ID   MPGP_SALTI              Reviewed;         271 AA.
AC   P65418; Q8XGE1;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 107.
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=STY2193, t0892;
OS   Salmonella typhi.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=90370;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CT18;
RX   PubMed=11677608; DOI=10.1038/35101607;
RA   Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J.,
RA   Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M.,
RA   Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A.,
RA   Davis P., Davies R.M., Dowd L., White N., Farrar J., Feltwell T.,
RA   Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A.,
RA   Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A.,
RA   Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S.,
RA   Barrell B.G.;
RT   "Complete genome sequence of a multiple drug resistant Salmonella enterica
RT   serovar Typhi CT18.";
RL   Nature 413:848-852(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700931 / Ty2;
RX   PubMed=12644504; DOI=10.1128/jb.185.7.2330-2337.2003;
RA   Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V.,
RA   Kodoyianni V., Schwartz D.C., Blattner F.R.;
RT   "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and
RT   CT18.";
RL   J. Bacteriol. 185:2330-2337(2003).
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; AL513382; CAD05733.1; -; Genomic_DNA.
DR   EMBL; AE014613; AAO68570.1; -; Genomic_DNA.
DR   RefSeq; NP_456546.1; NC_003198.1.
DR   RefSeq; WP_000948794.1; NZ_WSUR01000004.1.
DR   AlphaFoldDB; P65418; -.
DR   SMR; P65418; -.
DR   STRING; 220341.16503226; -.
DR   EnsemblBacteria; AAO68570; AAO68570; t0892.
DR   KEGG; stt:t0892; -.
DR   KEGG; sty:STY2193; -.
DR   PATRIC; fig|220341.7.peg.2209; -.
DR   eggNOG; COG3769; Bacteria.
DR   HOGENOM; CLU_063016_0_0_6; -.
DR   OMA; GPEGWNE; -.
DR   Proteomes; UP000000541; Chromosome.
DR   Proteomes; UP000002670; 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_0000184978"
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;  30925 MW;  46866C2E36B7008E CRC64;
     MLSIHDPLLI FTDLDGTLLN SHTFEWQPAA PWLTRLHESG VPVILCSSKT AAEMLQLQTT
     LNLQGLPLIA ENGAVIQLDV HWEDHPNYPR LIAGISHNEI RLVLHKLREK EQFKFTTFDD
     VDDQVISEWT GLNRAQSALT RLHEASVSLI WRDSDERMAQ FVARLNDLGL QFVHGARFWH
     VLDASAGKDQ AANWLIEAYR RQWRARPLTL GLGDGPNDAP LLDVMDYAVV VKGLNREGVH
     LRNDDPQRVY RSQNEGPDGW REGMDYFFSR S