ID   GPH_VIBPA               Reviewed;         228 AA.
AC   Q87L12;
DT   25-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 107.
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   Name=gph {ECO:0000255|HAMAP-Rule:MF_00495}; OrderedLocusNames=VP2805;
OS   Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=223926;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RIMD 2210633;
RX   PubMed=12620739; DOI=10.1016/s0140-6736(03)12659-1;
RA   Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K.,
RA   Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S.,
RA   Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.;
RT   "Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism
RT   distinct from that of V. cholerae.";
RL   Lancet 361:743-749(2003).
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;
CC         Evidence={ECO:0000255|HAMAP-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   -!- 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; BA000031; BAC61068.1; -; Genomic_DNA.
DR   RefSeq; NP_799184.1; NC_004603.1.
DR   RefSeq; WP_005480027.1; NC_004603.1.
DR   AlphaFoldDB; Q87L12; -.
DR   SMR; Q87L12; -.
DR   STRING; 223926.28807815; -.
DR   EnsemblBacteria; BAC61068; BAC61068; BAC61068.
DR   GeneID; 1190355; -.
DR   KEGG; vpa:VP2805; -.
DR   PATRIC; fig|223926.6.peg.2697; -.
DR   eggNOG; COG0546; Bacteria.
DR   HOGENOM; CLU_045011_19_1_6; -.
DR   OMA; YLCGKFG; -.
DR   UniPathway; UPA00865; UER00834.
DR   Proteomes; UP000002493; Chromosome 1.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008967; F:phosphoglycolate phosphatase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0046295; P:glycolate biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 1.10.150.240; -; 1.
DR   Gene3D; 3.40.50.1000; -; 1.
DR   HAMAP; MF_00495; GPH_hydrolase_bact; 1.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR006439; HAD-SF_hydro_IA.
DR   InterPro; IPR006549; HAD-SF_hydro_IIIA.
DR   InterPro; IPR041492; HAD_2.
DR   InterPro; IPR023214; HAD_sf.
DR   InterPro; IPR023198; PGP-like_dom2.
DR   InterPro; IPR006346; PGPase/MupP.
DR   InterPro; IPR037512; PGPase_prok.
DR   Pfam; PF13419; HAD_2; 1.
DR   SUPFAM; SSF56784; SSF56784; 1.
DR   TIGRFAMs; TIGR01549; HAD-SF-IA-v1; 1.
DR   TIGRFAMs; TIGR01509; HAD-SF-IA-v3; 1.
DR   TIGRFAMs; TIGR01662; HAD-SF-IIIA; 1.
DR   TIGRFAMs; TIGR01449; PGP_bact; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Hydrolase; Magnesium; Metal-binding;
KW   Reference proteome.
FT   CHAIN           1..228
FT                   /note="Phosphoglycolate phosphatase"
FT                   /id="PRO_0000108044"
FT   ACT_SITE        12
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00495"
FT   BINDING         12
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00495"
FT   BINDING         14
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00495"
FT   BINDING         177
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00495"
SQ   SEQUENCE   228 AA;  24646 MW;  BCE1260EA70E9437 CRC64;
     MTQQDIKLIA FDLDGTLLDS VPDLAVAADQ AVQALGYPAV SEEQVRDYVG NGADVLIGRA
     LSQSMTISSD LSEDLRAKGR ELFDDFYAQS GHQLSHLYPT VKETLEELHQ AGFTMALVTN
     KPSKFVPEIL EQHGIAKYFV DVLGGDAFPE KKPNPVALNW LMEKHQVKAS EMLMVGDSKN
     DILAAKNAGC ASFGLTYGYN HGEPISASNP DFVADSLSEL LEVVAVSA