PGP_THEAC
ID PGP_THEAC Reviewed; 224 AA.
AC Q9HLQ2;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Phosphoglycolate phosphatase;
DE Short=PGP;
DE Short=PGPase;
DE EC=3.1.3.18;
GN OrderedLocusNames=Ta0175;
OS Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC
OS 15155 / AMRC-C165).
OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC Thermoplasmataceae; Thermoplasma.
OX NCBI_TaxID=273075;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165;
RX PubMed=11029001; DOI=10.1038/35035069;
RA Ruepp A., Graml W., Santos-Martinez M.-L., Koretke K.K., Volker C.,
RA Mewes H.-W., Frishman D., Stocker S., Lupas A.N., Baumeister W.;
RT "The genome sequence of the thermoacidophilic scavenger Thermoplasma
RT acidophilum.";
RL Nature 407:508-513(2000).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS), FUNCTION, COFACTOR, KINETIC
RP PARAMETERS, AND SUBUNIT.
RC STRAIN=ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165;
RX PubMed=14555659; DOI=10.1074/jbc.m306054200;
RA Kim Y., Yakunin A.F., Kuznetsova E., Xu X., Pennycooke M., Gu J.,
RA Cheung F., Proudfoot M., Arrowsmith C.H., Joachimiak A., Edwards A.M.,
RA Christendat D.;
RT "Structure- and function-based characterization of a new phosphoglycolate
RT phosphatase from Thermoplasma acidophilum.";
RL J. Biol. Chem. 279:517-526(2004).
CC -!- FUNCTION: Catalyzes the dephosphorylation of 2-phosphoglycolate. Also
CC has significant, but less efficient, pyrophosphatase activity, since it
CC is able to catalyze the release of phosphate from inorganic
CC pyrophosphate (PPi). {ECO:0000269|PubMed:14555659}.
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:14555659};
CC Note=Binds 5 Mg(2+) ions per homodimer. {ECO:0000269|PubMed:14555659};
CC -!- ACTIVITY REGULATION: Inhibited by Ca(2+) ions and by high chloride ion
CC concentration. By contrast, low chloride concentration (up to 50 mM)
CC slightly activate the enzyme.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.037 mM for 2-phosphoglycolate {ECO:0000269|PubMed:14555659};
CC KM=3.1 mM for pNPP {ECO:0000269|PubMed:14555659};
CC KM=0.17 mM for pyrophosphate {ECO:0000269|PubMed:14555659};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:14555659}.
CC -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily. Archaeal
CC SPP-like hydrolase family. {ECO:0000305}.
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DR EMBL; AL445063; CAC11321.1; -; Genomic_DNA.
DR RefSeq; WP_010900602.1; NC_002578.1.
DR PDB; 1KYT; X-ray; 1.70 A; A/B=1-224.
DR PDB; 1L6R; X-ray; 1.40 A; A/B=1-224.
DR PDBsum; 1KYT; -.
DR PDBsum; 1L6R; -.
DR AlphaFoldDB; Q9HLQ2; -.
DR SMR; Q9HLQ2; -.
DR STRING; 273075.Ta0175; -.
DR DNASU; 1455819; -.
DR EnsemblBacteria; CAC11321; CAC11321; CAC11321.
DR GeneID; 1455819; -.
DR KEGG; tac:Ta0175; -.
DR eggNOG; arCOG01213; Archaea.
DR HOGENOM; CLU_044146_2_0_2; -.
DR OMA; DTGYAYH; -.
DR OrthoDB; 58398at2157; -.
DR BRENDA; 3.1.3.18; 6324.
DR SABIO-RK; Q9HLQ2; -.
DR EvolutionaryTrace; Q9HLQ2; -.
DR Proteomes; UP000001024; 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 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 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Hydrolase; Magnesium; Metal-binding;
KW Reference proteome.
FT CHAIN 1..224
FT /note="Phosphoglycolate phosphatase"
FT /id="PRO_0000146731"
FT ACT_SITE 8
FT /note="Nucleophile"
FT BINDING 8
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT BINDING 10
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT BINDING 11
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT BINDING 43
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT BINDING 151
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 174
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT BINDING 174
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT BINDING 175
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT BINDING 178
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT STRAND 4..8
FT /evidence="ECO:0007829|PDB:1L6R"
FT HELIX 9..12
FT /evidence="ECO:0007829|PDB:1L6R"
FT HELIX 22..33
FT /evidence="ECO:0007829|PDB:1L6R"
FT STRAND 37..41
FT /evidence="ECO:0007829|PDB:1L6R"
FT HELIX 46..56
FT /evidence="ECO:0007829|PDB:1L6R"
FT STRAND 62..64
FT /evidence="ECO:0007829|PDB:1L6R"
FT HELIX 65..67
FT /evidence="ECO:0007829|PDB:1L6R"
FT STRAND 69..71
FT /evidence="ECO:0007829|PDB:1L6R"
FT STRAND 77..81
FT /evidence="ECO:0007829|PDB:1L6R"
FT HELIX 84..93
FT /evidence="ECO:0007829|PDB:1L6R"
FT TURN 94..96
FT /evidence="ECO:0007829|PDB:1L6R"
FT HELIX 103..107
FT /evidence="ECO:0007829|PDB:1L6R"
FT STRAND 109..115
FT /evidence="ECO:0007829|PDB:1L6R"
FT HELIX 118..120
FT /evidence="ECO:0007829|PDB:1L6R"
FT HELIX 121..129
FT /evidence="ECO:0007829|PDB:1L6R"
FT TURN 130..132
FT /evidence="ECO:0007829|PDB:1L6R"
FT STRAND 133..138
FT /evidence="ECO:0007829|PDB:1L6R"
FT STRAND 141..146
FT /evidence="ECO:0007829|PDB:1L6R"
FT HELIX 151..161
FT /evidence="ECO:0007829|PDB:1L6R"
FT HELIX 166..168
FT /evidence="ECO:0007829|PDB:1L6R"
FT STRAND 169..172
FT /evidence="ECO:0007829|PDB:1L6R"
FT HELIX 176..178
FT /evidence="ECO:0007829|PDB:1L6R"
FT HELIX 179..182
FT /evidence="ECO:0007829|PDB:1L6R"
FT STRAND 184..190
FT /evidence="ECO:0007829|PDB:1L6R"
FT HELIX 196..201
FT /evidence="ECO:0007829|PDB:1L6R"
FT STRAND 203..205
FT /evidence="ECO:0007829|PDB:1L6R"
FT TURN 210..212
FT /evidence="ECO:0007829|PDB:1L6R"
FT HELIX 213..220
FT /evidence="ECO:0007829|PDB:1L6R"
SQ SEQUENCE 224 AA; 25279 MW; E98BE17558DE72E9 CRC64;
MIRLAAIDVD GTLTDRDRLI STKAIESIRS AEKKGLTVSL LSGNVIPVVY ALKIFLGING
PVFGENGGIM FDNDGSIKKF FSNEGTNKFL EEMSKRTSMR SILTNRWREA STGFDIDPED
VDYVRKEAES RGFVIFYSGY SWHLMNRGED KAFAVNKLKE MYSLEYDEIL VIGDSNNDMP
MFQLPVRKAC PANATDNIKA VSDFVSDYSY GEEIGQIFKH FELM
