ID   MPGP_PYRAB              Reviewed;         243 AA.
AC   Q9UZC0; G8ZKM6;
DT   12-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 121.
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=mngB {ECO:0000255|HAMAP-Rule:MF_00617}; OrderedLocusNames=PYRAB12280;
GN   ORFNames=PAB0817;
OS   Pyrococcus abyssi (strain GE5 / Orsay).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=272844;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GE5 / Orsay;
RX   PubMed=12622808; DOI=10.1046/j.1365-2958.2003.03381.x;
RA   Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O.,
RA   Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J.,
RA   Weissenbach J., Zivanovic Y., Forterre P.;
RT   "An integrated analysis of the genome of the hyperthermophilic archaeon
RT   Pyrococcus abyssi.";
RL   Mol. Microbiol. 47:1495-1512(2003).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=GE5 / Orsay;
RX   PubMed=22057919; DOI=10.1007/s00284-011-0035-x;
RA   Gao J., Wang J.;
RT   "Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and
RT   Pyrococcus furiosus DSM 3638.";
RL   Curr. Microbiol. 64:118-129(2012).
CC   -!- FUNCTION: Hydrolyzes mannosyl-3-phosphoglycerate (MPG) to form the
CC       osmolyte mannosylglycerate (MG). {ECO:0000255|HAMAP-Rule:MF_00617}.
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   -!- PATHWAY: Carbohydrate biosynthesis; 2-(alpha-D-mannosyl)-D-glycerate
CC       biosynthesis; 2-(alpha-D-mannosyl)-D-glycerate from GDP-alpha-D-mannose
CC       (MPG route): step 2/2. {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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AJ248286; CAB50139.1; -; Genomic_DNA.
DR   EMBL; HE613800; CCE70669.1; -; Genomic_DNA.
DR   PIR; F75104; F75104.
DR   RefSeq; WP_010868346.1; NC_000868.1.
DR   AlphaFoldDB; Q9UZC0; -.
DR   SMR; Q9UZC0; -.
DR   STRING; 272844.PAB0817; -.
DR   EnsemblBacteria; CAB50139; CAB50139; PAB0817.
DR   GeneID; 1496615; -.
DR   KEGG; pab:PAB0817; -.
DR   PATRIC; fig|272844.11.peg.1312; -.
DR   eggNOG; arCOG01215; Archaea.
DR   HOGENOM; CLU_063016_0_0_2; -.
DR   OMA; GPEGWNE; -.
DR   OrthoDB; 58084at2157; -.
DR   PhylomeDB; Q9UZC0; -.
DR   UniPathway; UPA00130; UER00193.
DR   Proteomes; UP000000810; Chromosome.
DR   Proteomes; UP000009139; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0050531; F:mannosyl-3-phosphoglycerate phosphatase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0051479; P:mannosylglycerate biosynthetic process; IEA:UniProtKB-UniPathway.
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   InterPro; IPR033980; MPG_Pase_thermophiles.
DR   SUPFAM; SSF56784; SSF56784; 1.
DR   TIGRFAMs; TIGR01484; HAD-SF-IIB; 1.
DR   TIGRFAMs; TIGR01486; HAD-SF-IIB-MPGP; 1.
DR   TIGRFAMs; TIGR02461; osmo_MPG_phos; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Hydrolase; Magnesium; Metal-binding.
FT   CHAIN           1..243
FT                   /note="Mannosyl-3-phosphoglycerate phosphatase"
FT                   /id="PRO_0000184971"
FT   ACT_SITE        8
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00617"
FT   BINDING         8
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00617"
FT   BINDING         10
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00617"
FT   BINDING         169
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00617"
FT   BINDING         204
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00617"
SQ   SEQUENCE   243 AA;  28307 MW;  8BFD520FF47D3939 CRC64;
     MIKVIFLDID KTLIPSYDPE PAEPVIKELK RKGFEIVFNS SKTRAEQEFY REKLDVKTPF
     ISENGSAIYI PKNYFPFEIK GRETKDYIVI ELGVKVEEIR RELRKLEDAY GIKYYANSTK
     EEIMEFTGMP EELVPLAMER EYSETIFKWS RESWKRTLSE RGFTVTMGSR FYSVHGNCDK
     GKAAKILLEL YRRLGPVRSY AVGDGYNDFP MFDVVDRAFL IGNLTHEKAQ NVSSIMEVLE
     VIE