ID PGP2_SULSO Reviewed; 233 AA. AC P95931; DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1997, sequence version 1. DT 16-JUN-2009, entry version 44. DE RecName: Full=Phosphoglycolate phosphatase 2; DE Short=PGPase 2; DE Short=PGP 2; DE EC=3.1.3.18; GN OrderedLocusNames=SSO2157; ORFNames=C01033; OS Sulfolobus solfataricus. OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae; OC Sulfolobus. OX NCBI_TaxID=2287; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2; RX MEDLINE=21332296; PubMed=11427726; DOI=10.1073/pnas.141222098; RA She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., RA Awayez M.J., Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., RA De Moors A., Erauso G., Fletcher C., Gordon P.M.K., RA Heikamp-de Jong I., Jeffries A.C., Kozera C.J., Medina N., Peng X., RA Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C., Tolstrup N., RA Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T., RA Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.; RT "The complete genome of the crenarchaeon Sulfolobus solfataricus P2."; RL Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001). 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; Y08256; CAA69435.1; -; Genomic_DNA. DR EMBL; AE006641; AAK42333.1; -; Genomic_DNA. DR PIR; S74064; S74064. DR RefSeq; NP_343543.1; -. DR GeneID; 1453660; -. DR GenomeReviews; AE006641_GR; SSO2157. DR KEGG; sso:SSO2157; -. DR NMPDR; fig|273057.1.peg.1966; -. DR HOGENOM; P95931; -. DR OMA; P95931; NDAMILP. DR BioCyc; SSOL273057:SSO2157-MON; -. DR BRENDA; 3.1.3.18; 2070. 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; 1. 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 1 233 Phosphoglycolate phosphatase 2. FT /FTId=PRO_0000146729. FT ACT_SITE 13 13 Nucleophile (By similarity). FT METAL 13 13 Magnesium (By similarity). FT METAL 15 15 Magnesium (By similarity). FT METAL 174 174 Magnesium (By similarity). FT METAL 178 178 Magnesium (By similarity). FT BINDING 152 152 Substrate (By similarity). SQ SEQUENCE 233 AA; 26215 MW; 5E3AE64515CAAD90 CRC64; MDIGSNEILV ASDYDRTLAS EENNFVISPI VSQKVNEFSK KYKFVVVTGR EKKFIDKLAV GLKPTAWILE NGSLILFNDR EFVLCEKSWF ERDRKKIIEI LDNLKVRYSI GRIILYVDGY GSKLDMLSEI EKYGRIEVNR NDAMILPKGV DKGVGVLKFK ELTGFKGKII ALGDSENDYA LFRVADIKVA VANAIPQIKE IADIVTENPN GLGVVEILDK ILSGNFGKEV DIY //