MPGP_ECOLU
ID MPGP_ECOLU Reviewed; 271 AA.
AC B7NBU7;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=Mannosyl-3-phosphoglycerate phosphatase {ECO:0000255|HAMAP-Rule:MF_00617};
DE Short=MPGP {ECO:0000255|HAMAP-Rule:MF_00617};
DE EC=3.1.3.70 {ECO:0000255|HAMAP-Rule:MF_00617};
GN OrderedLocusNames=ECUMN_2246;
OS Escherichia coli O17:K52:H18 (strain UMN026 / ExPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=585056;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UMN026 / ExPEC;
RX PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT "Organised genome dynamics in the Escherichia coli species results in
RT highly diverse adaptive paths.";
RL PLoS Genet. 5:E1000344-E1000344(2009).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-O-(alpha-D-mannosyl)-3-phosphoglycerate + H2O = (2R)-2-O-
CC (alpha-D-mannosyl)-glycerate + phosphate; Xref=Rhea:RHEA:19309,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57541,
CC ChEBI:CHEBI:57744; EC=3.1.3.70; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00617};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00617};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00617}.
CC -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily. MPGP family.
CC {ECO:0000255|HAMAP-Rule:MF_00617}.
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DR EMBL; CU928163; CAR13437.1; -; Genomic_DNA.
DR RefSeq; WP_000949103.1; NC_011751.1.
DR RefSeq; YP_002412966.1; NC_011751.1.
DR AlphaFoldDB; B7NBU7; -.
DR SMR; B7NBU7; -.
DR STRING; 585056.ECUMN_2246; -.
DR PRIDE; B7NBU7; -.
DR EnsemblBacteria; CAR13437; CAR13437; ECUMN_2246.
DR KEGG; eum:ECUMN_2246; -.
DR PATRIC; fig|585056.7.peg.2434; -.
DR HOGENOM; CLU_063016_1_0_6; -.
DR OMA; GPEGWNE; -.
DR Proteomes; UP000007097; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProt.
DR GO; GO:0050531; F:mannosyl-3-phosphoglycerate phosphatase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0051479; P:mannosylglycerate biosynthetic process; IEA:InterPro.
DR CDD; cd07507; HAD_Pase; 1.
DR Gene3D; 3.40.50.1000; -; 1.
DR HAMAP; MF_00617; MPGP_rel; 1.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR006381; HAD-SF-IIB-MPGP.
DR InterPro; IPR006379; HAD-SF_hydro_IIB.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR012815; MPG_Pase.
DR SFLD; SFLDG01142; C2.B.2:_Mannosyl-3-phosphoglyc; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR TIGRFAMs; TIGR01484; HAD-SF-IIB; 1.
DR TIGRFAMs; TIGR01486; HAD-SF-IIB-MPGP; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Hydrolase; Magnesium; Metal-binding.
FT CHAIN 1..271
FT /note="Mannosyl-3-phosphoglycerate phosphatase"
FT /id="PRO_1000130435"
FT ACT_SITE 13
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00617"
FT BINDING 13
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00617"
FT BINDING 15
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00617"
FT BINDING 214
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00617"
SQ SEQUENCE 271 AA; 30456 MW; 952D473683A7157E CRC64;
MLSIQQPLLV FSDLDGTLLD SHSYDWQPAA PWLSRLREAN VPVILCSSKT SAEMLYLQKM
LGLQGLPLIA ENGAVIQLAE QWQDIDGFPR IISGISHGEI SQVLNTLREK EHFKFTTFDD
VDDATIAEWT GLSRSQAALT QLHEASVTLI WRDSDERMAQ FTTRLHELGL QFMQGARFWH
VLDASAGKDQ AANWIIATYQ QLSGKRPTTL GLGDGPNDAP LLEVMDYAVI VKGLNREGVH
LHDEDPARVW RTQREGPEGW REGLDHFFSA H