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Database: UniProt
Entry: A0A139NPE3_9STRE
LinkDB: A0A139NPE3_9STRE
Original site: A0A139NPE3_9STRE 
ID   A0A139NPE3_9STRE        Unreviewed;       205 AA.
AC   A0A139NPE3;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   RecName: Full=thiamine diphosphokinase {ECO:0000256|ARBA:ARBA00013245};
DE            EC=2.7.6.2 {ECO:0000256|ARBA:ARBA00013245};
GN   ORFNames=STRDD13_01381 {ECO:0000313|EMBL:KXT77701.1};
OS   Streptococcus sp. DD13.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=1777881 {ECO:0000313|EMBL:KXT77701.1, ECO:0000313|Proteomes:UP000070387};
RN   [1] {ECO:0000313|EMBL:KXT77701.1, ECO:0000313|Proteomes:UP000070387}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DD13 {ECO:0000313|EMBL:KXT77701.1,
RC   ECO:0000313|Proteomes:UP000070387};
RA   Denapaite D., Rieger M., Koendgen S., Brueckner R., Ochigava I.,
RA   Kappeler P., Maetz-Rensing K., Leendertz F., Hakenbeck R.;
RT   "Highly variable Streptococcus oralis are common among viridans
RT   streptococci isolated from primates.";
RL   Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
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:KXT77701.1}.
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DR   EMBL; LQRH01000053; KXT77701.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A139NPE3; -.
DR   STRING; 1777881.STRDD13_01381; -.
DR   PATRIC; fig|1777881.3.peg.1465; -.
DR   Proteomes; UP000070387; 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; 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.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KXT77701.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000070387};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KXT77701.1}.
FT   DOMAIN          134..197
FT                   /note="Thiamin pyrophosphokinase thiamin-binding"
FT                   /evidence="ECO:0000259|SMART:SM00983"
SQ   SEQUENCE   205 AA;  22901 MW;  84B7CEA45CC0D52E CRC64;
     MAGGEVTGEV PSDADVYLGV DAGSLYLLDH RLPLDLAVGD FDSVTELGLD WIRQEAQELV
     QLPSEKNDTD LEYALKLVFH RFPTAQVSVY GCLGGRLDHT LAAVFLASEP DLAPFMGQIE
     LVSLDNRVQF RPKGTHQILR KEGMTYVSFM PADQTRVEII GAKYPLNQDN YFSKKCYSSN
     EFIGEEITIR VDQGYVVVIY SKDRS
//
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