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Database: UniProt
Entry: L1QBY3_9CLOT
LinkDB: L1QBY3_9CLOT
Original site: L1QBY3_9CLOT 
ID   L1QBY3_9CLOT            Unreviewed;       276 AA.
AC   L1QBY3;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 47.
DE   RecName: Full=pyridoxal kinase {ECO:0000256|ARBA:ARBA00012104};
DE            EC=2.7.1.35 {ECO:0000256|ARBA:ARBA00012104};
GN   ORFNames=HMPREF0216_02448 {ECO:0000313|EMBL:EKY25456.1};
OS   Clostridium celatum DSM 1785.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=545697 {ECO:0000313|EMBL:EKY25456.1, ECO:0000313|Proteomes:UP000010420};
RN   [1] {ECO:0000313|EMBL:EKY25456.1, ECO:0000313|Proteomes:UP000010420}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 1785 {ECO:0000313|EMBL:EKY25456.1,
RC   ECO:0000313|Proteomes:UP000010420};
RA   Weinstock G., Sodergren E., Lobos E.A., Fulton L., Fulton R., Courtney L.,
RA   Fronick C., O'Laughlin M., Godfrey J., Wilson R.M., Miner T., Farmer C.,
RA   Delehaunty K., Cordes M., Minx P., Tomlinson C., Chen J., Wollam A.,
RA   Pepin K.H., Bhonagiri V., Zhang X., Suruliraj S., Warren W., Mitreva M.,
RA   Mardis E.R., Wilson R.K.;
RL   Submitted (MAY-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:EKY25456.1}.
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DR   EMBL; AMEZ01000069; EKY25456.1; -; Genomic_DNA.
DR   RefSeq; WP_005214334.1; NZ_KB291659.1.
DR   AlphaFoldDB; L1QBY3; -.
DR   STRING; 545697.HMPREF0216_02448; -.
DR   PATRIC; fig|545697.3.peg.2409; -.
DR   eggNOG; COG2240; Bacteria.
DR   HOGENOM; CLU_046496_2_0_9; -.
DR   OrthoDB; 9800808at2; -.
DR   Proteomes; UP000010420; 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:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EKY25456.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010420};
KW   Transferase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EKY25456.1}.
FT   DOMAIN          76..258
FT                   /note="Pyridoxamine kinase/Phosphomethylpyrimidine kinase"
FT                   /evidence="ECO:0000259|Pfam:PF08543"
SQ   SEQUENCE   276 AA;  31280 MW;  12AF3E69EEB4FB33 CRC64;
     MREFNQKKIA LINDVTGFGR CSIAVALPII SILKVQCCFI PRAILSNHTG FDNFFFEDYT
     PKMKEYINNW EKLNLNFDGI CTGFLGSKEQ IEIVVEFLEK FKTENNIVIV DPVMGDYGKL
     YSTYTDEMCK KMQDLIKYAD VVTPNLTELC KLLDVPYPNE TPNHEELYIL CKNLSNKGPN
     KIVITGLQRG GCIENFIFES DKPYKVIKVE KIGDDRPGTG DVFSSIVSGS IVKNESFSVC
     VEKATSFISK SLKFTNDLNL PPNYGVCFEE FLSELK
//
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