WECB_ECOLI
ID WECB_ECOLI Reviewed; 376 AA.
AC P27828; P76753; Q2M894;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 2.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=UDP-N-acetylglucosamine 2-epimerase {ECO:0000255|HAMAP-Rule:MF_02028, ECO:0000305};
DE EC=5.1.3.14 {ECO:0000255|HAMAP-Rule:MF_02028, ECO:0000269|PubMed:15210128, ECO:0000269|Ref.9};
DE AltName: Full=Bacteriophage N4 adsorption protein C {ECO:0000305|PubMed:8226648};
DE AltName: Full=UDP-GlcNAc-2-epimerase {ECO:0000255|HAMAP-Rule:MF_02028, ECO:0000305};
GN Name=wecB {ECO:0000255|HAMAP-Rule:MF_02028};
GN Synonyms=nfrC {ECO:0000303|PubMed:8226648},
GN rffE {ECO:0000303|PubMed:2166030}, yifF; OrderedLocusNames=b3786, JW5600;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=8226648; DOI=10.1128/jb.175.21.7074-7080.1993;
RA Kiino D.R., Licudine R., Wilt K., Yang D.H.C., Rothman-Denes L.B.;
RT "A cytoplasmic protein, NfrC, is required for bacteriophage N4
RT adsorption.";
RL J. Bacteriol. 175:7074-7080(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=1379743; DOI=10.1126/science.1379743;
RA Daniels D.L., Plunkett G. III, Burland V.D., Blattner F.R.;
RT "Analysis of the Escherichia coli genome: DNA sequence of the region from
RT 84.5 to 86.5 minutes.";
RL Science 257:771-778(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP SEQUENCE REVISION TO 191.
RX PubMed=16397293; DOI=10.1093/nar/gkj405;
RA Riley M., Abe T., Arnaud M.B., Berlyn M.K.B., Blattner F.R.,
RA Chaudhuri R.R., Glasner J.D., Horiuchi T., Keseler I.M., Kosuge T.,
RA Mori H., Perna N.T., Plunkett G. III, Rudd K.E., Serres M.H., Thomas G.H.,
RA Thomson N.R., Wishart D., Wanner B.L.;
RT "Escherichia coli K-12: a cooperatively developed annotation snapshot
RT -- 2005.";
RL Nucleic Acids Res. 34:1-9(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [6]
RP PATHWAY.
RX PubMed=2166030; DOI=10.1016/s0021-9258(18)77373-0;
RA Meier-Dieter U., Starman R., Barr K., Mayer H., Rick P.D.;
RT "Biosynthesis of enterobacterial common antigen in Escherichia coli.
RT Biochemical characterization of Tn10 insertion mutants defective in
RT enterobacterial common antigen synthesis.";
RL J. Biol. Chem. 265:13490-13497(1990).
RN [7]
RP FUNCTION.
RC STRAIN=O7:K1 / VW187;
RX PubMed=7559340; DOI=10.1128/jb.177.19.5539-5546.1995;
RA Marolda C.L., Valvano M.A.;
RT "Genetic analysis of the dTDP-rhamnose biosynthesis region of the
RT Escherichia coli VW187 (O7:K1) rfb gene cluster: identification of
RT functional homologs of rfbB and rfbA in the rff cluster and correct
RT location of the rffE gene.";
RL J. Bacteriol. 177:5539-5546(1995).
RN [8]
RP FUNCTION.
RX PubMed=8170390; DOI=10.1111/j.1365-2958.1994.tb00308.x;
RA Macpherson D.F., Manning P.A., Morona R.;
RT "Characterization of the dTDP-rhamnose biosynthetic genes encoded in the
RT rfb locus of Shigella flexneri.";
RL Mol. Microbiol. 11:281-292(1994).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, AND REACTION MECHANISM.
RX DOI=10.1021/ja960266z;
RA Sala R.F., Morgan P.M., Tanner M.E.;
RT "Enzymatic formation and release of a stable glycal intermediate: the
RT mechanism of the reaction catalyzed by UDP-N-acetylglucosamine 2-
RT epimerase.";
RL J. Am. Chem. Soc. 118:3033-3034(1996).
