ID   PDXY_DEIGD              Reviewed;         299 AA.
AC   Q1J237;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   13-JUN-2006, sequence version 1.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=Pyridoxal kinase PdxY {ECO:0000255|HAMAP-Rule:MF_01639};
DE            Short=PL kinase {ECO:0000255|HAMAP-Rule:MF_01639};
DE            EC=2.7.1.35 {ECO:0000255|HAMAP-Rule:MF_01639};
GN   Name=pdxY {ECO:0000255|HAMAP-Rule:MF_01639}; OrderedLocusNames=Dgeo_0144;
OS   Deinococcus geothermalis (strain DSM 11300 / AG-3a).
OC   Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; Deinococcaceae;
OC   Deinococcus.
OX   NCBI_TaxID=319795;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 11300 / AG-3a;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Brettin T., Bruce D., Han C., Tapia R., Saunders E., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Daly M.J.,
RA   Fredrickson J.K., Makarova K.S., Gaidamakova E.K., Zhai M., Richardson P.;
RT   "Complete sequence of chromosome 1 of Deinococcus geothermalis DSM 11300.";
RL   Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Pyridoxal kinase involved in the salvage pathway of pyridoxal
CC       5'-phosphate (PLP). Catalyzes the phosphorylation of pyridoxal to PLP.
CC       {ECO:0000255|HAMAP-Rule:MF_01639}.
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:0000255|HAMAP-Rule:MF_01639};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01639};
CC   -!- PATHWAY: Cofactor metabolism; pyridoxal 5'-phosphate salvage; pyridoxal
CC       5'-phosphate from pyridoxal: step 1/1. {ECO:0000255|HAMAP-
CC       Rule:MF_01639}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01639}.
CC   -!- SIMILARITY: Belongs to the pyridoxine kinase family. PdxY subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01639}.
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DR   EMBL; CP000359; ABF44447.1; -; Genomic_DNA.
DR   RefSeq; WP_011529294.1; NC_008025.1.
DR   AlphaFoldDB; Q1J237; -.
DR   SMR; Q1J237; -.
DR   STRING; 319795.Dgeo_0144; -.
DR   EnsemblBacteria; ABF44447; ABF44447; Dgeo_0144.
DR   KEGG; dge:Dgeo_0144; -.
DR   eggNOG; COG2240; Bacteria.
DR   HOGENOM; CLU_046496_3_1_0; -.
DR   OMA; CPNQLEL; -.
DR   OrthoDB; 1480223at2; -.
DR   UniPathway; UPA01068; UER00298.
DR   Proteomes; UP000002431; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008478; F:pyridoxal kinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0009443; P:pyridoxal 5'-phosphate salvage; IEA:UniProtKB-UniRule.
DR   CDD; cd01173; pyridoxal_pyridoxamine_kinase; 1.
DR   Gene3D; 3.40.1190.20; -; 1.
DR   HAMAP; MF_01639; PdxY; 1.
DR   InterPro; IPR013749; PM/HMP-P_kinase-1.
DR   InterPro; IPR004625; PyrdxlKinase.
DR   InterPro; IPR023685; Pyridoxal_kinase_PdxY.
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   3: Inferred from homology;
KW   ATP-binding; Kinase; Magnesium; Nucleotide-binding; Reference proteome;
KW   Transferase.
FT   CHAIN           1..299
FT                   /note="Pyridoxal kinase PdxY"
FT                   /id="PRO_0000269804"
FT   BINDING         18
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01639"
FT   BINDING         120
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01639"
FT   BINDING         157
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01639"
FT   BINDING         235
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01639"
SQ   SEQUENCE   299 AA;  32161 MW;  B3D35D68E6F983C1 CRC64;
     MTSSSAPVLP QNILSIQSWV SYGHVGNAAA LFPLQRLGFE VWTINTVQFS NHTGYGEWTG
     SVFPPELVAD LLNGIAARGV LPTCAAVLSG YMGSEGTVSA VVEAVRRVRE ANPAALYCCD
     PVMGDVGRGV FVRPELPDLI RTQAVPEADI VTPNQFELEL LTGRRVTRLQ EALDASRMLR
     GTLREGGPRL VVVTSLVRED APQGVIETLA VTGEGAWLCR TPLLPLDPPR NGTGDAIAAL
     FLGHYLRTQD AGTALSLSMS ALFAVLDLTH RVGTREIQLV AAQDEYTRPS RVFEAERVA