PDXK_STAEQ
ID PDXK_STAEQ Reviewed; 276 AA.
AC Q5HRG7;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 2.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Putative pyridoxine kinase;
DE EC=2.7.1.35;
DE AltName: Full=PN/PL/PM kinase;
DE AltName: Full=Pyridoxal kinase;
DE AltName: Full=Pyridoxamine kinase;
DE AltName: Full=Vitamin B6 kinase;
GN Name=pdxK; OrderedLocusNames=SERP0226;
OS Staphylococcus epidermidis (strain ATCC 35984 / RP62A).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=176279;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35984 / RP62A;
RX PubMed=15774886; DOI=10.1128/jb.187.7.2426-2438.2005;
RA Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J.,
RA Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J.,
RA Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H.,
RA Vamathevan J.J., Khouri H., Utterback T.R., Lee C., Dimitrov G., Jiang L.,
RA Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E.,
RA Fraser C.M.;
RT "Insights on evolution of virulence and resistance from the complete genome
RT analysis of an early methicillin-resistant Staphylococcus aureus strain and
RT a biofilm-producing methicillin-resistant Staphylococcus epidermidis
RT strain.";
RL J. Bacteriol. 187:2426-2438(2005).
CC -!- FUNCTION: Phosphorylates B6 vitamers; functions in a salvage pathway.
CC Uses pyridoxal, pyridoxine, and pyridoxamine as substrates (By
CC similarity). {ECO:0000250}.
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;
CC -!- SIMILARITY: Belongs to the ThiD family. {ECO:0000305}.
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DR EMBL; CP000029; AAW53606.1; -; Genomic_DNA.
DR RefSeq; WP_032603372.1; NC_002976.3.
DR AlphaFoldDB; Q5HRG7; -.
DR SMR; Q5HRG7; -.
DR STRING; 176279.SERP0226; -.
DR EnsemblBacteria; AAW53606; AAW53606; SERP0226.
DR KEGG; ser:SERP0226; -.
DR eggNOG; COG0351; Bacteria.
DR HOGENOM; CLU_020520_0_0_9; -.
DR OMA; KDEVGYA; -.
DR OrthoDB; 461201at2; -.
DR Proteomes; UP000000531; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:InterPro.
DR GO; GO:0008478; F:pyridoxal kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro.
DR CDD; cd01169; HMPP_kinase; 1.
DR Gene3D; 3.40.1190.20; -; 1.
DR InterPro; IPR045029; HMP/HMP-P_kinase.
DR InterPro; IPR004399; HMP/HMP-P_kinase_dom.
DR InterPro; IPR013749; PM/HMP-P_kinase-1.
DR InterPro; IPR029056; Ribokinase-like.
DR PANTHER; PTHR20858; PTHR20858; 1.
DR Pfam; PF08543; Phos_pyr_kin; 1.
DR SUPFAM; SSF53613; SSF53613; 1.
DR TIGRFAMs; TIGR00097; HMP-P_kinase; 1.
PE 3: Inferred from homology;
KW ATP-binding; Kinase; Magnesium; Metal-binding; Nucleotide-binding;
KW Reference proteome; Transferase.
FT CHAIN 1..276
FT /note="Putative pyridoxine kinase"
FT /id="PRO_0000192034"
FT BINDING 139
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 142
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 176..180
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 188
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 213
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 238
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 276 AA; 29858 MW; C34AA1C9DF7D8C61 CRC64;
MALKKVLTIA GSDTSAGAGM QADLKTFQEL DVYGMVALTS IVTMDKETWS HDVTPIDMNI
FEKQLETAIS IGPNAIKTGM LGTQDIIKRA GDVFVESGAD YFVVDPVMVC KGEDEVLNPG
NTEAMIQYLL PKATVVTPNL FEAGQLSGLG KLTSIEDMKK AAQVIYDKGT PHVIIKGGKA
LDQDKSYDLY YDGQQFYQLT TDMFQQSYNH GAGCTFAAAT TAYLANGKSP KEAIIAAKAF
VASAIKNGWK MNDFVGPVDH GAYNRIEQIN VEVTEV
