GMM_ECO57
ID GMM_ECO57 Reviewed; 159 AA.
AC P65552; Q8X7N1;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=GDP-mannose mannosyl hydrolase {ECO:0000255|HAMAP-Rule:MF_00941};
DE Short=GDPMH {ECO:0000255|HAMAP-Rule:MF_00941};
DE EC=3.6.1.- {ECO:0000255|HAMAP-Rule:MF_00941};
GN Name=gmm {ECO:0000255|HAMAP-Rule:MF_00941}; Synonyms=nudD, wcaH;
GN OrderedLocusNames=Z3215, ECs2856;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
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 [2]
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: Hydrolyzes GDP-mannose. {ECO:0000255|HAMAP-Rule:MF_00941}.
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 Evidence={ECO:0000255|HAMAP-Rule:MF_00941};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00941};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_00941};
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00941}.
CC -!- SIMILARITY: Belongs to the Nudix hydrolase family. {ECO:0000255|HAMAP-
CC Rule:MF_00941}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG57111.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB36279.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AE005174; AAG57111.1; ALT_INIT; Genomic_DNA.
DR EMBL; BA000007; BAB36279.1; ALT_INIT; Genomic_DNA.
DR PIR; C85831; C85831.
DR PIR; H90985; H90985.
DR RefSeq; NP_310883.1; NC_002695.1.
DR RefSeq; WP_000479838.1; NZ_SWKA01000005.1.
DR AlphaFoldDB; P65552; -.
DR SMR; P65552; -.
DR STRING; 155864.EDL933_3124; -.
DR EnsemblBacteria; AAG57111; AAG57111; Z3215.
DR EnsemblBacteria; BAB36279; BAB36279; ECs_2856.
DR GeneID; 913694; -.
DR KEGG; ece:Z3215; -.
DR KEGG; ecs:ECs_2856; -.
DR PATRIC; fig|386585.9.peg.2989; -.
DR eggNOG; COG1051; Bacteria.
DR HOGENOM; CLU_037162_12_0_6; -.
DR OMA; HDNSRAY; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; Chromosome.
DR GO; GO:0008727; F:GDP-mannose mannosyl hydrolase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0030145; F:manganese ion binding; IEA:InterPro.
DR CDD; cd03430; GDPMH; 1.
DR HAMAP; MF_00941; GDPMH_gmm; 1.
DR InterPro; IPR033715; GDPMH.
DR InterPro; IPR028613; GDPMH_Gmm.
DR InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf.
DR InterPro; IPR020084; NUDIX_hydrolase_CS.
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.
DR PROSITE; PS00893; NUDIX_BOX; 1.
PE 3: Inferred from homology;
KW Hydrolase; Magnesium; Metal-binding; Reference proteome.
FT CHAIN 1..159
FT /note="GDP-mannose mannosyl hydrolase"
FT /id="PRO_0000056984"
FT DOMAIN 13..153
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00941"
FT MOTIF 50..71
FT /note="Nudix box"
FT BINDING 2..3
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00941"
FT BINDING 8
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00941"
FT BINDING 36
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00941"
FT BINDING 49
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00941"
FT BINDING 69
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00941"
FT BINDING 122
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00941"
SQ SEQUENCE 159 AA; 18238 MW; 37ADE025649AFD5D CRC64;
MFLRQEDFAT VVRSTPLVSL DFIVENSRGE FLLGKRTNRP AQGYWFVPGG RVQKDETLEA
AFERLTMAEL GLRLPITAGQ FYGVWQHFYD DNFSGTDFTT HYVVLGFRFR VAEEELLLPD
EQHDDYRWLT PDALLASNDV HANSRAYFLA EKRAGVPGL
