UniProt functional annotation for P40191



	UniProt functional annotation for P40191

UniProt code: P40191.

Organism: Escherichia coli (strain K12).

Taxonomy: Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia.

Function: B6-vitamer kinase involved in the salvage pathway of pyridoxal 5'-phosphate (PLP). Catalyzes the phosphorylation of pyridoxine (PN), pyridoxal (PL), and pyridoxamine (PM), forming their respective 5'-phosphorylated esters, i.e. PNP, PLP and PMP. {ECO:0000269|PubMed:15249053, ECO:0000269|PubMed:9537380}.

Catalytic activity: Reaction=ATP + pyridoxal = ADP + H(+) + pyridoxal 5'-phosphate; Xref=Rhea:RHEA:10224, ChEBI:CHEBI:15378, ChEBI:CHEBI:17310, ChEBI:CHEBI:30616, ChEBI:CHEBI:456216, ChEBI:CHEBI:597326; EC=2.7.1.35; Evidence={ECO:0000269|PubMed:15249053, ECO:0000269|PubMed:9537380};

Catalytic activity: Reaction=ATP + pyridoxine = ADP + H(+) + pyridoxine 5'-phosphate; Xref=Rhea:RHEA:25108, ChEBI:CHEBI:15378, ChEBI:CHEBI:16709, ChEBI:CHEBI:30616, ChEBI:CHEBI:58589, ChEBI:CHEBI:456216; EC=2.7.1.35; Evidence={ECO:0000269|PubMed:15249053, ECO:0000269|PubMed:9537380};

Catalytic activity: Reaction=ATP + pyridoxamine = ADP + H(+) + pyridoxamine 5'-phosphate; Xref=Rhea:RHEA:25104, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57761, ChEBI:CHEBI:58451, ChEBI:CHEBI:456216; EC=2.7.1.35; Evidence={ECO:0000269|PubMed:15249053};

Cofactor: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:15249053}; Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:15249053}; Note=Can use both zinc and magnesium that is complexed with ATP. However, magnesium seems to be the preferred metal used under physiological conditions. {ECO:0000269|PubMed:15249053};

Activity regulation: Is activated by the monovalent cation potassium. {ECO:0000269|PubMed:16740960}.

Biophysicochemical properties: Kinetic parameters: KM=100 uM for pyridoxal (in the presence of MgATP, at pH 7.3 and 37 degrees Celsius) {ECO:0000269|PubMed:15249053}; KM=50 uM for pyridoxal (in the presence of MgATP, at pH 7.3 and 37 degrees Celsius) {ECO:0000269|PubMed:16740960}; KM=190 uM for pyridoxal (in the presence of ZnATP, at pH 7.3 and 37 degrees Celsius) {ECO:0000269|PubMed:15249053}; KM=25 uM for pyridoxine (in the presence of MgATP, at pH 7.3 and 37 degrees Celsius) {ECO:0000269|PubMed:15249053}; KM=30 uM for pyridoxamine (in the presence of MgATP, at pH 7.3 and 37 degrees Celsius) {ECO:0000269|PubMed:15249053}; KM=10 uM for pyridoxamine (in the presence of ZnATP, at pH 7.3 and 37 degrees Celsius) {ECO:0000269|PubMed:15249053}; KM=600 uM for MgATP (at pH 7.3 and 37 degrees Celsius) {ECO:0000269|PubMed:15249053}; KM=450 uM for MgATP (at pH 7.3 and 37 degrees Celsius) {ECO:0000269|PubMed:16740960}; KM=2100 uM for MgATP (at pH 6.1 and 37 degrees Celsius) {ECO:0000269|PubMed:15249053}; KM=70 uM for ZnATP (in the presence of pyridoxal, at pH 7.3 and 37 degrees Celsius) {ECO:0000269|PubMed:15249053}; KM=45 uM for ZnATP (in the presence of pyridoxamine, at pH 7.3 and 37 degrees Celsius) {ECO:0000269|PubMed:15249053}; Note=kcat is 140 min(-1) for the phosphorylation of PL with MgATP. kcat is 120 min(-1) for the phosphorylation of PL with ZnATP. kcat is 20 min(-1) for the phosphorylation of PN with MgATP. kcat is 40 min(- 1) for the phosphorylation of PM with MgATP. kcat is 25 min(-1) for the phosphorylation of PM with ZnATP (at pH 7.3 and 37 degrees Celsius) (PubMed:15249053). kcat is 250 min(-1) for the phosphorylation of PL with MgATP (at pH 7.3 and 37 degrees Celsius) (PubMed:16740960). {ECO:0000269|PubMed:15249053, ECO:0000269|PubMed:16740960};

