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Database: UniProt
Entry: A0A150G9G4_GONPE
LinkDB: A0A150G9G4_GONPE
Original site: A0A150G9G4_GONPE 
ID   A0A150G9G4_GONPE        Unreviewed;       312 AA.
AC   A0A150G9G4;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   RecName: Full=Phosphoglycolate phosphatase {ECO:0000256|PIRNR:PIRNR000915};
DE            EC=3.1.3.18 {ECO:0000256|PIRNR:PIRNR000915};
GN   ORFNames=GPECTOR_43g920 {ECO:0000313|EMBL:KXZ46484.1};
OS   Gonium pectorale (Green alga).
OC   Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC   CS clade; Chlamydomonadales; Volvocaceae; Gonium.
OX   NCBI_TaxID=33097 {ECO:0000313|EMBL:KXZ46484.1, ECO:0000313|Proteomes:UP000075714};
RN   [1] {ECO:0000313|Proteomes:UP000075714}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIES-2863 {ECO:0000313|Proteomes:UP000075714};
RX   PubMed=27102219; DOI=10.1038/ncomms11370;
RA   Hanschen E.R., Marriage T.N., Ferris P.J., Hamaji T., Toyoda A.,
RA   Fujiyama A., Neme R., Noguchi H., Minakuchi Y., Suzuki M.,
RA   Kawai-Toyooka H., Smith D.R., Sparks H., Anderson J., Bakaric R., Luria V.,
RA   Karger A., Kirschner M.W., Durand P.M., Michod R.E., Nozaki H., Olson B.J.;
RT   "The Gonium pectorale genome demonstrates co-option of cell cycle
RT   regulation during the evolution of multicellularity.";
RL   Nat. Commun. 7:11370-11370(2016).
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|PIRNR:PIRNR000915};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|PIRSR:PIRSR000915-3};
CC       Note=Divalent metal ions. Mg(2+) is the most effective.
CC       {ECO:0000256|PIRSR:PIRSR000915-3};
CC   -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily.
CC       {ECO:0000256|PIRNR:PIRNR000915}.
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:KXZ46484.1}.
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DR   EMBL; LSYV01000044; KXZ46484.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A150G9G4; -.
DR   STRING; 33097.A0A150G9G4; -.
DR   OrthoDB; 217676at2759; -.
DR   Proteomes; UP000075714; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008967; F:phosphoglycolate phosphatase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 2.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR006357; HAD-SF_hydro_IIA.
DR   InterPro; IPR023214; HAD_sf.
DR   InterPro; IPR006349; PGP_euk.
DR   NCBIfam; TIGR01460; HAD-SF-IIA; 1.
DR   NCBIfam; TIGR01452; PGP_euk; 1.
DR   PANTHER; PTHR19288; 4-NITROPHENYLPHOSPHATASE-RELATED; 1.
DR   PANTHER; PTHR19288:SF75; PHOSPHOGLYCOLATE PHOSPHATASE 2; 1.
DR   Pfam; PF13344; Hydrolase_6; 1.
DR   Pfam; PF13242; Hydrolase_like; 1.
DR   PIRSF; PIRSF000915; PGP-type_phosphatase; 1.
DR   SUPFAM; SSF56784; HAD-like; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR000915};
KW   Magnesium {ECO:0000256|PIRSR:PIRSR000915-3};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000915-3};
KW   Reference proteome {ECO:0000313|Proteomes:UP000075714}.
FT   ACT_SITE        30
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000915-1"
FT   ACT_SITE        32
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000915-1"
FT   BINDING         30
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000915-3"
FT   BINDING         32
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000915-3"
FT   BINDING         225
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000915-2"
FT   BINDING         250
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000915-3"
SQ   SEQUENCE   312 AA;  33572 MW;  F68C4762A15C26B1 CRC64;
     MSKPESGSVK KATEQEKLQA FQHYEAFIFD LDGTIWKGSS LVPGAKEFVE LLRAYQKKVF
     FVTNNATKSR AANAAKLAAM GIPASQADVY TSSFAAAAYL KTTSFSKKAY VIGEEGLVEE
     LTAAGVSCFG GPEHRGKDVD WSQPDPHLEV DPEVGAVVVG LDRYINYYKL QYATTCLANS
     SCMFVACNTD ARGHFSNSDQ EWAGAGTMVA ALIGSSEREP MLLGKPASFI LDHLCATHQL
     ARDKCIVIGD RLDTDILWGT QNGMGTCCVL TGVTSEAHLA AEDNKVVPKL VLDSVGDFMT
     IKGQLPSSCT IM
//
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