ID   PDXK_ECO24              Reviewed;         283 AA.
AC   A7ZPL9;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   27-MAR-2024, entry version 89.
DE   RecName: Full=Pyridoxine/pyridoxal/pyridoxamine kinase {ECO:0000255|HAMAP-Rule:MF_01638};
DE            Short=PN/PL/PM kinase {ECO:0000255|HAMAP-Rule:MF_01638};
DE            EC=2.7.1.35 {ECO:0000255|HAMAP-Rule:MF_01638};
DE   AltName: Full=B6-vitamer kinase {ECO:0000255|HAMAP-Rule:MF_01638};
GN   Name=pdxK {ECO:0000255|HAMAP-Rule:MF_01638};
GN   OrderedLocusNames=EcE24377A_2705;
OS   Escherichia coli O139:H28 (strain E24377A / ETEC).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=331111;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E24377A / ETEC;
RX   PubMed=18676672; DOI=10.1128/jb.00619-08;
RA   Rasko D.A., Rosovitz M.J., Myers G.S.A., Mongodin E.F., Fricke W.F.,
RA   Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R.,
RA   Henderson I.R., Sperandio V., Ravel J.;
RT   "The pangenome structure of Escherichia coli: comparative genomic analysis
RT   of E. coli commensal and pathogenic isolates.";
RL   J. Bacteriol. 190:6881-6893(2008).
CC   -!- FUNCTION: B6-vitamer kinase involved in the salvage pathway of
CC       pyridoxal 5'-phosphate (PLP). Catalyzes the phosphorylation of
CC       pyridoxine (PN), pyridoxal (PL), and pyridoxamine (PM), forming their
CC       respective 5'-phosphorylated esters, i.e. PNP, PLP and PMP.
CC       {ECO:0000255|HAMAP-Rule:MF_01638}.
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_01638};
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:0000255|HAMAP-Rule:MF_01638};
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:0000255|HAMAP-Rule:MF_01638};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01638};
CC   -!- PATHWAY: Cofactor metabolism; pyridoxal 5'-phosphate salvage; pyridoxal
CC       5'-phosphate from pyridoxal: step 1/1. {ECO:0000255|HAMAP-
CC       Rule:MF_01638}.
CC   -!- PATHWAY: Cofactor metabolism; pyridoxal 5'-phosphate salvage;
CC       pyridoxine 5'-phosphate from pyridoxine: step 1/1. {ECO:0000255|HAMAP-
CC       Rule:MF_01638}.
CC   -!- PATHWAY: Cofactor metabolism; pyridoxal 5'-phosphate salvage;
CC       pyridoxamine 5'-phosphate from pyridoxamine: step 1/1.
CC       {ECO:0000255|HAMAP-Rule:MF_01638}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01638}.
CC   -!- SIMILARITY: Belongs to the pyridoxine kinase family. PdxK subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01638}.
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DR   EMBL; CP000800; ABV19738.1; -; Genomic_DNA.
DR   RefSeq; WP_000096660.1; NC_009801.1.
DR   AlphaFoldDB; A7ZPL9; -.
DR   SMR; A7ZPL9; -.
DR   GeneID; 75204311; -.
DR   KEGG; ecw:EcE24377A_2705; -.
DR   HOGENOM; CLU_046496_3_1_6; -.
DR   UniPathway; UPA01068; UER00298.
DR   UniPathway; UPA01068; UER00299.
DR   UniPathway; UPA01068; UER00300.
DR   Proteomes; UP000001122; 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:0008270; F:zinc ion binding; 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_01638; PdxK; 1.
DR   InterPro; IPR023479; PdxK.
DR   InterPro; IPR013749; PM/HMP-P_kinase-1.
DR   InterPro; IPR004625; PyrdxlKinase.
DR   InterPro; IPR029056; Ribokinase-like.
DR   NCBIfam; TIGR00687; pyridox_kin; 1.
DR   PANTHER; PTHR10534; PYRIDOXAL KINASE; 1.
DR   PANTHER; PTHR10534:SF15; PYRIDOXINE_PYRIDOXAL_PYRIDOXAMINE KINASE; 1.
DR   Pfam; PF08543; Phos_pyr_kin; 1.
DR   SUPFAM; SSF53613; Ribokinase-like; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Kinase; Magnesium; Metal-binding; Nucleotide-binding;
KW   Reference proteome; Transferase; Zinc.
FT   CHAIN           1..283
FT                   /note="Pyridoxine/pyridoxal/pyridoxamine kinase"
FT                   /id="PRO_1000069881"
FT   BINDING         23
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01638"
FT   BINDING         59
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01638"
FT   BINDING         125
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01638"
FT   BINDING         136
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01638"
FT   BINDING         157
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01638"
FT   BINDING         162
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01638"
FT   BINDING         162
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01638"
FT   BINDING         195
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01638"
FT   BINDING         221..224
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01638"
FT   BINDING         231
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01638"
FT   BINDING         233
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01638"
SQ   SEQUENCE   283 AA;  30860 MW;  902F8C55E5B7804B CRC64;
     MSSLLLFNDK SRALQADIVA VQSQVVYGSV GNSIAVPAIK QNGLNVFAVP TVLLSNTPHY
     DTFYGGAIPD EWFSGYLRAL QERDALRQLR AVTTGYMGTA SQIKILAEWL TALRKDHPDL
     LIMVDPVIGD IDSGIYVKPD LPEAYRQYLL PLAQGITPNI FELEILTGKN CRDLDSAIAA
     AKSLLSDTLK WVVITSASGN EENQEMQVVV VSADSVNVIS HSRVKTDLKG TGDLFCAQLI
     SGLLKGKALN DAVHRAGLRV LEVMRYTQQH ESDELILPPL AEA
//