PGP_PYRHO
ID PGP_PYRHO Reviewed; 231 AA.
AC O50129;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 128.
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=PH1421;
OS Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC
OS 100139 / OT-3).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=70601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RX PubMed=9679194; DOI=10.1093/dnares/5.2.55;
RA Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S.,
RA Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K.,
RA Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T., Tanaka T.,
RA Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T.,
RA Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H.;
RT "Complete sequence and gene organization of the genome of a hyper-
RT thermophilic archaebacterium, Pyrococcus horikoshii OT3.";
RL DNA Res. 5:55-76(1998).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS), SUBUNIT, CATALYTIC ACTIVITY, AND
RP COFACTOR.
RX PubMed=18931414; DOI=10.1107/s0907444908025948;
RA Yamamoto H., Takio K., Sugahara M., Kunishima N.;
RT "Structure of a haloacid dehalogenase superfamily phosphatase PH1421 from
RT Pyrococcus horikoshii OT3: oligomeric state and thermoadaptation
RT mechanism.";
RL Acta Crystallogr. D 64:1068-1077(2008).
CC -!- FUNCTION: Catalyzes the dephosphorylation of 2-phosphoglycolate (By
CC similarity). Has phosphatase activity towards p-nitrophenylphosphate
CC (in vitro). {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 ECO:0000269|PubMed:18931414};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01419,
CC ECO:0000269|PubMed:18931414};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:18931414}.
CC -!- SIMILARITY: Belongs to the archaeal SPP-like hydrolase family.
CC {ECO:0000255|HAMAP-Rule:MF_01419}.
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DR EMBL; BA000001; BAA30527.1; -; Genomic_DNA.
DR PIR; G71015; G71015.
DR RefSeq; WP_010885503.1; NC_000961.1.
DR PDB; 1WR8; X-ray; 1.60 A; A/B=1-231.
DR PDBsum; 1WR8; -.
DR AlphaFoldDB; O50129; -.
DR SMR; O50129; -.
DR STRING; 70601.3257844; -.
DR EnsemblBacteria; BAA30527; BAA30527; BAA30527.
DR GeneID; 1443741; -.
DR KEGG; pho:PH1421; -.
DR eggNOG; arCOG01213; Archaea.
DR OMA; DTGYAYH; -.
DR OrthoDB; 58398at2157; -.
DR EvolutionaryTrace; O50129; -.
DR Proteomes; UP000000752; 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.
FT CHAIN 1..231
FT /note="Phosphoglycolate phosphatase"
FT /id="PRO_0000146725"
FT ACT_SITE 9
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01419"
FT ACT_SITE 11
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 9
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01419"
FT BINDING 11
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01419"
FT BINDING 154
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01419"
FT BINDING 177
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01419"
FT BINDING 181
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01419"
FT STRAND 5..10
FT /evidence="ECO:0007829|PDB:1WR8"
FT TURN 11..13
FT /evidence="ECO:0007829|PDB:1WR8"
FT HELIX 23..34
FT /evidence="ECO:0007829|PDB:1WR8"
FT STRAND 39..42
FT /evidence="ECO:0007829|PDB:1WR8"
FT HELIX 47..57
FT /evidence="ECO:0007829|PDB:1WR8"
FT STRAND 63..65
FT /evidence="ECO:0007829|PDB:1WR8"
FT HELIX 66..68
FT /evidence="ECO:0007829|PDB:1WR8"
FT STRAND 70..73
FT /evidence="ECO:0007829|PDB:1WR8"
FT STRAND 76..80
FT /evidence="ECO:0007829|PDB:1WR8"
FT HELIX 85..96
FT /evidence="ECO:0007829|PDB:1WR8"
FT HELIX 106..108
FT /evidence="ECO:0007829|PDB:1WR8"
FT STRAND 113..115
FT /evidence="ECO:0007829|PDB:1WR8"
FT TURN 117..119
FT /evidence="ECO:0007829|PDB:1WR8"
FT HELIX 122..131
FT /evidence="ECO:0007829|PDB:1WR8"
FT STRAND 137..140
FT /evidence="ECO:0007829|PDB:1WR8"
FT STRAND 145..148
FT /evidence="ECO:0007829|PDB:1WR8"
FT HELIX 154..165
FT /evidence="ECO:0007829|PDB:1WR8"
FT HELIX 169..171
FT /evidence="ECO:0007829|PDB:1WR8"
FT STRAND 172..176
FT /evidence="ECO:0007829|PDB:1WR8"
FT HELIX 179..181
FT /evidence="ECO:0007829|PDB:1WR8"
FT HELIX 182..187
FT /evidence="ECO:0007829|PDB:1WR8"
FT STRAND 188..193
FT /evidence="ECO:0007829|PDB:1WR8"
FT HELIX 199..202
FT /evidence="ECO:0007829|PDB:1WR8"
FT STRAND 206..208
FT /evidence="ECO:0007829|PDB:1WR8"
FT HELIX 213..227
FT /evidence="ECO:0007829|PDB:1WR8"
SQ SEQUENCE 231 AA; 25606 MW; AAE2AEB8733E14A8 CRC64;
MKIKAISIDI DGTITYPNRM IHEKALEAIR RAESLGIPIM LVTGNTVQFA EAASILIGTS
GPVVAEDGGA ISYKKKRIFL ASMDEEWILW NEIRKRFPNA RTSYTMPDRR AGLVIMRETI
NVETVREIIN ELNLNLVAVD SGFAIHVKKP WINKGSGIEK ASEFLGIKPK EVAHVGDGEN
DLDAFKVVGY KVAVAQAPKI LKENADYVTK KEYGEGGAEA IYHILEKFGY L
