ID PGP_METBU Reviewed; 226 AA. AC Q12UG6; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 22-AUG-2006, sequence version 1. DT 16-JUN-2009, entry version 20. DE RecName: Full=Phosphoglycolate phosphatase; DE Short=PGPase; DE Short=PGP; DE EC=3.1.3.18; GN OrderedLocusNames=Mbur_2034; OS Methanococcoides burtonii (strain DSM 6242). OC Archaea; Euryarchaeota; Methanomicrobia; Methanosarcinales; OC Methanosarcinaceae; Methanococcoides. OX NCBI_TaxID=259564; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Kadner K., Aerts A., Dehal P., Pitluck S., Martinez M., Schmutz J., RA Larimer F., Land M., Hauser L., Kyrpides N., Anderson I., RA Franzmann P., Thomas T., Saunders N., Cavicchioli R., Sowers K., RA Richardson P.; RT "Complete sequence of Methanococcoides burtonii DSM 6242."; RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the dephosphorylation of 2-phosphoglycolate CC (By similarity). CC -!- CATALYTIC ACTIVITY: 2-phosphoglycolate + H(2)O = glycolate + CC phosphate. CC -!- COFACTOR: Magnesium (By similarity). CC -!- SIMILARITY: Belongs to the archaeal SPP-like hydrolase 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; CP000300; ABE52910.1; -; Genomic_DNA. DR RefSeq; YP_566660.1; -. DR GeneID; 3997416; -. DR GenomeReviews; CP000300_GR; Mbur_2034. DR KEGG; mbu:Mbur_2034; -. DR NMPDR; fig|259564.8.peg.1944; -. DR HOGENOM; Q12UG6; -. DR OMA; Q12UG6; NKCRKYD. DR BioCyc; MBUR259564:MBUR_2034-MON; -. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-KW. DR GO; GO:0008967; F:phosphoglycolate phosphatase activity; IEA:HAMAP. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW. DR HAMAP; MF_01419; -; 1. DR InterPro; IPR013200; HAD-SF_hydro-like_3. DR InterPro; IPR006379; HAD-SF_hydro_IIB. DR InterPro; IPR006382; SPPlik_hydro_arc. DR InterPro; IPR006378; Suc_phosP. DR Pfam; PF08282; Hydrolase_3; 2. DR TIGRFAMs; TIGR01484; HAD-SF-IIB; 1. DR TIGRFAMs; TIGR01487; SPP-like; 1. DR TIGRFAMs; TIGR01482; SPP-subfamily; 1. PE 3: Inferred from homology; KW Carbohydrate metabolism; Complete proteome; Hydrolase; Magnesium; KW Metal-binding. FT CHAIN 1 226 Phosphoglycolate phosphatase. FT /FTId=PRO_1000024289. FT ACT_SITE 9 9 Nucleophile (By similarity). FT METAL 9 9 Magnesium (By similarity). FT METAL 11 11 Magnesium (By similarity). FT METAL 173 173 Magnesium (By similarity). FT METAL 177 177 Magnesium (By similarity). FT BINDING 150 150 Substrate (By similarity). SQ SEQUENCE 226 AA; 24084 MW; C2B2DD05D6645E8C CRC64; MVLKAIVIDI DGTITNPDRS LDLDVAKRFR ELNVPVILST GNPLCYVHAA AKLIGISGIV IAENGGVIST GFDSPSIIAD GKEECEKAYE LLSQYHDLVK LDDAYRKTEV VLNRDVAVED LRSTLSENGI DIEIIDTGYA IHIKSTAMNK GTGLLKVAEL MGLEPTDYLA IGDSCNDAEM MQVAGFGIAV ANADSDAIKA ARHITKASFG KGALEAIEYA LSNGLL //