ID   PGP_METS5               Reviewed;         222 AA.
AC   A4YIL7;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=Phosphoglycolate phosphatase {ECO:0000255|HAMAP-Rule:MF_01419};
DE            Short=PGP {ECO:0000255|HAMAP-Rule:MF_01419};
DE            Short=PGPase {ECO:0000255|HAMAP-Rule:MF_01419};
DE            EC=3.1.3.18 {ECO:0000255|HAMAP-Rule:MF_01419};
GN   OrderedLocusNames=Msed_2130;
OS   Metallosphaera sedula (strain ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509
OS   / TH2).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Metallosphaera.
OX   NCBI_TaxID=399549;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509 / TH2;
RX   PubMed=18083856; DOI=10.1128/aem.02019-07;
RA   Auernik K.S., Maezato Y., Blum P.H., Kelly R.M.;
RT   "The genome sequence of the metal-mobilizing, extremely thermoacidophilic
RT   archaeon Metallosphaera sedula provides insights into bioleaching-
RT   associated metabolism.";
RL   Appl. Environ. Microbiol. 74:682-692(2008).
CC   -!- FUNCTION: Catalyzes the dephosphorylation of 2-phosphoglycolate.
CC       {ECO:0000255|HAMAP-Rule:MF_01419}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-phosphoglycolate + H2O = glycolate + phosphate;
CC         Xref=Rhea:RHEA:14369, ChEBI:CHEBI:15377, ChEBI:CHEBI:29805,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58033; EC=3.1.3.18;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01419};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01419};
CC   -!- SIMILARITY: Belongs to the archaeal SPP-like hydrolase family.
CC       {ECO:0000255|HAMAP-Rule:MF_01419}.
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DR   EMBL; CP000682; ABP96269.1; -; Genomic_DNA.
DR   RefSeq; WP_012022056.1; NC_009440.1.
DR   AlphaFoldDB; A4YIL7; -.
DR   SMR; A4YIL7; -.
DR   STRING; 399549.Msed_2130; -.
DR   EnsemblBacteria; ABP96269; ABP96269; Msed_2130.
DR   GeneID; 5104423; -.
DR   GeneID; 59456732; -.
DR   KEGG; mse:Msed_2130; -.
DR   eggNOG; arCOG01213; Archaea.
DR   HOGENOM; CLU_044146_2_0_2; -.
DR   OMA; DTGYAYH; -.
DR   Proteomes; UP000000242; Chromosome.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0008967; F:phosphoglycolate phosphatase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR   Gene3D; 3.40.50.1000; -; 1.
DR   HAMAP; MF_01419; GPH_hydrolase_arch; 1.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR006379; HAD-SF_hydro_IIB.
DR   InterPro; IPR023214; HAD_sf.
DR   InterPro; IPR006382; PGPase.
DR   SUPFAM; SSF56784; SSF56784; 1.
DR   TIGRFAMs; TIGR01484; HAD-SF-IIB; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Hydrolase; Magnesium; Metal-binding;
KW   Reference proteome.
FT   CHAIN           1..222
FT                   /note="Phosphoglycolate phosphatase"
FT                   /id="PRO_1000073510"
FT   ACT_SITE        8
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01419"
FT   BINDING         8
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01419"
FT   BINDING         10
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01419"
FT   BINDING         150
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01419"
FT   BINDING         173
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01419"
FT   BINDING         177
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01419"
SQ   SEQUENCE   222 AA;  24138 MW;  E5FE04AA46070ABF CRC64;
     MIKLLLTDLD GTLTEDRGTY VVDIGAIKAL RRAEKAGIRV ALVSGNSYPV LRGLHNYLGL
     SGGLVAENGC FVFHGGVTFR VCETVPREVV SEFAKTFNLR ESWQNEFRRS DFGFTPAELK
     DEMIKWAEER GLVVQSSGYA LHLSGKPGGK GAGVRKLLEL ANVKREETGA IGDSRTDIEM
     FREAGITAAV SNADPELKRV ASISLKLKSG AGVMEFIDML LS