ID A0A3B5AQN4_9TELE Unreviewed; 306 AA.
AC A0A3B5AQN4;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Glycerol-3-phosphate phosphatase {ECO:0000256|ARBA:ARBA00039737};
DE EC=3.1.3.21 {ECO:0000256|ARBA:ARBA00038981};
DE EC=3.1.3.48 {ECO:0000256|ARBA:ARBA00013064};
DE AltName: Full=Aspartate-based ubiquitous Mg(2+)-dependent phosphatase {ECO:0000256|ARBA:ARBA00042942};
DE AltName: Full=Phosphoglycolate phosphatase {ECO:0000256|ARBA:ARBA00042278};
GN Name=pgp {ECO:0000313|RefSeq:XP_008302537.1};
OS Stegastes partitus (bicolor damselfish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Stegastes.
OX NCBI_TaxID=144197 {ECO:0000313|Ensembl:ENSSPAP00000015842.1, ECO:0000313|Proteomes:UP000261400};
RN [1] {ECO:0000313|Ensembl:ENSSPAP00000015842.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_008302537.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] +
CC phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620; EC=3.1.3.48;
CC Evidence={ECO:0000256|ARBA:ARBA00001490};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + sn-glycerol 1-phosphate = glycerol + phosphate;
CC Xref=Rhea:RHEA:46084, ChEBI:CHEBI:15377, ChEBI:CHEBI:17754,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57685; EC=3.1.3.21;
CC Evidence={ECO:0000256|ARBA:ARBA00036142};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + sn-glycerol 3-phosphate = glycerol + phosphate;
CC Xref=Rhea:RHEA:66372, ChEBI:CHEBI:15377, ChEBI:CHEBI:17754,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57597; EC=3.1.3.21;
CC Evidence={ECO:0000256|ARBA:ARBA00035936};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|PIRSR:PIRSR000915-3};
CC Note=Divalent metal ions. Mg(2+) is the most effective.
CC {ECO:0000256|PIRSR:PIRSR000915-3};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily.
CC CbbY/CbbZ/Gph/YieH family. {ECO:0000256|ARBA:ARBA00006171}.
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DR RefSeq; XP_008302537.1; XM_008304315.1.
DR AlphaFoldDB; A0A3B5AQN4; -.
DR STRING; 144197.ENSSPAP00000015842; -.
DR Ensembl; ENSSPAT00000016098.1; ENSSPAP00000015842.1; ENSSPAG00000011948.1.
DR GeneID; 103374253; -.
DR CTD; 283871; -.
DR GeneTree; ENSGT00940000160577; -.
DR OrthoDB; 217676at2759; -.
DR Proteomes; UP000261400; Unplaced.
DR Proteomes; UP000694891; Unplaced.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016791; F:phosphatase activity; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 2.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR006357; HAD-SF_hydro_IIA.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR006349; PGP_euk.
DR NCBIfam; TIGR01460; HAD-SF-IIA; 1.
DR NCBIfam; TIGR01452; PGP_euk; 1.
DR PANTHER; PTHR19288; 4-NITROPHENYLPHOSPHATASE-RELATED; 1.
DR PANTHER; PTHR19288:SF93; GLYCEROL-3-PHOSPHATE PHOSPHATASE; 1.
DR Pfam; PF13344; Hydrolase_6; 1.
DR Pfam; PF13242; Hydrolase_like; 1.
DR PIRSF; PIRSF000915; PGP-type_phosphatase; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR000915};
KW Magnesium {ECO:0000256|PIRSR:PIRSR000915-3};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR000915-3};
KW Reference proteome {ECO:0000313|Proteomes:UP000694891}.
FT ACT_SITE 27
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR000915-1"
FT ACT_SITE 29
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000915-1"
FT BINDING 27
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000915-3"
FT BINDING 29
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000915-3"
FT BINDING 220
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000915-2"
FT BINDING 245
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000915-3"
SQ SEQUENCE 306 AA; 33083 MW; 8A35F6C12E321A80 CRC64;
MSGSKCTRLS GALVKQLLES VDSILFDCDG VIWRGDQAIP GAPQVINLLK ESGKKVFFVT
NNSTKTRKMY AEKMTALGFN VTEDEVFGTA YCSAMYLKTV CKVDGKVYLI GSNAMRQELE
AVGIQQTGVG PDPVTGKQAD WANVPLDPEV KAVVVGFDEH FSYMKLNRAL QYLIQQGCLF
VGTNRDTRLP LEGGKAVPGT GCLLQCVETA AQSQAQTVGK PNHFMFDCVA SQFGVERNRC
LMVGDRLDTD IMLGSNCGLK TLLTLTGVNT VADAEAHQKS GCAERQGMVP DYYVESIADL
LPALQG
//