RN [10]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND MUTAGENESIS OF LYS-15; ASP-95; GLU-117; GLU-131 AND
RP HIS-213.
RX PubMed=15210128; DOI=10.1016/j.bbapap.2004.03.017;
RA Samuel J., Tanner M.E.;
RT "Active site mutants of the 'non-hydrolyzing' UDP-N-acetylglucosamine 2-
RT epimerase from Escherichia coli.";
RL Biochim. Biophys. Acta 1700:85-91(2004).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH UDP, AND SUBUNIT.
RX PubMed=11106477; DOI=10.1021/bi001627x;
RA Campbell R.E., Mosimann S.C., Tanner M.E., Strynadka N.C.;
RT "The structure of UDP-N-acetylglucosamine 2-epimerase reveals homology to
RT phosphoglycosyl transferases.";
RL Biochemistry 39:14993-15001(2000).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.31 ANGSTROMS) OF 2-376 IN COMPLEX WITH
RP UDP-N-ACETYL-ALPHA-D-GLUCOSAMINE.
RX PubMed=16021622; DOI=10.1002/prot.20541;
RA Badger J., Sauder J.M., Adams J.M., Antonysamy S., Bain K., Bergseid M.G.,
RA Buchanan S.G., Buchanan M.D., Batiyenko Y., Christopher J.A., Emtage S.,
RA Eroshkina A., Feil I., Furlong E.B., Gajiwala K.S., Gao X., He D.,
RA Hendle J., Huber A., Hoda K., Kearins P., Kissinger C., Laubert B.,
RA Lewis H.A., Lin J., Loomis K., Lorimer D., Louie G., Maletic M.,
RA Marsh C.D., Miller I., Molinari J., Muller-Dieckmann H.J., Newman J.M.,
RA Noland B.W., Pagarigan B., Park F., Peat T.S., Post K.W., Radojicic S.,
RA Ramos A., Romero R., Rutter M.E., Sanderson W.E., Schwinn K.D., Tresser J.,
RA Winhoven J., Wright T.A., Wu L., Xu J., Harris T.J.R.;
RT "Structural analysis of a set of proteins resulting from a bacterial
RT genomics project.";
RL Proteins 60:787-796(2005).
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. Also involved in bacteriophage N4 adsorption.
CC {ECO:0000269|PubMed:15210128, ECO:0000269|PubMed:7559340,
CC ECO:0000269|PubMed:8170390, ECO:0000269|PubMed:8226648,
CC ECO:0000269|Ref.9}.
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, ECO:0000269|PubMed:15210128, ECO:0000269|Ref.9};
CC -!- ACTIVITY REGULATION: Allosterically activated by its substrate, UDP-
CC GlcNAc. {ECO:0000269|PubMed:15210128}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.6 mM for UDP-GlcNAc {ECO:0000269|PubMed:15210128};
CC Note=kcat is 7.1 sec(-1). {ECO:0000269|PubMed:15210128};
CC -!- PATHWAY: Bacterial outer membrane biogenesis; enterobacterial common
CC antigen biosynthesis. {ECO:0000255|HAMAP-Rule:MF_02028,
CC ECO:0000305|PubMed:2166030}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_02028,
CC ECO:0000269|PubMed:11106477}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02028,
CC ECO:0000269|PubMed:8226648}.
CC -!- SIMILARITY: Belongs to the UDP-N-acetylglucosamine 2-epimerase family.
CC {ECO:0000255|HAMAP-Rule:MF_02028, ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA67586.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; L18799; AAC36847.1; -; Unassigned_DNA.
DR EMBL; M87049; AAA67586.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAT48211.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77512.1; -; Genomic_DNA.
DR PIR; E65182; E65182.
DR RefSeq; WP_001340422.1; NZ_SSZK01000025.1.
DR RefSeq; YP_026253.1; NC_000913.3.
DR PDB; 1F6D; X-ray; 2.50 A; A/B/C/D=1-376.
DR PDB; 1VGV; X-ray; 2.31 A; A/B/C/D=2-376.
DR PDBsum; 1F6D; -.
DR PDBsum; 1VGV; -.
DR AlphaFoldDB; P27828; -.
DR SMR; P27828; -.
