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Database: UniProt
Entry: A0A0R1XLC2_9LACO
LinkDB: A0A0R1XLC2_9LACO
Original site: A0A0R1XLC2_9LACO 
ID   A0A0R1XLC2_9LACO        Unreviewed;       286 AA.
AC   A0A0R1XLC2;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 34.
DE   RecName: Full=pyridoxal kinase {ECO:0000256|ARBA:ARBA00012104};
DE            EC=2.7.1.35 {ECO:0000256|ARBA:ARBA00012104};
GN   ORFNames=FD32_GL001397 {ECO:0000313|EMBL:KRM30978.1};
OS   Limosilactobacillus panis DSM 6035.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Limosilactobacillus.
OX   NCBI_TaxID=1423782 {ECO:0000313|EMBL:KRM30978.1, ECO:0000313|Proteomes:UP000051412};
RN   [1] {ECO:0000313|EMBL:KRM30978.1, ECO:0000313|Proteomes:UP000051412}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 6035 {ECO:0000313|EMBL:KRM30978.1,
RC   ECO:0000313|Proteomes:UP000051412};
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:KRM30978.1}.
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DR   EMBL; AZGM01000003; KRM30978.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0R1XLC2; -.
DR   STRING; 1423782.FD32_GL001397; -.
DR   PATRIC; fig|1423782.4.peg.1455; -.
DR   Proteomes; UP000051412; 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:KRM30978.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051412};
KW   Transferase {ECO:0000313|EMBL:KRM30978.1}.
FT   DOMAIN          30..253
FT                   /note="Pyridoxamine kinase/Phosphomethylpyrimidine kinase"
FT                   /evidence="ECO:0000259|Pfam:PF08543"
SQ   SEQUENCE   286 AA;  31093 MW;  4523BEEA9FBBE431 CRC64;
     MAQVTVKLTL VIEDFTALGQ ISMVAATTVL QAMGRSTALL PTAVFSTQTE GFGQPVTIDT
     QQWLQRTINH WDQAGLVVNS VVIGYLGKTA LTHSVTQVLD HYQPEIRVID PVMADEGQLY
     PGLSSQLPGA LRELCKRATV ITPNWTELCL LAGEQPREFQ VGHLPTLIAQ LRAAGVSAAV
     VVTGIIRGGK VSCCLCSEED YQWYDSPHYP GHFYGSGDVF AALLCGYLAQ GCPLEGAVEK
     ASQALVVAIE ETKLLNNQDR KYGMEIQKLL AYLSREDENC ENAANH
//
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