ID A0A2V5IPH1_9EURO Unreviewed; 370 AA.
AC A0A2V5IPH1;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 13-SEP-2023, entry version 11.
DE RecName: Full=pyridoxal kinase {ECO:0000256|ARBA:ARBA00012104};
DE EC=2.7.1.35 {ECO:0000256|ARBA:ARBA00012104};
DE Flags: Fragment;
GN ORFNames=BP00DRAFT_383193 {ECO:0000313|EMBL:PYI25827.1};
OS Aspergillus indologenus CBS 114.80.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1450541 {ECO:0000313|EMBL:PYI25827.1, ECO:0000313|Proteomes:UP000248817};
RN [1] {ECO:0000313|EMBL:PYI25827.1, ECO:0000313|Proteomes:UP000248817}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 114.80 {ECO:0000313|EMBL:PYI25827.1,
RC ECO:0000313|Proteomes:UP000248817};
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 (FEB-2018) 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; KZ825623; PYI25827.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2V5IPH1; -.
DR Proteomes; UP000248817; 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:PYI25827.1};
KW Transferase {ECO:0000313|EMBL:PYI25827.1}.
FT DOMAIN 118..274
FT /note="Pyridoxamine kinase/Phosphomethylpyrimidine kinase"
FT /evidence="ECO:0000259|Pfam:PF08543"
FT NON_TER 370
FT /evidence="ECO:0000313|EMBL:PYI25827.1"
SQ SEQUENCE 370 AA; 40143 MW; 3CCCE72D31777176 CRC64;
MVADLFVPET RVLAVASHVV YGYVGNKMAS VVMQLLGCDV AALNTVHFSN HTGYRQFKGT
RATAEEITAL YEGLTQSHLT DFDVMLSGYA PSAAAVEAVG AIGMDLQRKA EKSPGSFFWV
LDPVMGDQGR LYVNNDVVPA YKEMIHHADL ILPNQFEAEV LSGVKITSLS TLAEAITAIH
ATYKVPHVII TSVQISNLSD SSSASSTASF ANTLTVIGST TRSDGSPRLF RVDVPALDCY
FSGTGDMFAA LTVARLREAV FAADPALRTT KSWVSPDDVP ATALPLAQST VKVLASMHCI
LEKTMEARNA ELQAEVVSNG DVLNEEERKK QEHLRESKAA EVRVVRHVQF LREPTVEFPA
QEWSKDDLPA
//
