PGP_SULTO
ID PGP_SULTO Reviewed; 226 AA.
AC Q96YM5;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 100.
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=STK_21470;
OS Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)
OS (Sulfolobus tokodaii).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Sulfurisphaera.
OX NCBI_TaxID=273063;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16993 / JCM 10545 / NBRC 100140 / 7;
RX PubMed=11572479; DOI=10.1093/dnares/8.4.123;
RA Kawarabayasi Y., Hino Y., Horikawa H., Jin-no K., Takahashi M., Sekine M.,
RA Baba S., Ankai A., Kosugi H., Hosoyama A., Fukui S., Nagai Y.,
RA Nishijima K., Otsuka R., Nakazawa H., Takamiya M., Kato Y., Yoshizawa T.,
RA Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K.,
RA Masuda S., Yanagii M., Nishimura M., Yamagishi A., Oshima T., Kikuchi H.;
RT "Complete genome sequence of an aerobic thermoacidophilic Crenarchaeon,
RT Sulfolobus tokodaii strain7.";
RL DNA Res. 8:123-140(2001).
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; BA000023; BAB67252.1; -; Genomic_DNA.
DR RefSeq; WP_010980227.1; NC_003106.2.
DR AlphaFoldDB; Q96YM5; -.
DR SMR; Q96YM5; -.
DR STRING; 273063.STK_21470; -.
DR EnsemblBacteria; BAB67252; BAB67252; STK_21470.
DR GeneID; 1460220; -.
DR KEGG; sto:STK_21470; -.
DR PATRIC; fig|273063.9.peg.2438; -.
DR eggNOG; arCOG01213; Archaea.
DR OMA; MWIVASD; -.
DR OrthoDB; 58398at2157; -.
DR Proteomes; UP000001015; 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_0000146730"
FT ACT_SITE 5
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01419"
FT BINDING 5
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
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 142
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01419"
FT BINDING 164
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01419"
FT BINDING 168
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01419"
SQ SEQUENCE 226 AA; 25654 MW; 8B46EEE9D6706B6C CRC64;
MVLSDFDRTL SDEKDNFIIK QEVVEVVNKF SAKFLFFVVT GRERKYMDIL AKGLFPTGWI
IENGGIIILR DKEIKLVDEK WYKIRKNLAK ILDKNGIKYS LGEVIIYVNS AIDYKDKLDK
INEAKIEWNR SDAMIMPKNV SKGEAVKILK SILNFEGVTI AIGDSQNDIS LFSVADIKVA
VANALPEIKA ISDIVLDKED GIGVMRFLEK ILNDGSYLEK LIGFRK