PDXK_SALTY
ID PDXK_SALTY Reviewed; 288 AA.
AC P40192;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2002, sequence version 2.
DT 03-AUG-2022, entry version 132.
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, ECO:0000303|PubMed:27987384};
GN OrderedLocusNames=STM2435;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=LT2;
RX PubMed=7612925; DOI=10.3109/10425179509029354;
RA Titgemeyer F.M., Reizer J., Reizer A., Tang J., Parr T.R. Jr.,
RA Saier M.H. Jr.;
RT "Nucleotide sequence of the region between crr and cysM in Salmonella
RT typhimurium: five novel ORFs including one encoding a putative
RT transcriptional regulator of the phosphotransferase system.";
RL DNA Seq. 5:145-152(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [3]
RP INDUCTION.
RC STRAIN=LT2;
RX PubMed=27987384; DOI=10.1111/febs.13994;
RA Tramonti A., Milano T., Nardella C., di Salvo M.L., Pascarella S.,
RA Contestabile R.;
RT "Salmonella typhimurium PtsJ is a novel MocR-like transcriptional repressor
RT involved in regulating the vitamin B6 salvage pathway.";
RL FEBS J. 284:466-484(2017).
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 -!- INDUCTION: Is repressed by the transcriptional regulator PtsJ.
CC {ECO:0000269|PubMed:27987384}.
CC -!- SIMILARITY: Belongs to the pyridoxine kinase family. PdxK subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01638}.
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DR EMBL; U11243; AAC43343.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL21329.1; -; Genomic_DNA.
DR RefSeq; NP_461370.1; NC_003197.2.
DR RefSeq; WP_000529613.1; NC_003197.2.
DR AlphaFoldDB; P40192; -.
DR SMR; P40192; -.
DR STRING; 99287.STM2435; -.
DR PaxDb; P40192; -.
DR EnsemblBacteria; AAL21329; AAL21329; STM2435.
DR GeneID; 1253957; -.
DR KEGG; stm:STM2435; -.
DR PATRIC; fig|99287.12.peg.2573; -.
DR HOGENOM; CLU_046496_3_1_6; -.
DR OMA; HVITHAR; -.
DR PhylomeDB; P40192; -.
DR BioCyc; SENT99287:STM2435-MON; -.
DR UniPathway; UPA01068; UER00298.
DR UniPathway; UPA01068; UER00299.
DR UniPathway; UPA01068; UER00300.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008902; F:hydroxymethylpyrimidine kinase activity; IBA:GO_Central.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008478; F:pyridoxal kinase activity; IBA:GO_Central.
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; IBA:GO_Central.
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 2: Evidence at transcript level;
KW ATP-binding; Kinase; Magnesium; Metal-binding; Nucleotide-binding;
KW Reference proteome; Transferase; Zinc.
FT CHAIN 1..288
FT /note="Pyridoxine/pyridoxal/pyridoxamine kinase"
FT /id="PRO_0000213344"
FT BINDING 28
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01638"
FT BINDING 64
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01638"
FT BINDING 130
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01638"
FT BINDING 141
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
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 167
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01638"
FT BINDING 167
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01638"
FT BINDING 200
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01638"
FT BINDING 225..228
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01638"
FT BINDING 235
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01638"
FT BINDING 237
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01638"
FT CONFLICT 241
FT /note="A -> P (in Ref. 1; AAC43343)"
FT /evidence="ECO:0000305"
FT CONFLICT 283
FT /note="Missing (in Ref. 1; AAC43343)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 288 AA; 30968 MW; CF3F701FEA841F7A CRC64;
MGQESDIQSV LFDDNHRALQ TDIVAVQSQV VYGSVGNSIA VPAIKAQGLR VTAVPTVLFS
NTPHYKTFYG GIIPAEWFAG YLTALNERDA LRELKAITTG YMGSADQIVL LSKWLMAIRA
SHPEVCILVD PVIGDTDSGM YVQAEIPQAY RTHLLPQAQG LTPNVFELEM LSGKPCRTLE
EAVAAAQSLL SDTLKWVVIT SAPGESLETI TVAVVTAQVV EVFAHPRVAT ELKGTGDLFC
AELVSGIVQG KKLTTAAKDA AQRVLEVMTW TQQCGCDELI LPPAGEAR
