ID   GPHP_CUPNH              Reviewed;         231 AA.
AC   P40853; Q7WWS5;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 2.
DT   03-AUG-2022, entry version 150.
DE   RecName: Full=Phosphoglycolate phosphatase, plasmid;
DE            Short=PGP;
DE            Short=PGPase;
DE            EC=3.1.3.18;
GN   Name=cbbZP; OrderedLocusNames=PHG419;
OS   Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442
OS   / H16 / Stanier 337) (Ralstonia eutropha).
OG   Plasmid megaplasmid pHG1.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=381666;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SUBUNIT.
RX   PubMed=8226680; DOI=10.1128/jb.175.22.7329-7340.1993;
RA   Schaeferjohann J., Yoo J.-G., Kusian B., Bowien B.;
RT   "The cbb operons of the facultative chemoautotroph Alcaligenes eutrophus
RT   encode phosphoglycolate phosphatase.";
RL   J. Bacteriol. 175:7329-7340(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier 337;
RX   PubMed=12948488; DOI=10.1016/s0022-2836(03)00894-5;
RA   Schwartz E., Henne A., Cramm R., Eitinger T., Friedrich B., Gottschalk G.;
RT   "Complete nucleotide sequence of pHG1: a Ralstonia eutropha H16 megaplasmid
RT   encoding key enzymes of H(2)-based lithoautotrophy and anaerobiosis.";
RL   J. Mol. Biol. 332:369-383(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 (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   -!- SUBUNIT: Homotrimer. {ECO:0000305|PubMed:8226680}.
CC   -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily.
CC       CbbY/CbbZ/Gph/YieH family. {ECO:0000305}.
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DR   EMBL; M68905; AAA20195.1; -; Unassigned_DNA.
DR   EMBL; AY305378; AAP86168.1; -; Genomic_DNA.
DR   PIR; D49934; D49934.
DR   RefSeq; WP_011154331.1; NZ_CP039289.1.
DR   AlphaFoldDB; P40853; -.
DR   SMR; P40853; -.
DR   STRING; 381666.PHG419; -.
DR   EnsemblBacteria; AAP86168; AAP86168; PHG419.
DR   GeneID; 39976703; -.
DR   KEGG; reh:PHG419; -.
DR   PATRIC; fig|381666.6.peg.347; -.
DR   eggNOG; COG0546; Bacteria.
DR   HOGENOM; CLU_045011_19_1_4; -.
DR   OMA; WHACRLL; -.
DR   OrthoDB; 1562270at2; -.
DR   UniPathway; UPA00865; UER00834.
DR   Proteomes; UP000008210; Plasmid megaplasmid pHG1.
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; TIGR01509; HAD-SF-IA-v3; 1.
DR   TIGRFAMs; TIGR01449; PGP_bact; 1.
PE   1: Evidence at protein level;
KW   Calvin cycle; Carbohydrate metabolism; Hydrolase; Magnesium; Metal-binding;
KW   Plasmid; Reference proteome.
FT   CHAIN           1..231
FT                   /note="Phosphoglycolate phosphatase, plasmid"
FT                   /id="PRO_0000108024"
FT   ACT_SITE        14
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   BINDING         14
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         16
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         175
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        157
FT                   /note="R -> Q (in Ref. 1; AAA20195)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   231 AA;  23603 MW;  80499E08185ABD56 CRC64;
     MATVSLPCTA VLIDLDGTLV DCAPDIVEAA NRMLADLGSP ALPFGTVAGF IGRGVPNLVR
     RVLETAQLAP RVDATDAVAM FHRHYADTNG RLGSVFPGVE AGLAALRRQG YRLACVTNKP
     RALAVPLLAL TGLSQYLEVL VAGDSIAQMK PDPEPLRHAC NLLDVDAAQG VLVGDSAVDV
     AAARAAGIPV CLVRYGYAGP GGPAALGADA LVDSLEALPA LLTPARLAPA A