ID A0A2K5HX56_COLAP Unreviewed; 267 AA.
AC A0A2K5HX56;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Phosphoethanolamine/phosphocholine phosphatase 1 {ECO:0008006|Google:ProtNLM};
OS Colobus angolensis palliatus (Peters' Angolan colobus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Colobinae; Colobus.
OX NCBI_TaxID=336983 {ECO:0000313|Ensembl:ENSCANP00000008959.1, ECO:0000313|Proteomes:UP000233080};
RN [1] {ECO:0000313|Ensembl:ENSCANP00000008959.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 RefSeq; XP_011815297.1; XM_011959907.1.
DR RefSeq; XP_011815298.1; XM_011959908.1.
DR RefSeq; XP_011815300.1; XM_011959910.1.
DR AlphaFoldDB; A0A2K5HX56; -.
DR STRING; 336983.ENSCANP00000008959; -.
DR Ensembl; ENSCANT00000031825.1; ENSCANP00000008959.1; ENSCANG00000027890.1.
DR GeneID; 105524589; -.
DR CTD; 162466; -.
DR OMA; FHSHECQ; -.
DR OrthoDB; 372892at2759; -.
DR Proteomes; UP000233080; Unplaced.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016791; F:phosphatase activity; IEA:InterPro.
DR CDD; cd16418; HAD_Pase; 1.
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:UP000233080}.
FT ACT_SITE 32
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR031051-1"
FT ACT_SITE 34
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR031051-1"
FT BINDING 32
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR031051-3"
FT BINDING 34
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR031051-3"
FT BINDING 43
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR031051-2"
FT BINDING 123
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR031051-2"
FT BINDING 203
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR031051-3"
SQ SEQUENCE 267 AA; 29667 MW; 4D7975E6C6981B4A CRC64;
MSGCFPVSGL RCLSRDGGMA AQGAPRFLLT FDFDETIVDE NSDDSIVRAA PGQRLPESLR
ATYREGFYNE YMQRVFKYLG EQGVRPRDLR AIYEAIPLSP GMGDLLQFVA KQGACFEVIL
ISDANTFGVE SALRAAGHHS LFRRILSNPS GPDARGLLAL RPFHTHSCTR CPANMCKHKV
LSDYLRERAH DGVHFERLFY VGDGANDFCP MGLLAGGDVA FPRRGYPMHR LIQEAQKAEP
SSFRASVVPW ETAADVRLHL QQVLKSC
//
