WECB_SALTI
ID WECB_SALTI Reviewed; 376 AA.
AC Q8Z388;
DT 05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 05-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=UDP-N-acetylglucosamine 2-epimerase {ECO:0000255|HAMAP-Rule:MF_02028};
DE EC=5.1.3.14 {ECO:0000255|HAMAP-Rule:MF_02028};
DE AltName: Full=UDP-GlcNAc-2-epimerase {ECO:0000255|HAMAP-Rule:MF_02028};
GN Name=wecB {ECO:0000255|HAMAP-Rule:MF_02028}; Synonyms=rffE;
GN OrderedLocusNames=STY3635, t3377;
OS Salmonella typhi.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=90370;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CT18;
RX PubMed=11677608; DOI=10.1038/35101607;
RA Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J.,
RA Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M.,
RA Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A.,
RA Davis P., Davies R.M., Dowd L., White N., Farrar J., Feltwell T.,
RA Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A.,
RA Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A.,
RA Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S.,
RA Barrell B.G.;
RT "Complete genome sequence of a multiple drug resistant Salmonella enterica
RT serovar Typhi CT18.";
RL Nature 413:848-852(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700931 / Ty2;
RX PubMed=12644504; DOI=10.1128/jb.185.7.2330-2337.2003;
RA Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V.,
RA Kodoyianni V., Schwartz D.C., Blattner F.R.;
RT "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and
RT CT18.";
RL J. Bacteriol. 185:2330-2337(2003).
CC -!- FUNCTION: Catalyzes the reversible epimerization at C-2 of UDP-N-
CC acetylglucosamine (UDP-GlcNAc) and thereby provides bacteria with UDP-
CC N-acetylmannosamine (UDP-ManNAc), the activated donor of ManNAc
CC residues. {ECO:0000255|HAMAP-Rule:MF_02028}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=UDP-N-acetyl-alpha-D-glucosamine = UDP-N-acetyl-alpha-D-
CC mannosamine; Xref=Rhea:RHEA:17213, ChEBI:CHEBI:57705,
CC ChEBI:CHEBI:68623; EC=5.1.3.14; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_02028};
CC -!- PATHWAY: Bacterial outer membrane biogenesis; enterobacterial common
CC antigen biosynthesis. {ECO:0000255|HAMAP-Rule:MF_02028}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_02028}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02028}.
CC -!- SIMILARITY: Belongs to the UDP-N-acetylglucosamine 2-epimerase family.
CC {ECO:0000255|HAMAP-Rule:MF_02028}.
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DR EMBL; AL513382; CAD09396.1; -; Genomic_DNA.
DR EMBL; AE014613; AAO70901.1; -; Genomic_DNA.
DR RefSeq; NP_457827.1; NC_003198.1.
DR RefSeq; WP_000866686.1; NZ_UCTX01000015.1.
DR AlphaFoldDB; Q8Z388; -.
DR SMR; Q8Z388; -.
DR STRING; 220341.16504514; -.
DR EnsemblBacteria; AAO70901; AAO70901; t3377.
DR KEGG; stt:t3377; -.
DR KEGG; sty:STY3635; -.
DR PATRIC; fig|220341.7.peg.3704; -.
DR eggNOG; COG0381; Bacteria.
DR HOGENOM; CLU_041674_1_0_6; -.
DR OMA; RYNTERP; -.
DR UniPathway; UPA00566; -.
DR Proteomes; UP000000541; Chromosome.
DR Proteomes; UP000002670; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008761; F:UDP-N-acetylglucosamine 2-epimerase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0009246; P:enterobacterial common antigen biosynthetic process; IEA:UniProtKB-UniRule.
DR HAMAP; MF_02028; WecB_RffE; 1.
DR InterPro; IPR003331; UDP_GlcNAc_Epimerase_2_dom.
DR InterPro; IPR032892; WecB.
DR InterPro; IPR029767; WecB-like.
DR PANTHER; PTHR43174; PTHR43174; 1.
DR Pfam; PF02350; Epimerase_2; 1.
DR TIGRFAMs; TIGR00236; wecB; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Isomerase.
FT CHAIN 1..376
FT /note="UDP-N-acetylglucosamine 2-epimerase"
FT /id="PRO_0000208529"
FT BINDING 10
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02028"
FT BINDING 15
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02028"
FT BINDING 95
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02028"
FT BINDING 117
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02028"
FT BINDING 213
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02028"
FT BINDING 271
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02028"
FT BINDING 276
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02028"
FT BINDING 290..292
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02028"
FT BINDING 296
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02028"
FT BINDING 313
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02028"
SQ SEQUENCE 376 AA; 42265 MW; 5209B9A92957EA99 CRC64;
MKVLTVFGTR PEAIKMAPLV HALEKDPHFE AKVCVTAQHR EMLDQVLTLF SIVPDYDLNI
MQPGQGLTEI TCRILERLKP ILADFKPDVV LVHGDTTTTI ATSLAAFYQR IPVGHVEAGL
RTGDLYSPWP EEANRTLTGH LAMYHFAPTE NSRQNLLREN IPDERIFVTG NTVIDALIWV
RDRVLTSDTL QAELAEQYPF LNANKKMILV TGHRRESFGQ GFEHICQALA EIAAANQNVQ
IVYPVHLNPN VSEPVNRILG HVENVVLIEP QDYLPFVWLM NHAWLILTDS GGIQEEAPSL
GKPVLVMRET TERPEAITAG TVRLIGTDSR RIVAEVMRLL HDENEYQTMS RAHNPYGDGQ
SCARILQALK SYRVSL
