ID A0A080N396_9BIFI Unreviewed; 266 AA.
AC A0A080N396;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=thiamine diphosphokinase {ECO:0000256|ARBA:ARBA00013245};
DE EC=2.7.6.2 {ECO:0000256|ARBA:ARBA00013245};
GN ORFNames=BBOMB_0774 {ECO:0000313|EMBL:KFF31421.1};
OS Bifidobacterium bombi DSM 19703.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=1341695 {ECO:0000313|EMBL:KFF31421.1, ECO:0000313|Proteomes:UP000028730};
RN [1] {ECO:0000313|EMBL:KFF31421.1, ECO:0000313|Proteomes:UP000028730}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19703 {ECO:0000313|EMBL:KFF31421.1,
RC ECO:0000313|Proteomes:UP000028730};
RX PubMed=25085493; DOI=10.1128/AEM.02308-14;
RA Milani C., Lugli G.A., Duranti S., Turroni F., Bottacini F., Mangifesta M.,
RA Sanchez B., Viappiani A., Mancabelli L., Taminiau B., Delcenserie V.,
RA Barrangou R., Margolles A., van Sinderen D., Ventura M.;
RT "Genomic encyclopedia of type strains of the genus Bifidobacterium.";
RL Appl. Environ. Microbiol. 80:6290-6302(2014).
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KFF31421.1}.
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; ATLK01000001; KFF31421.1; -; Genomic_DNA.
DR RefSeq; WP_044087129.1; NZ_JDTS01000002.1.
DR AlphaFoldDB; A0A080N396; -.
DR STRING; 1341695.BBOMB_0774; -.
DR eggNOG; COG1564; Bacteria.
DR OrthoDB; 9804377at2; -.
DR Proteomes; UP000028730; 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: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:KFF31421.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000028730};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 166..226
FT /note="Thiamin pyrophosphokinase thiamin-binding"
FT /evidence="ECO:0000259|SMART:SM00983"
FT REGION 246..266
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 266 AA; 28364 MW; EC189D33329E89A2 CRC64;
MDSNATSTSL SRDDAAEKIC VIYAAGEYYG DEPDAAHLPA HRLVVAADGG FDHACVLGVT
PDIVIGDFDS TSYADVLRRS SGATVIPLPA EHDDPDMLSA MKIGWRHGAR NFHIFGGLGH
RIDHSIANIQ MLSLLAQHNA VGFLYGNGYI TTAIRAGGLD FAARHHASGE MVSVFAYSDE
VHDVYEKGLK YELNAATFNN TSVHGVSNEF LDGRKASIGV ADGTLIVTFP SCTPLPKRIS
RLMPDKDGEA LGPLSTSISS ALAHPR
//
