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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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