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Database: UniProt
Entry: B6QMN7_TALMQ
LinkDB: B6QMN7_TALMQ
Original site: B6QMN7_TALMQ 
ID   B6QMN7_TALMQ            Unreviewed;       362 AA.
AC   B6QMN7;
DT   16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT   16-DEC-2008, sequence version 1.
DT   13-SEP-2023, entry version 57.
DE   RecName: Full=pyridoxal kinase {ECO:0000256|ARBA:ARBA00012104};
DE            EC=2.7.1.35 {ECO:0000256|ARBA:ARBA00012104};
GN   ORFNames=PMAA_051040 {ECO:0000313|EMBL:EEA21293.1};
OS   Talaromyces marneffei (strain ATCC 18224 / CBS 334.59 / QM 7333)
OS   (Penicillium marneffei).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC   Talaromyces sect. Talaromyces.
OX   NCBI_TaxID=441960 {ECO:0000313|EMBL:EEA21293.1, ECO:0000313|Proteomes:UP000001294};
RN   [1] {ECO:0000313|Proteomes:UP000001294}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 18224 / CBS 334.59 / QM 7333
RC   {ECO:0000313|Proteomes:UP000001294};
RX   PubMed=25676766; DOI=10.1128/genomea.01559-14;
RA   Nierman W.C., Fedorova-Abrams N.D., Andrianopoulos A.;
RT   "Genome sequence of the AIDS-associated pathogen Penicillium marneffei
RT   (ATCC18224) and its near taxonomic relative Talaromyces stipitatus
RT   (ATCC10500).";
RL   Genome Announc. 3:E0155914-E0155914(2015).
CC   -!- SIMILARITY: Belongs to the pyridoxine kinase family.
CC       {ECO:0000256|ARBA:ARBA00008805}.
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DR   EMBL; DS995903; EEA21293.1; -; Genomic_DNA.
DR   RefSeq; XP_002149902.1; XM_002149866.1.
DR   AlphaFoldDB; B6QMN7; -.
DR   STRING; 441960.B6QMN7; -.
DR   VEuPathDB; FungiDB:PMAA_051040; -.
DR   HOGENOM; CLU_046496_0_0_1; -.
DR   OrthoDB; 5472295at2759; -.
DR   PhylomeDB; B6QMN7; -.
DR   Proteomes; UP000001294; 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:EEA21293.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001294};
KW   Transferase {ECO:0000313|EMBL:EEA21293.1}.
FT   DOMAIN          121..254
FT                   /note="Pyridoxamine kinase/Phosphomethylpyrimidine kinase"
FT                   /evidence="ECO:0000259|Pfam:PF08543"
SQ   SEQUENCE   362 AA;  39569 MW;  C7605997885C6FC2 CRC64;
     MALSQEENTV PETKVLAIAS HVCYGFVGNT MATFVMQSLG CEVAAINTVH YSNHTGYRQV
     KGTKTTAEEI RTLYEGLTQS YLTDFDVLLS GYAPTAAVVE AVGDIAQDLK RRAEGKPGSF
     FWILDPVMGD LGRLYVAEDV VPAYKKTVHH ADLILPNQFE TEILSGIKIS NTTDLANAIT
     IIHKTYGVPH IIVTSVQLSN LGSSTPSGLM TVIGSTVRSD GSPRLFHVDI PALECNFNGT
     GDMFAALTVA RLREAVYATG PTLRNTKSWV SPDDVSPTEL PLAKSTEKVL SSMHSILLKT
     MESREVELAA TANTIDPTGL TEEQLQFREH LRRTKAAEVR VIRHADYLRN PVGMFKAQAW
     VE
//
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