ID GPH_XYLFA Reviewed; 229 AA. AC Q9PAM6; DT 05-DEC-2001, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 02-SEP-2026, entry version 126. 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=XF_2470; OS Xylella fastidiosa (strain 9a5c). OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Lysobacterales; Lysobacteraceae; Xylella. OX NCBI_TaxID=160492; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=9a5c; RX PubMed=10910347; DOI=10.1038/35018003; RA Simpson A.J.G., Reinach F.C., Arruda P., Abreu F.A., Acencio M., RA Alvarenga R., Alves L.M.C., Araya J.E., Baia G.S., Baptista C.S., RA Barros M.H., Bonaccorsi E.D., Bordin S., Bove J.M., Briones M.R.S., RA Bueno M.R.P., Camargo A.A., Camargo L.E.A., Carraro D.M., Carrer H., RA Colauto N.B., Colombo C., Costa F.F., Costa M.C.R., Costa-Neto C.M., RA Coutinho L.L., Cristofani M., Dias-Neto E., Docena C., El-Dorry H., RA Facincani A.P., Ferreira A.J.S., Ferreira V.C.A., Ferro J.A., Fraga J.S., RA Franca S.C., Franco M.C., Frohme M., Furlan L.R., Garnier M., Goldman G.H., RA Goldman M.H.S., Gomes S.L., Gruber A., Ho P.L., Hoheisel J.D., RA Junqueira M.L., Kemper E.L., Kitajima J.P., Krieger J.E., Kuramae E.E., RA Laigret F., Lambais M.R., Leite L.C.C., Lemos E.G.M., Lemos M.V.F., RA Lopes S.A., Lopes C.R., Machado J.A., Machado M.A., Madeira A.M.B.N., RA Madeira H.M.F., Marino C.L., Marques M.V., Martins E.A.L., Martins E.M.F., RA Matsukuma A.Y., Menck C.F.M., Miracca E.C., Miyaki C.Y., RA Monteiro-Vitorello C.B., Moon D.H., Nagai M.A., Nascimento A.L.T.O., RA Netto L.E.S., Nhani A. Jr., Nobrega F.G., Nunes L.R., Oliveira M.A., RA de Oliveira M.C., de Oliveira R.C., Palmieri D.A., Paris A., Peixoto B.R., RA Pereira G.A.G., Pereira H.A. Jr., Pesquero J.B., Quaggio R.B., RA Roberto P.G., Rodrigues V., de Rosa A.J.M., de Rosa V.E. Jr., de Sa R.G., RA Santelli R.V., Sawasaki H.E., da Silva A.C.R., da Silva A.M., RA da Silva F.R., Silva W.A. Jr., da Silveira J.F., Silvestri M.L.Z., RA Siqueira W.J., de Souza A.A., de Souza A.P., Terenzi M.F., Truffi D., RA Tsai S.M., Tsuhako M.H., Vallada H., Van Sluys M.A., Verjovski-Almeida S., RA Vettore A.L., Zago M.A., Zatz M., Meidanis J., Setubal J.C.; RT "The genome sequence of the plant pathogen Xylella fastidiosa."; RL Nature 406:151-159(2000). 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; Evidence={ECO:0000255|HAMAP- CC 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AE003849; AAF85268.1; -; Genomic_DNA. DR PIR; G82553; G82553. DR RefSeq; WP_010894913.1; NC_002488.3. DR AlphaFoldDB; Q9PAM6; -. DR SMR; Q9PAM6; -. DR STRING; 160492.XF_2470; -. DR KEGG; xfa:XF_2470; -. DR eggNOG; COG0546; Bacteria. DR HOGENOM; CLU_045011_19_1_6; -. DR UniPathway; UPA00865; UER00834. DR Proteomes; UP000000812; Chromosome. DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter. DR GO; GO:0008967; F:phosphoglycolate phosphatase activity; IEA:UniProtKB-UniRule. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro. DR GO; GO:0006281; P:DNA repair; IEA:TreeGrafter. DR GO; GO:0046295; P:glycolate biosynthetic process; IEA:UniProtKB-UniRule. DR FunFam; 3.40.50.1000:FF:000022; Phosphoglycolate phosphatase; 1. DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1. DR Gene3D; 1.10.150.240; Putative phosphatase, domain 2; 1. DR HAMAP; MF_00495; GPH_hydrolase_bact; 1. DR InterPro; IPR050155; HAD-like_hydrolase_sf. 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; IPR037512; PGPase_prok. DR NCBIfam; TIGR01549; HAD-SF-IA-v1; 1. DR NCBIfam; TIGR01509; HAD-SF-IA-v3; 1. DR NCBIfam; TIGR01449; PGP_bact; 1. DR NCBIfam; NF009700; PRK13226.1; 1. DR PANTHER; PTHR43434; PHOSPHOGLYCOLATE PHOSPHATASE; 1. DR PANTHER; PTHR43434:SF23; PHOSPHOGLYCOLATE PHOSPHATASE; 1. DR Pfam; PF13419; HAD_2; 1. DR PRINTS; PR00413; HADHALOGNASE. DR SFLD; SFLDG01129; C1.5:_HAD__Beta-PGM__Phosphata; 1. DR SFLD; SFLDS00003; Haloacid_Dehalogenase; 1. DR SUPFAM; SSF56784; HAD-like; 1. PE 3: Inferred from homology; KW Carbohydrate metabolism; Hydrolase; Magnesium; Metal-binding; KW Reference proteome. FT CHAIN 1..229 FT /note="Phosphoglycolate phosphatase" FT /id="PRO_0000108048" FT ACT_SITE 18 FT /note="Nucleophile" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00495" FT BINDING 18 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00495" FT BINDING 20 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00495" FT BINDING 176 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00495" SQ SEQUENCE 229 AA; 24760 MW; C72F1B9EEEFC869B CRC64; MPLNEPSSNA FPRTVLFDLD GTLLDSAPDM LATANAMLAA RGRAPITLAQ LRPVISIGTF RILAVAFPEL DAAAIQGLIP EFLQRYEALI GSVSKPFDGV EMMLDALECA GTVWGIVTNK PEFLARLILP LLGWTSRCAV LIGGDTLAER KPHPLPLLTA AERIGVMPTD CVYVGDDVSD IQAARAAGMP SMVALWGYRS HEDNPMTWQA DTLVEQPHLL SRPDVWPST //