ID D9Q0W4_ACIS3 Unreviewed; 236 AA.
AC D9Q0W4;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE RecName: Full=Phosphoglycolate phosphatase {ECO:0000256|HAMAP-Rule:MF_01419};
DE Short=PGP {ECO:0000256|HAMAP-Rule:MF_01419};
DE Short=PGPase {ECO:0000256|HAMAP-Rule:MF_01419};
DE EC=3.1.3.18 {ECO:0000256|HAMAP-Rule:MF_01419};
GN OrderedLocusNames=ASAC_0545 {ECO:0000313|EMBL:ADL18952.1};
OS Acidilobus saccharovorans (strain DSM 16705 / JCM 18335 / VKM B-2471 /
OS 345-15).
OC Archaea; Thermoproteota; Thermoprotei; Acidilobales; Acidilobaceae;
OC Acidilobus.
OX NCBI_TaxID=666510 {ECO:0000313|EMBL:ADL18952.1, ECO:0000313|Proteomes:UP000000346};
RN [1] {ECO:0000313|EMBL:ADL18952.1, ECO:0000313|Proteomes:UP000000346}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16705 / JCM 18335 / VKM B-2471 / 345-15
RC {ECO:0000313|Proteomes:UP000000346};
RX PubMed=20581186; DOI=10.1128/AEM.00599-10;
RA Mardanov A.V., Svetlitchnyi V.A., Beletsky A.V., Prokofeva M.I.,
RA Bonch-Osmolovskaya E.A., Ravin N.V., Skryabin K.G.;
RT "The genome sequence of the crenarchaeon Acidilobus saccharovorans supports
RT a new order, Acidilobales, and suggests an important ecological role in
RT terrestrial acidic hot springs.";
RL Appl. Environ. Microbiol. 76:5652-5657(2010).
CC -!- FUNCTION: Catalyzes the dephosphorylation of 2-phosphoglycolate.
CC {ECO:0000256|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:0000256|HAMAP-Rule:MF_01419};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01419};
CC -!- SIMILARITY: Belongs to the archaeal SPP-like hydrolase family.
CC {ECO:0000256|HAMAP-Rule:MF_01419}.
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DR EMBL; CP001742; ADL18952.1; -; Genomic_DNA.
DR RefSeq; WP_013266464.1; NC_014374.1.
DR AlphaFoldDB; D9Q0W4; -.
DR STRING; 666510.ASAC_0545; -.
DR GeneID; 9498777; -.
DR KEGG; asc:ASAC_0545; -.
DR eggNOG; arCOG01213; Archaea.
DR HOGENOM; CLU_044146_2_0_2; -.
DR InParanoid; D9Q0W4; -.
DR Proteomes; UP000000346; 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; 3.90.1070.10; -; 1.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 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 NCBIfam; TIGR01484; HAD-SF-IIB; 1.
DR NCBIfam; TIGR01487; Pglycolate_arch; 1.
DR PANTHER; PTHR10000:SF8; PHOSPHOGLYCOLATE PHOSPHATASE 1; 1.
DR PANTHER; PTHR10000; PHOSPHOSERINE PHOSPHATASE; 1.
DR Pfam; PF08282; Hydrolase_3; 2.
DR SUPFAM; SSF56784; HAD-like; 1.
DR PROSITE; PS01229; COF_2; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|HAMAP-Rule:MF_01419};
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01419};
KW Magnesium {ECO:0000256|HAMAP-Rule:MF_01419};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01419};
KW Reference proteome {ECO:0000313|Proteomes:UP000000346}.
FT ACT_SITE 9
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01419"
FT BINDING 9
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01419"
FT BINDING 11
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01419"
FT BINDING 159
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01419"
FT BINDING 182
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01419"
FT BINDING 186
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01419"
SQ SEQUENCE 236 AA; 25153 MW; AFC49B2D6992516E CRC64;
MPLKAVGSDV DGTLTVRRGD LRVSVHAIRG IRLLESRGVK VILVSGNSLP VTAGLSVYLG
SSGPVVAENG CVIMYRGQIY HVCSGRPPEG LLRKLQDLGL RPSWQNEFRY HDMAFFMPRG
VDENSKAELL RAVSEIAEAH GLRVLWSGYA VHINPGNGKG EGLLRALELI GVSASEAAAI
GDGENDLDML SVVPISGCPG DAAPAVKVKV KFVARGRGGA GFLEFARWLL AKGERN
//