DR BioGRID; 4263321; 147.
DR STRING; 511145.b3786; -.
DR DrugBank; DB03435; Uridine-5'-Diphosphate.
DR DrugBank; DB02196; Uridine-Diphosphate-N-Acetylgalactosamine.
DR jPOST; P27828; -.
DR PaxDb; P27828; -.
DR PRIDE; P27828; -.
DR EnsemblBacteria; AAT48211; AAT48211; b3786.
DR EnsemblBacteria; BAE77512; BAE77512; BAE77512.
DR GeneID; 944789; -.
DR KEGG; ecj:JW5600; -.
DR KEGG; eco:b3786; -.
DR PATRIC; fig|511145.12.peg.3902; -.
DR EchoBASE; EB1420; -.
DR eggNOG; COG0381; Bacteria.
DR HOGENOM; CLU_041674_1_0_6; -.
DR InParanoid; P27828; -.
DR OMA; RYNTERP; -.
DR PhylomeDB; P27828; -.
DR BioCyc; EcoCyc:UDPGLCNACEPIM-MON; -.
DR BioCyc; MetaCyc:UDPGLCNACEPIM-MON; -.
DR BRENDA; 3.2.1.183; 1960.
DR BRENDA; 5.1.3.14; 2026.
DR SABIO-RK; P27828; -.
DR UniPathway; UPA00566; -.
DR EvolutionaryTrace; P27828; -.
DR PRO; PR:P27828; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0042802; F:identical protein binding; IDA:EcoCyc.
DR GO; GO:0008761; F:UDP-N-acetylglucosamine 2-epimerase activity; IMP:EcoCyc.
DR GO; GO:0009246; P:enterobacterial common antigen biosynthetic process; IMP:EcoCyc.
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 1: Evidence at protein level;
KW 3D-structure; Allosteric enzyme; Cytoplasm; Isomerase; Reference proteome.
FT CHAIN 1..376
FT /note="UDP-N-acetylglucosamine 2-epimerase"
FT /id="PRO_0000208527"
FT BINDING 10
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02028,
FT ECO:0000269|PubMed:11106477, ECO:0000269|PubMed:16021622"
FT BINDING 15
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02028,
FT ECO:0000269|PubMed:16021622"
FT BINDING 95
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02028,
FT ECO:0000269|PubMed:16021622"
FT BINDING 117
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02028,
FT ECO:0000269|PubMed:16021622"
FT BINDING 213
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02028,
FT ECO:0000269|PubMed:11106477, ECO:0000269|PubMed:16021622"
FT BINDING 271
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02028,
FT ECO:0000269|PubMed:11106477, ECO:0000269|PubMed:16021622"
FT BINDING 276
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02028,
FT ECO:0000269|PubMed:11106477, ECO:0000269|PubMed:16021622"
FT BINDING 290..292
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02028,
FT ECO:0000269|PubMed:11106477, ECO:0000269|PubMed:16021622"
FT BINDING 296
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02028,
FT ECO:0000269|PubMed:11106477, ECO:0000269|PubMed:16021622"
FT BINDING 313
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02028,
FT ECO:0000269|PubMed:16021622"
FT MUTAGEN 15
FT /note="K->A: More than 100-fold increase in KM for UDP-
FT GlcNAc."
FT /evidence="ECO:0000269|PubMed:15210128"
FT MUTAGEN 95
FT /note="D->N: Strong decrease in activity."
FT /evidence="ECO:0000269|PubMed:15210128"
FT MUTAGEN 117
FT /note="E->Q: Strong decrease in activity."
FT /evidence="ECO:0000269|PubMed:15210128"
FT MUTAGEN 131
FT /note="E->Q: Strong decrease in activity."
FT /evidence="ECO:0000269|PubMed:15210128"
FT MUTAGEN 213
FT /note="H->N: 30-fold increase in KM for UDP-GlcNAc and 50-
FT fold decrease in kcat."
