WECB_SALTY
ID WECB_SALTY Reviewed; 376 AA.
AC Q9L6R5;
DT 05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 107.
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=STM3920; ORFNames=STMD1.70;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE006468; AAL22769.1; -; Genomic_DNA.
DR EMBL; AF233324; AAF33467.1; -; Genomic_DNA.
DR RefSeq; NP_462810.1; NC_003197.2.
DR RefSeq; WP_000866685.1; NC_003197.2.
DR AlphaFoldDB; Q9L6R5; -.
DR SMR; Q9L6R5; -.
DR STRING; 99287.STM3920; -.
DR PaxDb; Q9L6R5; -.
DR EnsemblBacteria; AAL22769; AAL22769; STM3920.
DR GeneID; 1255446; -.
DR KEGG; stm:STM3920; -.
DR PATRIC; fig|99287.12.peg.4141; -.
DR HOGENOM; CLU_041674_1_0_6; -.
DR OMA; RYNTERP; -.
DR PhylomeDB; Q9L6R5; -.
DR BioCyc; SENT99287:STM3920-MON; -.
DR UniPathway; UPA00566; -.
DR Proteomes; UP000001014; 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; Reference proteome.
FT CHAIN 1..376
FT /note="UDP-N-acetylglucosamine 2-epimerase"
FT /id="PRO_0000208530"
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; 42165 MW; A709B6083C57EE87 CRC64;
MKVLTVFGTR PEAIKMAPLV HALEKDPHFE AKVCVTAQHR EMLDQVLTLF SIVPDYDLNI
MQPGQGLTEI TCRILEGLKP 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
