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Database: UniProt
Entry: A0A3Q3A122_KRYMA
LinkDB: A0A3Q3A122_KRYMA
Original site: A0A3Q3A122_KRYMA 
ID   A0A3Q3A122_KRYMA        Unreviewed;       304 AA.
AC   A0A3Q3A122;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   24-JAN-2024, entry version 19.
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};
OS   Kryptolebias marmoratus (Mangrove killifish) (Rivulus marmoratus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Rivulidae; Kryptolebias.
OX   NCBI_TaxID=37003 {ECO:0000313|Ensembl:ENSKMAP00000009460.1, ECO:0000313|Proteomes:UP000264800};
RN   [1] {ECO:0000313|Ensembl:ENSKMAP00000009460.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-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   AlphaFoldDB; A0A3Q3A122; -.
DR   STRING; 37003.ENSKMAP00000009460; -.
DR   Ensembl; ENSKMAT00000009605.1; ENSKMAP00000009460.1; ENSKMAG00000007095.1.
DR   GeneTree; ENSGT00940000160577; -.
DR   OMA; PPMHRET; -.
DR   Proteomes; UP000264800; Unplaced.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016791; F:phosphatase activity; IEA:InterPro.
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:SF92; 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:UP000264800}.
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   304 AA;  33000 MW;  78C5ED31C53E1369 CRC64;
     MSGTKCTRLS GAPVRRLLDS VDSVLFDCDG VIWRGDQAVP GACRVIDLLK EHGKKVFFVT
     NNSSKTRRMY AEKMSALGFG VSEEEVFGTA YCCAAYLRTV CELEGKKVYL IGSAAMAHEL
     EAVGIRQTGV GPDHVSGKQG DWAAVPLDPD VRAVVVGFDE HFSYMKLNRA LQYLLREDCL
     FVGTNRDTRL PLEGGKAVPT GCLLQAVETA AQRRAQTVGK PNHFMFDCVA SHFGVQPERC
     LMVGDRLDTD ILLGSNCGLK TLLTLTGVST VADAEAHRES GCAERQGMVP DYYVDSIADL
     LPAL
//
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