FT /evidence="ECO:0000269|PubMed:15210128"
FT CONFLICT 191
FT /note="Missing (in Ref. 2; AAA67586)"
FT /evidence="ECO:0000305"
FT STRAND 2..7
FT /evidence="ECO:0007829|PDB:1VGV"
FT HELIX 10..25
FT /evidence="ECO:0007829|PDB:1VGV"
FT STRAND 30..35
FT /evidence="ECO:0007829|PDB:1VGV"
FT HELIX 40..43
FT /evidence="ECO:0007829|PDB:1VGV"
FT HELIX 44..49
FT /evidence="ECO:0007829|PDB:1VGV"
FT STRAND 55..57
FT /evidence="ECO:0007829|PDB:1VGV"
FT STRAND 62..65
FT /evidence="ECO:0007829|PDB:1F6D"
FT HELIX 67..85
FT /evidence="ECO:0007829|PDB:1VGV"
FT STRAND 88..93
FT /evidence="ECO:0007829|PDB:1VGV"
FT HELIX 97..107
FT /evidence="ECO:0007829|PDB:1VGV"
FT TURN 108..110
FT /evidence="ECO:0007829|PDB:1VGV"
FT STRAND 113..117
FT /evidence="ECO:0007829|PDB:1VGV"
FT HELIX 131..139
FT /evidence="ECO:0007829|PDB:1VGV"
FT STRAND 143..149
FT /evidence="ECO:0007829|PDB:1VGV"
FT HELIX 150..158
FT /evidence="ECO:0007829|PDB:1VGV"
FT HELIX 163..165
FT /evidence="ECO:0007829|PDB:1VGV"
FT STRAND 166..168
FT /evidence="ECO:0007829|PDB:1VGV"
FT HELIX 172..183
FT /evidence="ECO:0007829|PDB:1VGV"
FT TURN 184..186
FT /evidence="ECO:0007829|PDB:1VGV"
FT HELIX 188..195
FT /evidence="ECO:0007829|PDB:1VGV"
FT STRAND 205..211
FT /evidence="ECO:0007829|PDB:1VGV"
FT STRAND 215..217
FT /evidence="ECO:0007829|PDB:1VGV"
FT HELIX 220..235
FT /evidence="ECO:0007829|PDB:1VGV"
FT STRAND 239..244
FT /evidence="ECO:0007829|PDB:1VGV"
FT HELIX 249..259
FT /evidence="ECO:0007829|PDB:1VGV"
FT STRAND 265..268
FT /evidence="ECO:0007829|PDB:1VGV"
FT HELIX 273..282
FT /evidence="ECO:0007829|PDB:1VGV"
FT STRAND 284..291
FT /evidence="ECO:0007829|PDB:1VGV"
FT HELIX 293..295
FT /evidence="ECO:0007829|PDB:1VGV"
FT HELIX 297..300
FT /evidence="ECO:0007829|PDB:1VGV"
FT STRAND 304..309
FT /evidence="ECO:0007829|PDB:1VGV"
FT HELIX 314..318
FT /evidence="ECO:0007829|PDB:1VGV"
FT STRAND 321..325
FT /evidence="ECO:0007829|PDB:1VGV"
FT HELIX 329..341
FT /evidence="ECO:0007829|PDB:1VGV"
FT HELIX 343..350
FT /evidence="ECO:0007829|PDB:1VGV"
FT HELIX 361..371
FT /evidence="ECO:0007829|PDB:1VGV"
SQ SEQUENCE 376 AA; 42245 MW; 7B02EE6C2630DD77 CRC64;
MKVLTVFGTR PEAIKMAPLV HALAKDPFFE AKVCVTAQHR EMLDQVLKLF SIVPDYDLNI
MQPGQGLTEI TCRILEGLKP ILAEFKPDVV LVHGDTTTTL ATSLAAFYQR IPVGHVEAGL
RTGDLYSPWP EEANRTLTGH LAMYHFSPTE TSRQNLLREN VADSRIFITG NTVIDALLWV
RDQVMSSDKL RSELAANYPF IDPDKKMILV TGHRRESFGR GFEEICHALA DIATTHQDIQ
IVYPVHLNPN VREPVNRILG HVKNVILIDP QEYLPFVWLM NHAWLILTDS GGIQEEAPSL
GKPVLVMRDT TERPEAVTAG TVRLVGTDKQ RIVEEVTRLL KDENEYQAMS RAHNPYGDGQ
ACSRILEALK NNRISL
