ID   PDXY_SHISS              Reviewed;         287 AA.
AC   Q3Z1Z2;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 3.
DT   03-AUG-2022, entry version 91.
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=SSON_1520;
OS   Shigella sonnei (strain Ss046).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=300269;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ss046;
RX   PubMed=16275786; DOI=10.1093/nar/gki954;
RA   Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X., Wang J.,
RA   Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S., Nie H., Peng J.,
RA   Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y., Qiang B., Hou Y., Yu J.,
RA   Jin Q.;
RT   "Genome dynamics and diversity of Shigella species, the etiologic agents of
RT   bacillary dysentery.";
RL   Nucleic Acids Res. 33:6445-6458(2005).
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; CP000038; AAZ88220.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q3Z1Z2; -.
DR   SMR; Q3Z1Z2; -.
DR   EnsemblBacteria; AAZ88220; AAZ88220; SSON_1520.
DR   KEGG; ssn:SSON_1520; -.
DR   HOGENOM; CLU_046496_3_0_6; -.
DR   OMA; CPNQLEL; -.
DR   UniPathway; UPA01068; UER00298.
DR   Proteomes; UP000002529; 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; Transferase.
FT   CHAIN           1..287
FT                   /note="Pyridoxal kinase PdxY"
FT                   /id="PRO_0000269833"
FT   BINDING         10
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01639"
FT   BINDING         45..46
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01639"
FT   BINDING         112
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01639"
FT   BINDING         144
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01639"
FT   BINDING         149
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01639"
FT   BINDING         182
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01639"
FT   BINDING         209..212
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01639"
FT   BINDING         224
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01639"
SQ   SEQUENCE   287 AA;  31350 MW;  CD1316499BDCDFA1 CRC64;
     MMKNILAIQS HVVYGHAGNS AAEFPMRRLG ANVWPLNTVQ FSNHTQYGKW TGCVMPPSHL
     TEIVQGIAAI DKLHTCDAVL SGYLGSAEQG EHILGIVRQV KAANPQAKYF CDPVMGHPEK
     GCIVAPGVAE FHVRHGLPAS DIIAPNLVEL EILCEHAVNN VEEAVLAARE LIAQGPQIVL
     VKHLARAGYS RDRFEMLLVT ADEAWHISRP LVDFGMRQPV GVGDVTSGLL LVKLLQGATL
     QEVLEHVTAA VYEIMVTTKA MQEYELQVVA AQDRIAKPEH YFSATKL