ID B5RUF0_DEBHA Unreviewed; 302 AA.
AC B5RUF0;
DT 04-NOV-2008, integrated into UniProtKB/TrEMBL.
DT 04-NOV-2008, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE RecName: Full=pyridoxal kinase {ECO:0000256|ARBA:ARBA00012104};
DE EC=2.7.1.35 {ECO:0000256|ARBA:ARBA00012104};
GN OrderedLocusNames=DEHA2F12342g {ECO:0000313|EMBL:CAR66328.1};
OS Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX NCBI_TaxID=284592 {ECO:0000313|EMBL:CAR66328.1, ECO:0000313|Proteomes:UP000000599};
RN [1] {ECO:0000313|EMBL:CAR66328.1, ECO:0000313|Proteomes:UP000000599}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC
RC 2968 {ECO:0000313|Proteomes:UP000000599};
RX PubMed=15229592; DOI=10.1038/nature02579;
RG Genolevures;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.F., Straub M.L.,
RA Suleau A., Swennene D., Tekaia F., Wesolowski-Louvel M., Westhof E.,
RA Wirth B., Zeniou-Meyer M., Zivanovic I., Bolotin-Fukuhara M., Thierry A.,
RA Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA Wincker P., Souciet J.L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
CC -!- SIMILARITY: Belongs to the pyridoxine kinase family.
CC {ECO:0000256|ARBA:ARBA00008805}.
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DR EMBL; CR382138; CAR66328.1; -; Genomic_DNA.
DR RefSeq; XP_002770803.1; XM_002770757.1.
DR AlphaFoldDB; B5RUF0; -.
DR STRING; 284592.B5RUF0; -.
DR GeneID; 8998953; -.
DR KEGG; dha:DEHA2F12342g; -.
DR VEuPathDB; FungiDB:DEHA2F12342g; -.
DR eggNOG; KOG2599; Eukaryota.
DR HOGENOM; CLU_046496_1_0_1; -.
DR InParanoid; B5RUF0; -.
DR OMA; FLWICDP; -.
DR OrthoDB; 5472295at2759; -.
DR Proteomes; UP000000599; Chromosome F.
DR GO; GO:0008478; F:pyridoxal kinase activity; IEA:UniProtKB-EC.
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 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000000599}.
FT DOMAIN 66..235
FT /note="Pyridoxamine kinase/Phosphomethylpyrimidine kinase"
FT /evidence="ECO:0000259|Pfam:PF08543"
SQ SEQUENCE 302 AA; 33461 MW; 6177D57716B59CA0 CRC64;
MSVKTVLSIS SHVVHGYVGN RSTVFPLQYS GWDVDAIDTT NFSNHPGYGT FQGKASSPEL
VESLFEGISD IIDADWDYNM ILTGYAPNEA VLKVIHQKVD DIFQKATTRP VWVLDPVLGD
NGKLYVSEKV VPVYRAILSS GNVTVVTPNQ FEFELLSDTP ISNWESLATA FDRFHQHYDV
PYVVLSSVIL DNLMYSVGFT AAENKIFYIP IDKIDCNFNG CGDLFAALLA NAFYSNDSVL
TPRVLSDVVV KLTKILNHSY DCEKQITGSN DIKLVKDIRI VSSRHVLLSD NGNDLADAAT
YL
//
