ID   GPH_RHORT               Reviewed;         241 AA.
AC   Q2RPW9;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2006, sequence version 2.
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   Name=cbbZ; OrderedLocusNames=Rru_A3031;
OS   Rhodospirillum rubrum (strain ATCC 11170 / NCIB 8255).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Rhodospirillaceae; Rhodospirillum.
OX   NCBI_TaxID=269796;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Munk A.C., Brettin T., Bruce D.,
RA   Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M.,
RA   Kyrpides N., Mavrommatis K., Richardson P., Zhang Y., Roberts G.,
RA   Reslewic S., Zhou S., Schwartz D.C.;
RT   "Complete sequence of the chromosome of Rhodospirillum rubrum ATCC
RT   11170.";
RL   Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
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; CP000230; ABC23826.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; YP_428113.1; -.
DR   GeneID; 3836476; -.
DR   GenomeReviews; CP000230_GR; Rru_A3031.
DR   KEGG; rru:Rru_A3031; -.
DR   NMPDR; fig|1085.1.peg.672; -.
DR   HOGENOM; Q2RPW9; -.
DR   BioCyc; RRUB269796:RRU_A3031-MON; -.
DR   GO; GO:0008967; F:phosphoglycolate phosphatase activity; IEA:HAMAP.
DR   GO; GO:0019253; P:reductive pentose-phosphate cycle; IEA:UniProtKB-KW.
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   Calvin cycle; Carbohydrate metabolism; Complete proteome; Hydrolase;
KW   Photosynthesis.
FT   CHAIN         1    241       Phosphoglycolate phosphatase.
FT                                /FTId=PRO_0000238174.
FT   ACT_SITE      8      8       Nucleophile (By similarity).
SQ   SEQUENCE   241 AA;  24507 MW;  7D4F0C118BFBEA59 CRC64;
     MPKAVIFDLD GTLVHSLPGL TDALNKTLAE DDLAPLDEAA VKRMVGEGAG LLVARAFAAY
     GLGRADDADD TATQARLARF LAHYAPDPLA GASVYPGALA LLGALAARGI RLGVCTNKPE
     GPARALLEGL GLADPIMDVV GGDTLAQRKP DPAPLRALLD SLGVEADQAL MVGDSPTDVA
     TAKAAGVPVV VMSYGYSREP VASLGALAVF DDFASLGDWL GFPQPGGDRL GATPALSENP
     A
//