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Database: UniProt
Entry: R5CNG2_9BACT
LinkDB: R5CNG2_9BACT
Original site: R5CNG2_9BACT 
ID   R5CNG2_9BACT            Unreviewed;       272 AA.
AC   R5CNG2;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   RecName: Full=pyridoxal kinase {ECO:0000256|ARBA:ARBA00012104};
DE            EC=2.7.1.35 {ECO:0000256|ARBA:ARBA00012104};
GN   ORFNames=BN567_00082 {ECO:0000313|EMBL:CCX69485.1};
OS   Prevotella sp. CAG:255.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC   Prevotella.
OX   NCBI_TaxID=1262923 {ECO:0000313|EMBL:CCX69485.1, ECO:0000313|Proteomes:UP000017913};
RN   [1] {ECO:0000313|EMBL:CCX69485.1, ECO:0000313|Proteomes:UP000017913}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:255 {ECO:0000313|Proteomes:UP000017913};
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:CCX69485.1}.
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DR   EMBL; CAWV010000128; CCX69485.1; -; Genomic_DNA.
DR   RefSeq; WP_021853378.1; NZ_HF986758.1.
DR   AlphaFoldDB; R5CNG2; -.
DR   Proteomes; UP000017913; 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:CCX69485.1};
KW   Transferase {ECO:0000313|EMBL:CCX69485.1}.
FT   DOMAIN          72..253
FT                   /note="Pyridoxamine kinase/Phosphomethylpyrimidine kinase"
FT                   /evidence="ECO:0000259|Pfam:PF08543"
SQ   SEQUENCE   272 AA;  29995 MW;  4A9CE3B0C6CDB7CA CRC64;
     MKKKQILLIN DMAGYGKVAT AAMLPILSYM GHPTYNLPTA LVSNTLDYGK FNILETTEYI
     KGVFPVWREL GFSFDAIATG FMASETQARI IAAYCREQAE NGTVVYVDPI MGDEGKLYNG
     VTDEAIKSMR EMVSVAHLVF PNYTEACYLT DSQYDAAGVT AEGARRLLDS LLKLGTKSAL
     ITSIRVDGQP SVVGYNHVNG EYFTQPYTEI PVHFPGTGDI FSAVLIGYLL GGKELKPSTR
     KAMDVVYKLI DLNKDNTDKN RGIPLEKYLD VL
//
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