(data stored in SCRATCH zone)

SWISSPROT: B4SIG0_STRM5

ID   B4SIG0_STRM5            Unreviewed;       229 AA.
AC   B4SIG0;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   08-MAY-2019, entry version 76.
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   OrderedLocusNames=Smal_0460 {ECO:0000313|EMBL:ACF50165.1};
OS   Stenotrophomonas maltophilia (strain R551-3).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Stenotrophomonas;
OC   Stenotrophomonas maltophilia group.
OX   NCBI_TaxID=391008 {ECO:0000313|EMBL:ACF50165.1, ECO:0000313|Proteomes:UP000001867};
RN   [1] {ECO:0000313|EMBL:ACF50165.1, ECO:0000313|Proteomes:UP000001867}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R551-3 {ECO:0000313|EMBL:ACF50165.1,
RC   ECO:0000313|Proteomes:UP000001867};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L.,
RA   Lang D., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Taghavi S., Monchy S., Newman L., Vangronsveld J.,
RA   van der Lelie D., Richardson P.;
RT   "Complete sequence of Stenotrophomonas maltophilia R551-3.";
RL   Submitted (JUN-2008) 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. {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   -!- 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   -!- 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; CP001111; ACF50165.1; -; Genomic_DNA.
DR   STRING; 391008.Smal_0460; -.
DR   EnsemblBacteria; ACF50165; ACF50165; Smal_0460.
DR   KEGG; smt:Smal_0460; -.
DR   eggNOG; ENOG4108VXP; Bacteria.
DR   eggNOG; COG0546; LUCA.
DR   HOGENOM; HOG000248344; -.
DR   KO; K01091; -.
DR   OMA; CEHTIKA; -.
DR   UniPathway; UPA00865; UER00834.
DR   Proteomes; UP000001867; 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   SUPFAM; SSF56784; SSF56784; 1.
DR   TIGRFAMs; TIGR01549; HAD-SF-IA-v1; 1.
DR   TIGRFAMs; TIGR01449; PGP_bact; 1.
PE   3: Inferred from homology;
DR   PRODOM; B4SIG0.
DR   SWISS-2DPAGE; B4SIG0.
KW   Carbohydrate metabolism {ECO:0000256|HAMAP-Rule:MF_00495,
KW   ECO:0000256|SAAS:SAAS00960024};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001867};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00495,
KW   ECO:0000256|SAAS:SAAS00964139};
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}.
FT   ACT_SITE     22     22       Nucleophile. {ECO:0000256|HAMAP-Rule:
FT                                MF_00495}.
FT   METAL        22     22       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_00495}.
FT   METAL        24     24       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_00495}.
FT   METAL       181    181       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_00495}.
SQ   SEQUENCE   229 AA;  24651 MW;  B395692CA483CC15 CRC64;
     MDGPTSCRCR PLSYPYPLVV FDLDGTLVDS AADIAEALNR TLEDIGVARV PETTVLGWIG
     DGVRRLVEQA VHAAGREVDL AEVMPVFMVH YRECLLRSPR LFDGVAEALA RLRARNVPLA
     ICTNKPEALV PPLLQHLGIG DAFALVLGGD SLPQRKPSGE PLRHMAAHFG LPVEACLMVG
     DSLTDYRAAE DAGMPIALVR YGYPRGLDLA TAHAVAVIDD LRELPGLKG
//

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