ID   GPH_NITMU               Reviewed;         227 AA.
AC   Q2Y6G2;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 94.
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=Nmul_A2370;
OS   Nitrosospira multiformis (strain ATCC 25196 / NCIMB 11849 / C 71).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales;
OC   Nitrosomonadaceae; Nitrosospira.
OX   NCBI_TaxID=323848;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25196 / NCIMB 11849 / C 71;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M.,
RA   Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Lykidis A., Richardson P.;
RT   "Complete sequence of chromosome 1 of Nitrosospira multiformis ATCC
RT   25196.";
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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; CP000103; ABB75659.1; -; Genomic_DNA.
DR   RefSeq; WP_011381660.1; NZ_FNVK01000016.1.
DR   AlphaFoldDB; Q2Y6G2; -.
DR   SMR; Q2Y6G2; -.
DR   STRING; 323848.Nmul_A2370; -.
DR   EnsemblBacteria; ABB75659; ABB75659; Nmul_A2370.
DR   KEGG; nmu:Nmul_A2370; -.
DR   eggNOG; COG0546; Bacteria.
DR   HOGENOM; CLU_045011_19_1_4; -.
DR   OMA; YLCGKFG; -.
DR   OrthoDB; 1562270at2; -.
DR   UniPathway; UPA00865; UER00834.
DR   Proteomes; UP000002718; Chromosome.
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; 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   PRINTS; PR00413; HADHALOGNASE.
DR   SUPFAM; SSF56784; SSF56784; 1.
DR   TIGRFAMs; TIGR01549; HAD-SF-IA-v1; 1.
DR   TIGRFAMs; TIGR01509; HAD-SF-IA-v3; 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..227
FT                   /note="Phosphoglycolate phosphatase"
FT                   /id="PRO_0000238163"
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         176
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00495"
SQ   SEQUENCE   227 AA;  25018 MW;  24F35C53F3AEE359 CRC64;
     MHFPLPIKAV MIDLDGTLLD TAPDLATAAN MMLKELGKAE LPLETIQSYI GKGIEKLVKR
     SLTGDLDGEP DSDLLRRAMP LYERSYEKTL YVDTRAYPGV REGLNALRAG GFRLACVTNK
     AEAFTLPLLR AAELLDYFDI VVSGDSLPKK KPDPMPLLHA CERFEIQPHD MLLVGDSLND
     AQAARAAGSH VFCVPYGYNE GRDVYELDCD AIVPSLYEAT KLIQKSS