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Database: UniProt
Entry: A0A0R1SAM1_9LACO
LinkDB: A0A0R1SAM1_9LACO
Original site: A0A0R1SAM1_9LACO 
ID   A0A0R1SAM1_9LACO        Unreviewed;       266 AA.
AC   A0A0R1SAM1;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   RecName: Full=pyridoxal kinase {ECO:0000256|ARBA:ARBA00012104};
DE            EC=2.7.1.35 {ECO:0000256|ARBA:ARBA00012104};
GN   ORFNames=FC85_GL002949 {ECO:0000313|EMBL:KRL66103.1};
OS   Lentilactobacillus diolivorans DSM 14421.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lentilactobacillus.
OX   NCBI_TaxID=1423739 {ECO:0000313|EMBL:KRL66103.1, ECO:0000313|Proteomes:UP000052013};
RN   [1] {ECO:0000313|EMBL:KRL66103.1, ECO:0000313|Proteomes:UP000052013}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14421 {ECO:0000313|EMBL:KRL66103.1,
RC   ECO:0000313|Proteomes:UP000052013};
RX   PubMed=26415554; DOI=10.1038/ncomms9322;
RA   Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA   Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA   Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA   Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA   de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA   Zhang H., O'Toole P.W.;
RT   "Expanding the biotechnology potential of lactobacilli through comparative
RT   genomics of 213 strains and associated genera.";
RL   Nat. Commun. 6:8322-8322(2015).
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:KRL66103.1}.
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DR   EMBL; AZEY01000050; KRL66103.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0R1SAM1; -.
DR   STRING; 1423739.FC85_GL002949; -.
DR   PATRIC; fig|1423739.3.peg.3068; -.
DR   Proteomes; UP000052013; 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   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:KRL66103.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000052013};
KW   Transferase {ECO:0000313|EMBL:KRL66103.1}.
FT   DOMAIN          6..237
FT                   /note="Pyridoxamine kinase/Phosphomethylpyrimidine kinase"
FT                   /evidence="ECO:0000259|Pfam:PF08543"
SQ   SEQUENCE   266 AA;  28947 MW;  FAB296E403EE3D0D CRC64;
     MTAAISIFSG FGIQTAAIPT EILSTQSEGF GTPITTNNDD WIKKTIGHWN QITDLNLASA
     VVGYVGQPKT VKLLHDYLTT LKLKHVLVDP VMGDRGVMYD GFGDGYLDAI KQLIQAATVI
     TPNVTELQLL SGNQLTDNAS DAEVVRAIEA CRQKNKLNAR VVVTGIKRDA GIGCCFLSHG
     QLKWVSSPFV SGHFYGTGDL FSTLLCGYLN FGVSFETAVQ RSVFGVYEAV SRTGQVSENK
     RKFGLDLTKT LNDVTKFTLG KDREEI
//
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