ID A0A1H1AML9_9EURY Unreviewed; 225 AA.
AC A0A1H1AML9;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 38.
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=DWB78_01190 {ECO:0000313|EMBL:RDI70443.1}, SAMN05216278_1408
GN {ECO:0000313|EMBL:SDQ40907.1};
OS Halopelagius longus.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae.
OX NCBI_TaxID=1236180 {ECO:0000313|EMBL:SDQ40907.1, ECO:0000313|Proteomes:UP000199289};
RN [1] {ECO:0000313|Proteomes:UP000199289}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.12397 {ECO:0000313|Proteomes:UP000199289};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:SDQ40907.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.12397 {ECO:0000313|EMBL:SDQ40907.1};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:RDI70443.1, ECO:0000313|Proteomes:UP000255421}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BC12-B1 {ECO:0000313|EMBL:RDI70443.1,
RC ECO:0000313|Proteomes:UP000255421};
RA Zhang X.;
RT "Genome sequence of extremly halophilic archaeon Halopelagius longus strain
RT BC12-B1.";
RL Submitted (JUL-2018) 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; QQST01000001; RDI70443.1; -; Genomic_DNA.
DR EMBL; FNKQ01000002; SDQ40907.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H1AML9; -.
DR OrthoDB; 120822at2157; -.
DR Proteomes; UP000199289; Unassembled WGS sequence.
DR Proteomes; UP000255421; Unassembled WGS sequence.
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; 3.90.1070.10; -; 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 SUPFAM; SSF56784; HAD-like; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277, ECO:0000256|HAMAP-
KW Rule:MF_01419};
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01419, ECO:0000313|EMBL:RDI70443.1};
KW Magnesium {ECO:0000256|HAMAP-Rule:MF_01419};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01419}.
FT ACT_SITE 11
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01419"
FT BINDING 11
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01419"
FT BINDING 13
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01419"
FT BINDING 153
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01419"
FT BINDING 176
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01419"
FT BINDING 180
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01419"
SQ SEQUENCE 225 AA; 24014 MW; 36DCADDB08C0416B CRC64;
METAVPPIVL DIDGTLTDAP GRLDPRVFDV LPTWDAPVVL ATGKAFPYPV SLCHYIGIEQ
TVVAENGGVV LAAGEVSYNA DRDAAQAAAE EFEARGGDVG WGEFDPVNKW RETEVAVNLS
ADEDLLREVA AEYDLEVLDT GYAYHVKTPG IEKGDGLRAI CETLDLDPAE FVAIGDSEND
ASTFEVAGRS YAVANADDVA KAAADEVLEE SYMDGTLSVL DSLRE
//
