WBBD_ECOLX
ID WBBD_ECOLX Reviewed; 275 AA.
AC Q03084;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=UDP-Gal:alpha-D-GlcNAc-diphosphoundecaprenol beta-1,3-galactosyltransferase;
DE EC=2.4.1.303 {ECO:0000269|PubMed:15625181, ECO:0000269|PubMed:18536883};
GN Name=wbbD;
OS Escherichia coli.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=562;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=O7:K1 / VW187;
RX PubMed=7677991; DOI=10.1128/jb.175.1.148-158.1993;
RA Marolda C.L., Valvano M.A.;
RT "Identification, expression, and DNA sequence of the GDP-mannose
RT biosynthesis genes encoded by the O7 rfb gene cluster of strain VW187
RT (Escherichia coli O7:K1).";
RL J. Bacteriol. 175:148-158(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND GENE NAME.
RC STRAIN=O7:K1 / VW187;
RX PubMed=10517601; DOI=10.1099/00221287-145-9-2485;
RA Marolda C.L., Feldman M.F., Valvano M.A.;
RT "Genetic organization of the O7-specific lipopolysaccharide biosynthesis
RT cluster of Escherichia coli VW187 (O7:K1).";
RL Microbiology 145:2485-2495(1999).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES,
RP PATHWAY, AND SUBCELLULAR LOCATION.
RC STRAIN=O7:K1 / VW187;
RX PubMed=15625181; DOI=10.1093/glycob/cwi038;
RA Riley J.G., Menggad M., Montoya-Peleaz P.J., Szarek W.A., Marolda C.L.,
RA Valvano M.A., Schutzbach J.S., Brockhausen I.;
RT "The wbbD gene of E. coli strain VW187 (O7:K1) encodes a UDP-Gal:
RT GlcNAc{alpha}-pyrophosphate-R {beta}1,3-galactosyltransferase involved in
RT the biosynthesis of O7-specific lipopolysaccharide.";
RL Glycobiology 15:605-613(2005).
RN [4]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=O7:K1 / VW187;
RX PubMed=18536883; DOI=10.1007/s10719-008-9127-7;
RA Brockhausen I., Riley J.G., Joynt M., Yang X., Szarek W.A.;
RT "Acceptor substrate specificity of UDP-Gal: GlcNAc-R beta1,3-
RT galactosyltransferase (WbbD) from Escherichia coli O7:K1.";
RL Glycoconj. J. 25:663-673(2008).
CC -!- FUNCTION: Catalyzes the addition of Gal, the second sugar moiety of the
CC O7-antigen repeating unit, to GlcNAc-pyrophosphate-undecaprenol.
CC {ECO:0000269|PubMed:15625181, ECO:0000269|PubMed:18536883}.
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->3)-alpha-D-
CC GlcNAc-di-trans,octa-cis-undecaprenyl diphosphate + H(+) + UDP;
CC Xref=Rhea:RHEA:36747, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:62959, ChEBI:CHEBI:66914, ChEBI:CHEBI:73973;
CC EC=2.4.1.303; Evidence={ECO:0000269|PubMed:15625181,
CC ECO:0000269|PubMed:18536883};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:15625181};
CC Note=Mn(2+) ion. Can also use other divalent metal cations.
CC {ECO:0000269|PubMed:15625181};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.2 mM for UDP-Gal {ECO:0000269|PubMed:15625181};
CC KM=0.08 mM for GlcNAc-PP-PhU {ECO:0000269|PubMed:15625181};
CC Vmax=0.042 umol/min/mg enzyme toward UDP-Gal
CC {ECO:0000269|PubMed:15625181};
CC Vmax=0.027 umol/min/mg enzyme toward GlcNAc-PP-phenylundecyl
CC {ECO:0000269|PubMed:15625181};
CC pH dependence:
CC Optimum pH is 7. {ECO:0000269|PubMed:15625181};
CC -!- PATHWAY: Bacterial outer membrane biogenesis; LPS O-antigen
CC biosynthesis. {ECO:0000269|PubMed:15625181}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000269|PubMed:15625181}; Peripheral membrane protein
CC {ECO:0000269|PubMed:15625181}; Cytoplasmic side
CC {ECO:0000269|PubMed:15625181}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. {ECO:0000305}.
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DR EMBL; AF125322; AAC27537.1; -; Genomic_DNA.
DR PIR; B40630; B40630.
DR RefSeq; WP_001278665.1; NZ_WVVU01000003.1.
DR AlphaFoldDB; Q03084; -.
DR SMR; Q03084; -.
DR CAZy; GT2; Glycosyltransferase Family 2.
DR GeneID; 58390426; -.
DR KEGG; ag:AAC27537; -.
DR PATRIC; fig|562.10476.peg.4398; -.
DR BioCyc; MetaCyc:MON-21487; -.
DR BRENDA; 2.4.1.303; 2026.
DR UniPathway; UPA00281; -.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0009243; P:O antigen biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR001173; Glyco_trans_2-like.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR Pfam; PF00535; Glycos_transf_2; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
PE 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Glycosyltransferase;
KW Lipopolysaccharide biosynthesis; Manganese; Membrane; Transferase.
FT CHAIN 1..275
FT /note="UDP-Gal:alpha-D-GlcNAc-diphosphoundecaprenol beta-
FT 1,3-galactosyltransferase"
FT /id="PRO_0000424139"
SQ SEQUENCE 275 AA; 31873 MW; 5535D95BF07FB981 CRC64;
MSDDTPKFSV LMAIYIKDSP LFLSEALQSI YKNTVAPDEV IIIRDGKVTS ELNSVIDSWR
RYLNIKDFTL EKNMGLGAAL NFGLNQCMHD LVIRADSDDI NRTNRFECIL DFMTKNGDVH
ILSSWVEEFE FNPGDKGIIK KVPSRNSILK YSKNRSPFNH PAVAFKKCEI MRVGGYGNEY
LYEDYALWLK SLANGCNGDN IQQVLVDMRF SKETAKRRGG IKYAISEIKA QYHFYRANYI
SYQDFIINII TRIFVRLLPT SFRGYIYKKV IRRFL
