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Database: UniProt
Entry: C7N4V7_SLAHD
LinkDB: C7N4V7_SLAHD
Original site: C7N4V7_SLAHD 
ID   C7N4V7_SLAHD            Unreviewed;       228 AA.
AC   C7N4V7;
DT   13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT   13-OCT-2009, sequence version 1.
DT   27-MAR-2024, entry version 58.
DE   RecName: Full=thiamine diphosphokinase {ECO:0000256|ARBA:ARBA00013245};
DE            EC=2.7.6.2 {ECO:0000256|ARBA:ARBA00013245};
GN   OrderedLocusNames=Shel_08960 {ECO:0000313|EMBL:ACV21942.1};
OS   Slackia heliotrinireducens (strain ATCC 29202 / DSM 20476 / NCTC 11029 /
OS   RHS 1) (Peptococcus heliotrinreducens).
OC   Bacteria; Actinomycetota; Coriobacteriia; Eggerthellales; Eggerthellaceae;
OC   Slackia.
OX   NCBI_TaxID=471855 {ECO:0000313|EMBL:ACV21942.1, ECO:0000313|Proteomes:UP000002026};
RN   [1] {ECO:0000313|EMBL:ACV21942.1, ECO:0000313|Proteomes:UP000002026}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29202 / DSM 20476 / NCTC 11029 / RHS 1
RC   {ECO:0000313|Proteomes:UP000002026};
RX   PubMed=21304663; DOI=10.4056/sigs.37633;
RA   Pukall R., Lapidus A., Nolan M., Copeland A., Glavina Del Rio T., Lucas S.,
RA   Chen F., Tice H., Cheng J.F., Chertkov O., Bruce D., Goodwin L., Kuske C.,
RA   Brettin T., Detter J.C., Han C., Pitluck S., Pati A., Mavrommatis K.,
RA   Ivanova N., Ovchinnikova G., Chen A., Palaniappan K., Schneider S.,
RA   Rohde M., Chain P., D'haeseleer P., Goker M., Bristow J., Eisen J.A.,
RA   Markowitz V., Kyrpides N.C., Klenk H.P., Hugenholtz P.;
RT   "Complete genome sequence of Slackia heliotrinireducens type strain (RHS
RT   1).";
RL   Stand. Genomic Sci. 1:234-241(2009).
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DR   EMBL; CP001684; ACV21942.1; -; Genomic_DNA.
DR   AlphaFoldDB; C7N4V7; -.
DR   STRING; 471855.Shel_08960; -.
DR   KEGG; shi:Shel_08960; -.
DR   eggNOG; COG1564; Bacteria.
DR   HOGENOM; CLU_044237_1_2_11; -.
DR   Proteomes; UP000002026; 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:InterPro.
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:ACV21942.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002026};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          150..217
FT                   /note="Thiamin pyrophosphokinase thiamin-binding"
FT                   /evidence="ECO:0000259|SMART:SM00983"
SQ   SEQUENCE   228 AA;  24316 MW;  E26CA50B0D72282E CRC64;
     MQTLPADRNH KEATNMDIAK TCAIVGASDF NAEHFLAHPF GFVIAADGGL AHLEACGAHP
     DMALGDFDSL GYVPERPVVE RHPVMKDESD LELAIDRALE FGCADIVLYG ALGGRADHTY
     ATQQTMVHAV RHGARVYAVG ADHMETVLHG PAALDLPACS AETFSVFAVS DRVEGLCESG
     SLYETDGLVL TNDLSRGLSN EFTGSPVRIT LESGDLIVFL PVLPLVDL
//
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