ID   GPH_COLP3               Reviewed;         226 AA.
AC   Q48A85;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   16-JUN-2009, entry version 22.
DE   RecName: Full=Phosphoglycolate phosphatase;
DE            Short=PGPase;
DE            Short=PGP;
DE            EC=3.1.3.18;
GN   OrderedLocusNames=CPS_0261;
OS   Colwellia psychrerythraea (strain 34H / ATCC BAA-681) (Vibrio
OS   psychroerythus).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Colwelliaceae; Colwellia.
OX   NCBI_TaxID=167879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16043709; DOI=10.1073/pnas.0504766102;
RA   Methe B.A., Nelson K.E., Deming J.W., Momen B., Melamud E., Zhang X.,
RA   Moult J., Madupu R., Nelson W.C., Dodson R.J., Brinkac L.M.,
RA   Daugherty S.C., Durkin A.S., DeBoy R.T., Kolonay J.F., Sullivan S.A.,
RA   Zhou L., Davidsen T.M., Wu M., Huston A.L., Lewis M., Weaver B.,
RA   Weidman J.F., Khouri H., Utterback T.R., Feldblyum T.V., Fraser C.M.;
RT   "The psychrophilic lifestyle as revealed by the genome sequence of
RT   Colwellia psychrerythraea 34H through genomic and proteomic
RT   analyses.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:10913-10918(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.
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DR   EMBL; CP000083; AAZ25705.1; -; Genomic_DNA.
DR   RefSeq; YP_267028.1; -.
DR   GeneID; 3519951; -.
DR   GenomeReviews; CP000083_GR; CPS_0261.
DR   KEGG; cps:CPS_0261; -.
DR   NMPDR; fig|167879.3.peg.320; -.
DR   TIGR; CPS_0261; -.
DR   HOGENOM; Q48A85; -.
DR   OMA; Q48A85; EIKLIAF.
DR   BioCyc; CPSY167879:CPS_0261-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; IPR006346; PGP_bact.
DR   Pfam; PF00702; Hydrolase; 1.
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    226       Phosphoglycolate phosphatase.
FT                                /FTId=PRO_0000238156.
FT   ACT_SITE     12     12       Nucleophile (By similarity).
SQ   SEQUENCE   226 AA;  24921 MW;  FA9A818C14D90DD2 CRC64;
     MKLQEKEVLL FDLDGTLVDS APDLALAVNR TLKDLNKATF DQDTIHHWVG NGAKVLIERA
     LSGSAIIDKE LDETLTKDAL TIFLAHYQQC LCIESVLYDD VQEGLLSLKA AGFRLAIITN
     KPAIFIQPIL TGLGIDNLFE LLIGGDTLAD KKPHPAPLHY AMKQLNVVAE QCVMIGDSKN
     DILAAKAANI DSVGLTYGYN YGEDINQYGP QWCFDTFNEL LISLKR
//