ID L0NKT7_9HYPH Unreviewed; 289 AA.
AC L0NKT7;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 28-JAN-2026, entry version 59.
DE RecName: Full=pyridoxal kinase {ECO:0000256|ARBA:ARBA00012104};
DE EC=2.7.1.35 {ECO:0000256|ARBA:ARBA00012104};
GN Name=pdxK {ECO:0000313|EMBL:CCF21524.1};
GN ORFNames=NT26_3802 {ECO:0000313|EMBL:CCF21524.1};
OS Pseudorhizobium banfieldiae.
OC Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
OC Pseudorhizobium.
OX NCBI_TaxID=1125847 {ECO:0000313|EMBL:CCF21524.1, ECO:0000313|Proteomes:UP000010792};
RN [1] {ECO:0000313|EMBL:CCF21524.1, ECO:0000313|Proteomes:UP000010792}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NT-26 {ECO:0000313|EMBL:CCF21524.1,
RC ECO:0000313|Proteomes:UP000010792};
RX PubMed=23589360; DOI=10.1093/gbe/evt061;
RA Andres J., Arsene-Ploetze F., Barbe V., Brochier-Armanet C.,
RA Cleiss-Arnold J., Coppee J.Y., Dillies M.A., Geist, L, Joublin A.,
RA Koechler S., Lassalle F., Marchal M., Medigue C., Muller D., Nesme X.,
RA Plewniak F., Proux C., Ramirez-Bahena M.H., Schenowitz C., Sismeiro O.,
RA Vallenet D., Santini J.M., Bertin P.N.;
RT "Life in an arsenic-containing gold mine: genome and physiology of the
RT autotrophic arsenite-oxidizing bacterium rhizobium sp. NT-26.";
RL Genome Biol. Evol. 5:934-953(2013).
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DR EMBL; FO082820; CCF21524.1; -; Genomic_DNA.
DR RefSeq; WP_052640765.1; NZ_FO082820.1.
DR AlphaFoldDB; L0NKT7; -.
DR STRING; 1125847.NT26_3802; -.
DR KEGG; rht:NT26_3802; -.
DR OrthoDB; 9800808at2; -.
DR Proteomes; UP000010792; Chromosome.
DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008478; F:pyridoxal kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0009443; P:pyridoxal 5'-phosphate salvage; IEA:InterPro.
DR CDD; cd01173; pyridoxal_pyridoxamine_kinase; 1.
DR Gene3D; 3.40.1190.20; -; 1.
DR InterPro; IPR013749; PM/HMP-P_kinase-1.
DR InterPro; IPR004625; PyrdxlKinase.
DR InterPro; IPR029056; Ribokinase-like.
DR NCBIfam; NF004398; PRK05756.1; 1.
DR NCBIfam; TIGR00687; pyridox_kin; 1.
DR PANTHER; PTHR10534; PYRIDOXAL KINASE; 1.
DR PANTHER; PTHR10534:SF2; PYRIDOXAL KINASE; 1.
DR Pfam; PF08543; Phos_pyr_kin; 1.
DR SUPFAM; SSF53613; Ribokinase-like; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:CCF21524.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000010792};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:CCF21524.1}.
FT DOMAIN 77..256
FT /note="Pyridoxamine kinase/Phosphomethylpyrimidine kinase"
FT /evidence="ECO:0000259|Pfam:PF08543"
SQ SEQUENCE 289 AA; 31125 MW; C9BFCBFA60C4823F CRC64;
MQNSGAVIVI SSHVVRGSVG NRAAVFAFET LGFPVWALPT VVLPWHPGHG PSTRLTFAAD
EFDKAIDDLI NARWLGEVSA VLTGYFANER QPKAVARLVR ALQERNPSLL YVCDPVIGDV
GGLYIPQSTA EAIRDELLPL ASVATPNRYE LAWLAGSELD SNAAIMEAAL ALGPSRMLVT
SAIPMMAGGT GNLYLTGTHA LLAEHRLIDN PPNGLGDLLS ALFLARLMTG ADEERALRLA
TASVYEILAR TAKRGSDELT LETDAASLTS PMAMVHMRRL IHPLQRVRR
//
