PDXK_BOVIN
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 03-AUG-2022, entry version 98.
DE RecName: Full=Pyridoxal kinase;
DE EC=2.7.1.35 {ECO:0000250|UniProtKB:O00764};
DE AltName: Full=Pyridoxine kinase;
GN Name=PDXK;
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=Hypothalamus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the phosphorylation of the dietary vitamin B6
CC vitamers pyridoxal (PL), pyridoxine (PN) and pyridoxamine (PM) to form
CC pyridoxal 5'-phosphate (PLP), pyridoxine 5'-phosphate (PNP) and
CC pyridoxamine 5'-phosphate (PMP), respectively (By similarity). PLP is
CC the active form of vitamin B6, and acts as a cofactor for over 140
CC different enzymatic reactions (By similarity).
CC {ECO:0000250|UniProtKB:O00764}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + pyridoxal = ADP + H(+) + pyridoxal 5'-phosphate;
CC Xref=Rhea:RHEA:10224, ChEBI:CHEBI:15378, ChEBI:CHEBI:17310,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:456216, ChEBI:CHEBI:597326;
CC EC=2.7.1.35; Evidence={ECO:0000250|UniProtKB:O00764};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10225;
CC Evidence={ECO:0000250|UniProtKB:O00764};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + pyridoxamine = ADP + H(+) + pyridoxamine 5'-phosphate;
CC Xref=Rhea:RHEA:25104, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:57761, ChEBI:CHEBI:58451, ChEBI:CHEBI:456216;
CC EC=2.7.1.35; Evidence={ECO:0000250|UniProtKB:O00764};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25105;
CC Evidence={ECO:0000250|UniProtKB:O00764};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + pyridoxine = ADP + H(+) + pyridoxine 5'-phosphate;
CC Xref=Rhea:RHEA:25108, ChEBI:CHEBI:15378, ChEBI:CHEBI:16709,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:58589, ChEBI:CHEBI:456216;
CC EC=2.7.1.35; Evidence={ECO:0000250|UniProtKB:O00764};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25109;
CC Evidence={ECO:0000250|UniProtKB:O00764};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P82197};
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:O00764};
CC -!- ACTIVITY REGULATION: Activity is increased in the presence of K(+)or
CC Na(+). {ECO:0000250|UniProtKB:O00764}.
CC -!- PATHWAY: Cofactor metabolism; pyridoxal 5'-phosphate salvage; pyridoxal
CC 5'-phosphate from pyridoxal: step 1/1. {ECO:0000250|UniProtKB:O00764}.
CC -!- PATHWAY: Cofactor metabolism; pyridoxal 5'-phosphate salvage;
CC pyridoxine 5'-phosphate from pyridoxine: step 1/1.
CC {ECO:0000250|UniProtKB:O00764}.
CC -!- PATHWAY: Cofactor metabolism; pyridoxal 5'-phosphate salvage;
CC pyridoxamine 5'-phosphate from pyridoxamine: step 1/1.
CC {ECO:0000250|UniProtKB:O00764}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:O00764}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:O00764}.
CC -!- SIMILARITY: Belongs to the pyridoxine kinase family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC122793; AAI22794.1; -; mRNA.
DR RefSeq; NP_001069119.1; NM_001075651.2.
DR AlphaFoldDB; Q0II59; -.
DR SMR; Q0II59; -.
DR STRING; 9913.ENSBTAP00000024203; -.
DR PaxDb; Q0II59; -.
DR PeptideAtlas; Q0II59; -.
DR PRIDE; Q0II59; -.
DR Ensembl; ENSBTAT00000024203; ENSBTAP00000024203; ENSBTAG00000018186.
DR GeneID; 514168; -.
DR KEGG; bta:514168; -.
DR CTD; 8566; -.
DR VEuPathDB; HostDB:ENSBTAG00000018186; -.
DR VGNC; VGNC:50243; PDXK.
DR eggNOG; KOG2599; Eukaryota.
DR GeneTree; ENSGT00390000003874; -.
DR HOGENOM; CLU_046496_1_1_1; -.
DR InParanoid; Q0II59; -.
DR OMA; CPNQLEL; -.
DR OrthoDB; 1091630at2759; -.
DR TreeFam; TF315004; -.
DR Reactome; R-BTA-6798695; Neutrophil degranulation.
DR Reactome; R-BTA-964975; Vitamins B6 activation to pyridoxal phosphate.
DR UniPathway; UPA01068; UER00298.
DR UniPathway; UPA01068; UER00299.
DR UniPathway; UPA01068; UER00300.
DR Proteomes; UP000009136; Chromosome 1.
DR Bgee; ENSBTAG00000018186; Expressed in parenchyma of mammary gland and 104 other tissues.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0031403; F:lithium ion binding; IEA:Ensembl.
DR GO; GO:0000287; F:magnesium ion binding; IEA:Ensembl.
DR GO; GO:0030955; F:potassium ion binding; IEA:Ensembl.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
DR GO; GO:0008478; F:pyridoxal kinase activity; IBA:GO_Central.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:Ensembl.
DR GO; GO:0031402; F:sodium ion binding; IEA:Ensembl.
DR GO; GO:0008270; F:zinc ion binding; IEA:Ensembl.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0009443; P:pyridoxal 5'-phosphate salvage; IBA:GO_Central.
DR CDD; cd01173; pyridoxal_pyridoxamine_kinase; 1.
DR Gene3D; 3.40.1190.20; -; 1.
DR InterPro; IPR013749; PM/HMP-P_kinase-1.
DR InterPro; IPR004625; PyrdxlKinase.
DR InterPro; IPR029056; Ribokinase-like.
DR PANTHER; PTHR10534; PTHR10534; 1.
DR Pfam; PF08543; Phos_pyr_kin; 1.
DR SUPFAM; SSF53613; SSF53613; 1.
DR TIGRFAMs; TIGR00687; pyridox_kin; 1.
PE 2: Evidence at transcript level;
KW Acetylation; ATP-binding; Cytoplasm; Kinase; Magnesium; Metal-binding;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Sodium;
KW Transferase; Zinc.
FT CHAIN 1..312
FT /note="Pyridoxal kinase"
FT /id="PRO_0000268830"
FT ACT_SITE 235
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:O00764"
FT BINDING 12
FT /ligand="pyridoxal"
FT /ligand_id="ChEBI:CHEBI:17310"
FT /evidence="ECO:0000250|UniProtKB:O00764"
FT BINDING 47
FT /ligand="pyridoxal"
FT /ligand_id="ChEBI:CHEBI:17310"
FT /evidence="ECO:0000250|UniProtKB:O00764"
FT BINDING 47
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:O00764"
FT BINDING 113
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O00764"
FT BINDING 113
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /evidence="ECO:0000250|UniProtKB:O00764"
FT BINDING 118
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:O00764"
FT BINDING 148
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /evidence="ECO:0000250|UniProtKB:O00764"
FT BINDING 150..153
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O00764"
FT BINDING 186..187
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O00764"
FT BINDING 186
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /evidence="ECO:0000250|UniProtKB:O00764"
FT BINDING 226..228
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O00764"
FT BINDING 233
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O00764"
FT BINDING 234..235
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:O00764"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P82197"
FT MOD_RES 59
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00764"
FT MOD_RES 213
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00764"
FT MOD_RES 285
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00764"
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
