ID D2TSF6_CITRI Unreviewed; 277 AA.
AC D2TSF6;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 72.
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:CBG89123.1};
GN OrderedLocusNames=ROD_23771 {ECO:0000313|EMBL:CBG89123.1};
OS Citrobacter rodentium (strain ICC168) (Citrobacter freundii biotype 4280).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Citrobacter.
OX NCBI_TaxID=637910 {ECO:0000313|EMBL:CBG89123.1, ECO:0000313|Proteomes:UP000001889};
RN [1] {ECO:0000313|EMBL:CBG89123.1, ECO:0000313|Proteomes:UP000001889}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ICC168 {ECO:0000313|EMBL:CBG89123.1,
RC ECO:0000313|Proteomes:UP000001889};
RX PubMed=19897651; DOI=10.1128/JB.01144-09;
RA Petty N.K., Bulgin R., Crepin V.F., Cerdeno-Tarraga A.M., Schroeder G.N.,
RA Quail M.A., Lennard N., Corton C., Barron A., Clark L., Toribio A.L.,
RA Parkhill J., Dougan G., Frankel G., Thomson N.R.;
RT "The Citrobacter rodentium genome sequence reveals convergent evolution
RT with human pathogenic Escherichia coli.";
RL J. Bacteriol. 192:525-538(2010).
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DR EMBL; FN543502; CBG89123.1; -; Genomic_DNA.
DR AlphaFoldDB; D2TSF6; -.
DR STRING; 637910.ROD_23771; -.
DR KEGG; cro:ROD_23771; -.
DR eggNOG; COG2240; Bacteria.
DR HOGENOM; CLU_046496_3_1_6; -.
DR Proteomes; UP000001889; Chromosome.
DR GO; GO:0008478; F:pyridoxal kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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; TIGR00687; pyridox_kin; 1.
DR PANTHER; PTHR10534; PYRIDOXAL KINASE; 1.
DR PANTHER; PTHR10534:SF15; PYRIDOXINE_PYRIDOXAL_PYRIDOXAMINE KINASE; 1.
DR Pfam; PF08543; Phos_pyr_kin; 1.
DR SUPFAM; SSF53613; Ribokinase-like; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:CBG89123.1};
KW Transferase {ECO:0000313|EMBL:CBG89123.1}.
FT DOMAIN 64..260
FT /note="Pyridoxamine kinase/Phosphomethylpyrimidine kinase"
FT /evidence="ECO:0000259|Pfam:PF08543"
SQ SEQUENCE 277 AA; 29818 MW; 8B6C649AF023D527 CRC64;
MLFDDKHRAL QTDIVAVQSQ VVYGSVGNSI AVPAIKAKGL RVTAVPTVLF SNTPHYETFY
GGVIPADWFS GYLRALSERD ALRELKAVTT GYMGSAQQIA LLAQWLTTVQ KRHPQATIVV
DPVIGDIDSG MYVKAEIPEA YRQHLLPLAQ GLTPNVFELE MLSGKPCGTL EEAVIAARSL
LTETLKWVVI TSAPGQTDDA INVAVVTADS LEVIAHPRVE TDLKGTGDLF CAELTCGLVL
GHPLAKATRL AAERVLAVMN WTQQCGCDEL ILPPAGE
//
