ID   PGP_AERPE               Reviewed;         239 AA.
AC   Q9YE03;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 106.
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=APE_0766;
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: 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; BA000002; BAA79744.1; -; Genomic_DNA.
DR   PIR; H72667; H72667.
DR   AlphaFoldDB; Q9YE03; -.
DR   SMR; Q9YE03; -.
DR   STRING; 272557.APE_0766; -.
DR   EnsemblBacteria; BAA79744; BAA79744; APE_0766.
DR   KEGG; ape:APE_0766; -.
DR   eggNOG; arCOG01213; Archaea.
DR   OMA; DTGYAYH; -.
DR   Proteomes; UP000002518; 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; 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_0000146713"
FT   ACT_SITE        14
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01419"
FT   BINDING         14
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01419"
FT   BINDING         16
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01419"
FT   BINDING         160
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01419"
FT   BINDING         183
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01419"
FT   BINDING         187
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01419"
SQ   SEQUENCE   239 AA;  24758 MW;  EA30A3CDFD86B3DE CRC64;
     MQGLAGSVRV AALDIDGTLT ERRGAARLDG CSIAVARLLN DLGVTSILMT GNSLPVARGV
     AVYLGLEGPV VAENGCVAVV GGERVHICSG RPPEGLVKRI MELGFKPSWQ NEYRYHEYSL
     IPVKAAPGIV ERASAIAEEE GYRAIWSGYA LHIQPPGGGK ARGVGEVLAR IGAGWSEVLA
     IGDGENDVEV LARAGYSGAP GDAAEQAKRA AKIVARSPGA RGTLEIIQRV LGGARAPAC