PDXK_TREPA
ID PDXK_TREPA Reviewed; 269 AA.
AC O83153;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 113.
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=TP_0115;
OS Treponema pallidum (strain Nichols).
OC Bacteria; Spirochaetes; Spirochaetales; Treponemataceae; Treponema.
OX NCBI_TaxID=243276;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nichols;
RX PubMed=9665876; DOI=10.1126/science.281.5375.375;
RA Fraser C.M., Norris S.J., Weinstock G.M., White O., Sutton G.G.,
RA Dodson R.J., Gwinn M.L., Hickey E.K., Clayton R.A., Ketchum K.A.,
RA Sodergren E., Hardham J.M., McLeod M.P., Salzberg S.L., Peterson J.D.,
RA Khalak H.G., Richardson D.L., Howell J.K., Chidambaram M., Utterback T.R.,
RA McDonald L.A., Artiach P., Bowman C., Cotton M.D., Fujii C., Garland S.A.,
RA Hatch B., Horst K., Roberts K.M., Sandusky M., Weidman J.F., Smith H.O.,
RA Venter J.C.;
RT "Complete genome sequence of Treponema pallidum, the syphilis spirochete.";
RL Science 281:375-388(1998).
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; AE000520; AAC65105.1; -; Genomic_DNA.
DR PIR; B71365; B71365.
DR RefSeq; WP_010881564.1; NC_021490.2.
DR AlphaFoldDB; O83153; -.
DR SMR; O83153; -.
DR IntAct; O83153; 2.
DR STRING; 243276.TPANIC_0115; -.
DR EnsemblBacteria; AAC65105; AAC65105; TP_0115.
DR GeneID; 57878658; -.
DR KEGG; tpa:TP_0115; -.
DR eggNOG; COG0351; Bacteria.
DR HOGENOM; CLU_020520_1_0_12; -.
DR OMA; KDEVGYA; -.
DR OrthoDB; 461201at2; -.
DR Proteomes; UP000000811; 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..269
FT /note="Putative pyridoxine kinase"
FT /id="PRO_0000192037"
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 189
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 205
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 214
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 239
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 269 AA; 28943 MW; F6E71F29650993D1 CRC64;
MVKLLSIGGS DASGGAGIEA DLKTFQEYGA FGVATLTAIV TMDPSRNWSH RVHSLEEDCV
RDQLETAFAG VGVSAVKSGM LASVHAIECV AEYLERFAVA AYVFDPVMVC KGSGDALHRE
LNELMIQKLL PRATVVTPNL FETAQIAGIS VPRTVDEMKE GARLIHERGA SHVFVKGGGR
LPGCKHALDV FYDGKTFHLV EDELVQSGWN HGAGCTVSAA ITAGLGRGLT AYDAILSAKR
FVTTGLRHGF QVNQWVGTGN LSKWRDRFH
