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
