GPH_SALTY
ID GPH_SALTY Reviewed; 252 AA.
AC Q8ZLK5;
DT 03-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 116.
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=gph {ECO:0000255|HAMAP-Rule:MF_00495}; OrderedLocusNames=STM3482;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
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 -!- COFACTOR:
CC Name=chloride; Xref=ChEBI:CHEBI:17996;
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 -!- SUBUNIT: Monomer. {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; AE006468; AAL22344.1; -; Genomic_DNA.
DR RefSeq; NP_462385.1; NC_003197.2.
DR RefSeq; WP_000359655.1; NC_003197.2.
DR AlphaFoldDB; Q8ZLK5; -.
DR SMR; Q8ZLK5; -.
DR STRING; 99287.STM3482; -.
DR PaxDb; Q8ZLK5; -.
DR EnsemblBacteria; AAL22344; AAL22344; STM3482.
DR GeneID; 1255005; -.
DR KEGG; stm:STM3482; -.
DR PATRIC; fig|99287.12.peg.3680; -.
DR HOGENOM; CLU_045011_19_1_6; -.
DR OMA; YLCGKFG; -.
DR PhylomeDB; Q8ZLK5; -.
DR BioCyc; SENT99287:STM3482-MON; -.
DR UniPathway; UPA00865; UER00834.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008967; F:phosphoglycolate phosphatase activity; IBA:GO_Central.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0016311; P:dephosphorylation; IBA:GO_Central.
DR GO; GO:0006281; P:DNA repair; IBA:GO_Central.
DR GO; GO:0046295; P:glycolate biosynthetic process; IEA:UniProtKB-UniPathway.
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 3: Inferred from homology;
KW Carbohydrate metabolism; Chloride; Hydrolase; Magnesium; Metal-binding;
KW Reference proteome.
FT CHAIN 1..252
FT /note="Phosphoglycolate phosphatase"
FT /id="PRO_0000108041"
FT ACT_SITE 13
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00495"
FT BINDING 13
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00495"
FT BINDING 15
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00495"
FT BINDING 192
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00495"
SQ SEQUENCE 252 AA; 27303 MW; 1216F19E6D086B97 CRC64;
MDKLQNIRGV AFDLDGTLVD SAPGLAAAVD MALYALELPV AGEERVITWI GNGADVLMER
ALTWAREERA TLRKTMGKPP VDEDIPAEEQ VRILRKLFDR YYGEVAEEGT VLFPHVADTL
GALHASGLSL GLVTNKPTPF VAPLLESLDI AKYFSVVIGG DDVQNKKPHP EPLLLVASRL
GMMPEQMLFV GDSRNDIQAA KAAGCPSVGL TYGYNYGEAI ALSEPDVIYD SFNDLLPALG
LPHSDNQEIK ND
