(data stored in ACNUC1104 zone)

SWISSPROT: D3UY26_XENBS

ID   D3UY26_XENBS            Unreviewed;       234 AA.
AC   D3UY26;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAY-2019, entry version 70.
DE   RecName: Full=Phosphoglycolate phosphatase {ECO:0000256|HAMAP-Rule:MF_00495};
DE            Short=PGP {ECO:0000256|HAMAP-Rule:MF_00495};
DE            Short=PGPase {ECO:0000256|HAMAP-Rule:MF_00495};
DE            EC=3.1.3.18 {ECO:0000256|HAMAP-Rule:MF_00495};
GN   Name=gph {ECO:0000256|HAMAP-Rule:MF_00495,
GN   ECO:0000313|EMBL:CBJ79204.1};
GN   OrderedLocusNames=XBJ1_0053 {ECO:0000313|EMBL:CBJ79204.1};
OS   Xenorhabdus bovienii (strain SS-2004).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Xenorhabdus.
OX   NCBI_TaxID=406818 {ECO:0000313|EMBL:CBJ79204.1, ECO:0000313|Proteomes:UP000002045};
RN   [1] {ECO:0000313|EMBL:CBJ79204.1, ECO:0000313|Proteomes:UP000002045}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SS-2004 {ECO:0000313|EMBL:CBJ79204.1,
RC   ECO:0000313|Proteomes:UP000002045};
RX   PubMed=22125637; DOI=10.1371/journal.pone.0027909;
RA   Chaston J.M., Suen G., Tucker S.L., Andersen A.W., Bhasin A., Bode E.,
RA   Bode H.B., Brachmann A.O., Cowles C.E., Cowles K.N., Darby C.,
RA   de Leon L., Drace K., Du Z., Givaudan A., Herbert Tran E.E.,
RA   Jewell K.A., Knack J.J., Krasomil-Osterfeld K.C., Kukor R., Lanois A.,
RA   Latreille P., Leimgruber N.K., Lipke C.M., Liu R., Lu X.,
RA   Martens E.C., Marri P.R., Medigue C., Menard M.L., Miller N.M.,
RA   Morales-Soto N., Norton S., Ogier J.C., Orchard S.S., Park D.,
RA   Park Y., Qurollo B.A., Sugar D.R., Richards G.R., Rouy Z.,
RA   Slominski B., Slominski K., Snyder H., Tjaden B.C., van der Hoeven R.,
RA   Welch R.D., Wheeler C., Xiang B., Barbazuk B., Gaudriault S.,
RA   Goodner B., Slater S.C., Forst S., Goldman B.S., Goodrich-Blair H.;
RT   "The entomopathogenic bacterial endosymbionts xenorhabdus and
RT   photorhabdus: convergent lifestyles from divergent genomes.";
RL   PLoS ONE 6:e27909-e27909(2011).
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. {ECO:0000256|HAMAP-Rule:MF_00495}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-phosphoglycolate + H2O = glycolate + phosphate;
CC         Xref=Rhea:RHEA:14369, ChEBI:CHEBI:15377, ChEBI:CHEBI:29805,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58033; EC=3.1.3.18;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00495,
CC         ECO:0000256|SAAS:SAAS01115150};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00495, ECO:0000256|SAAS:SAAS00964146};
CC   -!- COFACTOR:
CC       Name=chloride; Xref=ChEBI:CHEBI:17996;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00495};
CC   -!- PATHWAY: Organic acid metabolism; glycolate biosynthesis;
CC       glycolate from 2-phosphoglycolate: step 1/1. {ECO:0000256|HAMAP-
CC       Rule:MF_00495, ECO:0000256|SAAS:SAAS00956658}.
CC   -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00495}.
CC   -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily.
CC       CbbY/CbbZ/Gph/YieH family. {ECO:0000256|HAMAP-Rule:MF_00495,
CC       ECO:0000256|SAAS:SAAS00960030}.
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DR   EMBL; FN667741; CBJ79204.1; -; Genomic_DNA.
DR   RefSeq; WP_012986677.1; NC_013892.1.
DR   STRING; 406818.XBJ1_0053; -.
DR   EnsemblBacteria; CBJ79204; CBJ79204; XBJ1_0053.
DR   GeneID; 8829681; -.
DR   KEGG; xbo:XBJ1_0053; -.
DR   PATRIC; fig|406818.4.peg.46; -.
DR   eggNOG; ENOG4108VXP; Bacteria.
DR   eggNOG; COG0546; LUCA.
DR   HOGENOM; HOG000248344; -.
DR   KO; K01091; -.
DR   OMA; YLCGKFG; -.
DR   BioCyc; XBOV406818:XBJ1_RS00245-MONOMER; -.
DR   UniPathway; UPA00865; UER00834.
DR   Proteomes; UP000002045; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008967; F:phosphoglycolate phosphatase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0046295; P:glycolate biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 1.10.150.240; -; 1.
DR   Gene3D; 3.40.50.1000; -; 1.
DR   HAMAP; MF_00495; GPH_hydrolase_bact; 1.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR006439; HAD-SF_hydro_IA.
DR   InterPro; IPR041492; HAD_2.
DR   InterPro; IPR023214; HAD_sf.
DR   InterPro; IPR023198; PGP-like_dom2.
DR   InterPro; IPR006346; PGPase/MupP.
DR   InterPro; IPR037512; PGPase_prok.
DR   Pfam; PF13419; HAD_2; 1.
DR   PRINTS; PR00413; HADHALOGNASE.
DR   SUPFAM; SSF56784; SSF56784; 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;
DR   PRODOM; D3UY26.
DR   SWISS-2DPAGE; D3UY26.
KW   Carbohydrate metabolism {ECO:0000256|HAMAP-Rule:MF_00495,
KW   ECO:0000256|SAAS:SAAS00960024};
KW   Chloride {ECO:0000256|HAMAP-Rule:MF_00495};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002045};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00495,
KW   ECO:0000256|SAAS:SAAS00964139, ECO:0000313|EMBL:CBJ79204.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00495,
KW   ECO:0000256|SAAS:SAAS00964134};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00495,
KW   ECO:0000256|SAAS:SAAS00960052};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002045}.
FT   ACT_SITE     15     15       Nucleophile. {ECO:0000256|HAMAP-Rule:
FT                                MF_00495}.
FT   METAL        15     15       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_00495}.
FT   METAL        17     17       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_00495}.
FT   METAL       177    177       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_00495}.
SQ   SEQUENCE   234 AA;  25313 MW;  3C2E9F58A132C4EC CRC64;
     MVTSIKKNLR AIAFDLDGTL VDSASGLAEA LDQALIAKGL PPAGKERVAI WIGNGADVMV
     ERALKWAGVE STPELHRETR KLFDGFYETT VTTGSQLFPY VKETLATLAQ HNLPMAIVTN
     KPTPFIAPLL ESLGISEYFS LVLGGDDVKE KKPHPAPLYL TMGMFGIHKE ELLFVGDSRN
     DILAAQAAGC PCVGLTYGYN YGESIALSHP DYILDHFPDL LPAIGLSTLK LQEA
//

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