Pathway: Cofactor metabolism; pyridoxal 5'-phosphate salvage; pyridoxal 5'-phosphate from pyridoxal: step 1/1. {ECO:0000269|PubMed:9537380}.

Pathway: Cofactor metabolism; pyridoxal 5'-phosphate salvage; pyridoxine 5'-phosphate from pyridoxine: step 1/1. {ECO:0000269|PubMed:9537380}.

Pathway: Cofactor metabolism; pyridoxal 5'-phosphate salvage; pyridoxamine 5'-phosphate from pyridoxamine: step 1/1. {ECO:0000305|PubMed:15249053}.

Subunit: Homodimer. {ECO:0000269|PubMed:16740960}.

Disruption phenotype: Cells lacking this gene lack pyridoxine kinase activity but still contain pyridoxal kinase activity (PubMed:8764513). Cells lacking this gene and cells lacking both pdxY and pdxK are not auxotrophs, meaning that the de novo pathway of PLP biosynthesis is functional. For PLP salvage, the pdxY single mutant can use both pyridoxine and pyridoxal, the pdxK single mutant can use pyridoxal but not pyridoxine, and the double mutant can no longer use both compounds (PubMed:9537380). {ECO:0000269|PubMed:8764513, ECO:0000269|PubMed:9537380}.

Similarity: Belongs to the pyridoxine kinase family. PdxK subfamily. {ECO:0000305}.

Annotations taken from UniProtKB at the EBI.


Organism:		Escherichia coli (strain K12).
Taxonomy:		Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia.



Function:		B6-vitamer kinase involved in the salvage pathway of pyridoxal 5'-phosphate (PLP). Catalyzes the phosphorylation of pyridoxine (PN), pyridoxal (PL), and pyridoxamine (PM), forming their respective 5'-phosphorylated esters, i.e. PNP, PLP and PMP. {ECO:0000269\|PubMed:15249053, ECO:0000269\|PubMed:9537380}.


