ID A0A1C8ZSE9_9CREN Unreviewed; 227 AA.
AC A0A1C8ZSE9;
DT 30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Phosphoglycolate phosphatase {ECO:0000256|HAMAP-Rule:MF_01419};
DE Short=PGP {ECO:0000256|HAMAP-Rule:MF_01419};
DE Short=PGPase {ECO:0000256|HAMAP-Rule:MF_01419};
DE EC=3.1.3.18 {ECO:0000256|HAMAP-Rule:MF_01419};
GN ORFNames=BFU36_05390 {ECO:0000313|EMBL:AOL16234.1};
OS Sulfolobus sp. A20.
OC Archaea; Thermoproteota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Sulfolobus.
OX NCBI_TaxID=1891280 {ECO:0000313|EMBL:AOL16234.1, ECO:0000313|Proteomes:UP000094286};
RN [1] {ECO:0000313|Proteomes:UP000094286}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A20 {ECO:0000313|Proteomes:UP000094286};
RA Dai X.;
RT "Genome sequencing of Sulfolobus sp. A20 from Costa Rica and comparative
RT analyses of central carbon, nitrogen and sulfur metabolism in various
RT Sulfolobus strains.";
RL Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the dephosphorylation of 2-phosphoglycolate.
CC {ECO:0000256|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:0000256|HAMAP-Rule:MF_01419};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01419};
CC -!- SIMILARITY: Belongs to the archaeal SPP-like hydrolase family.
CC {ECO:0000256|HAMAP-Rule:MF_01419}.
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DR EMBL; CP017006; AOL16234.1; -; Genomic_DNA.
DR RefSeq; WP_069282602.1; NZ_CP017006.1.
DR AlphaFoldDB; A0A1C8ZSE9; -.
DR STRING; 1891280.BFU36_05390; -.
DR GeneID; 28695271; -.
DR KEGG; sula:BFU36_05390; -.
DR OrthoDB; 120822at2157; -.
DR Proteomes; UP000094286; 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 CDD; cd07514; HAD_Pase; 1.
DR Gene3D; 3.90.1070.10; -; 1.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 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 NCBIfam; TIGR01487; Pglycolate_arch; 1.
DR NCBIfam; TIGR01482; SPP-subfamily; 1.
DR PANTHER; PTHR10000:SF8; PHOSPHOGLYCOLATE PHOSPHATASE 1; 1.
DR PANTHER; PTHR10000; PHOSPHOSERINE PHOSPHATASE; 1.
DR Pfam; PF08282; Hydrolase_3; 2.
DR SFLD; SFLDG01140; C2.B:_Phosphomannomutase_and_P; 1.
DR SFLD; SFLDF00446; phosphoglycolate_phosphatase_3; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277, ECO:0000256|HAMAP-
KW Rule:MF_01419}; Hydrolase {ECO:0000256|HAMAP-Rule:MF_01419};
KW Magnesium {ECO:0000256|HAMAP-Rule:MF_01419};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01419}.
FT ACT_SITE 8
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01419"
FT BINDING 8
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01419"
FT BINDING 10
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01419"
FT BINDING 150
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01419"
FT BINDING 173
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01419"
FT BINDING 177
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01419"
SQ SEQUENCE 227 AA; 25407 MW; CB40FBFFB40EA5E1 CRC64;
MIRLLLLDLD GTLTEDRNVT NLDIHAIESI RELQKTGIKV GLVSGNSYPV LRGLYTYLGL
NGGLVAENGC IVFFKGEKHI LCRKLEADII QQFKITFGVK DTWQNEFRYC DFGFTPPKLT
EEMVKWAKDR GLYIKSSGYA VHIAFEPAGK GIGVKKLIEF HNVDRKEVAA IGDSSTDIEL
FNEVGLKIAV GNADEELKKI ADYITHDKSG KGVKEFITKL LEGVRLR
//
