U21942; AAB49738.1; -; Genomic_DNA.
DR EMBL; AE014133; AAN58602.1; ALT_INIT; Genomic_DNA.
DR PIR; JC5313; JC5313.
DR RefSeq; NP_721296.1; NC_004350.2.
DR RefSeq; WP_002262881.1; NC_004350.2.
DR AlphaFoldDB; P96995; -.
DR SMR; P96995; -.
DR STRING; 210007.SMU_888; -.
DR PRIDE; P96995; -.
DR EnsemblBacteria; AAN58602; AAN58602; SMU_888.
DR KEGG; smu:SMU_888; -.
DR PATRIC; fig|210007.7.peg.795; -.
DR eggNOG; COG1087; Bacteria.
DR HOGENOM; CLU_007383_1_10_9; -.
DR OMA; GEHLICN; -.
DR UniPathway; UPA00214; -.
DR Proteomes; UP000002512; Chromosome.
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;
KW Reference proteome.
FT CHAIN 1..333
FT /note="UDP-glucose 4-epimerase"
FT /id="PRO_0000183220"
FT ACT_SITE 143
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 11..12
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 32..37
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 52..53
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 75..79
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 94
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 119
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 119
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 143
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 143
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 147
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 171
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 172
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 191..192
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 208..210
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 223
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 284..287
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CONFLICT 127
FT /note="D -> N (in Ref. 1; AAB49738)"
FT /evidence="ECO:0000305"
FT CONFLICT 168
FT /note="L -> V (in Ref. 1; AAB49738)"
FT /evidence="ECO:0000305"
FT CONFLICT 234
FT /note="A -> R (in Ref. 1; AAB49738)"
FT /evidence="ECO:0000305"
FT CONFLICT 302
FT /note="L -> V (in Ref. 1; AAB49738)"
FT /evidence="ECO:0000305"
FT CONFLICT 325
FT /note="Y -> H (in Ref. 1; AAB49738)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 333 AA; 36921 MW; 51ED86CF34B5A413 CRC64;
MAILVLGGAG YIGSHMVDRL IEKGEEEVVV VDSLVTGHRA AVHPAAKFYQ GDLADREFMS
MVFRENPDVD AVIHFAAYSL VAESMKKPLK YFDNNTAGMI KLLEVMSEFG VKYIVFSSTA
ATYGIPDEIP IKETTPQRPI NPYGESKLMM ETIMKWSDRA YGIKFVPLRY FNVAGAKPDG
SIGEDHSPET HLLPIILQVA QGVREKIMIF GDDYNTPDGT NVRDYVHPFD LADAHLLALN
YLRQGNPSTA FNLGSSTGFS NLQILEAARK VTGQKIPAEK AARRSGDPDT LIASSEKARE
VLGWKPQFDD IEKIIASAWA WHSSYPKGYD DRD
