ID   MPGP_SALTY              Reviewed;         271 AA.
AC   P65417; Q8XGE1;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   28-JAN-2026, entry version 110.
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=STM1986;
OS   Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Enterobacterales; Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=99287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA   Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL   Nature 413:852-856(2001).
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; Evidence={ECO:0000255|HAMAP-
CC         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; AE006468; AAL20896.1; -; Genomic_DNA.
DR   RefSeq; NP_460937.1; NC_003197.2.
DR   RefSeq; WP_000948794.1; NC_003197.2.
DR   AlphaFoldDB; P65417; -.
DR   SMR; P65417; -.
DR   STRING; 99287.STM1986; -.
DR   PaxDb; 99287-STM1986; -.
DR   GeneID; 1253507; -.
DR   KEGG; stm:STM1986; -.
DR   PATRIC; fig|99287.12.peg.2102; -.
DR   HOGENOM; CLU_063016_0_0_6; -.
DR   OMA; KGNRMSH; -.
DR   PhylomeDB; P65417; -.
DR   BioCyc; SENT99287:STM1986-MONOMER; -.
DR   Proteomes; UP000001014; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0000287; F:magnesium ion binding; IBA:GO_Central.
DR   GO; GO:0050531; F:mannosyl-3-phosphoglycerate phosphatase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016791; F:phosphatase activity; IBA:GO_Central.
DR   GO; GO:0051479; P:mannosylglycerate biosynthetic process; IEA:InterPro.
DR   CDD; cd07507; HAD_Pase; 1.
DR   Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR   Gene3D; 3.30.980.20; Putative mannosyl-3-phosphoglycerate phosphatase, domain 2; 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   NCBIfam; TIGR01484; HAD-SF-IIB; 1.
DR   NCBIfam; TIGR01486; HAD-SF-IIB-MPGP; 1.
DR   NCBIfam; TIGR02463; MPGP_rel; 1.
DR   NCBIfam; NF002976; PRK03669.1; 1.
DR   PANTHER; PTHR10000:SF8; HAD SUPERFAMILY HYDROLASE-LIKE, TYPE 3; 1.
DR   PANTHER; PTHR10000; PHOSPHOSERINE PHOSPHATASE; 1.
DR   Pfam; PF08282; Hydrolase_3; 1.
DR   SFLD; SFLDG01142; C2.B.2:_Mannosyl-3-phosphoglyc; 1.
DR   SFLD; SFLDG01140; C2.B:_Phosphomannomutase_and_P; 1.
DR   SFLD; SFLDS00003; Haloacid_Dehalogenase; 1.
DR   SUPFAM; SSF56784; HAD-like; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Hydrolase; Magnesium; Metal-binding; Reference proteome.
FT   CHAIN           1..271
FT                   /note="Mannosyl-3-phosphoglycerate phosphatase"
FT                   /id="PRO_0000184977"
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
//