ID   GPH_RHOCA               Reviewed;         219 AA.
AC   O33512;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Phosphoglycolate phosphatase;
DE            Short=PGP;
DE            Short=PGPase;
DE            EC=3.1.3.18;
GN   Name=cbbZ;
OS   Rhodobacter capsulatus (Rhodopseudomonas capsulata).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Rhodobacter.
OX   NCBI_TaxID=1061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 11166 / DSM 1710 / CCUG 31484 / JCM 21090 / LMG 2962 / NBRC
RC   16435 / NCIMB 8254 / ATH 2.3.1;
RA   Larimer F.W., Lu T.-Y.S., Buley D.M.;
RL   Submitted (APR-1995) 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 (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; U23145; AAB82051.1; -; Genomic_DNA.
DR   PIR; T10509; T10509.
DR   RefSeq; WP_055208338.1; NZ_QKZO01000002.1.
DR   AlphaFoldDB; O33512; -.
DR   SMR; O33512; -.
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-UniRule.
DR   GO; GO:0046295; P:glycolate biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0019253; P:reductive pentose-phosphate cycle; IEA:UniProtKB-KW.
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; TIGR01449; PGP_bact; 1.
PE   3: Inferred from homology;
KW   Calvin cycle; Carbohydrate metabolism; Hydrolase; Magnesium; Metal-binding.
FT   CHAIN           1..219
FT                   /note="Phosphoglycolate phosphatase"
FT                   /id="PRO_0000108038"
FT   ACT_SITE        8
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   BINDING         8
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         10
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         167
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   219 AA;  23853 MW;  135AACC8B54157D6 CRC64;
     MAPALIFDLD GTLIDSAPAI HKVSNDVLRA RGYAPLGLDQ IRSFVGQGAP HLVRCLLTTA
     GEDPEGPLFD AIYADLVSRY ETDVEGNTLY PGVITALQRL REMGCPMAIT TNKPYKPALA
     AIAHVGLTDY FQLVIGGDSL PTRKPNPEMV NEARRVLRRP HALYIGDSEI DAQTAQNAGL
     PFVIYTEGYR KTPLDALPHA AKFHDFSALP GIVEGWTWS