PDXK_PIG
ID PDXK_PIG Reviewed; 322 AA.
AC O46560;
DT 05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Pyridoxal kinase;
DE EC=2.7.1.35 {ECO:0000269|PubMed:9924807};
DE AltName: Full=Pyridoxine kinase;
GN Name=PDXK; Synonyms=PKH;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND
RP PROTEIN SEQUENCE OF 17-322.
RC TISSUE=Brain cortex;
RX PubMed=9924807; DOI=10.1016/s1357-2725(98)00092-2;
RA Gao Z.G., Lau C.-K., Lo S.C.L., Choi S.Y., Churchich J.E., Kwok F.;
RT "Porcine pyridoxal kinase c-DNA cloning, expression and confirmation of its
RT primary sequence.";
RL Int. J. Biochem. Cell Biol. 30:1379-1388(1998).
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 (PubMed:9924807)
CC (Probable). PLP is the active form of vitamin B6, and acts as a
CC cofactor for over 140 different enzymatic reactions (By similarity).
CC {ECO:0000250|UniProtKB:O00764, ECO:0000269|PubMed:9924807,
CC ECO:0000305}.
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:0000269|PubMed:9924807};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10225;
CC Evidence={ECO:0000305|PubMed:9924807};
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:0000269|PubMed:9924807};
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:9924807};
CC Note=Divalent metal cations. Zn(2+) is more efficient than Mg(2+).
CC {ECO:0000269|PubMed:9924807};
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 -!- PTM: The N-terminus is blocked.
CC -!- SIMILARITY: Belongs to the pyridoxine kinase family. {ECO:0000305}.
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DR EMBL; AF041255; AAB96794.1; -; mRNA.
DR RefSeq; NP_999108.1; NM_213943.1.
DR AlphaFoldDB; O46560; -.
DR SMR; O46560; -.
DR STRING; 9823.ENSSSCP00000028021; -.
DR PeptideAtlas; O46560; -.
DR GeneID; 396983; -.
DR KEGG; ssc:396983; -.
DR CTD; 8566; -.
DR eggNOG; KOG2599; Eukaryota.
DR InParanoid; O46560; -.
DR OrthoDB; 1091630at2759; -.
DR UniPathway; UPA01068; UER00298.
DR UniPathway; UPA01068; UER00299.
DR UniPathway; UPA01068; UER00300.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; 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:0008478; F:pyridoxal kinase activity; IBA:GO_Central.
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 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..322
FT /note="Pyridoxal kinase"
FT /id="PRO_0000213337"
FT ACT_SITE 245
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:O00764"
FT BINDING 22
FT /ligand="pyridoxal"
FT /ligand_id="ChEBI:CHEBI:17310"
FT /evidence="ECO:0000250|UniProtKB:O00764"
FT BINDING 57
FT /ligand="pyridoxal"
FT /ligand_id="ChEBI:CHEBI:17310"
FT /evidence="ECO:0000250|UniProtKB:O00764"
FT BINDING 57
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:O00764"
FT BINDING 123
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O00764"
FT BINDING 123
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /evidence="ECO:0000250|UniProtKB:O00764"
FT BINDING 128
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:O00764"
FT BINDING 158
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /evidence="ECO:0000250|UniProtKB:O00764"
FT BINDING 160..163
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O00764"
FT BINDING 196..197
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O00764"
FT BINDING 196
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /evidence="ECO:0000250|UniProtKB:O00764"
FT BINDING 236..238
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O00764"
FT BINDING 243
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O00764"
FT BINDING 244..245
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 69
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00764"
FT MOD_RES 174
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00764"
FT MOD_RES 223
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00764"
FT MOD_RES 295
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00764"
SQ SEQUENCE 322 AA; 35614 MW; 1C25E2E36CCB92B8 CRC64;
MQAGSWVVGG GDSDSRVLSI QSHVVRGYVG NRAATFPLQV LGFEVDAVNS VQFSNHTGYA
HWKGQVLNSD ELHALYEGLK LNNVNQYDYV LTGYTRDKSF LAMVVDIVRE LKQQNPRLVY
VCDPVMGDKW DGEGSMYVPE DLLPVYREKV VPVADIITPN QFEAELLTGR RIHSEEEALA
VMDMLHAMGP DTVVITSSDL PSPRGKDYLI ALGSQRTRSP DGSVATQRIR MEICKVDAVF
VGTGDLFAAM LLAWTHKHPN NLKVACEKTV SAMHHVLRRT IQCAKAKAGE GLKPSPAQLE
LRMVQSKRDI EDPEVVVQAT VL
