ID   A0A165HBT2_9BASI        Unreviewed;       368 AA.
AC   A0A165HBT2;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   RecName: Full=pyridoxal kinase {ECO:0000256|ARBA:ARBA00012104};
DE            EC=2.7.1.35 {ECO:0000256|ARBA:ARBA00012104};
GN   ORFNames=CALCODRAFT_214432 {ECO:0000313|EMBL:KZT59093.1};
OS   Calocera cornea HHB12733.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Dacrymycetes;
OC   Dacrymycetales; Dacrymycetaceae; Calocera.
OX   NCBI_TaxID=1353952 {ECO:0000313|EMBL:KZT59093.1, ECO:0000313|Proteomes:UP000076842};
RN   [1] {ECO:0000313|EMBL:KZT59093.1, ECO:0000313|Proteomes:UP000076842}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HHB12733 {ECO:0000313|EMBL:KZT59093.1,
RC   ECO:0000313|Proteomes:UP000076842};
RX   PubMed=26659563; DOI=10.1093/molbev/msv337;
RA   Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA   Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA   Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA   Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT   "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT   Insights into the Origins of Lignocellulose Decay Capabilities.";
RL   Mol. Biol. Evol. 33:959-970(2016).
CC   -!- SIMILARITY: Belongs to the pyridoxine kinase family.
CC       {ECO:0000256|ARBA:ARBA00008805}.
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DR   EMBL; KV423944; KZT59093.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A165HBT2; -.
DR   STRING; 1353952.A0A165HBT2; -.
DR   InParanoid; A0A165HBT2; -.
DR   OrthoDB; 5472295at2759; -.
DR   Proteomes; UP000076842; 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:KZT59093.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000076842};
KW   Transferase {ECO:0000313|EMBL:KZT59093.1}.
FT   DOMAIN          97..182
FT                   /note="Pyridoxamine kinase/Phosphomethylpyrimidine kinase"
FT                   /evidence="ECO:0000259|Pfam:PF08543"
SQ   SEQUENCE   368 AA;  40106 MW;  4ECFAC100D46CAF6 CRC64;
     MDTHNRVLSI QSHVCSGYVG NRAATFPLQL LGYDVDVVNT VQFSNHSGYG RLKGTRTDAD
     QLASILQGLE ENGLLRMGRL LTGYVPGAPA LMVVADLARK LHARNPELIY LLDPVMGDDN
     KIYVAPECVP IYKDLLDCAT IITPNWFEVE LLTGVKLDSP AALQEALRSL HIQHGVPHVV
     ISSLLPTASV SAALPPTIRG DLQPNGVSPT SPYAGDTQLV VCSSLLPEPE RTVGNVSVVH
     VGSVKRIRGY FSGVGDLFSA LVLAHFPSPS SPPPQEPDTP LSRATAFATS SVQAILISTH
     HYVQSLPEQE RPETDPELDL RDAERRVRRM RARELRLIQG RDYILNPGQG GKGEGRMIPW
     EGFWAQHA
//