ID C4ZEU9_AGARV Unreviewed; 214 AA.
AC C4ZEU9;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE RecName: Full=thiamine diphosphokinase {ECO:0000256|ARBA:ARBA00013245};
DE EC=2.7.6.2 {ECO:0000256|ARBA:ARBA00013245};
GN OrderedLocusNames=EUBREC_2336 {ECO:0000313|EMBL:ACR76070.1};
OS Agathobacter rectalis (strain ATCC 33656 / DSM 3377 / JCM 17463 / KCTC 5835
OS / VPI 0990) (Eubacterium rectale).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Agathobacter.
OX NCBI_TaxID=515619 {ECO:0000313|EMBL:ACR76070.1, ECO:0000313|Proteomes:UP000001477};
RN [1] {ECO:0000313|EMBL:ACR76070.1, ECO:0000313|Proteomes:UP000001477}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33656 / DSM 3377 / JCM 17463 / KCTC 5835 / LMG 30912 / VPI
RC 0990 {ECO:0000313|Proteomes:UP000001477};
RX PubMed=19321416; DOI=10.1073/pnas.0901529106;
RA Mahowald M.A., Rey F.E., Seedorf H., Turnbaugh P.J., Fulton R.S.,
RA Wollam A., Shah N., Wang C., Magrini V., Wilson R.K., Cantarel B.L.,
RA Coutinho P.M., Henrissat B., Crock L.W., Russell A., Verberkmoes N.C.,
RA Hettich R.L., Gordon J.I.;
RT "Characterizing a model human gut microbiota composed of members of its two
RT dominant bacterial phyla.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:5859-5864(2009).
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; CP001107; ACR76070.1; -; Genomic_DNA.
DR RefSeq; WP_012743164.1; NC_012781.1.
DR AlphaFoldDB; C4ZEU9; -.
DR STRING; 515619.EUBREC_2336; -.
DR PaxDb; 515619-EUBREC_2336; -.
DR KEGG; ere:EUBREC_2336; -.
DR HOGENOM; CLU_044237_1_1_9; -.
DR Proteomes; UP000001477; 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:ACR76070.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 147..208
FT /note="Thiamin pyrophosphokinase thiamin-binding"
FT /evidence="ECO:0000259|SMART:SM00983"
SQ SEQUENCE 214 AA; 23631 MW; 3BB3E16A52379A80 CRC64;
MRYLIVCGGK IDKEFGLNEI KTDGIDAIIA ADSGMDFLYE NGVTPDIIVG DFDSTTTNAL
EYFERKGQTE IRRLNPIKDD TDTEYAIRLA ISEGARSIVL LGATGSRIDH VLGNISLLGI
GLESGTDISI IDTNNRIRMA DKPVTIEKSA QYGRFVSLIA LTDDNEVSLK GFKYPVTDYS
FDRFTSLGIS NEIVDDHALI DIHRGKFIII ESKD
//
