ID K9FV75_PEND2 Unreviewed; 361 AA.
AC K9FV75;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=pyridoxal kinase {ECO:0000256|ARBA:ARBA00012104};
DE EC=2.7.1.35 {ECO:0000256|ARBA:ARBA00012104};
GN ORFNames=PDIG_37140 {ECO:0000313|EMBL:EKV13525.1};
OS Penicillium digitatum (strain PHI26 / CECT 20796) (Green mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=1170229 {ECO:0000313|EMBL:EKV13525.1, ECO:0000313|Proteomes:UP000009882};
RN [1] {ECO:0000313|Proteomes:UP000009882}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PHI26 / CECT 20796 {ECO:0000313|Proteomes:UP000009882};
RX PubMed=23171342; DOI=10.1186/1471-2164-13-646;
RA Marcet-Houben M., Ballester A.-R., de la Fuente B., Harries E.,
RA Marcos J.F., Gonzalez-Candelas L., Gabaldon T.;
RT "Genome sequence of the necrotrophic fungus Penicillium digitatum, the main
RT postharvest pathogen of citrus.";
RL BMC Genomics 13:646-646(2012).
CC -!- SIMILARITY: Belongs to the pyridoxine kinase family.
CC {ECO:0000256|ARBA:ARBA00008805}.
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:EKV13525.1}.
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DR EMBL; AKCT01000159; EKV13525.1; -; Genomic_DNA.
DR AlphaFoldDB; K9FV75; -.
DR STRING; 1170229.K9FV75; -.
DR eggNOG; KOG2599; Eukaryota.
DR HOGENOM; CLU_046496_0_0_1; -.
DR InParanoid; K9FV75; -.
DR OMA; GLCQSHL; -.
DR OrthoDB; 5472295at2759; -.
DR Proteomes; UP000009882; 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 3: Inferred from homology;
KW Kinase {ECO:0000313|EMBL:EKV13525.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000009882};
KW Transferase {ECO:0000313|EMBL:EKV13525.1}.
FT DOMAIN 108..263
FT /note="Pyridoxamine kinase/Phosphomethylpyrimidine kinase"
FT /evidence="ECO:0000259|Pfam:PF08543"
SQ SEQUENCE 361 AA; 39243 MW; 989A37FAB29C7B52 CRC64;
MATFVMQSLG CEVAALNTVH FSTLQPGRLN PNPDSQAIAG NHTGYRQFKG TRATAQEISD
LYQGLCQSNL TDFDVMLSGY APSAAAVESV GTIGIDLQEK AEKKPGSFFW VLDPVMGDQG
RLYVNDDVVP AYKKIIPFAD LILPNQFEAE TLSGVKITSL ETLASAVTAI HRLYSVPHVI
ITSVQLFKLS QSGSTPPPPE NFLTVIGSTT RSDGSPRLFR VDVPALDCFF SGTGDMFAAL
TVARLSEAVS AVDGLRTTKS WVSPDDVAAT DLPLASSTVK VLSSMHSVLE RTLESRDAEL
AVAVPALDGK ASAVELQKRD YLRRTKAAEV RLVRNTRVLR DPKILFEVQD WKKEDLPKDL
R
//
