ID   GPH_PSEPU               Reviewed;         251 AA.
AC   P42509;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=Probable phosphoglycolate phosphatase;
DE            Short=PGP;
DE            Short=PGPase;
DE            EC=3.1.3.18;
DE   Flags: Fragment;
GN   Name=gph;
OS   Pseudomonas putida (Arthrobacter siderocapsulatus).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=303;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 23287 / C1S;
RX   PubMed=2404959; DOI=10.1128/jb.172.2.867-883.1990;
RA   Essar D.W., Eberly L., Crawford I.P.;
RT   "Evolutionary differences in chromosomal locations of four early genes of
RT   the tryptophan pathway in fluorescent pseudomonads: DNA sequences and
RT   characterization of Pseudomonas putida trpE and trpGDC.";
RL   J. Bacteriol. 172:867-883(1990).
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 (By
CC       similarity). {ECO:0000250}.
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   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- PATHWAY: Organic acid metabolism; glycolate biosynthesis; glycolate
CC       from 2-phosphoglycolate: step 1/1.
CC   -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily.
CC       CbbY/CbbZ/Gph/YieH family. {ECO:0000305}.
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DR   EMBL; M33799; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   PIR; F35115; F35115.
DR   AlphaFoldDB; P42509; -.
DR   SMR; P42509; -.
DR   UniPathway; UPA00865; UER00834.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008967; F:phosphoglycolate phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
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.
FT   CHAIN           <1..251
FT                   /note="Probable phosphoglycolate phosphatase"
FT                   /id="PRO_0000108035"
FT   BINDING         161
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   NON_TER         1
SQ   SEQUENCE   251 AA;  27465 MW;  41D77642C946F23E CRC64;
     GTLIDSVPDL AAAVDRMLLE LGRPPADLEA VRHWVGNGAQ VLVRRALAGG IEHDAVDDVL
     AEQGLALFME AYAQSHELTV VYPGVKDTLR WLQKQGVEMA LITNKPERFV APLLDQMKIG
     RYFRWMIGGD TLPQKKPDPA ALLFVMQMAG VTPQQSLFVG DSRSDVLAAK AAGVQCVGLT
     YGYNHGRPIH DETPSLVIDD LRALLPGCED PATGITLADL QASQDRESTV AVTGKFWMKV
     IKALARWRWR A