WFED_SHIBO
ID WFED_SHIBO Reviewed; 237 AA.
AC B5L3X1;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 1.
DT 25-MAY-2022, entry version 24.
DE RecName: Full=UDP-Gal:alpha-D-GlcNAc-diphosphoundecaprenol beta-1,4-galactosyltransferase;
DE EC=2.4.1.304;
GN Name=wfeD;
OS Shigella boydii.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=621;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=18422615; DOI=10.1111/j.1574-6976.2008.00114.x;
RA Liu B., Knirel Y.A., Feng L., Perepelov A.V., Senchenkova S.N., Wang Q.,
RA Reeves P.R., Wang L.;
RT "Structure and genetics of Shigella O antigens.";
RL FEMS Microbiol. Rev. 32:627-653(2008).
RN [2]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, CATALYTIC ACTIVITY, AND
RP MUTAGENESIS OF ASP-99; GLU-101; GLU-103; ARG-210; LYS-211 AND ARG-212.
RC STRAIN=B14;
RX PubMed=21057010; DOI=10.1128/jb.00737-10;
RA Xu C., Liu B., Hu B., Han Y., Feng L., Allingham J.S., Szarek W.A.,
RA Wang L., Brockhausen I.;
RT "Biochemical characterization of UDP-Gal:GlcNAc-pyrophosphate-lipid beta-
RT 1,4-Galactosyltransferase WfeD, a new enzyme from Shigella boydii type 14
RT that catalyzes the second step in O-antigen repeating-unit synthesis.";
RL J. Bacteriol. 193:449-459(2011).
CC -!- FUNCTION: Galactosyltransferase that adds one galactose residue in the
CC beta-1-4 linkage to GlcNAc-alpha-pyrophosphate-lipid in the
CC biosynthesis of the O-polysaccharide repeating unit of the O antigen.
CC {ECO:0000269|PubMed:21057010}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N-acetyl-alpha-D-glucosaminyl-di-trans,octa-cis-undecaprenyl
CC diphosphate + UDP-alpha-D-galactose = beta-D-Gal-(1->4)-alpha-D-
CC GlcNAc-di-trans,octa-cis-undecaprenyl diphosphate + H(+) + UDP;
CC Xref=Rhea:RHEA:36751, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:62959, ChEBI:CHEBI:66914, ChEBI:CHEBI:73984;
CC EC=2.4.1.304; Evidence={ECO:0000269|PubMed:21057010};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:21057010};
CC Name=Ni(2+); Xref=ChEBI:CHEBI:49786;
CC Evidence={ECO:0000269|PubMed:21057010};
CC Name=Pb(2+); Xref=ChEBI:CHEBI:49807;
CC Evidence={ECO:0000269|PubMed:21057010};
CC Note=Divalent metal cation. Mn(2+), Ni(2+), and Pb(2+) enhance the
CC enzyme activity. {ECO:0000269|PubMed:21057010};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.25 mM for UDP-alpha-D-galactose {ECO:0000269|PubMed:21057010};
CC KM=0.1 mM for N-acetyl-alpha-D-glucosaminyl-diphospho-
CC ditrans,octacis-undecaprenol {ECO:0000269|PubMed:21057010};
CC Vmax=40 umol/h/mg enzyme with UDP-alpha-D-galactose as substrate
CC {ECO:0000269|PubMed:21057010};
CC Vmax=42 umol/h/mg enzyme with N-acetyl-alpha-D-glucosaminyl-
CC diphospho-ditrans,octacis-undecaprenol as substrate
CC {ECO:0000269|PubMed:21057010};
CC -!- PATHWAY: Bacterial outer membrane biogenesis; LPS O-antigen
CC biosynthesis.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 26 family.
CC {ECO:0000305}.
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DR EMBL; EU296409; ACD37055.1; -; Genomic_DNA.
DR RefSeq; WP_000566739.1; NZ_LPSW01000433.1.
DR AlphaFoldDB; B5L3X1; -.
DR SMR; B5L3X1; -.
DR CAZy; GT26; Glycosyltransferase Family 26.
DR KEGG; ag:ACD37055; -.
DR UniPathway; UPA00281; -.
DR GO; GO:0003831; F:beta-N-acetylglucosaminylglycopeptide beta-1,4-galactosyltransferase activity; IDA:CACAO.
DR GO; GO:0016758; F:hexosyltransferase activity; IDA:UniProtKB.
DR GO; GO:0009243; P:O antigen biosynthetic process; IDA:UniProtKB.
DR CDD; cd06533; Glyco_transf_WecG_TagA; 1.
DR InterPro; IPR004629; WecG_TagA_CpsF.
DR PANTHER; PTHR34136; PTHR34136; 1.
DR Pfam; PF03808; Glyco_tran_WecG; 1.
PE 1: Evidence at protein level;
KW Glycosyltransferase; Lipopolysaccharide biosynthesis; Transferase.
FT CHAIN 1..237
FT /note="UDP-Gal:alpha-D-GlcNAc-diphosphoundecaprenol beta-
FT 1,4-galactosyltransferase"
FT /id="PRO_0000424132"
FT ACT_SITE 101
FT /note="Nucleophile"
FT /evidence="ECO:0000255"
FT MUTAGEN 99
FT /note="D->A: Does not affect catalytic activity."
FT /evidence="ECO:0000269|PubMed:21057010"
FT MUTAGEN 101
FT /note="E->A: Abolishes catalytic activity."
FT /evidence="ECO:0000269|PubMed:21057010"
FT MUTAGEN 103
FT /note="E->A: Does not affect catalytic activity."
FT /evidence="ECO:0000269|PubMed:21057010"
FT MUTAGEN 210
FT /note="R->A: Does not affect catalytic activity."
FT /evidence="ECO:0000269|PubMed:21057010"
FT MUTAGEN 211
FT /note="K->A: Abolishes catalytic activity."
FT /evidence="ECO:0000269|PubMed:21057010"
FT MUTAGEN 212
FT /note="R->A: Does not affect catalytic activity."
FT /evidence="ECO:0000269|PubMed:21057010"
SQ SEQUENCE 237 AA; 27941 MW; 73593EDB6085C694 CRC64;
MIDNLIKRTP EINRLLENKR VTGVVTFVNP YSYYKIKEYN KISQLDYIYI DGILLLKLFN
FVNGTKIKRH SFDYSSIAKT VFNYSIQNKM KIGLIGSKDY EIEQAVKNIR KKHPGIDISY
FHSGYFSSLE EKSSVIDSVI KKSDIIICGL GTPAQEELAL DIKIKSNEHL IFTCGGFFTQ
TASRADFYYP WIKRYNLMWL QRIVLYKHVR KRFFIDYPKF IVRFISENLM KIFTRSN
