PGP_METTH
ID PGP_METTH Reviewed; 221 AA.
AC O27143;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 111.
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=MTH_1071;
OS Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM
OS 10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum).
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanothermobacter.
OX NCBI_TaxID=187420;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
RX PubMed=9371463; DOI=10.1128/jb.179.22.7135-7155.1997;
RA Smith D.R., Doucette-Stamm L.A., Deloughery C., Lee H.-M., Dubois J.,
RA Aldredge T., Bashirzadeh R., Blakely D., Cook R., Gilbert K., Harrison D.,
RA Hoang L., Keagle P., Lumm W., Pothier B., Qiu D., Spadafora R., Vicare R.,
RA Wang Y., Wierzbowski J., Gibson R., Jiwani N., Caruso A., Bush D.,
RA Safer H., Patwell D., Prabhakar S., McDougall S., Shimer G., Goyal A.,
RA Pietrovski S., Church G.M., Daniels C.J., Mao J.-I., Rice P., Noelling J.,
RA Reeve J.N.;
RT "Complete genome sequence of Methanobacterium thermoautotrophicum deltaH:
RT functional analysis and comparative genomics.";
RL J. Bacteriol. 179:7135-7155(1997).
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; AE000666; AAB85560.1; -; Genomic_DNA.
DR PIR; C69009; C69009.
DR RefSeq; WP_010876695.1; NC_000916.1.
DR AlphaFoldDB; O27143; -.
DR SMR; O27143; -.
DR STRING; 187420.MTH_1071; -.
DR EnsemblBacteria; AAB85560; AAB85560; MTH_1071.
DR GeneID; 1471479; -.
DR KEGG; mth:MTH_1071; -.
DR PATRIC; fig|187420.15.peg.1048; -.
DR HOGENOM; CLU_044146_2_0_2; -.
DR OMA; DTGYAYH; -.
DR Proteomes; UP000005223; 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..221
FT /note="Phosphoglycolate phosphatase"
FT /id="PRO_0000146720"
FT ACT_SITE 7
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01419"
FT BINDING 7
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
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 148
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01419"
FT BINDING 171
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01419"
FT BINDING 175
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01419"
SQ SEQUENCE 221 AA; 23785 MW; EFEFE6AE5BBF449F CRC64;
MRAIAVDIDG TITDKKRRLS LEAVKALRGA EEAGVPVIMV TGNILCFAMA TSVLIGASGG
VVAENGGVLH INDEVRVLGD ISKAEMAYSH LKGIYPVRKV QFSDLRVSEI ALTRDVPADT
VREALRDFDV EVYDTGFAIH LTDPSVNKGS SLEILLESMG IEMEDVMAIG DSENDLEFIE
AAGFRVAVAN ADPELREMAD YVTSAAHGEG VAEAVRRFMG W