GPH_CERS4
ID GPH_CERS4 Reviewed; 218 AA.
AC Q3IYC6;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 101.
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}; OrderedLocusNames=RHOS4_28900;
GN ORFNames=RSP_1278;
OS Cereibacter sphaeroides (strain ATCC 17023 / DSM 158 / JCM 6121 / CCUG
OS 31486 / LMG 2827 / NBRC 12203 / NCIMB 8253 / ATH 2.4.1.) (Rhodobacter
OS sphaeroides).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Cereibacter.
OX NCBI_TaxID=272943;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17023 / DSM 158 / JCM 6121 / CCUG 31486 / LMG 2827 / NBRC 12203
RC / NCIMB 8253 / ATH 2.4.1.;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Richardson P., Mackenzie C.,
RA Choudhary M., Larimer F., Hauser L.J., Land M., Donohue T.J., Kaplan S.;
RT "Complete sequence of chromosome 1 of Rhodobacter sphaeroides 2.4.1.";
RL Submitted (SEP-2005) 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; CP000143; ABA80458.1; -; Genomic_DNA.
DR RefSeq; WP_011338841.1; NZ_CP030271.1.
DR RefSeq; YP_354359.1; NC_007493.2.
DR AlphaFoldDB; Q3IYC6; -.
DR SMR; Q3IYC6; -.
DR STRING; 272943.RSP_1278; -.
DR EnsemblBacteria; ABA80458; ABA80458; RSP_1278.
DR KEGG; rsp:RSP_1278; -.
DR PATRIC; fig|272943.9.peg.3259; -.
DR eggNOG; COG0546; Bacteria.
DR OMA; WAVPYGY; -.
DR PhylomeDB; Q3IYC6; -.
DR UniPathway; UPA00865; UER00834.
DR Proteomes; UP000002703; Chromosome 1.
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-UniRule.
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; Reference proteome.
FT CHAIN 1..218
FT /note="Phosphoglycolate phosphatase"
FT /id="PRO_0000238173"
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; 23310 MW; 6198C9CB039FFA33 CRC64;
MPGVVFDLDG TLVHSAPDIH AAVNKALAEE GGAPFTLAEI TGFIGNGVPV LIQRVLAARG
EAPDAHRQAE LQGRFMAHYE ADPATLTSVY PGAEAAIRHL RAEGWRIGLC TNKPVGASRQ
ILSLFGLLEL FDAIIGGDSL PQRKPDPAPL RATAAALNEE VVLYVGDSEV DAATAEAAGL
RFALFTEGYR HAPVHELPHH GLFSHHDELQ DLLRRLLA
