ID A0A317WS19_9EURO Unreviewed; 365 AA.
AC A0A317WS19;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 13-SEP-2023, entry version 14.
DE RecName: Full=pyridoxal kinase {ECO:0000256|ARBA:ARBA00012104};
DE EC=2.7.1.35 {ECO:0000256|ARBA:ARBA00012104};
GN ORFNames=BO70DRAFT_311989 {ECO:0000313|EMBL:PWY86970.1};
OS Aspergillus heteromorphus CBS 117.55.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1448321 {ECO:0000313|EMBL:PWY86970.1, ECO:0000313|Proteomes:UP000247233};
RN [1] {ECO:0000313|EMBL:PWY86970.1, ECO:0000313|Proteomes:UP000247233}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 117.55 {ECO:0000313|EMBL:PWY86970.1,
RC ECO:0000313|Proteomes:UP000247233};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De Vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
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:PWY86970.1}.
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DR EMBL; MSFL01000007; PWY86970.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A317WS19; -.
DR STRING; 1448321.A0A317WS19; -.
DR VEuPathDB; FungiDB:BO70DRAFT_311989; -.
DR OrthoDB; 5472295at2759; -.
DR Proteomes; UP000247233; 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:PWY86970.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000247233};
KW Transferase {ECO:0000313|EMBL:PWY86970.1}.
FT DOMAIN 118..247
FT /note="Pyridoxamine kinase/Phosphomethylpyrimidine kinase"
FT /evidence="ECO:0000259|Pfam:PF08543"
FT REGION 302..331
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 365 AA; 39882 MW; 1EFDC9BB7C86608A CRC64;
MSTDLLVPET RVLAVASHVV YGYVGNKMAS LVMQLLGCDV AALNTVHFSN HTGYRQFKGT
RATAEEITAL YEGLTQSNLT DFDVMLSGYA PSAAAVEAVG AIGMDLQRKA EKNPGSFFWV
LDPVMGDQGR LYVNDDVVPA YKNIIRHADL ILPNQFEAEV LSNTKITSLS TLASAITAIH
NTYKIPHVII TSVSLPTLTP NTLTIIGSTT RSDGSARLFR VDVPALDCYF SGTGDMFAAL
TVARLREAVF TDPDPQLRNT KSWVSPDEVP ATELPLARST VKVLASMHSV LERTLEVRDR
EMKSGKPVVD GVDGVDGEDS AERKKSEHLR ESKAAEVRVV RYGGLLRQPE VEFQATEWRS
EDLPV
//
