PGP_METMA
ID PGP_METMA Reviewed; 226 AA.
AC Q8PZN6;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Phosphoglycolate phosphatase {ECO:0000255|HAMAP-Rule:MF_01419};
DE Short=PGP {ECO:0000255|HAMAP-Rule:MF_01419};
DE Short=PGPase {ECO:0000255|HAMAP-Rule:MF_01419};
DE EC=3.1.3.18 {ECO:0000255|HAMAP-Rule:MF_01419};
GN OrderedLocusNames=MM_0456;
OS Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM
OS 11833 / OCM 88) (Methanosarcina frisia).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=192952;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88;
RX PubMed=12125824;
RA Deppenmeier U., Johann A., Hartsch T., Merkl R., Schmitz R.A.,
RA Martinez-Arias R., Henne A., Wiezer A., Baeumer S., Jacobi C.,
RA Brueggemann H., Lienard T., Christmann A., Boemecke M., Steckel S.,
RA Bhattacharyya A., Lykidis A., Overbeek R., Klenk H.-P., Gunsalus R.P.,
RA Fritz H.-J., Gottschalk G.;
RT "The genome of Methanosarcina mazei: evidence for lateral gene transfer
RT between Bacteria and Archaea.";
RL J. Mol. Microbiol. Biotechnol. 4:453-461(2002).
CC -!- FUNCTION: Catalyzes the dephosphorylation of 2-phosphoglycolate.
CC {ECO:0000255|HAMAP-Rule:MF_01419}.
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:0000255|HAMAP-Rule:MF_01419};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01419};
CC -!- SIMILARITY: Belongs to the archaeal SPP-like hydrolase family.
CC {ECO:0000255|HAMAP-Rule:MF_01419}.
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DR EMBL; AE008384; AAM30152.1; -; Genomic_DNA.
DR RefSeq; WP_011032409.1; NC_003901.1.
DR AlphaFoldDB; Q8PZN6; -.
DR SMR; Q8PZN6; -.
DR STRING; 192952.MM_0456; -.
DR EnsemblBacteria; AAM30152; AAM30152; MM_0456.
DR GeneID; 44086324; -.
DR GeneID; 66134367; -.
DR KEGG; mma:MM_0456; -.
DR PATRIC; fig|192952.21.peg.551; -.
DR eggNOG; arCOG01213; Archaea.
DR HOGENOM; CLU_044146_2_0_2; -.
DR OMA; DTGYAYH; -.
DR Proteomes; UP000000595; Chromosome.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0008967; F:phosphoglycolate phosphatase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR Gene3D; 3.40.50.1000; -; 1.
DR HAMAP; MF_01419; GPH_hydrolase_arch; 1.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR006379; HAD-SF_hydro_IIB.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR006382; PGPase.
DR SUPFAM; SSF56784; SSF56784; 1.
DR TIGRFAMs; TIGR01484; HAD-SF-IIB; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism; Hydrolase; Magnesium; Metal-binding;
KW Reference proteome.
FT CHAIN 1..226
FT /note="Phosphoglycolate phosphatase"
FT /id="PRO_0000146719"
FT ACT_SITE 9
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01419"
FT BINDING 9
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01419"
FT BINDING 11
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01419"
FT BINDING 150
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01419"
FT BINDING 173
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01419"
FT BINDING 177
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01419"
SQ SEQUENCE 226 AA; 24677 MW; 9ED4C75961057A5D CRC64;
MKFKALVIDI DGTITCKNRE LHLGAVKKMR TLNVPVVLAT GNILCYARTA SRLIGLGGAV
IAENGGAVTV RYDVNGIFEG SLEECEKAFS FLSQHFKLTK LDPTYRKTEI ALRRDFDLEE
ARSLLETQPF DIELVDTKYA IHIKSIKINK GIGLQKLAGM MGFEAEDFVA IGDSANDAEM
FEAAGFGIAV ANGDERVKEV ANYVTEASFG DGAVEAIEFL ESNGWI