ID   GPH_PSEF5               Reviewed;         272 AA.
AC   Q4K4Z4;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   16-JUN-2009, entry version 24.
DE   RecName: Full=Phosphoglycolate phosphatase;
DE            Short=PGPase;
DE            Short=PGP;
DE            EC=3.1.3.18;
GN   OrderedLocusNames=PFL_5630;
OS   Pseudomonas fluorescens (strain Pf-5 / ATCC BAA-477).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=220664;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15980861; DOI=10.1038/nbt1110;
RA   Paulsen I.T., Press C.M., Ravel J., Kobayashi D.Y., Myers G.S.A.,
RA   Mavrodi D.V., DeBoy R.T., Seshadri R., Ren Q., Madupu R., Dodson R.J.,
RA   Durkin A.S., Brinkac L.M., Daugherty S.C., Sullivan S.A.,
RA   Rosovitz M.J., Gwinn M.L., Zhou L., Schneider D.J., Cartinhour S.W.,
RA   Nelson W.C., Weidman J., Watkins K., Tran K., Khouri H., Pierson E.A.,
RA   Pierson L.S. III, Thomashow L.S., Loper J.E.;
RT   "Complete genome sequence of the plant commensal Pseudomonas
RT   fluorescens Pf-5.";
RL   Nat. Biotechnol. 23:873-878(2005).
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; CP000076; AAY94823.1; -; Genomic_DNA.
DR   RefSeq; YP_262689.1; -.
DR   GeneID; 3480005; -.
DR   GenomeReviews; CP000076_GR; PFL_5630.
DR   KEGG; pfl:PFL_5630; -.
DR   NMPDR; fig|220664.3.peg.1200; -.
DR   HOGENOM; Q4K4Z4; -.
DR   OMA; Q4K4Z4; DSSNDAQ.
DR   BioCyc; PFLU220664:PFL_5630-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    272       Phosphoglycolate phosphatase.
FT                                /FTId=PRO_0000238166.
FT   ACT_SITE     19     19       Nucleophile (By similarity).
SQ   SEQUENCE   272 AA;  29893 MW;  F990F75669CF02AA CRC64;
     MSAFEQLFQG RLPRLVMFDL DGTLVDSVPD LAAAVDQMLL KLGRKPAGVE AVREWVGNGA
     PMLVRRALAN SLEAQGVDDV EAEYALELFN TAYEDSHELT VVYPGARETL KWLHKQGVEM
     ALITNKPERF VAPLLDQMKI GRYFRWIIGG DTLPQKKPDP AALFFVMKMA SVPASQSLFV
     GDSRSDVLAA KAAGVKCVAL SYGYNHGRPI AEESPALVID NLRALIPGCL EPAAEITLPD
     AVPSHSGNSI VVVTRKLWMK VIKALARWRW RA
//