ID   PLPP_BOVIN              Reviewed;         296 AA.
AC   Q3ZBF9;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2005, sequence version 1.
DT   10-FEB-2009, entry version 27.
DE   RecName: Full=Pyridoxal phosphate phosphatase;
DE            Short=PLP phosphatase;
DE            EC=3.1.3.74;
GN   Name=PDXP;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
OC   Pecora; Bovidae; Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Pyridoxal phosphate phosphatase. Has some activity
CC       towards pyridoxal 5'-phosphate (PLP), pyridoxine 5'-phosphate
CC       (PMP) and Pyridoxine 5'-phosphate (PNP), with a highest activity
CC       with PLP followed by PNP (By similarity).
CC   -!- CATALYTIC ACTIVITY: Pyridoxal 5'-phosphate + H(2)O = pyridoxal +
CC       phosphate.
CC   -!- COFACTOR: Divalent ions. Magnesium is the most effective (By
CC       similarity).
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily.
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DR   EMBL; BC103329; AAI03330.1; -; mRNA.
DR   IPI; IPI00713190; -.
DR   RefSeq; NP_001030207.1; -.
DR   UniGene; Bt.45290; -.
DR   SMR; Q3ZBF9; 1-294.
DR   Ensembl; ENSBTAG00000030255; Bos taurus.
DR   GeneID; 506308; -.
DR   KEGG; bta:506308; -.
DR   HOVERGEN; Q3ZBF9; -.
DR   BRENDA; 3.1.3.74; 251.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0033883; F:pyridoxal phosphatase activity; IEA:EC.
DR   GO; GO:0008152; P:metabolic process; IEA:InterPro.
DR   InterPro; IPR005834; Dehalogen-like_hydro.
DR   InterPro; IPR006357; HAD-SF_hydro_IIA.
DR   InterPro; IPR006349; PGP_euk.
DR   Pfam; PF00702; Hydrolase; 1.
DR   TIGRFAMs; TIGR01460; HAD-SF-IIA; 1.
DR   TIGRFAMs; TIGR01452; PGP_euk; 1.
PE   2: Evidence at transcript level;
KW   Hydrolase; Magnesium; Metal-binding; Pyridoxal phosphate.
FT   CHAIN         1    296       Pyridoxal phosphate phosphatase.
FT                                /FTId=PRO_0000254016.
FT   ACT_SITE     25     25       Nucleophile (By similarity).
FT   ACT_SITE     27     27       Proton donor (By similarity).
FT   METAL        25     25       Magnesium (By similarity).
FT   METAL        27     27       Magnesium (By similarity).
FT   METAL       238    238       Magnesium (By similarity).
SQ   SEQUENCE   296 AA;  31749 MW;  A3F0B3AA9D5D1E19 CRC64;
     MARCERLRGA ALRDVVGRAQ GVLFDCNGVL WNGERAVPGA PELLERLAQA GKATLFVSNN
     SRRARPELAL RFARLGFGGL RSEQLFSSAL CAARLLRQRL LGPPDTQGAV FVLGGEGLRA
     ELRAAGLRLA GDPSEDPGAA PRVRAVLVGY DEHFSFAKLS EACAHLRDPD CLLVATDRDP
     WHPLSDGSRT PGTGSLAAAV ETASGRQALV VGKPSPYMFE CITEHFSVDP GRTLMVGDRL
     ETDILFGHRC GMTTVLTLTG VSSLEEAQAY LAAGQHDLVP HYYVESIADL MEGLED
//