ID D8J4Q7_HALJB Unreviewed; 223 AA.
AC D8J4Q7;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 72.
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=HacjB3_10705 {ECO:0000313|EMBL:ADJ15524.1};
GN ORFNames=C497_11962 {ECO:0000313|EMBL:ELY36067.1};
OS Halalkalicoccus jeotgali (strain DSM 18796 / CECT 7217 / JCM 14584 / KCTC
OS 4019 / B3).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Halococcaceae; Halalkalicoccus.
OX NCBI_TaxID=795797 {ECO:0000313|EMBL:ADJ15524.1, ECO:0000313|Proteomes:UP000000390};
RN [1] {ECO:0000313|EMBL:ADJ15524.1, ECO:0000313|Proteomes:UP000000390}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B3 {ECO:0000313|EMBL:ADJ15524.1}, and DSM 18796 / CECT 7217 /
RC JCM 14584 / KCTC 4019 / B3 {ECO:0000313|Proteomes:UP000000390};
RX PubMed=20601480; DOI=10.1128/JB.00663-10;
RA Roh S.W., Nam Y.D., Nam S.H., Choi S.H., Park H.S., Bae J.W.;
RT "Complete genome sequence of Halalkalicoccus jeotgali B3(T), an extremely
RT halophilic archaeon.";
RL J. Bacteriol. 192:4528-4529(2010).
RN [2] {ECO:0000313|Proteomes:UP000011645}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B3 {ECO:0000313|Proteomes:UP000011645};
RA Becker E.A., Seitzer P., Tritt A., Larsen D., Yao A., Wu D., Darling A.,
RA Eisen J.A., Facciotti M.T.;
RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:ELY36067.1, ECO:0000313|Proteomes:UP000011645}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B3 {ECO:0000313|EMBL:ELY36067.1,
RC ECO:0000313|Proteomes:UP000011645};
RX PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT strategies for static and dynamic osmo-response.";
RL PLoS Genet. 10:E1004784-E1004784(2014).
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; CP002062; ADJ15524.1; -; Genomic_DNA.
DR EMBL; AOHV01000030; ELY36067.1; -; Genomic_DNA.
DR RefSeq; WP_008416947.1; NZ_AXZD01000008.1.
DR AlphaFoldDB; D8J4Q7; -.
DR STRING; 795797.HacjB3_10705; -.
DR GeneID; 9419951; -.
DR KEGG; hje:HacjB3_10705; -.
DR PATRIC; fig|795797.18.peg.2140; -.
DR eggNOG; arCOG01213; Archaea.
DR HOGENOM; CLU_044146_2_0_2; -.
DR OrthoDB; 120822at2157; -.
DR Proteomes; UP000000390; Chromosome.
DR Proteomes; UP000011645; Unassembled WGS sequence.
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 CDD; cd01427; HAD_like; 1.
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 NCBIfam; TIGR01482; SPP-subfamily; 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.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277, ECO:0000256|HAMAP-
KW Rule:MF_01419};
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01419, ECO:0000313|EMBL:ADJ15524.1};
KW Magnesium {ECO:0000256|HAMAP-Rule:MF_01419};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01419}.
FT ACT_SITE 8
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01419"
FT BINDING 8
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01419"
FT BINDING 10
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01419"
FT BINDING 152
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01419"
FT BINDING 175
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01419"
FT BINDING 179
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01419"
SQ SEQUENCE 223 AA; 23467 MW; D0FC0CA2B0BEAC5C CRC64;
MTPPIVVDID GTITRGDGSS AVDHRAFEEL RAWPAPVVIA TGKAFPYPVA LCQFVGIEPL
VIAENGGIVL AGGEVRVTGD ASGPREAARE YREAGYELGW GETDLVNRWR ETEVALSRES
PLAPLEEIAA EYGLEVVDTG YAYHLKDPAI SKGAGLEAVC DALGRTPEEF VAIGDSENDV
STFEVAGRSF AVANADGAAR AAADEVLEGR YSAGTVSVLS SLR
//
