PDXK_ECO81
ID PDXK_ECO81 Reviewed; 283 AA.
AC B7MY71;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 74.
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}; OrderedLocusNames=ECED1_2862;
OS Escherichia coli O81 (strain ED1a).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=585397;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ED1a;
RX PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT "Organised genome dynamics in the Escherichia coli species results in
RT highly diverse adaptive paths.";
RL PLoS Genet. 5:E1000344-E1000344(2009).
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;
CC Evidence={ECO:0000255|HAMAP-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; CU928162; CAR09037.2; -; Genomic_DNA.
DR RefSeq; WP_000096640.1; NC_011745.1.
DR AlphaFoldDB; B7MY71; -.
DR SMR; B7MY71; -.
DR EnsemblBacteria; CAR09037; CAR09037; ECED1_2862.
DR KEGG; ecq:ECED1_2862; -.
DR HOGENOM; CLU_046496_3_1_6; -.
DR OMA; HVITHAR; -.
DR UniPathway; UPA01068; UER00298.
DR UniPathway; UPA01068; UER00299.
DR UniPathway; UPA01068; UER00300.
DR Proteomes; UP000000748; 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 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; Metal-binding; Nucleotide-binding;
KW Transferase; Zinc.
FT CHAIN 1..283
FT /note="Pyridoxine/pyridoxal/pyridoxamine kinase"
FT /id="PRO_1000186803"
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; 30848 MW; 303C85C8DEDA369D CRC64;
MSSLLLFNDK SRALQADIVA VQSQVVYGSV GNSIAVPAIK QNGLNVFAVP TVLLSNTPHY
DTFYGGAIPD EWFSGYLRAL QERDALRQLR AVTTGYMGTA SQIKILAEWL TALRKDHPDL
LIMVDPVIGD IDSGIYVKPD LPEAYRQYLL PLAQGITPNI FELEILTGKD CRDLDSAIAA
AKSLLSDTLK WVVITSASGN EENQEMQVVV VSADSVNVIS HSRVKTDLKG TGDLFCAQLI
SGLLKGKALT DAVHRAGLRV LEVMRYTQQH ESDELILPPL AEA
