ID   GPH_COLP3               Reviewed;         226 AA.
AC   Q48A85;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 103.
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=CPS_0261;
OS   Colwellia psychrerythraea (strain 34H / ATCC BAA-681) (Vibrio
OS   psychroerythus).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Colwelliaceae; Colwellia.
OX   NCBI_TaxID=167879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=34H / ATCC BAA-681;
RX   PubMed=16043709; DOI=10.1073/pnas.0504766102;
RA   Methe B.A., Nelson K.E., Deming J.W., Momen B., Melamud E., Zhang X.,
RA   Moult J., Madupu R., Nelson W.C., Dodson R.J., Brinkac L.M.,
RA   Daugherty S.C., Durkin A.S., DeBoy R.T., Kolonay J.F., Sullivan S.A.,
RA   Zhou L., Davidsen T.M., Wu M., Huston A.L., Lewis M., Weaver B.,
RA   Weidman J.F., Khouri H., Utterback T.R., Feldblyum T.V., Fraser C.M.;
RT   "The psychrophilic lifestyle as revealed by the genome sequence of
RT   Colwellia psychrerythraea 34H through genomic and proteomic analyses.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:10913-10918(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;
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; CP000083; AAZ25705.1; -; Genomic_DNA.
DR   RefSeq; WP_011041135.1; NC_003910.7.
DR   AlphaFoldDB; Q48A85; -.
DR   SMR; Q48A85; -.
DR   STRING; 167879.CPS_0261; -.
DR   EnsemblBacteria; AAZ25705; AAZ25705; CPS_0261.
DR   KEGG; cps:CPS_0261; -.
DR   HOGENOM; CLU_045011_19_1_6; -.
DR   OMA; YLCGKFG; -.
DR   OrthoDB; 1562270at2; -.
DR   UniPathway; UPA00865; UER00834.
DR   Proteomes; UP000000547; 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   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..226
FT                   /note="Phosphoglycolate phosphatase"
FT                   /id="PRO_0000238156"
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   226 AA;  24921 MW;  FA9A818C14D90DD2 CRC64;
     MKLQEKEVLL FDLDGTLVDS APDLALAVNR TLKDLNKATF DQDTIHHWVG NGAKVLIERA
     LSGSAIIDKE LDETLTKDAL TIFLAHYQQC LCIESVLYDD VQEGLLSLKA AGFRLAIITN
     KPAIFIQPIL TGLGIDNLFE LLIGGDTLAD KKPHPAPLHY AMKQLNVVAE QCVMIGDSKN
     DILAAKAANI DSVGLTYGYN YGEDINQYGP QWCFDTFNEL LISLKR