ID A0A161XM14_9EURY Unreviewed; 224 AA.
AC A0A161XM14;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-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=A4G99_06650 {ECO:0000313|EMBL:KZN24124.1};
OS Haladaptatus sp. R4.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Haladaptataceae; Haladaptatus.
OX NCBI_TaxID=1679489 {ECO:0000313|EMBL:KZN24124.1, ECO:0000313|Proteomes:UP000076599};
RN [1] {ECO:0000313|EMBL:KZN24124.1, ECO:0000313|Proteomes:UP000076599}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R4 {ECO:0000313|EMBL:KZN24124.1,
RC ECO:0000313|Proteomes:UP000076599};
RA Mukhopadhyay S.K.;
RT "Genome sequence of halophilic archaea.";
RL Submitted (APR-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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KZN24124.1}.
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DR EMBL; LWHG01000021; KZN24124.1; -; Genomic_DNA.
DR RefSeq; WP_066143083.1; NZ_LWHG01000021.1.
DR AlphaFoldDB; A0A161XM14; -.
DR STRING; 1679489.A4G99_06650; -.
DR OrthoDB; 120822at2157; -.
DR Proteomes; UP000076599; 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 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; IPR006379; HAD-SF_hydro_IIB.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR006382; PGPase.
DR NCBIfam; TIGR01484; HAD-SF-IIB; 1.
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}; 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 224 AA; 24397 MW; 3C032D3EEA31FAE4 CRC64;
MVPPLVLDID GTMTRPDDSI DPRFFDLLPD WEAPVVIATG KAFPYPVSLC HFLQIPELVI
AENGGIVLAN DEITRNGDGD AARSVAEKYR EAGHELGWGE VDLTNRWRET EIAVQRDQPL
GPLSELASEY GQEVVDTGFA YHVKSSGVSK GMGIKAVAEL LGRDLEEFVA IGDSENDVST
FGVVGESYAV ANADEKAKRA AETVIEESYS EGTISVLEEV REWP
//