Catalytic activity:		Reaction=ATP + pyridoxal = ADP + H(+) + pyridoxal 5'-phosphate; Xref=Rhea:RHEA:10224, ChEBI:CHEBI:15378, ChEBI:CHEBI:17310, ChEBI:CHEBI:30616, ChEBI:CHEBI:456216, ChEBI:CHEBI:597326; EC=2.7.1.35; Evidence={ECO:0000269\|PubMed:15249053, ECO:0000269\|PubMed:9537380};
Catalytic activity:		Reaction=ATP + pyridoxine = ADP + H(+) + pyridoxine 5'-phosphate; Xref=Rhea:RHEA:25108, ChEBI:CHEBI:15378, ChEBI:CHEBI:16709, ChEBI:CHEBI:30616, ChEBI:CHEBI:58589, ChEBI:CHEBI:456216; EC=2.7.1.35; Evidence={ECO:0000269\|PubMed:15249053, ECO:0000269\|PubMed:9537380};
Catalytic activity:		Reaction=ATP + pyridoxamine = ADP + H(+) + pyridoxamine 5'-phosphate; Xref=Rhea:RHEA:25104, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57761, ChEBI:CHEBI:58451, ChEBI:CHEBI:456216; EC=2.7.1.35; Evidence={ECO:0000269\|PubMed:15249053};
Cofactor:		Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269\|PubMed:15249053}; Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269\|PubMed:15249053}; Note=Can use both zinc and magnesium that is complexed with ATP. However, magnesium seems to be the preferred metal used under physiological conditions. {ECO:0000269\|PubMed:15249053};
Activity regulation:		Is activated by the monovalent cation potassium. {ECO:0000269\|PubMed:16740960}.
Biophysicochemical properties:		Kinetic parameters: KM=100 uM for pyridoxal (in the presence of MgATP, at pH 7.3 and 37 degrees Celsius) {ECO:0000269\|PubMed:15249053}; KM=50 uM for pyridoxal (in the presence of MgATP, at pH 7.3 and 37 degrees Celsius) {ECO:0000269\|PubMed:16740960}; KM=190 uM for pyridoxal (in the presence of ZnATP, at pH 7.3 and 37 degrees Celsius) {ECO:0000269\|PubMed:15249053}; KM=25 uM for pyridoxine (in the presence of MgATP, at pH 7.3 and 37 degrees Celsius) {ECO:0000269\|PubMed:15249053}; KM=30 uM for pyridoxamine (in the presence of MgATP, at pH 7.3 and 37 degrees Celsius) {ECO:0000269\|PubMed:15249053}; KM=10 uM for pyridoxamine (in the presence of ZnATP, at pH 7.3 and 37 degrees Celsius) {ECO:0000269\|PubMed:15249053}; KM=600 uM for MgATP (at pH 7.3 and 37 degrees Celsius) {ECO:0000269\|PubMed:15249053}; KM=450 uM for MgATP (at pH 7.3 and 37 degrees Celsius) {ECO:0000269\|PubMed:16740960}; KM=2100 uM for MgATP (at pH 6.1 and 37 degrees Celsius) {ECO:0000269\|PubMed:15249053}; KM=70 uM for ZnATP (in the presence of pyridoxal, at pH 7.3 and 37 degrees Celsius) {ECO:0000269\|PubMed:15249053}; KM=45 uM for ZnATP (in the presence of pyridoxamine, at pH 7.3 and 37 degrees Celsius) {ECO:0000269\|PubMed:15249053}; Note=kcat is 140 min(-1) for the phosphorylation of PL with MgATP. kcat is 120 min(-1) for the phosphorylation of PL with ZnATP. kcat is 20 min(-1) for the phosphorylation of PN with MgATP. kcat is 40 min(- 1) for the phosphorylation of PM with MgATP. kcat is 25 min(-1) for the phosphorylation of PM with ZnATP (at pH 7.3 and 37 degrees Celsius) (PubMed:15249053). kcat is 250 min(-1) for the phosphorylation of PL with MgATP (at pH 7.3 and 37 degrees Celsius) (PubMed:16740960). {ECO:0000269\|PubMed:15249053, ECO:0000269\|PubMed:16740960};
Pathway:		Cofactor metabolism; pyridoxal 5'-phosphate salvage; pyridoxal 5'-phosphate from pyridoxal: step 1/1. {ECO:0000269\|PubMed:9537380}.
Pathway:		Cofactor metabolism; pyridoxal 5'-phosphate salvage; pyridoxine 5'-phosphate from pyridoxine: step 1/1. {ECO:0000269\|PubMed:9537380}.
Pathway:		Cofactor metabolism; pyridoxal 5'-phosphate salvage; pyridoxamine 5'-phosphate from pyridoxamine: step 1/1. {ECO:0000305\|PubMed:15249053}.
Subunit:		Homodimer. {ECO:0000269\|PubMed:16740960}.
Disruption phenotype:		Cells lacking this gene lack pyridoxine kinase activity but still contain pyridoxal kinase activity (PubMed:8764513). Cells lacking this gene and cells lacking both pdxY and pdxK are not auxotrophs, meaning that the de novo pathway of PLP biosynthesis is functional. For PLP salvage, the pdxY single mutant can use both pyridoxine and pyridoxal, the pdxK single mutant can use pyridoxal but not pyridoxine, and the double mutant can no longer use both compounds (PubMed:9537380). {ECO:0000269\|PubMed:8764513, ECO:0000269\|PubMed:9537380}.
Similarity:		Belongs to the pyridoxine kinase family. PdxK subfamily. {ECO:0000305}.