ID   GPHC_CUPNH              Reviewed;         231 AA.
AC   P40852; Q0K1E8;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   03-AUG-2022, entry version 133.
DE   RecName: Full=Phosphoglycolate phosphatase, chromosomal;
DE            Short=PGP;
DE            Short=PGPase;
DE            EC=3.1.3.18;
GN   Name=cbbZC; Synonyms=cbbZ2; OrderedLocusNames=H16_B1387;
OS   Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442
OS   / H16 / Stanier 337) (Ralstonia eutropha).
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=16964242; DOI=10.1038/nbt1244;
RA   Pohlmann A., Fricke W.F., Reinecke F., Kusian B., Liesegang H., Cramm R.,
RA   Eitinger T., Ewering C., Poetter M., Schwartz E., Strittmatter A., Voss I.,
RA   Gottschalk G., Steinbuechel A., Friedrich B., Bowien B.;
RT   "Genome sequence of the bioplastic-producing 'Knallgas' bacterium Ralstonia
RT   eutropha H16.";
RL   Nat. Biotechnol. 24:1257-1262(2006).
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; M68904; AAA20197.1; -; Unassigned_DNA.
DR   EMBL; AM260480; CAJ96176.1; -; Genomic_DNA.
DR   PIR; B49934; B49934.
DR   RefSeq; WP_010809297.1; NC_008314.1.
DR   AlphaFoldDB; P40852; -.
DR   SMR; P40852; -.
DR   STRING; 381666.H16_B1387; -.
DR   EnsemblBacteria; CAJ96176; CAJ96176; H16_B1387.
DR   KEGG; reh:H16_B1387; -.
DR   eggNOG; COG0546; Bacteria.
DR   HOGENOM; CLU_045011_19_1_4; -.
DR   OMA; YLCGKFG; -.
DR   OrthoDB; 1562270at2; -.
DR   BRENDA; 3.1.3.18; 231.
DR   UniPathway; UPA00865; UER00834.
DR   Proteomes; UP000008210; Chromosome 2.
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   Reference proteome.
FT   CHAIN           1..231
FT                   /note="Phosphoglycolate phosphatase, chromosomal"
FT                   /id="PRO_0000108023"
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"
SQ   SEQUENCE   231 AA;  23770 MW;  EC8A8C42060066D8 CRC64;
     MATVSMPCTA VLIDLDGTLV DSAPDIVEAA NRMLADFGSP ALPFDTVAGF IGRGVPNLVR
     RVLETAGLTP RVEAAEAVAM FHRHYAETNG RLGSVFPGVE AGLEALRRQG YRLACVTNKP
     RALAVPLLAL TGLSQYLEVL VAGDSIAQMK PDPEPLRHAC NLLDVDTAQG VLVGDSAVDV
     AAARAAGIPV CLVRYGYAGP GGPAALGADA LLDSLEALPA LLTPARLAPA A