MPGP_SHISS
ID MPGP_SHISS Reviewed; 271 AA.
AC Q3Z0N4;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 92.
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=SSON_2012;
OS Shigella sonnei (strain Ss046).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=300269;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ss046;
RX PubMed=16275786; DOI=10.1093/nar/gki954;
RA Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X., Wang J.,
RA Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S., Nie H., Peng J.,
RA Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y., Qiang B., Hou Y., Yu J.,
RA Jin Q.;
RT "Genome dynamics and diversity of Shigella species, the etiologic agents of
RT bacillary dysentery.";
RL Nucleic Acids Res. 33:6445-6458(2005).
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; CP000038; AAZ88678.1; -; Genomic_DNA.
DR AlphaFoldDB; Q3Z0N4; -.
DR SMR; Q3Z0N4; -.
DR EnsemblBacteria; AAZ88678; AAZ88678; SSON_2012.
DR KEGG; ssn:SSON_2012; -.
DR HOGENOM; CLU_063016_1_0_6; -.
DR OMA; GPEGWNE; -.
DR Proteomes; UP000002529; 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_0000273963"
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; 30502 MW; 27E5C73B8E4405D6 CRC64;
MFSIQQPLLV FSDLDGTLLD SHSYDWQPTA LWLSRLREAN VPVILCSSKT SAEMLYLQKT
LGLQGLPLIA ENGAVIQLAE QWQDIDGFPR IISGISHGEI SQVLNTLREK EHFKFTTFDD
VDDATIAEWT GLSRSQAALT QLHEASVTLI WRDSDERMAQ FTARLNELGL QFMQGARFWH
VLDASAGKDQ AANWIIATYQ QLSGKRPTTL GLGDGPNDAP LLEVMDYAVI VKGLNREGVH
LHDEDPTRVW RTQREGPEGW REGLDHFFSA R
