ID V5EZU3_KALBG Unreviewed; 729 AA.
AC V5EZU3;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=thiamine diphosphokinase {ECO:0000256|ARBA:ARBA00013245};
DE EC=2.7.6.2 {ECO:0000256|ARBA:ARBA00013245};
GN ORFNames=PSEUBRA_SCAF10g05439 {ECO:0000313|EMBL:EST09473.1};
OS Kalmanozyma brasiliensis (strain GHG001) (Yeast) (Pseudozyma brasiliensis).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Kalmanozyma.
OX NCBI_TaxID=1365824 {ECO:0000313|EMBL:EST09473.1, ECO:0000313|Proteomes:UP000019377};
RN [1] {ECO:0000313|Proteomes:UP000019377}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GHG001 {ECO:0000313|Proteomes:UP000019377};
RX PubMed=24356824; DOI=10.1128/genomea.00920-13;
RA Oliveira J.V.D.C., dos Santos R.A.C., Borges T.A., Riano-Pachon D.M.,
RA Goldman G.H.;
RT "Draft genome sequence of Pseudozyma brasiliensis sp. nov. strain GHG001, a
RT high producer of endo-1,4-xylanase isolated from an insect pest of
RT sugarcane.";
RL Genome Announc. 1:E0092013-E0092013(2013).
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DR EMBL; KI545852; EST09473.1; -; Genomic_DNA.
DR RefSeq; XP_016294462.1; XM_016434009.1.
DR AlphaFoldDB; V5EZU3; -.
DR STRING; 1365824.V5EZU3; -.
DR eggNOG; KOG2121; Eukaryota.
DR eggNOG; KOG3153; Eukaryota.
DR HOGENOM; CLU_330127_0_0_1; -.
DR OMA; HESTNIA; -.
DR OrthoDB; 5471005at2759; -.
DR Proteomes; UP000019377; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; 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:InterPro.
DR GO; GO:0006772; P:thiamine metabolic process; IEA:InterPro.
DR CDD; cd07995; TPK; 1.
DR Gene3D; 3.60.15.10; Ribonuclease Z/Hydroxyacylglutathione hydrolase-like; 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; IPR001279; Metallo-B-lactamas.
DR InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR InterPro; IPR006282; Thi_PPkinase.
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 PANTHER; PTHR46018; ZINC PHOSPHODIESTERASE ELAC PROTEIN 1; 1.
DR PANTHER; PTHR46018:SF2; ZINC PHOSPHODIESTERASE ELAC PROTEIN 1; 1.
DR Pfam; PF00753; Lactamase_B; 1.
DR Pfam; PF04265; TPK_B1_binding; 1.
DR Pfam; PF04263; TPK_catalytic; 1.
DR SMART; SM00849; Lactamase_B; 1.
DR SMART; SM00983; TPK_B1_binding; 1.
DR SUPFAM; SSF56281; Metallo-hydrolase/oxidoreductase; 1.
DR SUPFAM; SSF63999; Thiamin pyrophosphokinase, catalytic domain; 1.
DR SUPFAM; SSF63862; Thiamin pyrophosphokinase, substrate-binding domain; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000019377};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 22..266
FT /note="Metallo-beta-lactamase"
FT /evidence="ECO:0000259|SMART:SM00849"
FT DOMAIN 645..715
FT /note="Thiamin pyrophosphokinase thiamin-binding"
FT /evidence="ECO:0000259|SMART:SM00983"
FT REGION 157..184
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 329..348
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 418..449
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 162..184
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 329..344
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 418..436
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 729 AA; 79439 MW; E17C0D9A8936B887 CRC64;
MVAPRMSIKF LGTSSMPNST RNYSSLLFKL DNHTVMVDCG EGTQRQLRSR YVGVDERLAN
LKTILITHLH ADHVLGLVPL LMSMMGPSGV SAPAEPSTPR VEIYGPPGLR ALIRTTLSLC
YSQLSGKYVV HEFVWPSPAQ MPEDAPHALK DQPERTIPNL PLYEGESSSG RNLDMDPRSS
SWPNFLSLKP SAQGPARRPV HLPDGTVLHP PPLNLPGRKV TVMGDTSDGT GGFTETQLRA
GHGLPALAYE SDVLVHESTN IALPPHLNKN GKADSLEEVA AKALSRGHSV PQVAGRFAAL
VNAKRLILNH FSTKYPSPPH YLLDTAGTHA ESSNVQSQGQ PAPQDRQLGD PERKALIMKE
FEVQAYRAWQ QAPRTGTQLE TYSAFDGFHF EVPARPQVDE TAPVRDGGNV FARPWEQDSS
AEHDNGLKRK HVEQGSAVAD ETSTWDPSPF LMPPSSSEKP SYAMVLLNSP IDPRQVGHFR
RLWDSASLRL CADGAANRLL DCFGAAAFEQ QNSPSSVHLP NAILGDLDSI RPDTQKFFES
KGVAVHTRPS QYATDLQKTI QEIEDQEAGA GDGQEHTLII FGGLAGRLDQ SVHTLHVLWQ
LAPGTEHLGS VLDPDNPTDR GNQLKKRQRT FAIGDGSVAW LLPKGKHVLK MAREVMGKTC
GILPLGVGNS GAKVTTKGLE WNLEGDSTTL GGFLSTSNHL HDKDGVVQVE NDEPVYWTVE
LRPDGDCSL
//
