ID   B1C8U6_9FIRM            Unreviewed;       277 AA.
AC   B1C8U6;
DT   29-APR-2008, integrated into UniProtKB/TrEMBL.
DT   29-APR-2008, 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=ANASTE_01714 {ECO:0000313|EMBL:EDS72006.1};
OS   Anaerofustis stercorihominis DSM 17244.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Eubacteriaceae;
OC   Anaerofustis.
OX   NCBI_TaxID=445971 {ECO:0000313|EMBL:EDS72006.1, ECO:0000313|Proteomes:UP000005178};
RN   [1] {ECO:0000313|EMBL:EDS72006.1, ECO:0000313|Proteomes:UP000005178}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17244 {ECO:0000313|EMBL:EDS72006.1,
RC   ECO:0000313|Proteomes:UP000005178};
RA   Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA   Gordon J.;
RT   "Draft genome sequence of Anaerofustis stercorihominis (DSM 17244).";
RL   Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EDS72006.1, ECO:0000313|Proteomes:UP000005178}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17244 {ECO:0000313|EMBL:EDS72006.1,
RC   ECO:0000313|Proteomes:UP000005178};
RA   Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA   Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL   Submitted (JAN-2008) 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:EDS72006.1}.
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DR   EMBL; ABIL02000006; EDS72006.1; -; Genomic_DNA.
DR   RefSeq; WP_007050476.1; NZ_DS560019.1.
DR   AlphaFoldDB; B1C8U6; -.
DR   STRING; 445971.ANASTE_01714; -.
DR   eggNOG; COG2240; Bacteria.
DR   HOGENOM; CLU_046496_2_0_9; -.
DR   OrthoDB; 9800808at2; -.
DR   Proteomes; UP000005178; 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:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EDS72006.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005178};
KW   Transferase {ECO:0000313|EMBL:EDS72006.1}.
FT   DOMAIN          72..258
FT                   /note="Pyridoxamine kinase/Phosphomethylpyrimidine kinase"
FT                   /evidence="ECO:0000259|Pfam:PF08543"
SQ   SEQUENCE   277 AA;  31183 MW;  825E3D09DA6C8B58 CRC64;
     MDKNKDILLI NDLPGVGKVA LSAMMPIVSS MGFRVHNLPT AIVSNTLDYG LFEILDMSEY
     MKKTIGIWDE LGFKFDAICT GFINSDEQVG LIEKIISDNK ENDPLVMVDP IMGDDGNLYL
     GLSKNVVKNM REMCALADIV TPNFTEASFI LYDEMKKDEL DSHEIKEYID EFRKLGSKSV
     VITSVKNKES GNYSIEGYSY SEDEYFSVPY DYINVRFPGT GDVFSGVMVG KVLEGKTLKE
     ACKIASDFVR KAMEKDEKIV VDKRKGMNIE DNLQFLK
//