(data stored in SCRATCH zone)

SWISSPROT: D3VG55_XENNA

ID   D3VG55_XENNA            Unreviewed;       240 AA.
AC   D3VG55;
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:CBJ88145.1};
GN   OrderedLocusNames=XNC1_0057 {ECO:0000313|EMBL:CBJ88145.1};
OS   Xenorhabdus nematophila (strain ATCC 19061 / DSM 3370 / LMG 1036 /
OS   NCIB 9965 / AN6).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Xenorhabdus.
OX   NCBI_TaxID=406817 {ECO:0000313|EMBL:CBJ88145.1, ECO:0000313|Proteomes:UP000008075};
RN   [1] {ECO:0000313|Proteomes:UP000008075}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19061 / DSM 3370 / LMG 1036 / NCIB 9965 / AN6
RC   {ECO:0000313|Proteomes:UP000008075};
RA   Goodrich-Blair H., Barbazuk B., Bode H.B., Darby C., Du Z., Forst S.,
RA   Gaudriault S., Goldman B.S., Goodner B., Henkhaus J., Latreille P.,
RA   Medigue C., Miller N., Norton S., Ogier J.C., Rouy Z., Slater S.,
RA   Suen G.;
RT   "Complete genome sequence of Xenorhabdus nematophila (strain ATCC
RT   19061 / DSM 3370 / LMG 1036 / NCIB 9965 / AN6).";
RL   Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CBJ88145.1, ECO:0000313|Proteomes:UP000008075}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19061 / DSM 3370 / LMG 1036 / NCIB 9965 / AN6
RC   {ECO:0000313|Proteomes:UP000008075};
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; FN667742; CBJ88145.1; -; Genomic_DNA.
DR   RefSeq; WP_010847518.1; NC_014228.1.
DR   STRING; 406817.XNC1_0057; -.
DR   EnsemblBacteria; CBJ88145; CBJ88145; XNC1_0057.
DR   KEGG; xne:XNC1_0057; -.
DR   eggNOG; ENOG4108VXP; Bacteria.
DR   eggNOG; COG0546; LUCA.
DR   HOGENOM; HOG000248344; -.
DR   KO; K01091; -.
DR   OMA; YLCGKFG; -.
DR   UniPathway; UPA00865; UER00834.
DR   Proteomes; UP000008075; 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; D3VG55.
DR   SWISS-2DPAGE; D3VG55.
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:UP000008075};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00495,
KW   ECO:0000256|SAAS:SAAS00964139, ECO:0000313|EMBL:CBJ88145.1};
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:UP000008075}.
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   240 AA;  25989 MW;  2C997FE0E72E0A28 CRC64;
     MLNNVVKKIR AIAFDLDGTL VDSADGLADA LDQALIAKGL PAAGKDQVAV WIGNGADIMV
     ERALKWAGAE PSPELHRETR KLFDTFYETS ITTGSKLFPQ VKETLAELAK HRLPMAIITN
     KPTPFIAPLL ESLGISEYFS VVLGGDDVKE KKPHPAPLYL TMGMFGLHKE ELLFVGDSRN
     DILAAQSAGC PCVGLTYGYN YGESIALSHP TYVLDHFSDL FPTIGLSTLN LLSTSKIQEA
//

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