ID GPH_THIDA Reviewed; 227 AA. AC Q3SGR5; DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2005, sequence version 1. DT 16-JUN-2009, entry version 29. DE RecName: Full=Phosphoglycolate phosphatase; DE Short=PGPase; DE Short=PGP; DE EC=3.1.3.18; GN OrderedLocusNames=Tbd_2229; OS Thiobacillus denitrificans (strain ATCC 25259). OC Bacteria; Proteobacteria; Betaproteobacteria; Hydrogenophilales; OC Hydrogenophilaceae; Thiobacillus. OX NCBI_TaxID=292415; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16452431; DOI=10.1128/JB.188.4.1473-1488.2006; RA Beller H.R., Chain P.S., Letain T.E., Chakicherla A., Larimer F.W., RA Richardson P.M., Coleman M.A., Wood A.P., Kelly D.P.; RT "The genome sequence of the obligately chemolithoautotrophic, RT facultatively anaerobic bacterium Thiobacillus denitrificans."; RL J. Bacteriol. 188:1473-1488(2006). 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; CP000116; AAZ98182.1; -; Genomic_DNA. DR RefSeq; YP_315987.1; -. DR GeneID; 3673919; -. DR GenomeReviews; CP000116_GR; Tbd_2229. DR KEGG; tbd:Tbd_2229; -. DR NMPDR; fig|292415.3.peg.2160; -. DR HOGENOM; Q3SGR5; -. DR OMA; Q3SGR5; DSSNDAQ. DR BioCyc; TDEN292415:TBD_2229-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 1 227 Phosphoglycolate phosphatase. FT /FTId=PRO_0000238181. FT ACT_SITE 14 14 Nucleophile (By similarity). SQ SEQUENCE 227 AA; 24331 MW; 4A8399AA64E5334D CRC64; MKSFPLPIKA VVIDLDGTLL NTAPDLAHAA ELMMAELGRP CPSLETISTY IGNGVSRLVK RVLTGEMDAE PDPALFAQAI ASYQKHYGEH VSLHSRPFDG VVEGLQAFKA MGLHMACITN KAEQFTVPLL KGTGLYDYFE LILSGDTLPK RKPDPLPLLH ACEVFGVAPA ELLLIGDSLN DTQAARAAGC PVFCVPYGYN RGRPVTELDL DAVVPSLAEA ALMVTKA //