ID   PDXY_GRABC              Reviewed;         286 AA.
AC   Q0BSF0;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 79.
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};
GN   OrderedLocusNames=GbCGDNIH1_1354;
OS   Granulibacter bethesdensis (strain ATCC BAA-1260 / CGDNIH1).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Granulibacter.
OX   NCBI_TaxID=391165;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1260 / CGDNIH1;
RX   PubMed=17827295; DOI=10.1128/jb.00793-07;
RA   Greenberg D.E., Porcella S.F., Zelazny A.M., Virtaneva K., Sturdevant D.E.,
RA   Kupko J.J. III, Barbian K.D., Babar A., Dorward D.W., Holland S.M.;
RT   "Genome sequence analysis of the emerging human pathogenic acetic acid
RT   bacterium Granulibacter bethesdensis.";
RL   J. Bacteriol. 189:8727-8736(2007).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABI62252.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000394; ABI62252.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_025318908.1; NC_008343.2.
DR   AlphaFoldDB; Q0BSF0; -.
DR   SMR; Q0BSF0; -.
DR   STRING; 391165.GbCGDNIH1_1354; -.
DR   EnsemblBacteria; ABI62252; ABI62252; GbCGDNIH1_1354.
DR   KEGG; gbe:GbCGDNIH1_1354; -.
DR   eggNOG; COG2240; Bacteria.
DR   HOGENOM; CLU_046496_3_1_5; -.
DR   UniPathway; UPA01068; UER00298.
DR   Proteomes; UP000001963; 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..286
FT                   /note="Pyridoxal kinase PdxY"
FT                   /id="PRO_0000269811"
FT   BINDING         8
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01639"
FT   BINDING         110
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01639"
FT   BINDING         147
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01639"
FT   BINDING         223
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01639"
SQ   SEQUENCE   286 AA;  30628 MW;  83674D0AC0B48A01 CRC64;
     MNILSIQSWV CYGHVGNASA VFPLQLLGAE VWAVNTVQFS NHTGYGDWTG QVFGGDDIAA
     LMKGIADRGV LPRCDAVLSG YMGSDAIGGA ILDAVASVRA ANPEALYCCD PVIGDTGRGI
     FVRPGLPELF RDRAVPTANI LTPNQFELEW LTGHHCRTLA DARAAVKVLA ESMIRQGPRI
     ILVTSLHVAE TPSGSLDMLV YENGRFYLLR TPLLPVSING AGDAIAALFL FHRLDTGDAR
     QALEKAASSV YGLLKRTAEA GSMEILTVAA RQEFLTPSTC FYAQIC