ID   PDXK_BOVIN              Reviewed;         312 AA.
AC   Q0II59;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2006, sequence version 1.
DT   16-JUN-2009, entry version 22.
DE   RecName: Full=Pyridoxal kinase;
DE            EC=2.7.1.35;
DE   AltName: Full=Pyridoxine kinase;
GN   Name=PDXK;
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=Hypothalamus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Required for synthesis of pyridoxal-5-phosphate from
CC       vitamin B6 (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + pyridoxal = ADP + pyridoxal 5'-
CC       phosphate.
CC   -!- COFACTOR: Divalent cations. Zinc is more efficient than magnesium
CC       (By similarity).
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the pyridoxine kinase family.
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DR   EMBL; BC122793; AAI22794.1; -; mRNA.
DR   IPI; IPI00701044; -.
DR   RefSeq; NP_001069119.1; -.
DR   UniGene; Bt.74137; -.
DR   SMR; Q0II59; 4-312.
DR   Ensembl; ENSBTAG00000018186; Bos taurus.
DR   GeneID; 514168; -.
DR   KEGG; bta:514168; -.
DR   HOVERGEN; Q0II59; -.
DR   BRENDA; 2.7.1.35; 251.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008478; F:pyridoxal kinase activity; IEA:EC.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008615; P:pyridoxine biosynthetic process; IEA:InterPro.
DR   InterPro; IPR011611; Carb/pur_kinase.
DR   InterPro; IPR004625; PyrdxlP_synth_PyrdxlKinase.
DR   Pfam; PF00294; PfkB; 1.
DR   TIGRFAMs; TIGR00687; pyridox_kin; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; ATP-binding; Cytoplasm; Kinase; Metal-binding;
KW   Nucleotide-binding; Phosphoprotein; Transferase; Zinc.
FT   CHAIN         1    312       Pyridoxal kinase.
FT                                /FTId=PRO_0000268830.
FT   NP_BIND     186    187       ATP (By similarity).
FT   NP_BIND     223    234       ATP (By similarity).
FT   BINDING      12     12       Substrate (By similarity).
FT   BINDING      47     47       Substrate (By similarity).
FT   BINDING     127    127       Substrate (By similarity).
FT   BINDING     235    235       Substrate (By similarity).
FT   MOD_RES       1      1       N-acetylmethionine (By similarity).
FT   MOD_RES     213    213       Phosphoserine (By similarity).
FT   MOD_RES     285    285       Phosphoserine (By similarity).
SQ   SEQUENCE   312 AA;  34817 MW;  7FDD3E0153DFB7CC CRC64;
     MEEECRVLSI QSHVVRGYVG NRAATFPLQV LGFEVDAVNS VQFSNHTGYS HWKGQVLNSD
     ELQELYDGLK LNSVNQYDYV LTGYTRDKSF LAMVVDIVQE LKQQNPRLVY VCDPVMGDQR
     DGEGAMYVPD DLLPVYREKV VPVADIITPN QFEAELLTGR KIHTQEEALE VMDMLHSMGP
     DTVVITSSDL LSPRGSDYLM ALGSQRTRAP DGSMVTQRIR MEMHKVDAVF VGTGDLFAAM
     LLAWTHKHPN NLKVACEKTV SAMHHVLQRT IKCAKAKSGE GVKPSPAQLE LRMVQSKKDI
     ESPEIVVQAT VL
//