ID   GPH_SHISS               Reviewed;         252 AA.
AC   Q3YWN8;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-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=SSON_3516;
OS   Shigella sonnei (strain Ss046).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=300269;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16275786; DOI=10.1093/nar/gki954;
RA   Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X.,
RA   Wang J., Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S.,
RA   Nie H., Peng J., Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y.,
RA   Qiang B., Hou Y., Yu J., Jin Q.;
RT   "Genome dynamics and diversity of Shigella species, the etiologic
RT   agents of bacillary dysentery.";
RL   Nucleic Acids Res. 33:6445-6458(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   -!- COFACTOR: Chloride (By similarity).
CC   -!- COFACTOR: Magnesium (By similarity).
CC   -!- PATHWAY: Organic acid metabolism; glycolic acid biosynthesis;
CC       glycolic acid from 2-phosphoglycolic acid: step 1/1.
CC   -!- SUBUNIT: Monomer (By similarity).
CC   -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily.
CC       CbbY/cbbZ/gph/yieH family.
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DR   EMBL; CP000038; AAZ90074.1; -; Genomic_DNA.
DR   RefSeq; YP_312309.1; -.
DR   GeneID; 3667362; -.
DR   GenomeReviews; CP000038_GR; SSON_3516.
DR   KEGG; ssn:SSON_3516; -.
DR   HOGENOM; Q3YWN8; -.
DR   OMA; Q3YWN8; AVCEQFS.
DR   BioCyc; SSON300269:SSO_3516-MON; -.
DR   GO; GO:0031404; F:chloride ion binding; IEA:UniProtKB-KW.
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: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; Chloride; Complete proteome; Hydrolase;
KW   Magnesium.
FT   CHAIN         1    252       Phosphoglycolate phosphatase.
FT                                /FTId=PRO_0000238180.
FT   ACT_SITE     13     13       Nucleophile (By similarity).
SQ   SEQUENCE   252 AA;  27403 MW;  4DCCDA65B37A0E72 CRC64;
     MNKFEDIRGV AFDLDGTLVD SAPGLAAAVD MALYALELPI AGEERVITWI GNGADVLMER
     ALTWARQERA TQRKTMGKPP VDDDIPAEEQ VRILRKLFDR YYGEVAEEGT FLFPHVADTL
     GALQAKGLPL GLVTNKPTPF VAPLLEALDI AKYFSVVIGG DDVQNKKPHP DPLLLVAERM
     GIAPQQMLFV GDSRNDIQAA KAAGCPSVGL TYGYNYGEAI DLSQPDVIYQ SINDLLPALG
     LPHSENQESK ND
//