ID A0A5N7AMJ3_9EURO Unreviewed; 372 AA.
AC A0A5N7AMJ3;
DT 22-APR-2020, integrated into UniProtKB/TrEMBL.
DT 22-APR-2020, sequence version 1.
DT 28-JAN-2026, entry version 16.
DE RecName: Full=pyridoxal kinase {ECO:0000256|ARBA:ARBA00012104};
DE EC=2.7.1.35 {ECO:0000256|ARBA:ARBA00012104};
GN ORFNames=BDV26DRAFT_149087 {ECO:0000313|EMBL:KAE8371087.1};
OS Aspergillus bertholletiae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=1226010 {ECO:0000313|EMBL:KAE8371087.1, ECO:0000313|Proteomes:UP000326198};
RN [1] {ECO:0000313|EMBL:KAE8371087.1, ECO:0000313|Proteomes:UP000326198}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 29228 {ECO:0000313|EMBL:KAE8371087.1,
RC ECO:0000313|Proteomes:UP000326198};
RG DOE Joint Genome Institute;
RA Kjaerbolling I., Vesth T., Frisvad J.C., Nybo J.L., Theobald S.,
RA Kildgaard S., Isbrandt T., Kuo A., Sato A., Lyhne E.K., Kogle M.E.,
RA Wiebenga A., Kun R.S., Lubbers R.J., Makela M.R., Barry K., Chovatia M.,
RA Clum A., Daum C., Haridas S., He G., LaButti K., Lipzen A., Mondo S.,
RA Riley R., Salamov A., Simmons B.A., Magnuson J.K., Henrissat B.,
RA Mortensen U.H., Larsen T.O., Devries R.P., Grigoriev I.V., Machida M.,
RA Baker S.E., Andersen M.R.;
RT "Friends and foes A comparative genomics studyof 23 Aspergillus species
RT from section Flavi.";
RL Submitted (APR-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the pyridoxine kinase family.
CC {ECO:0000256|ARBA:ARBA00008805}.
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DR EMBL; ML736484; KAE8371087.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5N7AMJ3; -.
DR OrthoDB; 2104723at2759; -.
DR Proteomes; UP000326198; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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 FunFam; 3.40.1190.20:FF:000070; Putative pyridoxal kinase C6F6.11c; 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 ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KAE8371087.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000326198};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 118..257
FT /note="Pyridoxamine kinase/Phosphomethylpyrimidine kinase"
FT /evidence="ECO:0000259|Pfam:PF08543"
SQ SEQUENCE 372 AA; 40813 MW; ED8D29E96F100841 CRC64;
MSADSLVPET RVLAIASHVV YGYVGNKMAT LVMQLLGCDV ASLNTVHFSN HTGYRQFKGT
RATAEQITEL YEGLCQSHLT DFDVMLSGYA PSAAAVEAVG AIGMDLQCKA EKSPGSFFWV
LDPVMGDQGR LYVNNDVVPA YKKLIRHADL ILPNQFEAET LSGIKITSLS TLAEAITAIH
ATYNTPHIII TSVDLSKFTQ SSAQPTTTPS DSLTVIGSTT RSDGSPRLFR IDVPALDCYF
SGTGDMFAAL IVARLREAVF AADPQLRTTK SWVSPDEVQA TDLPLARATV QVLASMHSVL
EKTMEARDAE LRAADIRGDE LLSDEERLKR QHLRKSKAAE VRLVRNVQYL RNPTVVFHAQ
DWKKEDLPAR SQ
//
