ID A0AAI9J286_BORPT Unreviewed; 284 AA. AC A0AAI9J286; DT 24-JUL-2024, integrated into UniProtKB/TrEMBL. DT 24-JUL-2024, sequence version 1. DT 02-OCT-2024, entry version 2. DE RecName: Full=Pyridoxine/pyridoxal/pyridoxamine kinase {ECO:0000256|HAMAP-Rule:MF_01638}; DE Short=PN/PL/PM kinase {ECO:0000256|HAMAP-Rule:MF_01638}; DE EC=2.7.1.35 {ECO:0000256|HAMAP-Rule:MF_01638}; DE AltName: Full=B6-vitamer kinase {ECO:0000256|HAMAP-Rule:MF_01638}; GN Name=pdxK {ECO:0000256|HAMAP-Rule:MF_01638, GN ECO:0000313|EMBL:ETH31175.1}; GN ORFNames=L566_2605 {ECO:0000313|EMBL:ETH31175.1}; OS Bordetella pertussis CHLA-26. OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; OC Alcaligenaceae; Bordetella. OX NCBI_TaxID=1331284 {ECO:0000313|EMBL:ETH31175.1, ECO:0000313|Proteomes:UP000018679}; RN [1] {ECO:0000313|EMBL:ETH31175.1, ECO:0000313|Proteomes:UP000018679} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CHLA-26 {ECO:0000313|EMBL:ETH31175.1, RC ECO:0000313|Proteomes:UP000018679}; RX PubMed=24356839; RA Harvill E.T., Goodfield L.L., Ivanov Y., Meyer J.A., Newth C., Cassiday P., RA Tondella M.L., Liao P., Zimmerman J., Meert K., Wessel D., Berger J., RA Dean J.M., Holubkov R., Burr J., Liu T., Brinkac L., Kim M., Losada L.; RT "Genome Sequences of 28 Bordetella pertussis U.S. Outbreak Strains Dating RT from 2010 to 2012."; RL Genome Announc. 1:e01075-e01013(2013). 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:0000256|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:0000256|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 Evidence={ECO:0000256|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 Evidence={ECO:0000256|HAMAP-Rule:MF_01638}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01638}; CC -!- PATHWAY: Cofactor metabolism; pyridoxal 5'-phosphate salvage; pyridoxal CC 5'-phosphate from pyridoxal: step 1/1. {ECO:0000256|HAMAP- CC Rule:MF_01638}. CC -!- PATHWAY: Cofactor metabolism; pyridoxal 5'-phosphate salvage; CC pyridoxamine 5'-phosphate from pyridoxamine: step 1/1. CC {ECO:0000256|HAMAP-Rule:MF_01638}. CC -!- PATHWAY: Cofactor metabolism; pyridoxal 5'-phosphate salvage; CC pyridoxine 5'-phosphate from pyridoxine: step 1/1. {ECO:0000256|HAMAP- CC Rule:MF_01638}. CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01638}. CC -!- SIMILARITY: Belongs to the pyridoxine kinase family. PdxK subfamily. CC {ECO:0000256|HAMAP-Rule:MF_01638}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:ETH31175.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AXSB02000022; ETH31175.1; -; Genomic_DNA. DR Proteomes; UP000018679; Unassembled WGS sequence. DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW. 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; 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 {ECO:0000256|HAMAP-Rule:MF_01638}; KW Kinase {ECO:0000256|HAMAP-Rule:MF_01638, ECO:0000313|EMBL:ETH31175.1}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_01638}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_01638}; Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01638}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_01638, ECO:0000313|EMBL:ETH31175.1}; KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_01638}. FT DOMAIN 92..273 FT /note="Pyridoxamine kinase/Phosphomethylpyrimidine kinase" FT /evidence="ECO:0000259|Pfam:PF08543" FT BINDING 24 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01638" FT BINDING 60 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01638" FT BINDING 126 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01638" FT BINDING 137 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01638" FT BINDING 158 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01638" FT BINDING 163 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01638" FT BINDING 163 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01638" FT BINDING 196 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01638" FT BINDING 223..226 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01638" FT BINDING 233 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01638" FT BINDING 235 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01638" SQ SEQUENCE 284 AA; 29574 MW; 4C4B619FC9D5DFD7 CRC64; MMKLAAPNPQ ALAPLPIDVV SIQSQVVYGQ VGNSVAVPVF NGFGLRVAAV PTVVLSNTPH YPSMHGGAVP LDWFEGYLAD LGARGALAGV RVVQLGYLGG PAQAEALGRW IAGLVAERPD LRVHIDPVIG DHDSGVYVAP GMVAAYRDHL LSLAQGLTPN GFELECLTGL PTGTMEQTIA AARTLLGGRA RWVIVTSAAP ATWPPGRVRV AVVTHDDAQV LEHAHVDTAP KGTGDMFGAA LTGHRLAGQP VAEAARRAAL QVIEALERTR EAGCGELLLA GPLR //