ID PGP_SULAC Reviewed; 227 AA. AC Q4J8P4; DT 27-SEP-2005, integrated into UniProtKB/Swiss-Prot. DT 02-AUG-2005, sequence version 1. DT 16-JUN-2009, entry version 26. DE RecName: Full=Phosphoglycolate phosphatase; DE Short=PGPase; DE Short=PGP; DE EC=3.1.3.18; GN OrderedLocusNames=Saci_1518; OS Sulfolobus acidocaldarius. OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae; OC Sulfolobus. OX NCBI_TaxID=2285; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33909 / DSM 639 / IFO 15157 / JCM 8929 / NCIB 11770; RX PubMed=15995215; DOI=10.1128/JB.187.14.4992-4999.2005; RA Chen L., Bruegger K., Skovgaard M., Redder P., She Q., Torarinsson E., RA Greve B., Awayez M., Zibat A., Klenk H.-P., Garrett R.A.; RT "The genome of Sulfolobus acidocaldarius, a model organism of the RT Crenarchaeota."; RL J. Bacteriol. 187:4992-4999(2005). 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; CP000077; AAY80837.1; -; Genomic_DNA. DR RefSeq; YP_256130.1; -. DR GeneID; 3474642; -. DR GenomeReviews; CP000077_GR; Saci_1518. DR KEGG; sai:Saci_1518; -. DR NMPDR; fig|330779.3.peg.178; -. DR HOGENOM; Q4J8P4; -. DR OMA; Q4J8P4; NKCRKYD. DR BioCyc; SACI330779:SACI_1518-MON; -. DR BRENDA; 3.1.3.18; 434. 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 Pfam; PF08282; Hydrolase_3; 2. DR TIGRFAMs; TIGR01484; HAD-SF-IIB; 1. DR TIGRFAMs; TIGR01487; SPP-like; 1. PE 3: Inferred from homology; KW Carbohydrate metabolism; Complete proteome; Hydrolase; Magnesium; KW Metal-binding. FT CHAIN 1 227 Phosphoglycolate phosphatase. FT /FTId=PRO_0000146727. FT ACT_SITE 8 8 Nucleophile (By similarity). FT METAL 8 8 Magnesium (By similarity). FT METAL 10 10 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 227 AA; 25468 MW; 03CAD324863C5D55 CRC64; MIRLILTDVD GTLTFDRDTY NIDLDAVDLL RKVEKKGIKV GLVSGNSYPV LRALYTYFGF NGGIVAENGC IVYYDNQLKE VCERVERSLI SEFENRFGVK GSWQNQFKVC DFSFYPPILK DEMVKWALDK GLYIKTSGYA VHISKSKRGK AEGVRELIKM HGLDKAEVVG IGDSSTDIEF LEEVGIRVVV GNADESLKSI GDFVMREKSG KAVVEFIKKV ITGEINE //