ID GPH_PSEPF Reviewed; 272 AA. AC Q3K5U8; DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot. DT 08-NOV-2005, sequence version 1. DT 16-JUN-2009, entry version 30. DE RecName: Full=Phosphoglycolate phosphatase; DE Short=PGPase; DE Short=PGP; DE EC=3.1.3.18; GN OrderedLocusNames=Pfl01_5119; OS Pseudomonas fluorescens (strain Pf0-1). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=205922; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., RA Hammon N., Israni S., Pitluck S., Saunders E.H., Schmutz J., RA Larimer F., Land M., Kyripides N., Anderson I., Richardson P.; RT "Complete sequence of Pseudomonas fluorescens PfO-1."; RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Specifically catalyzes the dephosphorylation of 2- CC phosphoglycolate. Is involved in the dissimilation of the CC intracellular 2-phosphoglycolate formed during the DNA repair of CC 3'-phosphoglycolate ends, a major class of DNA lesions induced by CC oxidative stress (By similarity). CC -!- CATALYTIC ACTIVITY: 2-phosphoglycolate + H(2)O = glycolate + CC phosphate. CC -!- PATHWAY: Organic acid metabolism; glycolic acid biosynthesis; CC glycolic acid from 2-phosphoglycolic acid: step 1/1. CC -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily. CC CbbY/cbbZ/gph/yieH family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000094; ABA76856.1; -; Genomic_DNA. DR RefSeq; YP_350847.1; -. DR GeneID; 3717037; -. DR GenomeReviews; CP000094_GR; Pfl01_5119. DR KEGG; pfo:Pfl01_5119; -. DR HOGENOM; Q3K5U8; -. DR OMA; Q3K5U8; DSSNDAQ. DR BioCyc; PFLU205922:PFL_5119-MON; -. DR GO; GO:0008967; F:phosphoglycolate phosphatase activity; IEA:HAMAP. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:HAMAP. DR HAMAP; MF_00495; -; 1. DR InterPro; IPR005834; Dehalogen-like_hydro. DR InterPro; IPR006439; HAD-SF_hydro_IA_v1. DR InterPro; IPR006402; HAD-SF_hydro_IA_v3. DR InterPro; IPR005833; Haloacid_DH/epoxide_hydro. DR InterPro; IPR006346; PGP_bact. DR Pfam; PF00702; Hydrolase; 1. DR PRINTS; PR00413; HADHALOGNASE. 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; Complete proteome; Hydrolase. FT CHAIN 1 272 Phosphoglycolate phosphatase. FT /FTId=PRO_0000238167. FT ACT_SITE 19 19 Nucleophile (By similarity). SQ SEQUENCE 272 AA; 29558 MW; 0E4BC755EE6F830D CRC64; MSGFEQLFPG QLPRLVMFDL DGTLIDSVPD LAAAVDNMLL SLGRKPAGIE SVREWVGNGA PVLVRRALAG GIDHSSVDDV EAEHALEVFM EAYGASHELT VVYPGVRDTL KWLHKQGVAM ALITNKPERF VAPLLDQMKI GRYFKWIIGG DTLPQKKPDP AALFFVMKMS GIPASQSLFV GDSRSDVLAA KAAGVKCVGL SYGYNHGRPI AEESPTLVID DLRKLIPGCL DTAAEITLPD AAQSPSGNAI VVVTRKLWMK VIKALARWRW RA //