ID   J7VDS9_BACCE            Unreviewed;       274 AA.
AC   J7VDS9;
DT   31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2012, sequence version 1.
DT   24-JAN-2024, entry version 36.
DE   RecName: Full=pyridoxal kinase {ECO:0000256|ARBA:ARBA00012104};
DE            EC=2.7.1.35 {ECO:0000256|ARBA:ARBA00012104};
DE   AltName: Full=PN/PL/PM kinase {ECO:0000256|ARBA:ARBA00042348};
DE   AltName: Full=Pyridoxal kinase {ECO:0000256|ARBA:ARBA00042396};
DE   AltName: Full=Pyridoxamine kinase {ECO:0000256|ARBA:ARBA00042307};
DE   AltName: Full=Vitamin B6 kinase {ECO:0000256|ARBA:ARBA00042531};
GN   ORFNames=IC3_04473 {ECO:0000313|EMBL:EJP86330.1};
OS   Bacillus cereus VD142.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=718224 {ECO:0000313|EMBL:EJP86330.1, ECO:0000313|Proteomes:UP000006969};
RN   [1] {ECO:0000313|EMBL:EJP86330.1, ECO:0000313|Proteomes:UP000006969}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VD142 {ECO:0000313|EMBL:EJP86330.1,
RC   ECO:0000313|Proteomes:UP000006969};
RG   The Broad Institute Genome Sequencing Platform;
RG   The Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Feldgarden M., Van der Auwera G.A., Mahillon J., Duprez V., Timmery S.,
RA   Mattelet C., Dierick K., Sun M., Yu Z., Zhu L., Hu X., Shank E.B.,
RA   Swiecicka I., Hansen B.M., Andrup L., Walker B., Young S.K., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Dewar J., Goldberg J., Griggs A.,
RA   Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C.,
RA   Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA   Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Bacillus cereus VD142.";
RL   Submitted (JAN-2013) to the EMBL/GenBank/DDBJ databases.
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; Evidence={ECO:0000256|ARBA:ARBA00036247};
CC   -!- SIMILARITY: Belongs to the ThiD family.
CC       {ECO:0000256|ARBA:ARBA00009879}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EJP86330.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AHCL02000027; EJP86330.1; -; Genomic_DNA.
DR   RefSeq; WP_002089861.1; NZ_KE150047.1.
DR   AlphaFoldDB; J7VDS9; -.
DR   PATRIC; fig|718224.3.peg.4582; -.
DR   HOGENOM; CLU_020520_0_0_9; -.
DR   Proteomes; UP000006969; Unassembled WGS sequence.
DR   GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:InterPro.
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; IPR004399; HMP/HMP-P_kinase_dom.
DR   InterPro; IPR013749; PM/HMP-P_kinase-1.
DR   InterPro; IPR029056; Ribokinase-like.
DR   NCBIfam; TIGR00097; HMP-P_kinase; 1.
DR   PANTHER; PTHR20858; PHOSPHOMETHYLPYRIMIDINE KINASE; 1.
DR   PANTHER; PTHR20858:SF19; PYRIDOXINE KINASE; 1.
DR   Pfam; PF08543; Phos_pyr_kin; 1.
DR   SUPFAM; SSF53613; Ribokinase-like; 1.
PE   3: Inferred from homology;
KW   Kinase {ECO:0000313|EMBL:EJP86330.1};
KW   Transferase {ECO:0000313|EMBL:EJP86330.1}.
FT   DOMAIN          13..260
FT                   /note="Pyridoxamine kinase/Phosphomethylpyrimidine kinase"
FT                   /evidence="ECO:0000259|Pfam:PF08543"
SQ   SEQUENCE   274 AA;  29301 MW;  F7F45D82141EED1E CRC64;
     MTLNKALTIA GSDTSGGAGI QADLKTFQEL GVYGMTSLTT IVTMDPHNGW AHNVFPIPAS
     TLKPQLETTI EGVGVDALKT GMLGSVEIIE MVAETIEKHN FENVVVDPVM VCKGADEALH
     PETNDCLRDV LVPKALVVTP NLFEAYQLSG VKINSLEDMK EAAKKIHALG AKYVLIKGGS
     KLGTETAIDV LYDGGTFDLL ESEKIDTTNT HGAGCTYSAA ITAELAKGKT VKEAVKTAKE
     FITAAIRHSF KINEYVGPTH HGAYRKFVAP KELV
//