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   16-JUN-2009, entry version 26.
DE   RecName: Full=Pyridoxal phosphate phosphatase PHOSPHO2;
DE            EC=3.1.3.74;
GN   Name=PHOSPHO2;
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=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
CC       pyrophosphate, phosphoethanolamine (PEA), phosphocholine (PCho),
CC       phospho-l-tyrosine, fructose-6-phosphate, p-nitrophenyl phosphate,
CC       and h-glycerophosphate (By similarity).
CC   -!- CATALYTIC ACTIVITY: Pyridoxal 5'-phosphate + H(2)O = pyridoxal +
CC       phosphate.
CC   -!- COFACTOR: Magnesium (By similarity).
CC   -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily. PHOSPHO
CC       family.
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DR   EMBL; BC112815; AAI12816.1; -; mRNA.
DR   IPI; IPI00704487; -.
DR   RefSeq; NP_001039430.1; -.
DR   UniGene; Bt.52539; -.
DR   Ensembl; ENSBTAG00000001092; Bos taurus.
DR   GeneID; 507308; -.
DR   KEGG; bta:507308; -.
DR   HOVERGEN; Q2KI06; -.
DR   OMA; Q2KI06; NDVAMPR.
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; IPR006383; HAD-SF_hydro_IB_PSP-like.
DR   InterPro; IPR006384; PyrdxlP_Pase-rel.
DR   InterPro; IPR016965; PyrdxlP_Pase_PHOSPHO2.
DR   Pfam; PF06888; Put_Phosphatase; 1.
DR   PIRSF; PIRSF031051; PyrdxlP_Pase_PHOSPHO2; 1.
DR   TIGRFAMs; TIGR01489; DKMTPPase-SF; 1.
DR   TIGRFAMs; TIGR01488; HAD-SF-IB; 1.
PE   2: Evidence at transcript level;
KW   Hydrolase; Magnesium; Metal-binding; Pyridoxal phosphate.
FT   CHAIN         1    241       Pyridoxal phosphate phosphatase PHOSPHO2.
FT                                /FTId=PRO_0000254017.
FT   ACT_SITE      8      8       Nucleophile (By similarity).
FT   ACT_SITE     10     10       Proton donor (By similarity).
FT   METAL         8      8       Magnesium (By similarity).
FT   METAL        10     10       Magnesium (By similarity).
FT   METAL       179    179       Magnesium (By similarity).
FT   BINDING      19     19       Substrate (By similarity).
FT   BINDING      99     99       Substrate (By similarity).
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
//