PDXK_RAT
ID PDXK_RAT Reviewed; 312 AA.
AC O35331;
DT 05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Pyridoxal kinase;
DE EC=2.7.1.35 {ECO:0000250|UniProtKB:O00764};
DE AltName: Full=Pyridoxine kinase;
GN Name=Pdxk; Synonyms=Pkh;
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 [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RA Wu Y., Ngo E., Nutter L.M.;
RL Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROTEIN SEQUENCE OF 77-102; 161-177 AND 276-292, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Hippocampus, and Spinal cord;
RA Lubec G., Afjehi-Sadat L., Chen W.-Q.;
RL Submitted (APR-2007) to UniProtKB.
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}.
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DR EMBL; AF020346; AAB71400.1; -; mRNA.
DR RefSeq; NP_113957.1; NM_031769.1.
DR AlphaFoldDB; O35331; -.
DR SMR; O35331; -.
DR STRING; 10116.ENSRNOP00000001589; -.
DR iPTMnet; O35331; -.
DR PhosphoSitePlus; O35331; -.
DR jPOST; O35331; -.
DR PaxDb; O35331; -.
DR PRIDE; O35331; -.
DR GeneID; 83578; -.
DR KEGG; rno:83578; -.
DR UCSC; RGD:621324; rat.
DR CTD; 8566; -.
DR RGD; 621324; Pdxk.
DR eggNOG; KOG2599; Eukaryota.
DR InParanoid; O35331; -.
DR OrthoDB; 1091630at2759; -.
DR PhylomeDB; O35331; -.
DR BRENDA; 2.7.1.35; 5301.
DR Reactome; R-RNO-6798695; Neutrophil degranulation.
DR Reactome; R-RNO-964975; Vitamins B6 activation to pyridoxal phosphate.
DR UniPathway; UPA01068; UER00298.
DR UniPathway; UPA01068; UER00299.
DR UniPathway; UPA01068; UER00300.
DR PRO; PR:O35331; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0097159; F:organic cyclic compound binding; IPI:RGD.
DR GO; GO:0070280; F:pyridoxal binding; IDA:RGD.
DR GO; GO:0008478; F:pyridoxal kinase activity; IDA:RGD.
DR GO; GO:0036094; F:small molecule binding; IPI:RGD.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:RGD.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0009443; P:pyridoxal 5'-phosphate salvage; IBA:GO_Central.
DR GO; GO:0042823; P:pyridoxal phosphate biosynthetic process; IDA:RGD.
DR GO; GO:0014075; P:response to amine; IEP:RGD.
DR GO; GO:0032094; P:response to food; IEP:RGD.
DR GO; GO:0017085; P:response to insecticide; IEP:RGD.
DR GO; GO:0032570; P:response to progesterone; IEP:RGD.
DR GO; GO:0009636; P:response to toxic substance; IEP:RGD.
DR GO; GO:0010165; P:response to X-ray; IEP:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
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 1: Evidence at protein level;
KW Acetylation; ATP-binding; Cytoplasm; Direct protein sequencing; Kinase;
KW Magnesium; Metal-binding; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Sodium; Transferase; Zinc.
FT CHAIN 1..312
FT /note="Pyridoxal kinase"
FT /id="PRO_0000213338"
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 164
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; 34908 MW; 34C27148122268ED CRC64;
MEGECRVLSI QSHVVRGYVG NRAAMFPLQV LGFEVDAVNS VQFSNHTGYA HWKGQVLTSQ
ELHALYEGLK ANNVNKYDYV LTGYTRDKSF LGMVVDIVQE LKQQNSRLVY VCDPVMGDKW
NGEGSMYVPQ DLLPVYREKV VPMADIITPN QFEAELLSGR KIHSQEEAFA VMDVLHRMGP
DTVVITSSDL PSPKGSDYLM ALGSQRMRKP DGSTVTQRIR MEMRKVDPVF VGTGDLFAAM
LLAWTHKHPD NLKVACEKTV SAMQHVLQRT IRCAKAEAGE GQKPSPAQLE LRMVQSRKDI
EDPEIVVQAT VL
