ID   PDXK_CAEEL              Reviewed;         321 AA.
AC   O01824;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 2.
DT   03-AUG-2022, entry version 134.
DE   RecName: Full=Putative pyridoxal kinase;
DE            EC=2.7.1.35 {ECO:0000250|UniProtKB:O46560};
DE   AltName: Full=Pyridoxine kinase;
GN   Name=pdxk-1 {ECO:0000312|WormBase:F57C9.1a};
GN   ORFNames=F57C9.1 {ECO:0000312|WormBase:F57C9.1a};
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
CC   -!- FUNCTION: Required for synthesis of pyridoxal-5-phosphate from vitamin
CC       B6. {ECO:0000250|UniProtKB:O46560}.
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:O46560};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000250|UniProtKB:O46560};
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:O46560};
CC       Note=Divalent metal cations. Zn(2+) is more efficient than Mg(2+).
CC       {ECO:0000250|UniProtKB:O46560};
CC   -!- SIMILARITY: Belongs to the pyridoxine kinase family. {ECO:0000305}.
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DR   EMBL; FO080263; CCD62433.2; -; Genomic_DNA.
DR   PIR; T15219; T15219.
DR   RefSeq; NP_491463.2; NM_059062.2.
DR   AlphaFoldDB; O01824; -.
DR   SMR; O01824; -.
DR   STRING; 6239.F57C9.1b; -.
DR   EPD; O01824; -.
DR   PaxDb; O01824; -.
DR   EnsemblMetazoa; F57C9.1a.1; F57C9.1a.1; WBGene00019008.
DR   GeneID; 172101; -.
DR   UCSC; F57C9.1b; c. elegans.
DR   CTD; 172101; -.
DR   WormBase; F57C9.1a; CE46957; WBGene00019008; pdxk-1.
DR   eggNOG; KOG2599; Eukaryota.
DR   GeneTree; ENSGT00390000003874; -.
DR   HOGENOM; CLU_046496_1_1_1; -.
DR   InParanoid; O01824; -.
DR   PhylomeDB; O01824; -.
DR   Reactome; R-CEL-6798695; Neutrophil degranulation.
DR   Reactome; R-CEL-964975; Vitamins B6 activation to pyridoxal phosphate.
DR   PRO; PR:O01824; -.
DR   Proteomes; UP000001940; Chromosome I.
DR   Bgee; WBGene00019008; Expressed in germ line (C elegans) and 4 other tissues.
DR   ExpressionAtlas; O01824; baseline and differential.
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; IPR011611; PfkB_dom.
DR   InterPro; IPR004625; PyrdxlKinase.
DR   InterPro; IPR029056; Ribokinase-like.
DR   PANTHER; PTHR10534; PTHR10534; 1.
DR   Pfam; PF00294; PfkB; 1.
DR   SUPFAM; SSF53613; SSF53613; 1.
DR   TIGRFAMs; TIGR00687; pyridox_kin; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Kinase; Metal-binding; Nucleotide-binding; Reference proteome;
KW   Transferase; Zinc.
FT   CHAIN           1..321
FT                   /note="Putative pyridoxal kinase"
FT                   /id="PRO_0000213340"
FT   BINDING         23
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P82197"
FT   BINDING         144
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P82197"
FT   BINDING         203..204
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P82197"
FT   BINDING         230..242
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P82197"
FT   BINDING         243
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P82197"
SQ   SEQUENCE   321 AA;  35986 MW;  5B0CFEE056B4D18E CRC64;
     MSSSELIAEL ERERDRRVLS IQSHVVHGYA GNKCSVFPLQ LHGFEVDFIN SVQFSNHAGN
     IEYLTLPTRY EHVKGQKLTE KELEELYEGL TLNNINNYTH VLTGYCGNVT FLQKIADVVK
     DLKKKNGNTT FVCDPVMGDN GRYYTPKELM PVYRDLIIPL ADVLTPNAFE LGELTGSPIE
     TEEDCLRAVN ELHAKGVKTV VVTSGVTGAQ TNESLRCYAS VKGSHVYRFT FPRLVGQFVG
     TGDTFTSLLV VWLDELNGDV SEAVKRVLAS MQCLIRKTSS YAQLQVDTNS RAMCELRLIQ
     SRKDLLWPPT CDQIQVEKIG Q