ID   PGP_PYRFU               Reviewed;         231 AA.
AC   Q8U111;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   16-JUN-2009, entry version 30.
DE   RecName: Full=Phosphoglycolate phosphatase;
DE            Short=PGPase;
DE            Short=PGP;
DE            EC=3.1.3.18;
GN   OrderedLocusNames=PF1419;
OS   Pyrococcus furiosus.
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=2261;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RA   Weiss R.B., Dunn D.M., Robb F.T., Brown J.R.;
RT   "The complete sequence of the Pyrococcus furiosus genome.";
RL   Submitted (FEB-2002) 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.
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DR   EMBL; AE010245; AAL81543.1; -; Genomic_DNA.
DR   RefSeq; NP_579148.1; -.
DR   SMR; Q8U111; 1-231.
DR   GeneID; 1469295; -.
DR   GenomeReviews; AE009950_GR; PF1419.
DR   KEGG; pfu:PF1419; -.
DR   NMPDR; fig|186497.1.peg.1466; -.
DR   HOGENOM; Q8U111; -.
DR   OMA; Q8U111; DEEWILW.
DR   BRENDA; 3.1.3.18; 321.
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; IPR005834; Dehalogen-like_hydro.
DR   InterPro; IPR006379; HAD-SF_hydro_IIB.
DR   InterPro; IPR006382; SPPlik_hydro_arc.
DR   InterPro; IPR006378; Suc_phosP.
DR   Pfam; PF00702; Hydrolase; 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    231       Phosphoglycolate phosphatase.
FT                                /FTId=PRO_0000146724.
FT   ACT_SITE      9      9       Nucleophile (By similarity).
FT   METAL         9      9       Magnesium (By similarity).
FT   METAL        11     11       Magnesium (By similarity).
FT   METAL       177    177       Magnesium (By similarity).
FT   METAL       181    181       Magnesium (By similarity).
FT   BINDING     154    154       Substrate (By similarity).
SQ   SEQUENCE   231 AA;  25506 MW;  CA251F366C743441 CRC64;
     MKIKAISLDI DGTITYPNRM IHEEALQAIR KAESLGVPIM LVTGNTVQFA EAASILIGTS
     GPVVAEDGGA ISYKKKRIFL TSMDEEWILW GELKKRFPNV KTSHTMPDRR AGLVIMRETI
     DVETVRKLIK ELNLNLVAVD SGFAIHVKKP WINKGSGIEK ACELLGLNPK EVAHVGDGEN
     DLDAFKVVGY RIAVAQAPKI LKENADYITQ NEYGKGGAEA IYHILEKFGY I
//