PHOP2_BOVIN
ID PHOP2_BOVIN Reviewed; 241 AA.
AC Q2KI06;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Pyridoxal phosphate phosphatase PHOSPHO2;
DE EC=3.1.3.74 {ECO:0000250|UniProtKB:Q8TCD6};
GN Name=PHOSPHO2;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Heart ventricle;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Phosphatase that has high activity toward pyridoxal 5'-
CC phosphate (PLP). Also active at much lower level toward pyrophosphate,
CC phosphoethanolamine (PEA), phosphocholine (PCho), phospho-l-tyrosine,
CC fructose-6-phosphate, p-nitrophenyl phosphate, and h-glycerophosphate.
CC {ECO:0000250|UniProtKB:Q8TCD6}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + pyridoxal 5'-phosphate = phosphate + pyridoxal;
CC Xref=Rhea:RHEA:20533, ChEBI:CHEBI:15377, ChEBI:CHEBI:17310,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:597326; EC=3.1.3.74;
CC Evidence={ECO:0000250|UniProtKB:Q8TCD6};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q8TCT1};
CC -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily. PHOSPHO
CC family. {ECO:0000305}.
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DR EMBL; BC112815; AAI12816.1; -; mRNA.
DR RefSeq; NP_001039430.1; NM_001045965.2.
DR RefSeq; XP_010800188.1; XM_010801886.2.
DR AlphaFoldDB; Q2KI06; -.
DR STRING; 9913.ENSBTAP00000001446; -.
DR PaxDb; Q2KI06; -.
DR PRIDE; Q2KI06; -.
DR Ensembl; ENSBTAT00000001446; ENSBTAP00000001446; ENSBTAG00000001092.
DR GeneID; 507308; -.
DR KEGG; bta:507308; -.
DR CTD; 493911; -.
DR VEuPathDB; HostDB:ENSBTAG00000001092; -.
DR VGNC; VGNC:32843; PHOSPHO2.
DR eggNOG; KOG3120; Eukaryota.
DR GeneTree; ENSGT00390000007741; -.
DR HOGENOM; CLU_068983_0_1_1; -.
DR InParanoid; Q2KI06; -.
DR OMA; HNLADCF; -.
DR OrthoDB; 1454608at2759; -.
DR TreeFam; TF300112; -.
DR Proteomes; UP000009136; Chromosome 2.
DR Bgee; ENSBTAG00000001092; Expressed in oocyte and 108 other tissues.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016791; F:phosphatase activity; IBA:GO_Central.
DR GO; GO:0033883; F:pyridoxal phosphatase activity; IEA:UniProtKB-EC.
DR Gene3D; 3.40.50.1000; -; 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 PANTHER; PTHR20889; PTHR20889; 1.
DR Pfam; PF06888; Put_Phosphatase; 1.
DR PIRSF; PIRSF031051; PyrdxlP_Pase_PHOSPHO2; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR TIGRFAMs; TIGR01489; DKMTPPase-SF; 1.
PE 2: Evidence at transcript level;
KW Hydrolase; Magnesium; Metal-binding; Pyridoxal phosphate;
KW Reference proteome.
FT CHAIN 1..241
FT /note="Pyridoxal phosphate phosphatase PHOSPHO2"
FT /id="PRO_0000254017"
FT ACT_SITE 8
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q8TCT1"
FT ACT_SITE 10
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q96GD0"
FT BINDING 8
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q96GD0"
FT BINDING 10
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q96GD0"
FT BINDING 19
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8TCT1"
FT BINDING 99
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8TCT1"
FT BINDING 179
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q96GD0"
SQ SEQUENCE 241 AA; 27751 MW; 86EF01C1A6A54325 CRC64;
MKILLVFDFD NTIIDDNSDT WIVQCAPEKK LPLELKDSYK KGFWTEFMGR VFKYLGDEGV
REDEMKRAMI SMPFTPGMVE LLNFIRKNKN KFDCIIISDS NSVFIDWVLE ATNFHDVFDK
VFTNPAAFDS NGHLTVEKHH THSCTRCPQN LCKNVVLVEF VGEQLQQGVN YTRIVYIGDG
GNDVCPVTFL KKNDIAMPRK GYALQKTLYR MCQNLEPMES SVVSWSSGVE IISYLQFLIK
E