GPH_CERS5
ID GPH_CERS5 Reviewed; 218 AA.
AC A4WW31;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 91.
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 Name=cbbZ {ECO:0000255|HAMAP-Rule:MF_00495};
GN OrderedLocusNames=Rsph17025_2708;
OS Cereibacter sphaeroides (strain ATCC 17025 / ATH 2.4.3) (Rhodobacter
OS sphaeroides).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Cereibacter.
OX NCBI_TaxID=349102;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17025 / ATH 2.4.3;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chertkov O., Brettin T., Bruce D., Han C., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E., Richardson P., Mackenzie C., Choudhary M.,
RA Donohue T.J., Kaplan S.;
RT "Complete sequence of chromosome of Rhodobacter sphaeroides ATCC 17025.";
RL Submitted (APR-2007) 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.
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; CP000661; ABP71595.1; -; Genomic_DNA.
DR AlphaFoldDB; A4WW31; -.
DR SMR; A4WW31; -.
DR STRING; 349102.Rsph17025_2708; -.
DR EnsemblBacteria; ABP71595; ABP71595; Rsph17025_2708.
DR KEGG; rsq:Rsph17025_2708; -.
DR eggNOG; COG0546; Bacteria.
DR HOGENOM; CLU_045011_19_1_5; -.
DR OMA; WAVPYGY; -.
DR OrthoDB; 1562270at2; -.
DR BioCyc; RSPH349102:G1G8M-2788-MON; -.
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;
KW Photosynthesis.
FT CHAIN 1..218
FT /note="Phosphoglycolate phosphatase"
FT /id="PRO_1000050596"
FT ACT_SITE 7
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00495"
FT BINDING 7
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00495"
FT BINDING 9
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00495"
FT BINDING 167
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00495"
SQ SEQUENCE 218 AA; 23526 MW; B018A83F938596F8 CRC64;
MPGVVFDLDG TLVHSAPDIH AAVNRALAEE GAEPFSLAEI TGFIGNGVPV LIKRVLAARG
ETPDGHRHAE MQDRFMKHYE ADPTALTSVY PGAEAALRHL HSEGWRIALC TNKPYAASRQ
ILSNFGILDL FDAIVGGDCL PQRKPDPAPL RAAAAALTEE VVLYVGDSEV DAATAEAAGL
RFALFTEGYR HAPVHDLPHH GLFSHHDELP DLLRHLLA
