ID   GPH_XANCP               Reviewed;         221 AA.
AC   Q8P8H3;
DT   10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   10-OCT-2002, sequence version 1.
DT   16-JUN-2009, entry version 40.
DE   RecName: Full=Phosphoglycolate phosphatase;
DE            Short=PGPase;
DE            Short=PGP;
DE            EC=3.1.3.18;
GN   Name=gph; Synonyms=cbbZ; OrderedLocusNames=XCC2268;
OS   Xanthomonas campestris pv. campestris.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=340;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33913 / NCPPB 528 / LMG 568;
RX   MEDLINE=22022145; PubMed=12024217; DOI=10.1038/417459a;
RA   da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R.,
RA   Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A.,
RA   Almeida N.F. Jr., Alves L.M.C., do Amaral A.M., Bertolini M.C.,
RA   Camargo L.E.A., Camarotte G., Cannavan F., Cardozo J., Chambergo F.,
RA   Ciapina L.P., Cicarelli R.M.B., Coutinho L.L., Cursino-Santos J.R.,
RA   El-Dorry H., Faria J.B., Ferreira A.J.S., Ferreira R.C.C.,
RA   Ferro M.I.T., Formighieri E.F., Franco M.C., Greggio C.C., Gruber A.,
RA   Katsuyama A.M., Kishi L.T., Leite R.P., Lemos E.G.M., Lemos M.V.F.,
RA   Locali E.C., Machado M.A., Madeira A.M.B.N., Martinez-Rossi N.M.,
RA   Martins E.C., Meidanis J., Menck C.F.M., Miyaki C.Y., Moon D.H.,
RA   Moreira L.M., Novo M.T.M., Okura V.K., Oliveira M.C., Oliveira V.R.,
RA   Pereira H.A., Rossi A., Sena J.A.D., Silva C., de Souza R.F.,
RA   Spinola L.A.F., Takita M.A., Tamura R.E., Teixeira E.C., Tezza R.I.D.,
RA   Trindade dos Santos M., Truffi D., Tsai S.M., White F.F.,
RA   Setubal J.C., Kitajima J.P.;
RT   "Comparison of the genomes of two Xanthomonas pathogens with differing
RT   host specificities.";
RL   Nature 417:459-463(2002).
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; AE012334; AAM41547.1; -; Genomic_DNA.
DR   RefSeq; NP_637623.1; -.
DR   GeneID; 998838; -.
DR   GenomeReviews; AE008922_GR; XCC2268.
DR   KEGG; xcc:XCC2268; -.
DR   HOGENOM; Q8P8H3; -.
DR   OMA; Q8P8H3; APDFIAI.
DR   BioCyc; XCAM190485:XCC2268-MON; -.
DR   BRENDA; 3.1.3.18; 281360.
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    221       Phosphoglycolate phosphatase.
FT                                /FTId=PRO_0000108047.
FT   ACT_SITE     10     10       Nucleophile (By similarity).
SQ   SEQUENCE   221 AA;  24075 MW;  BFF0E5487F276B21 CRC64;
     MRFPRAVLFD LDGTLLDSAP DMLATVNAML SERGLPCITL AQLRPVVSKG SRAMLAVAFA
     HLDAAAREAL VPEFLKRYEA LLGTQAQLFD GVEVMLQRLE QAGCVWGIVT NKPEYLAQLI
     LPQLGWQQRC AVLIGGDTLA ERKPHPLPLL VAADRIGVAA TQCVYVGDDE RDILAARAAG
     MPSVAALWGY RLGDDDPLSW QADVLVEQPP QLWEPAAWPQ P
//