PDXY_PSEPW
ID PDXY_PSEPW Reviewed; 290 AA.
AC B1JFM7;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 71.
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=PputW619_5135;
OS Pseudomonas putida (strain W619).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=390235;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=W619;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S.,
RA Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Kim E., Taghavi S., Vangronsveld D., van der Lelie D.,
RA Richardson P.;
RT "Complete sequence of Pseudomonas putida W619.";
RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
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 ---------------------------------------------------------------------------
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; CP000949; ACA75611.1; -; Genomic_DNA.
DR RefSeq; WP_012316887.1; NC_010501.1.
DR AlphaFoldDB; B1JFM7; -.
DR SMR; B1JFM7; -.
DR STRING; 390235.PputW619_5135; -.
DR EnsemblBacteria; ACA75611; ACA75611; PputW619_5135.
DR KEGG; ppw:PputW619_5135; -.
DR eggNOG; COG2240; Bacteria.
DR HOGENOM; CLU_046496_3_0_6; -.
DR OMA; CPNQLEL; -.
DR OrthoDB; 1480223at2; -.
DR UniPathway; UPA01068; UER00298.
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; Transferase.
FT CHAIN 1..290
FT /note="Pyridoxal kinase PdxY"
FT /id="PRO_1000186814"
FT BINDING 12
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01639"
FT BINDING 47..48
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01639"
FT BINDING 114
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01639"
FT BINDING 151
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01639"
FT BINDING 184
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01639"
FT BINDING 211..214
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01639"
FT BINDING 225
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01639"
SQ SEQUENCE 290 AA; 31961 MW; 267B5DD092481EE3 CRC64;
MKRTPHLLAI QSHVVFGHAG NSAAVFPMQR IGVNVWPLNT VQFSNHTQYG QWAGEVLAPA
QIPALVEGIS NIGELGHCDA VLSGYLGSAE QGRAILAGVE RIKAVNPKAL YLCDPVMGHA
EKGCIVPQEV SEFLLDDAVA QADILCPNQL ELDSFCGRRA QSLEDCVRMA RGLLERGPQV
VLVKHLAYPG RCEDMFEMLL VTRDHSWHLR RPLLAFPRQP VGVGDLTSGL FLARVLLGDS
WVQAFEYTAA AVHEVLLETQ ACASYELQLV RAQDRIAYPR VRFEAQRLAF
