ID B8PAE5_POSPM Unreviewed; 233 AA.
AC B8PAE5;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 13-SEP-2023, entry version 58.
DE RecName: Full=thiamine diphosphokinase {ECO:0000256|ARBA:ARBA00013245};
DE EC=2.7.6.2 {ECO:0000256|ARBA:ARBA00013245};
DE Flags: Fragment;
GN ORFNames=POSPLDRAFT_36180 {ECO:0000313|EMBL:EED82138.1};
OS Postia placenta (strain ATCC 44394 / Madison 698-R) (Brown rot fungus)
OS (Poria monticola).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Postiaceae; Postia.
OX NCBI_TaxID=561896 {ECO:0000313|Proteomes:UP000001743};
RN [1] {ECO:0000313|EMBL:EED82138.1, ECO:0000313|Proteomes:UP000001743}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 44394 / Madison 698-R {ECO:0000313|Proteomes:UP000001743};
RX PubMed=19193860; DOI=10.1073/pnas.0809575106;
RA Martinez D., Challacombe J., Morgenstern I., Hibbett D., Schmoll M.,
RA Kubicek C.P., Ferreira P., Ruiz-Duenas F.J., Martinez A.T., Kersten P.,
RA Hammel K.E., Vanden Wymelenberg A., Gaskell J., Lindquist E., Sabat G.,
RA Splinter BonDurant S., Larrondo L.F., Canessa P., Vicuna R., Yadav J.,
RA Doddapaneni H., Subramanian V., Pisabarro A.G., Lavin J.L., Oguiza J.A.,
RA Master E., Henrissat B., Coutinho P.M., Harris P., Magnuson J.K.,
RA Baker S.E., Bruno K., Kenealy W., Hoegger P.J., Kuees U., Ramaiya P.,
RA Lucas S., Salamov A., Shapiro H., Tu H., Chee C.L., Misra M., Xie G.,
RA Teter S., Yaver D., James T., Mokrejs M., Pospisek M., Grigoriev I.V.,
RA Brettin T., Rokhsar D., Berka R., Cullen D.;
RT "Genome, transcriptome, and secretome analysis of wood decay fungus Postia
RT placenta supports unique mechanisms of lignocellulose conversion.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:1954-1959(2009).
CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis;
CC thiamine diphosphate from thiamine: step 1/1.
CC {ECO:0000256|ARBA:ARBA00005078}.
CC -!- SIMILARITY: Belongs to the thiamine pyrophosphokinase family.
CC {ECO:0000256|ARBA:ARBA00006785}.
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DR EMBL; EQ966293; EED82138.1; -; Genomic_DNA.
DR RefSeq; XP_002472642.1; XM_002472597.1.
DR AlphaFoldDB; B8PAE5; -.
DR STRING; 561896.B8PAE5; -.
DR KEGG; ppl:POSPLDRAFT_36180; -.
DR HOGENOM; CLU_044237_0_0_1; -.
DR InParanoid; B8PAE5; -.
DR OMA; HHLYMMT; -.
DR OrthoDB; 102116at2759; -.
DR UniPathway; UPA00060; UER00597.
DR Proteomes; UP000001743; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0030975; F:thiamine binding; IEA:InterPro.
DR GO; GO:0004788; F:thiamine diphosphokinase activity; IEA:UniProtKB-EC.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006772; P:thiamine metabolic process; IEA:InterPro.
DR CDD; cd07995; TPK; 1.
DR Gene3D; 3.40.50.10240; Thiamin pyrophosphokinase, catalytic domain; 1.
DR Gene3D; 2.60.120.320; Thiamin pyrophosphokinase, thiamin-binding domain; 1.
DR InterPro; IPR006282; Thi_PPkinase.
DR InterPro; IPR016966; Thiamin_pyrophosphokinase_euk.
DR InterPro; IPR007373; Thiamin_PyroPKinase_B1-bd.
DR InterPro; IPR036371; TPK_B1-bd_sf.
DR InterPro; IPR007371; TPK_catalytic.
DR InterPro; IPR036759; TPK_catalytic_sf.
DR NCBIfam; TIGR01378; thi_PPkinase; 1.
DR PANTHER; PTHR13622; THIAMIN PYROPHOSPHOKINASE; 1.
DR PANTHER; PTHR13622:SF8; THIAMIN PYROPHOSPHOKINASE 1; 1.
DR Pfam; PF04265; TPK_B1_binding; 1.
DR Pfam; PF04263; TPK_catalytic; 1.
DR PIRSF; PIRSF031057; Thiamin_pyrophosphokinase; 1.
DR SMART; SM00983; TPK_B1_binding; 1.
DR SUPFAM; SSF63999; Thiamin pyrophosphokinase, catalytic domain; 1.
DR SUPFAM; SSF63862; Thiamin pyrophosphokinase, substrate-binding domain; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000001743};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 158..226
FT /note="Thiamin pyrophosphokinase thiamin-binding"
FT /evidence="ECO:0000259|SMART:SM00983"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EED82138.1"
FT NON_TER 233
FT /evidence="ECO:0000313|EMBL:EED82138.1"
SQ SEQUENCE 233 AA; 26291 MW; 0D251AB9077DF4DC CRC64;
ADHRYVLIIL NQPFSYPLLK RLWNGCSLRY CADGGANRLH DPRHPHPAAR LARYLPDLIK
GDLDSLRSGV REYYTSKNIT VVEDHDQYST DLMKCISALA EKEKAEGMED SNLVILGGLS
GRLDQTVHTL SFLHKLRKGK RRVFAITDDS VAWVLPEGEH RIHINHAMLG PTCGLLPLGV
DSTILSTTGL RWNLTDTESS FDGLVSTSNH LVPEEEIVWV KTSRPIWWTA ELR
//
