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PGP_PYRAE
ID   PGP_PYRAE               Reviewed;         228 AA.
AC   Q8ZT04;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 98.
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=PAE3495;
OS   Pyrobaculum aerophilum (strain ATCC 51768 / DSM 7523 / JCM 9630 / CIP
OS   104966 / NBRC 100827 / IM2).
OC   Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC   Pyrobaculum.
OX   NCBI_TaxID=178306;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 / IM2;
RX   PubMed=11792869; DOI=10.1073/pnas.241636498;
RA   Fitz-Gibbon S.T., Ladner H., Kim U.-J., Stetter K.O., Simon M.I.,
RA   Miller J.H.;
RT   "Genome sequence of the hyperthermophilic crenarchaeon Pyrobaculum
RT   aerophilum.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:984-989(2002).
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; AE009441; AAL64959.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8ZT04; -.
DR   SMR; Q8ZT04; -.
DR   STRING; 178306.PAE3495; -.
DR   EnsemblBacteria; AAL64959; AAL64959; PAE3495.
DR   KEGG; pai:PAE3495; -.
DR   PATRIC; fig|178306.9.peg.2632; -.
DR   eggNOG; arCOG01213; Archaea.
DR   HOGENOM; CLU_044146_2_0_2; -.
DR   InParanoid; Q8ZT04; -.
DR   OMA; DTGYAYH; -.
DR   Proteomes; UP000002439; 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..228
FT                   /note="Phosphoglycolate phosphatase"
FT                   /id="PRO_0000146723"
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         151
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01419"
FT   BINDING         174
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01419"
FT   BINDING         178
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01419"
SQ   SEQUENCE   228 AA;  24032 MW;  51C64823E64356CB CRC64;
     MACKVLVVDL DGTLTLGRNT YELSAEALLA LRRARDAGIR VVLATANGLD FALTVARYLG
     IRDVIAENGC LVHLDGVTYE LCSGDMAEVD RLVLSTGVVK PSHQNKCRKY DLAYIPLRED
     AVERLRDVLG PGYVVESSGY AIHVRPAGVD KGTAVKWLCQ RLGVPCFQVA SVGDSDVDVG
     MLSVSWGFAV GNATPAAKKA AKVVVDGPSG IGFKEAVEII LSGGACAP
 
 
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