WBDQ_ECO57
ID WBDQ_ECO57 Reviewed; 169 AA.
AC O85341;
DT 27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=GDP-mannose mannosyl hydrolase WbdQ/WbhG;
DE Short=GDPMH;
DE EC=3.6.1.-;
GN Name=wbdQ; Synonyms=wbhG; OrderedLocusNames=Z3196, ECs2837;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=O157:H7 / C664-1992 / EHEC;
RX PubMed=9673232; DOI=10.1128/iai.66.8.3545-3551.1998;
RA Wang L., Reeves P.R.;
RT "Organization of Escherichia coli O157 O antigen gene cluster and
RT identification of its specific genes.";
RL Infect. Immun. 66:3545-3551(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=O157:H- / 184 / EHEC;
RX PubMed=10222209; DOI=10.1006/mpat.1998.0253;
RA Shimizu T., Yamasaki S., Tsukamoto T., Takeda Y.;
RT "Analysis of the genes responsible for the O-antigen synthesis in
RT enterohaemorrhagic Escherichia coli O157.";
RL Microb. Pathog. 26:235-247(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
CC -!- FUNCTION: It could participate in the regulation of cell wall
CC biosynthesis by influencing the concentration of GDP-mannose or GDP-
CC glucose in the cell. May be involved in the degradation of GDP-mannose
CC and GDP-glucose, diverting the GDP to the synthesis of GDP-fucose as
CC required (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GDP-alpha-D-mannose + H2O = D-mannose + GDP + H(+);
CC Xref=Rhea:RHEA:28102, ChEBI:CHEBI:4208, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57527, ChEBI:CHEBI:58189;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250};
CC -!- PATHWAY: Bacterial outer membrane biogenesis; LPS O-antigen
CC biosynthesis.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the Nudix hydrolase family. {ECO:0000305}.
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DR EMBL; AF061251; AAC32347.1; -; Genomic_DNA.
DR EMBL; AB008676; BAA77732.1; -; Genomic_DNA.
DR EMBL; AE005174; AAG57092.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB36260.1; -; Genomic_DNA.
DR PIR; E90983; E90983.
DR PIR; H85828; H85828.
DR RefSeq; NP_310864.1; NC_002695.1.
DR RefSeq; WP_000478513.1; NZ_SWKA01000005.1.
DR AlphaFoldDB; O85341; -.
DR SMR; O85341; -.
DR STRING; 155864.EDL933_3104; -.
DR PRIDE; O85341; -.
DR EnsemblBacteria; AAG57092; AAG57092; Z3196.
DR EnsemblBacteria; BAB36260; BAB36260; ECs_2837.
DR GeneID; 912421; -.
DR KEGG; ece:Z3196; -.
DR KEGG; ecs:ECs_2837; -.
DR PATRIC; fig|386585.9.peg.2970; -.
DR eggNOG; COG1051; Bacteria.
DR HOGENOM; CLU_037162_12_0_6; -.
DR OMA; HYIVLAY; -.
DR UniPathway; UPA00281; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; Chromosome.
DR GO; GO:0008727; F:GDP-mannose mannosyl hydrolase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009243; P:O antigen biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd03430; GDPMH; 1.
DR InterPro; IPR033715; GDPMH.
DR InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf.
DR InterPro; IPR000086; NUDIX_hydrolase_dom.
DR Pfam; PF00293; NUDIX; 1.
DR PIRSF; PIRSF037599; GDPMH; 1.
DR SUPFAM; SSF55811; SSF55811; 1.
DR PROSITE; PS51462; NUDIX; 1.
PE 3: Inferred from homology;
KW Hydrolase; Lipopolysaccharide biosynthesis; Magnesium; Metal-binding;
KW Reference proteome.
FT CHAIN 1..169
FT /note="GDP-mannose mannosyl hydrolase WbdQ/WbhG"
FT /id="PRO_0000056988"
FT DOMAIN 13..152
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00794"
FT MOTIF 50..71
FT /note="Nudix box"
FT BINDING 2..3
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 8
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 36..38
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 49
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 51
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 64
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 69
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 102
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 122
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT SITE 123
FT /note="Critical for catalysis"
FT /evidence="ECO:0000250"
SQ SEQUENCE 169 AA; 19568 MW; 4FD41DAC771750B8 CRC64;
MFLHSQDFAT IVRSTPLISI DLIVENEFGE ILLGKRINRP AQGYWFVPGG RVLKDEKLQT
AFERLTEIEL GIRLPLSVGK FYGIWQHFYE DNSMGGDFST HYIVIAFLLK LQPNILKLPK
SQHNAYCWLS RAKLINDDDV HYNCRAYFNN KTNDAIGLDN KDIICLMRQ
