ID   R5J2Z0_9BACE            Unreviewed;       290 AA.
AC   R5J2Z0;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   24-JAN-2024, entry version 40.
DE   RecName: Full=pyridoxal kinase {ECO:0000256|ARBA:ARBA00012104};
DE            EC=2.7.1.35 {ECO:0000256|ARBA:ARBA00012104};
GN   ORFNames=BN523_01773 {ECO:0000313|EMBL:CCY48933.1};
OS   Bacteroides sp. CAG:189.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=1262737 {ECO:0000313|EMBL:CCY48933.1, ECO:0000313|Proteomes:UP000018406};
RN   [1] {ECO:0000313|EMBL:CCY48933.1, ECO:0000313|Proteomes:UP000018406}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:189 {ECO:0000313|Proteomes:UP000018406};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-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:CCY48933.1}.
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DR   EMBL; CAYI010000064; CCY48933.1; -; Genomic_DNA.
DR   RefSeq; WP_007478441.1; NZ_HF991062.1.
DR   AlphaFoldDB; R5J2Z0; -.
DR   GeneID; 77204704; -.
DR   Proteomes; UP000018406; 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:0000313|EMBL:CCY48933.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018406};
KW   Transferase {ECO:0000313|EMBL:CCY48933.1}.
FT   DOMAIN          75..260
FT                   /note="Pyridoxamine kinase/Phosphomethylpyrimidine kinase"
FT                   /evidence="ECO:0000259|Pfam:PF08543"
SQ   SEQUENCE   290 AA;  32599 MW;  19EA8EDFFC12FE11 CRC64;
     MYANKVKKVV AVHDLSGVGR VSLTVVIPIL SSMGFQVCPL PTAVLSSHTQ YPNFSFLDLT
     DEMPKIISEW KKLGVQFDAF YTGYLGSPLQ IQIVTDFIDD FRQSESLVVV DPVLGDNGKL
     YANFHDSMIK EMRQLVTKAD VITPNLTELF YLLDLPYKEQ NTDEELKSYL RQLSDKGPEV
     VIITSVPVLN DIHKTSVYAY NRTGNRFWKV TCPYLPAHYP GTGDTFTSVI TGALLQGDSL
     PIALDRATQF ILQGIRATFG YEYDNREGIL LEKVLHNLDM PIQSSSYELI
//