ID M7WX10_RHOT1 Unreviewed; 356 AA.
AC M7WX10;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE RecName: Full=pyridoxal kinase {ECO:0000256|ARBA:ARBA00012104};
DE EC=2.7.1.35 {ECO:0000256|ARBA:ARBA00012104};
GN ORFNames=RHTO_07984 {ECO:0000313|EMBL:EMS22631.1};
OS Rhodotorula toruloides (strain NP11) (Yeast) (Rhodosporidium toruloides).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX NCBI_TaxID=1130832 {ECO:0000313|EMBL:EMS22631.1, ECO:0000313|Proteomes:UP000016926};
RN [1] {ECO:0000313|EMBL:EMS22631.1, ECO:0000313|Proteomes:UP000016926}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NP11 {ECO:0000313|EMBL:EMS22631.1,
RC ECO:0000313|Proteomes:UP000016926};
RX PubMed=23047670; DOI=10.1038/ncomms2112;
RA Zhu Z., Zhang S., Liu H., Shen H., Lin X., Yang F., Zhou Y.J., Jin G.,
RA Ye M., Zou H., Zou H., Zhao Z.K.;
RT "A multi-omic map of the lipid-producing yeast Rhodosporidium toruloides.";
RL Nat. Commun. 3:1112-1112(2012).
CC -!- SIMILARITY: Belongs to the pyridoxine kinase family.
CC {ECO:0000256|ARBA:ARBA00008805}.
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DR EMBL; KB722650; EMS22631.1; -; Genomic_DNA.
DR RefSeq; XP_016273750.1; XM_016421638.1.
DR AlphaFoldDB; M7WX10; -.
DR GeneID; 27371997; -.
DR eggNOG; KOG2599; Eukaryota.
DR HOGENOM; CLU_046496_1_0_1; -.
DR OrthoDB; 5472295at2759; -.
DR Proteomes; UP000016926; 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 NCBIfam; TIGR00687; pyridox_kin; 1.
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 Kinase {ECO:0000313|EMBL:EMS22631.1};
KW Transferase {ECO:0000313|EMBL:EMS22631.1}.
FT DOMAIN 85..190
FT /note="Pyridoxamine kinase/Phosphomethylpyrimidine kinase"
FT /evidence="ECO:0000259|Pfam:PF08543"
SQ SEQUENCE 356 AA; 38519 MW; EED0889442E1C098 CRC64;
MAQANVTQEK RILSIQSHVV CGYVGNKSAS FPLQLLGWEV DAALTVSFSN HTGYGRWGGS
KFDAAHLEDV FSALDANGLL RQSHVLTGYV PGADALKVVV RAVDRLRAIN PSLVYILDPV
MGDDGRIYVS ESVIPIYKAL LPRATCATPN YFEAELLTDI KILDATSLQL ALRTFHERYR
TPNIVVSAVS LPLSELVKLG FVDAPALSTS SSTSRMLVCA GSTLLSAPGE PLKTTSFGIA
FPELAEHYEG VGDVFSALVA GRFPSASDPA FSDHPISPLA RTVELAIASL QGILAKTRQH
ALSLAKGRAD LIVPREGESA EERVRRLRTV ELRLVQSQHE ILNPDVKYRA VRFSGI
//
