ID   E5VH29_9FIRM            Unreviewed;       290 AA.
AC   E5VH29;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   27-MAR-2024, entry version 52.
DE   RecName: Full=pyridoxal kinase {ECO:0000256|ARBA:ARBA00012104};
DE            EC=2.7.1.35 {ECO:0000256|ARBA:ARBA00012104};
GN   ORFNames=HMPREF0996_00357 {ECO:0000313|EMBL:EFV17864.1};
OS   Lachnospiraceae bacterium 5_1_63FAA.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX   NCBI_TaxID=658089 {ECO:0000313|EMBL:EFV17864.1, ECO:0000313|Proteomes:UP000005278};
RN   [1] {ECO:0000313|EMBL:EFV17864.1, ECO:0000313|Proteomes:UP000005278}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=5_1_63FAA {ECO:0000313|EMBL:EFV17864.1,
RC   ECO:0000313|Proteomes:UP000005278};
RG   The Broad Institute Genome Sequencing Platform;
RA   Ward D., Earl A., Feldgarden M., Young S.K., Gargeya S., Zeng Q.,
RA   Alvarado L., Berlin A., Bochicchio J., Chapman S.B., Chen Z., Freedman E.,
RA   Gellesch M., Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D.,
RA   Howarth C., Mehta T., Neiman D., Pearson M., Roberts A., Saif S., Shea T.,
RA   Shenoy N., Sisk P., Stolte C., Sykes S., White J., Yandava C.,
RA   Allen-Vercoe E., Ambrose C., Strauss J., Daigneault M., Haas B.,
RA   Nusbaum C., Birren B.;
RT   "The Genome Sequence of Lachnospiraceae bacterium strain 5_1_63FAA.";
RL   Submitted (OCT-2010) 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:EFV17864.1}.
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DR   EMBL; ACTS01000006; EFV17864.1; -; Genomic_DNA.
DR   AlphaFoldDB; E5VH29; -.
DR   HOGENOM; CLU_046496_2_0_9; -.
DR   Proteomes; UP000005278; 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:EFV17864.1};
KW   Transferase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EFV17864.1}.
FT   DOMAIN          29..260
FT                   /note="Pyridoxamine kinase/Phosphomethylpyrimidine kinase"
FT                   /evidence="ECO:0000259|Pfam:PF08543"
SQ   SEQUENCE   290 AA;  32329 MW;  184E486A2BD7D325 CRC64;
     MKHSVKRVAA IHDLSGFGRA SLTAIIPILS SMGVQVCPLP TAILSNHTGG FDTFSFVDFT
     DHMQDYIDHW KELNIDFDCI YSGFLGSERQ IEIVSGFIDD FGTEDNMVVI DPVLGDNGNL
     YSTMDQGLVE GMKRLVTKAD IITPNFTEVS LLLGEEYKQT TTDEEIKEWV KRLSDMGPDI
     IVVTSVPDKE KDKDSNVIAY DRTCNTYWKI KCRYIPTFYP GTGDAYTSVM IGSLLDGDSL
     PIALDKGVQF ITQAIKASYG FDYPNREGVL LERVLEVLKM PVVLGGYEMI
//