ID   PHOP2_RAT               Reviewed;         241 AA.
AC   Q66HC4;
DT   10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=Pyridoxal phosphate phosphatase PHOSPHO2;
DE            EC=3.1.3.74 {ECO:0000250|UniProtKB:Q8TCD6};
GN   Name=Phospho2;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
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; BC081926; AAH81926.1; -; mRNA.
DR   RefSeq; NP_001007643.1; NM_001007642.1.
DR   AlphaFoldDB; Q66HC4; -.
DR   SMR; Q66HC4; -.
DR   STRING; 10116.ENSRNOP00000010489; -.
DR   PaxDb; Q66HC4; -.
DR   DNASU; 295663; -.
DR   Ensembl; ENSRNOT00000010489; ENSRNOP00000010489; ENSRNOG00000007979.
DR   Ensembl; ENSRNOT00000106872; ENSRNOP00000088734; ENSRNOG00000007979.
DR   Ensembl; ENSRNOT00000112246; ENSRNOP00000090811; ENSRNOG00000007979.
DR   GeneID; 295663; -.
DR   KEGG; rno:295663; -.
DR   UCSC; RGD:1359274; rat.
DR   CTD; 493911; -.
DR   RGD; 1359274; Phospho2.
DR   eggNOG; KOG3120; Eukaryota.
DR   GeneTree; ENSGT00390000007741; -.
DR   HOGENOM; CLU_068983_0_1_1; -.
DR   InParanoid; Q66HC4; -.
DR   OMA; HNLADCF; -.
DR   OrthoDB; 1454608at2759; -.
DR   PhylomeDB; Q66HC4; -.
DR   TreeFam; TF300112; -.
DR   PRO; PR:Q66HC4; -.
DR   Proteomes; UP000002494; Chromosome 3.
DR   Bgee; ENSRNOG00000007979; Expressed in testis and 20 other tissues.
DR   Genevisible; Q66HC4; RN.
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_0000068835"
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;  27627 MW;  8BA3CFE909C224CF CRC64;
     MKVLLVFDFD NTIIDDNSDT WIIQCAPDKK LPIELQDSYQ KGLWTEFMGR VFKYLRDEGV
     KEEELKRAVT SLPFTSGMIE LLSFLRMNKD RFDCIIISDS NSIFIDWVLE AAAFHDVFDT
     VFTNPASFDS TGRLTVRNCH THACTRCPKN LCKNTVLGEF IDKQLQKGVR YTRIVYIGDG
     GNDVCPVTFL KKNDVAMPRE GYTLHRTLDK MSQNLEPMAS SIVVWSSGME IISHLQFLIQ
     M