ID   GPH_SHISS               Reviewed;         252 AA.
AC   Q3YWN8;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2005, sequence version 1.
DT   02-SEP-2026, entry version 111.
DE   RecName: Full=Phosphoglycolate phosphatase {ECO:0000255|HAMAP-Rule:MF_00495};
DE            Short=PGP {ECO:0000255|HAMAP-Rule:MF_00495};
DE            Short=PGPase {ECO:0000255|HAMAP-Rule:MF_00495};
DE            EC=3.1.3.18 {ECO:0000255|HAMAP-Rule:MF_00495};
GN   OrderedLocusNames=SSON_3516;
OS   Shigella sonnei (strain Ss046).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Enterobacterales; Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=300269;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ss046;
RX   PubMed=16275786; DOI=10.1093/nar/gki954;
RA   Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X., Wang J.,
RA   Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S., Nie H., Peng J.,
RA   Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y., Qiang B., Hou Y., Yu J.,
RA   Jin Q.;
RT   "Genome dynamics and diversity of Shigella species, the etiologic agents of
RT   bacillary dysentery.";
RL   Nucleic Acids Res. 33:6445-6458(2005).
CC   -!- FUNCTION: Specifically catalyzes the dephosphorylation of 2-
CC       phosphoglycolate. Is involved in the dissimilation of the intracellular
CC       2-phosphoglycolate formed during the DNA repair of 3'-phosphoglycolate
CC       ends, a major class of DNA lesions induced by oxidative stress.
CC       {ECO:0000255|HAMAP-Rule:MF_00495}.
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_00495};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00495};
CC   -!- COFACTOR:
CC       Name=chloride; Xref=ChEBI:CHEBI:17996; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00495};
CC   -!- PATHWAY: Organic acid metabolism; glycolate biosynthesis; glycolate
CC       from 2-phosphoglycolate: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00495}.
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00495}.
CC   -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily.
CC       CbbY/CbbZ/Gph/YieH family. {ECO:0000255|HAMAP-Rule:MF_00495}.
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DR   EMBL; CP000038; AAZ90074.1; -; Genomic_DNA.
DR   RefSeq; WP_001031707.1; NC_007384.1.
DR   AlphaFoldDB; Q3YWN8; -.
DR   SMR; Q3YWN8; -.
DR   GeneID; 93778613; -.
DR   KEGG; ssn:SSON_3516; -.
DR   HOGENOM; CLU_045011_19_1_6; -.
DR   UniPathway; UPA00865; UER00834.
DR   Proteomes; UP000002529; Chromosome.
DR   GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-ARBA.
DR   GO; GO:0008967; F:phosphoglycolate phosphatase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0006281; P:DNA repair; IEA:TreeGrafter.
DR   GO; GO:0046295; P:glycolate biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd16417; HAD_PGPase; 1.
DR   FunFam; 1.10.150.240:FF:000003; Phosphoglycolate phosphatase; 1.
DR   FunFam; 3.40.50.1000:FF:000022; Phosphoglycolate phosphatase; 1.
DR   Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR   Gene3D; 1.10.150.240; Putative phosphatase, domain 2; 1.
DR   HAMAP; MF_00495; GPH_hydrolase_bact; 1.
DR   InterPro; IPR050155; HAD-like_hydrolase_sf.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR006439; HAD-SF_hydro_IA.
DR   InterPro; IPR023214; HAD_sf.
DR   InterPro; IPR023198; PGP-like_dom2.
DR   InterPro; IPR037512; PGPase_prok.
DR   NCBIfam; TIGR01549; HAD-SF-IA-v1; 1.
DR   NCBIfam; TIGR01509; HAD-SF-IA-v3; 1.
DR   NCBIfam; TIGR01449; PGP_bact; 1.
DR   NCBIfam; NF009694; PRK13222.1-1; 1.
DR   NCBIfam; NF009695; PRK13222.1-2; 1.
DR   NCBIfam; NF009697; PRK13222.1-4; 1.
DR   PANTHER; PTHR43434; PHOSPHOGLYCOLATE PHOSPHATASE; 1.
DR   PANTHER; PTHR43434:SF1; PHOSPHOGLYCOLATE PHOSPHATASE; 1.
DR   Pfam; PF00702; Hydrolase; 1.
DR   PRINTS; PR00413; HADHALOGNASE.
DR   SFLD; SFLDG01135; C1.5.6:_HAD__Beta-PGM__Phospha; 1.
DR   SFLD; SFLDG01129; C1.5:_HAD__Beta-PGM__Phosphata; 1.
DR   SFLD; SFLDS00003; Haloacid_Dehalogenase; 1.
DR   SUPFAM; SSF56784; HAD-like; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Chloride; Hydrolase; Magnesium; Metal-binding;
KW   Reference proteome.
FT   CHAIN           1..252
FT                   /note="Phosphoglycolate phosphatase"
FT                   /id="PRO_0000238180"
FT   ACT_SITE        13
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00495"
FT   BINDING         13
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00495"
FT   BINDING         15
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00495"
FT   BINDING         192
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00495"
SQ   SEQUENCE   252 AA;  27403 MW;  4DCCDA65B37A0E72 CRC64;
     MNKFEDIRGV AFDLDGTLVD SAPGLAAAVD MALYALELPI AGEERVITWI GNGADVLMER
     ALTWARQERA TQRKTMGKPP VDDDIPAEEQ VRILRKLFDR YYGEVAEEGT FLFPHVADTL
     GALQAKGLPL GLVTNKPTPF VAPLLEALDI AKYFSVVIGG DDVQNKKPHP DPLLLVAERM
     GIAPQQMLFV GDSRNDIQAA KAAGCPSVGL TYGYNYGEAI DLSQPDVIYQ SINDLLPALG
     LPHSENQESK ND
//