ID PGP_ARCFU Reviewed; 223 AA.
AC O29805;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 27-MAR-2024, entry version 120.
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=AF_0444;
OS Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC
OS 100126 / VC-16).
OC Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC Archaeoglobus.
OX NCBI_TaxID=224325;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX PubMed=9389475; DOI=10.1038/37052;
RA Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A.,
RA Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L.,
RA Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D.,
RA Quackenbush J., Lee N.H., Sutton G.G., Gill S.R., Kirkness E.F.,
RA Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N.,
RA Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R.,
RA Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D.,
RA Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P.,
RA Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M.,
RA Smith H.O., Woese C.R., Venter J.C.;
RT "The complete genome sequence of the hyperthermophilic, sulphate-reducing
RT archaeon Archaeoglobus fulgidus.";
RL Nature 390:364-370(1997).
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; AE000782; AAB90791.1; -; Genomic_DNA.
DR PIR; D69305; D69305.
DR RefSeq; WP_010877951.1; NC_000917.1.
DR AlphaFoldDB; O29805; -.
DR SMR; O29805; -.
DR STRING; 224325.AF_0444; -.
DR PaxDb; 224325-AF_0444; -.
DR EnsemblBacteria; AAB90791; AAB90791; AF_0444.
DR GeneID; 24793981; -.
DR KEGG; afu:AF_0444; -.
DR eggNOG; arCOG01213; Archaea.
DR HOGENOM; CLU_044146_2_0_2; -.
DR OrthoDB; 120822at2157; -.
DR PhylomeDB; O29805; -.
DR Proteomes; UP000002199; 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; 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 SFLD; SFLDS00003; Haloacid_Dehalogenase; 1.
DR SFLD; SFLDF00446; phosphoglycolate_phosphatase_3; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism; Hydrolase; Magnesium; Metal-binding;
KW Reference proteome.
FT CHAIN 1..223
FT /note="Phosphoglycolate phosphatase"
FT /id="PRO_0000146714"
FT ACT_SITE 10
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01419"
FT BINDING 10
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01419"
FT BINDING 12
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01419"
FT BINDING 149
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01419"
FT BINDING 172
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01419"
FT BINDING 176
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01419"
SQ SEQUENCE 223 AA; 24481 MW; 50BFD904946A1B9D CRC64;
MFKPKAIAVD IDGTLTDRKR ALNCRAVEAL RKVKIPVILA TGNISCFARA AAKLIGVSDV
VICENGGVVR FEYDGEDIVL GDKEKCVEAV RVLEKHYEVE LLDFEYRKSE VCMRRSFDIN
EARKLIEGMG VKLVDSGFAY HIMDADVSKG KALKFVAERL GISSAEFAVI GDSENDIDMF
RVAGFGIAVA NADERLKEYA DLVTPSPDGE GVVEALQFLG LLR
//
