ID   A0A0A7FUL1_9CLOT        Unreviewed;       274 AA.
AC   A0A0A7FUL1;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   RecName: Full=pyridoxal kinase {ECO:0000256|ARBA:ARBA00012104};
DE            EC=2.7.1.35 {ECO:0000256|ARBA:ARBA00012104};
GN   ORFNames=U729_2694 {ECO:0000313|EMBL:AIY82640.1};
OS   Clostridium baratii str. Sullivan.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1415775 {ECO:0000313|EMBL:AIY82640.1, ECO:0000313|Proteomes:UP000030635};
RN   [1] {ECO:0000313|EMBL:AIY82640.1, ECO:0000313|Proteomes:UP000030635}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sullivan {ECO:0000313|EMBL:AIY82640.1};
RX   PubMed=25489752; DOI=10.1016/j.meegid.2014.12.002;
RA   Smith T.J., Hill K.K., Xie G., Foley B.T., Williamson C.H., Foster J.T.,
RA   Johnson S.L., Chertkov O., Teshima H., Gibbons H.S., Johnsky L.A.,
RA   Karavis M.A., Smith L.A.;
RT   "Genomic sequences of six botulinum neurotoxin-producing strains
RT   representing three clostridial species illustrate the mobility and
RT   diversity of botulinum neurotoxin genes.";
RL   Infect. Genet. Evol. 30:102-113(2014).
CC   -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004948}.
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DR   EMBL; CP006905; AIY82640.1; -; Genomic_DNA.
DR   RefSeq; WP_039315908.1; NZ_CP006905.1.
DR   AlphaFoldDB; A0A0A7FUL1; -.
DR   STRING; 1561.NPD11_334; -.
DR   KEGG; cbv:U729_2694; -.
DR   eggNOG; COG2240; Bacteria.
DR   HOGENOM; CLU_046496_2_0_9; -.
DR   OrthoDB; 9800808at2; -.
DR   Proteomes; UP000030635; 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   PANTHER; PTHR20858:SF17; HYDROXYMETHYLPYRIMIDINE_PHOSPHOMETHYLPYRIMIDINE KINASE THI20-RELATED; 1.
DR   PANTHER; PTHR20858; PHOSPHOMETHYLPYRIMIDINE KINASE; 1.
DR   Pfam; PF08543; Phos_pyr_kin; 1.
DR   SUPFAM; SSF53613; Ribokinase-like; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:AIY82640.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030635};
KW   Transferase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:AIY82640.1}.
FT   DOMAIN          73..257
FT                   /note="Pyridoxamine kinase/Phosphomethylpyrimidine kinase"
FT                   /evidence="ECO:0000259|Pfam:PF08543"
SQ   SEQUENCE   274 AA;  31208 MW;  E5C3CF2F5DFCD62D CRC64;
     MISQKRVVVI NDLSGLGKCS LTVSISILSA LNIQPCPLPT AILSNQTQFN EYSFYDLTNN
     MKDYIKIWEK QQEKFDAIYT GFLGSYNQID IILEFIKKQR DTLIIVDPVM GDNGEIYETY
     NKDMCNKMKE LVSLSYIVTP NITEACILAD EKLDIKNLTN DDLKRLGTKI SNLGPKYVII
     TGIINKNKIS NVLYDKEKEE ISIVTTNFNN ISYSGTGDIF ASMLTALILN GNSVYKSMEF
     TTNFISKAIQ YTNKFNIDPN YGIYYEKFLR EVII
//