ID   MPGP_AERPE              Reviewed;         277 AA.
AC   Q9YDM7;
DT   12-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT   26-JUN-2007, sequence version 2.
DT   03-AUG-2022, entry version 106.
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=APE_0887.1;
OS   Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 /
OS   K1).
OC   Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales;
OC   Desulfurococcaceae; Aeropyrum.
OX   NCBI_TaxID=272557;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1;
RX   PubMed=10382966; DOI=10.1093/dnares/6.2.83;
RA   Kawarabayasi Y., Hino Y., Horikawa H., Yamazaki S., Haikawa Y., Jin-no K.,
RA   Takahashi M., Sekine M., Baba S., Ankai A., Kosugi H., Hosoyama A.,
RA   Fukui S., Nagai Y., Nishijima K., Nakazawa H., Takamiya M., Masuda S.,
RA   Funahashi T., Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A.,
RA   Aoki K., Kubota K., Nakamura Y., Nomura N., Sako Y., Kikuchi H.;
RT   "Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon,
RT   Aeropyrum pernix K1.";
RL   DNA Res. 6:83-101(1999).
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}.
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DR   EMBL; BA000002; BAA79870.2; -; Genomic_DNA.
DR   PIR; F72683; F72683.
DR   AlphaFoldDB; Q9YDM7; -.
DR   SMR; Q9YDM7; -.
DR   STRING; 272557.APE_0887.1; -.
DR   EnsemblBacteria; BAA79870; BAA79870; APE_0887.1.
DR   KEGG; ape:APE_0887.1; -.
DR   eggNOG; arCOG01215; Archaea.
DR   UniPathway; UPA00130; UER00193.
DR   Proteomes; UP000002518; 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; Reference proteome.
FT   CHAIN           1..277
FT                   /note="Mannosyl-3-phosphoglycerate phosphatase"
FT                   /id="PRO_0000184970"
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         219
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00617"
SQ   SEQUENCE   277 AA;  30128 MW;  1A817EEAFB559F74 CRC64;
     MEARPCSGVI FTDLDNTLVG PGGEAGEAGE VYLEALDLGY RVVPVTSKSI YEIVELWDSI
     GVPPGERIAL AESGGAIYGP RGSLARPTGF NSEVGLEYTA LGKPLASIDA LLDSLAETCG
     AVRLSKADAT EAQLITGLPR ERAALAARRE YLEVIWSRSQ ECLDTILSTA LRYRELTYVH
     RAPRTVQIAA HRGKGMAIDA ALQEPLLRPC AKVVVTAGDS SHDIPIIERG MLAFRVDYNR
     DWSRLVKPIY MVIPYEAPKA WTMLIETVKT RSNTPSL