GenomeNet

Database: UniProt
Entry: N0AX80_9BACI
LinkDB: N0AX80_9BACI
Original site: N0AX80_9BACI 
ID   N0AX80_9BACI            Unreviewed;       214 AA.
AC   N0AX80;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   24-JAN-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=B1NLA3E_06360 {ECO:0000313|EMBL:AGK53036.1};
OS   Bacillus sp. 1NLA3E.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=666686 {ECO:0000313|EMBL:AGK53036.1, ECO:0000313|Proteomes:UP000013300};
RN   [1] {ECO:0000313|EMBL:AGK53036.1, ECO:0000313|Proteomes:UP000013300}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1NLA3E {ECO:0000313|EMBL:AGK53036.1};
RX   PubMed=23833140;
RA   Venkatramanan R., Prakash O., Woyke T., Chain P., Goodwin L.A., Watson D.,
RA   Brooks S., Kostka J.E., Green S.J.;
RT   "Genome sequences for three denitrifying bacterial strains isolated from a
RT   uranium- and nitrate-contaminated subsurface environment.";
RL   Genome Announc. 1:e00449-13(2013).
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP005586; AGK53036.1; -; Genomic_DNA.
DR   RefSeq; WP_015593096.1; NC_021171.1.
DR   AlphaFoldDB; N0AX80; -.
DR   STRING; 666686.B1NLA3E_06360; -.
DR   KEGG; baci:B1NLA3E_06360; -.
DR   eggNOG; COG1564; Bacteria.
DR   HOGENOM; CLU_044237_1_0_9; -.
DR   OrthoDB; 9804377at2; -.
DR   Proteomes; UP000013300; Chromosome.
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:InterPro.
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   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   NCBIfam; TIGR01378; thi_PPkinase; 1.
DR   PANTHER; PTHR41299; THIAMINE PYROPHOSPHOKINASE; 1.
DR   PANTHER; PTHR41299:SF1; THIAMINE PYROPHOSPHOKINASE; 1.
DR   Pfam; PF04265; TPK_B1_binding; 1.
DR   Pfam; PF04263; TPK_catalytic; 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   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:AGK53036.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000013300};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          143..208
FT                   /note="Thiamin pyrophosphokinase thiamin-binding"
FT                   /evidence="ECO:0000259|SMART:SM00983"
SQ   SEQUENCE   214 AA;  23956 MW;  F3782BDCD8D38324 CRC64;
     MIVNIVGGGP AELLPDLRQY DQENCVWVGV DRGVSILLEK GIIPALGFGD FDSVSEDEWR
     EIERKVKGLK KFLPEKDEPD MELALNWGIE QGASEIRIFG GTGGRLDHFL ANVQLLLKPI
     IQASQTVVMI VDQKNQLFLK QEGIHPIHRM PKKKYISFIP ITNVENLSLI GFKYPLTNRH
     IPLGSTLCIS NELNKDSGTF SFTKGILLVI RSCD
//
DBGET integrated database retrieval system