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
//