ID I3KYN6_ORENI Unreviewed; 284 AA.
AC I3KYN6;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 2.
DT 27-MAR-2024, entry version 55.
DE SubName: Full=Phosphoethanolamine/phosphocholine phosphatase 1 {ECO:0000313|Ensembl:ENSONIP00000026233.2};
OS Oreochromis niloticus (Nile tilapia) (Tilapia nilotica).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Oreochromini; Oreochromis.
OX NCBI_TaxID=8128 {ECO:0000313|Ensembl:ENSONIP00000026233.2, ECO:0000313|Proteomes:UP000005207};
RN [1] {ECO:0000313|Proteomes:UP000005207}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Broad Institute Genome Assembly Team;
RG Broad Institute Sequencing Platform;
RA Di Palma F., Johnson J., Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Oreochromis niloticus (Nile Tilapia).";
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSONIP00000026233.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946,
CC ECO:0000256|PIRSR:PIRSR031051-3};
CC -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily. PHOSPHO
CC family. {ECO:0000256|ARBA:ARBA00008541}.
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DR AlphaFoldDB; I3KYN6; -.
DR STRING; 8128.ENSONIP00000026233; -.
DR Ensembl; ENSONIT00000026256.2; ENSONIP00000026233.2; ENSONIG00000020930.2.
DR eggNOG; KOG3120; Eukaryota.
DR GeneTree; ENSGT00390000007741; -.
DR HOGENOM; CLU_068983_0_1_1; -.
DR InParanoid; I3KYN6; -.
DR OMA; FHSHECQ; -.
DR TreeFam; TF300112; -.
DR Proteomes; UP000005207; Linkage group LG4.
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; 1.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR006384; HAD_hydro_PyrdxlP_Pase-like.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR016965; Pase_PHOSPHO-typ.
DR NCBIfam; TIGR01489; DKMTPPase-SF; 1.
DR NCBIfam; TIGR01488; HAD-SF-IB; 1.
DR PANTHER; PTHR20889; PHOSPHATASE, ORPHAN 1, 2; 1.
DR PANTHER; PTHR20889:SF2; PHOSPHOETHANOLAMINE_PHOSPHOCHOLINE PHOSPHATASE; 1.
DR Pfam; PF06888; Put_Phosphatase; 1.
DR PIRSF; PIRSF031051; PyrdxlP_Pase_PHOSPHO2; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
PE 3: Inferred from homology;
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRSR:PIRSR031051-3};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR031051-3};
KW Reference proteome {ECO:0000313|Proteomes:UP000005207}.
FT ACT_SITE 48
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR031051-1"
FT ACT_SITE 50
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR031051-1"
FT BINDING 48
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR031051-3"
FT BINDING 50
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR031051-3"
FT BINDING 59
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR031051-2"
FT BINDING 140
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR031051-2"
FT BINDING 221
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR031051-3"
SQ SEQUENCE 284 AA; 32905 MW; 8C3F16350558F225 CRC64;
MGDSFFNCCY VPPHPPGEEE PQRPRRSEIM ASHPAHISPD KRFLIFFDFD ETIVDETSDD
MVVQAAPGQH LPGWLTDTYQ PGRYNEYMQR VLAYLAEQGV TESDIRSVME KIPATPGMLT
LFQFLRNRPA KDFEVILLSD ANTYFIECWL RRVGARQLFH RIFSNPATFN KDGRLVLRPF
HSHDCPRCPD NMCKQVIVRD YVARRTQERG RPYQRIFYVG DGANDFCPAL SLGPRDVAFP
RRDFPMHRLI TETHEAQPGE FKAVTVPWVS AEDVVQRLRK LVQE
//
