ID   GPH_HAEI8               Reviewed;         224 AA.
AC   Q4QMY0;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   16-JUN-2009, entry version 27.
DE   RecName: Full=Phosphoglycolate phosphatase;
DE            Short=PGPase;
DE            Short=PGP;
DE            EC=3.1.3.18;
GN   OrderedLocusNames=NTHI0697;
OS   Haemophilus influenzae (strain 86-028NP).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=281310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15968074; DOI=10.1128/JB.187.13.4627-4636.2005;
RA   Harrison A., Dyer D.W., Gillaspy A., Ray W.C., Mungur R., Carson M.B.,
RA   Zhong H., Gipson J., Gipson M., Johnson L.S., Lewis L., Bakaletz L.O.,
RA   Munson R.S. Jr.;
RT   "Genomic sequence of an otitis media isolate of nontypeable
RT   Haemophilus influenzae: comparative study with H. influenzae serotype
RT   d, strain KW20.";
RL   J. Bacteriol. 187:4627-4636(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; CP000057; AAX87617.1; -; Genomic_DNA.
DR   RefSeq; YP_248277.1; -.
DR   SMR; Q4QMY0; 3-223.
DR   GeneID; 3430005; -.
DR   GenomeReviews; CP000057_GR; NTHI0697.
DR   KEGG; hit:NTHI0697; -.
DR   HOGENOM; Q4QMY0; -.
DR   OMA; Q4QMY0; AVCEQFS.
DR   BioCyc; HINF281310:NTHI0697-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    224       Phosphoglycolate phosphatase.
FT                                /FTId=PRO_0000238159.
FT   ACT_SITE     11     11       Nucleophile (By similarity).
SQ   SEQUENCE   224 AA;  24734 MW;  A5DA61CAAA66FFC9 CRC64;
     MNTQFKLIGF DLDGTLVNSL PDLALSVNSA LAEFNLPKAP EELVLTWIGN GAPVLIARAL
     DWAKKQTGKV LTETEVKQVT ERFNFYYGEN LCNVSRLYPN VKETLETLKE KGYVLAVVTN
     KPTRHVQPVL AAFGIDHLFS EMLGGQSLPA IKPHPAPLYY LCGKFGFEPR QVLFVGDSKN
     DIIAAHAAGC AVVGLTYGYN YNIPITESNP DWVFDDFAQL LTIL
//