ID GPH_XANC8 Reviewed; 221 AA. AC Q4UVL3; DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2005, sequence version 1. DT 16-JUN-2009, entry version 25. DE RecName: Full=Phosphoglycolate phosphatase; DE Short=PGPase; DE Short=PGP; DE EC=3.1.3.18; GN OrderedLocusNames=XC_1847; OS Xanthomonas campestris pv. campestris (strain 8004). OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Xanthomonas. OX NCBI_TaxID=314565; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15899963; DOI=10.1101/gr.3378705; RA Qian W., Jia Y., Ren S.-X., He Y.-Q., Feng J.-X., Lu L.-F., Sun Q., RA Ying G., Tang D.-J., Tang H., Wu W., Hao P., Wang L., Jiang B.-L., RA Zeng S., Gu W.-Y., Lu G., Rong L., Tian Y., Yao Z., Fu G., Chen B., RA Fang R., Qiang B., Chen Z., Zhao G.-P., Tang J.-L., He C.; RT "Comparative and functional genomic analyses of the pathogenicity of RT phytopathogen Xanthomonas campestris pv. campestris."; RL Genome Res. 15:757-767(2005). 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; CP000050; AAY48910.1; -; Genomic_DNA. DR RefSeq; YP_242930.1; -. DR GeneID; 3380394; -. DR GenomeReviews; CP000050_GR; XC_1847. DR KEGG; xcb:XC_1847; -. DR HOGENOM; Q4UVL3; -. DR OMA; Q4UVL3; APDFIAI. DR BioCyc; XCAM314565:XC_1847-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 1 221 Phosphoglycolate phosphatase. FT /FTId=PRO_0000238183. FT ACT_SITE 10 10 Nucleophile (By similarity). SQ SEQUENCE 221 AA; 24075 MW; BFF0E5487F276B21 CRC64; MRFPRAVLFD LDGTLLDSAP DMLATVNAML SERGLPCITL AQLRPVVSKG SRAMLAVAFA HLDAAAREAL VPEFLKRYEA LLGTQAQLFD GVEVMLQRLE QAGCVWGIVT NKPEYLAQLI LPQLGWQQRC AVLIGGDTLA ERKPHPLPLL VAADRIGVAA TQCVYVGDDE RDILAARAAG MPSVAALWGY RLGDDDPLSW QADVLVEQPP QLWEPAAWPQ P //