ID   PGP_THEKO               Reviewed;         239 AA.
AC   Q5JDB7;
DT   07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 105.
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=TK2301;
OS   Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
OS   (Pyrococcus kodakaraensis (strain KOD1)).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Thermococcus.
OX   NCBI_TaxID=69014;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX   PubMed=15710748; DOI=10.1101/gr.3003105;
RA   Fukui T., Atomi H., Kanai T., Matsumi R., Fujiwara S., Imanaka T.;
RT   "Complete genome sequence of the hyperthermophilic archaeon Thermococcus
RT   kodakaraensis KOD1 and comparison with Pyrococcus genomes.";
RL   Genome Res. 15:352-363(2005).
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; AP006878; BAD86490.1; -; Genomic_DNA.
DR   RefSeq; WP_011251251.1; NC_006624.1.
DR   AlphaFoldDB; Q5JDB7; -.
DR   SMR; Q5JDB7; -.
DR   STRING; 69014.TK2301; -.
DR   PRIDE; Q5JDB7; -.
DR   EnsemblBacteria; BAD86490; BAD86490; TK2301.
DR   GeneID; 3233718; -.
DR   KEGG; tko:TK2301; -.
DR   PATRIC; fig|69014.16.peg.2256; -.
DR   eggNOG; arCOG01213; Archaea.
DR   HOGENOM; CLU_044146_2_0_2; -.
DR   InParanoid; Q5JDB7; -.
DR   OMA; DTGYAYH; -.
DR   OrthoDB; 58398at2157; -.
DR   PhylomeDB; Q5JDB7; -.
DR   Proteomes; UP000000536; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0000287; F:magnesium ion binding; IBA:GO_Central.
DR   GO; GO:0016791; F:phosphatase activity; IBA:GO_Central.
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; IPR023214; HAD_sf.
DR   InterPro; IPR006382; PGPase.
DR   SUPFAM; SSF56784; SSF56784; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Hydrolase; Magnesium; Metal-binding;
KW   Reference proteome.
FT   CHAIN           1..239
FT                   /note="Phosphoglycolate phosphatase"
FT                   /id="PRO_0000146726"
FT   ACT_SITE        9
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01419"
FT   BINDING         9
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01419"
FT   BINDING         11
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01419"
FT   BINDING         157
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01419"
FT   BINDING         180
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01419"
FT   BINDING         184
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01419"
SQ   SEQUENCE   239 AA;  26056 MW;  556B0D5F6A2B0299 CRC64;
     MTIKAISVDI DGTITYPDRR LHEKALEAIR LAESLGVPVM LVTGNTVQFG EAAAILIGTS
     GPVVGEDGGA LSIKEGKLRK RVYLTNMDEE WILWGELKKR YPEALLSFSM PERKAGLVVL
     RTVPVKAVRE LIKELGLNLI AVDSGFAIHI KKPWINKGTG IEKACEYLGI SPKEVAHIGD
     GENDLDAFGV VGYRVAVAQA PESLKEKADY VTTKPYGEGG AEAIEHILRK FGYLPEEKT