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Database: UniProt
Entry: E5FGD8_ECOLX
LinkDB: E5FGD8_ECOLX
Original site: E5FGD8_ECOLX 
ID   E5FGD8_ECOLX            Unreviewed;       336 AA.
AC   E5FGD8;
DT   08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT   08-FEB-2011, sequence version 1.
DT   27-MAR-2024, entry version 56.
DE   RecName: Full=UDP-glucose 4-epimerase {ECO:0000256|ARBA:ARBA00018569};
DE            EC=5.1.3.2 {ECO:0000256|ARBA:ARBA00013189};
DE   AltName: Full=UDP-galactose 4-epimerase {ECO:0000256|ARBA:ARBA00031367};
GN   Name=weiS {ECO:0000313|EMBL:ADR74244.1};
GN   Synonyms=fnl1 {ECO:0000313|EMBL:GDH39063.1};
GN   ORFNames=BvCmsKKP061_01879 {ECO:0000313|EMBL:GDH39063.1}, FZU14_27175
GN   {ECO:0000313|EMBL:EFD6887762.1};
OS   Escherichia coli.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=562 {ECO:0000313|EMBL:ADR74244.1};
RN   [1] {ECO:0000313|EMBL:ADR74244.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=20964722; DOI=10.1111/j.1574-695X.2010.00745.x;
RA   Perepelov A.V., Ni Z., Wang Q., Shevelev S.D., Senchenkova S.N.,
RA   Shahskov A.S., Wang L., Knirel Y.A.;
RT   "Structure and gene cluster of the O-antigen of Escherichia coli O109;
RT   chemical and genetic evidences of the presence of L-RhaN3N derivatives in
RT   the O-antigens of E. coli O109 and O119.";
RL   FEMS Immunol. Med. Microbiol. 61:47-53(2011).
RN   [2] {ECO:0000313|EMBL:GDH39063.1, ECO:0000313|Proteomes:UP000303027}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KK-P061 {ECO:0000313|EMBL:GDH39063.1,
RC   ECO:0000313|Proteomes:UP000303027};
RA   Arimizu Y., Ogura Y.;
RT   "Large scale genomics of bovine and human commensal E. coli to reveal the
RT   emerging process of EHEC.";
RL   Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:EFD6887762.1, ECO:0000313|Proteomes:UP000531962}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=19MD07CB01-EC {ECO:0000313|EMBL:EFD6887762.1,
RC   ECO:0000313|Proteomes:UP000531962};
RG   NARMS: The National Antimicrobial Resistance Monitoring System;
RL   Submitted (AUG-2019) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00000083};
CC   -!- SIMILARITY: Belongs to the polysaccharide synthase family.
CC       {ECO:0000256|ARBA:ARBA00007430}.
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DR   EMBL; HM485572; ADR74244.1; -; Genomic_DNA.
DR   EMBL; AASKVF010000085; EFD6887762.1; -; Genomic_DNA.
DR   EMBL; BFXY01000054; GDH39063.1; -; Genomic_DNA.
DR   RefSeq; WP_001567696.1; NZ_WCER01000020.1.
DR   PATRIC; fig|562.7992.peg.1470; -.
DR   Proteomes; UP000303027; Unassembled WGS sequence.
DR   Proteomes; UP000531962; Unassembled WGS sequence.
DR   GO; GO:0003978; F:UDP-glucose 4-epimerase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009103; P:lipopolysaccharide biosynthetic process; IEA:InterPro.
DR   CDD; cd05237; UDP_invert_4-6DH_SDR_e; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR013692; CapD_C.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR003869; Polysac_CapD-like.
DR   PANTHER; PTHR43318; UDP-N-ACETYLGLUCOSAMINE 4,6-DEHYDRATASE; 1.
DR   PANTHER; PTHR43318:SF2; UDP-N-ACETYLGLUCOSAMINE 4,6-DEHYDRATASE (INVERTING); 1.
DR   Pfam; PF08485; Polysacc_syn_2C; 1.
DR   Pfam; PF02719; Polysacc_synt_2; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   3: Inferred from homology;
FT   DOMAIN          7..282
FT                   /note="Polysaccharide biosynthesis protein CapD-like"
FT                   /evidence="ECO:0000259|Pfam:PF02719"
FT   DOMAIN          285..332
FT                   /note="UDP-glucose 4-epimerase CapD C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08485"
SQ   SEQUENCE   336 AA;  37742 MW;  94B7DB17BB88EB59 CRC64;
     MFKNKRLMIT GGTGSFGNTV LKRFLKTDVK EIIVFSRDEK KQEDMRIALG DSKVKFYIGD
     TRCYTSIEQA MRGVDYVFHA AALKQVPSCE FYPMEAIKTN ILGTENVLNA AIANNVKRVV
     LLSTDKAVYP INAMGMSKAM AEKVLIAKSR MIDADKGPVL CATRYGNVMA SRGSVIPLFI
     DKIKNNQELT ITDPKMTRFL MSLEDSVDLV LHAFENGQQG DIFVQKAPAS TIEDLAQAIK
     GLFNSEASNK IIGTRHGEKL YETLVSREEM VKAQDMGKYY RIPADNRDLN YDKYILDGKV
     EANNIDDYTS HNTTRLSVKE VTELLLTLDY VKEQLN
//
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