ID   MPGP_ECOUT              Reviewed;         271 AA.
AC   Q1RAI5;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 1.
DT   03-AUG-2022, entry version 84.
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   Name=yedP; OrderedLocusNames=UTI89_C2156;
OS   Escherichia coli (strain UTI89 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=364106;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UTI89 / UPEC;
RX   PubMed=16585510; DOI=10.1073/pnas.0600938103;
RA   Chen S.L., Hung C.-S., Xu J., Reigstad C.S., Magrini V., Sabo A.,
RA   Blasiar D., Bieri T., Meyer R.R., Ozersky P., Armstrong J.R., Fulton R.S.,
RA   Latreille J.P., Spieth J., Hooton T.M., Mardis E.R., Hultgren S.J.,
RA   Gordon J.I.;
RT   "Identification of genes subject to positive selection in uropathogenic
RT   strains of Escherichia coli: a comparative genomics approach.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:5977-5982(2006).
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; CP000243; ABE07629.1; -; Genomic_DNA.
DR   RefSeq; WP_000949113.1; NC_007946.1.
DR   AlphaFoldDB; Q1RAI5; -.
DR   SMR; Q1RAI5; -.
DR   EnsemblBacteria; ABE07629; ABE07629; UTI89_C2156.
DR   KEGG; eci:UTI89_C2156; -.
DR   HOGENOM; CLU_063016_1_0_6; -.
DR   OMA; GPEGWNE; -.
DR   Proteomes; UP000001952; 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_0000273957"
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;  30396 MW;  3A4CFA7E78FE20EC CRC64;
     MLSIQQPLLV FSDLDGTLLD SHSYDWQPAA PWLSRLREAN VPVILCSSKT SAEMLYLQKT
     LGLQGLPLIA ENGAVIQLAE QWQDIDGFPR IISGISHGEI SQVLNTLREK EHFKFTTFDD
     VDDATIAEWT GLSRSQAALT QLHEASVTLI WRDSDERMAQ FTARLNELGL QFMQGARFWH
     VLDASAGKDQ AANWIIATYQ QSSGKRPTTL GLGDGPNDAP LLEVMDYAVI VKGLNREGVH
     LHDEDPTRVW RTQREGPEGW REGLDHFFSA R