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Database: UniProt
Entry: R6Y3Y4_9FIRM
LinkDB: R6Y3Y4_9FIRM
Original site: R6Y3Y4_9FIRM 
ID   R6Y3Y4_9FIRM            Unreviewed;       289 AA.
AC   R6Y3Y4;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, 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};
GN   ORFNames=BN815_01893 {ECO:0000313|EMBL:CDD30688.1};
OS   Firmicutes bacterium CAG:94.
OC   Bacteria; Bacillota.
OX   NCBI_TaxID=1262989 {ECO:0000313|EMBL:CDD30688.1, ECO:0000313|Proteomes:UP000018237};
RN   [1] {ECO:0000313|EMBL:CDD30688.1, ECO:0000313|Proteomes:UP000018237}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:94 {ECO:0000313|Proteomes:UP000018237};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
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:CDD30688.1}.
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DR   EMBL; CBGU010000307; CDD30688.1; -; Genomic_DNA.
DR   AlphaFoldDB; R6Y3Y4; -.
DR   Proteomes; UP000018237; Unassembled WGS sequence.
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; 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   Kinase {ECO:0000313|EMBL:CDD30688.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018237};
KW   Transferase {ECO:0000313|EMBL:CDD30688.1}.
FT   DOMAIN          75..259
FT                   /note="Pyridoxamine kinase/Phosphomethylpyrimidine kinase"
FT                   /evidence="ECO:0000259|Pfam:PF08543"
SQ   SEQUENCE   289 AA;  31406 MW;  4CC1D30289A609F6 CRC64;
     MNYKEMSCLA IHDISGVGKC SLTVALPVLS CCGVETSVLP TAVLSTHTGG FTGFTYRDLT
     GDILPMARHW KSLGCRFQAL YTGFLGSEAQ IGLVEEMFDW FGGEDTLILV DPVMGDGGKL
     YQTYTPEMAS GMARLCGRAD IVVPNMTEAC HLLGRPYNPG PYTQGEIAEI LQGLCAMGPK
     MAVLTGVWLQ EGALGTACYD SQVGEAKLFL TDRIEGFYHG TGDLFASALL GGLLNGAPLE
     EACALATEFT WRTIETTFEK SPDHRFGPKF ECHLPWLGEK MEELRKNHP
//
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