ID F0F8C1_9BACT Unreviewed; 255 AA.
AC F0F8C1;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE SubName: Full=Thiamine diphosphokinase {ECO:0000313|EMBL:EGC19580.1};
DE EC=2.7.6.2 {ECO:0000313|EMBL:EGC19580.1};
GN ORFNames=HMPREF9141_1838 {ECO:0000313|EMBL:EGC19580.1};
OS Prevotella multiformis DSM 16608.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Prevotella.
OX NCBI_TaxID=888743 {ECO:0000313|EMBL:EGC19580.1, ECO:0000313|Proteomes:UP000005697};
RN [1] {ECO:0000313|EMBL:EGC19580.1, ECO:0000313|Proteomes:UP000005697}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16608 {ECO:0000313|EMBL:EGC19580.1,
RC ECO:0000313|Proteomes:UP000005697};
RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L.,
RA Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., Korchina V.,
RA Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N., Okwuonu G.,
RA Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W., Jakkamsetti A.,
RA Pham P., Ruth R., San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C.,
RA Zhu D., Lee S., Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S.,
RA Hirani K., Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S.,
RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L.,
RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P.,
RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K.,
RA Petrosino J., Highlander S., Gibbs R.;
RL Submitted (JAN-2011) 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:EGC19580.1}.
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DR EMBL; AEWX01000026; EGC19580.1; -; Genomic_DNA.
DR RefSeq; WP_007366591.1; NZ_GL872282.1.
DR AlphaFoldDB; F0F8C1; -.
DR STRING; 888743.HMPREF9141_1838; -.
DR eggNOG; COG1564; Bacteria.
DR HOGENOM; CLU_044237_2_0_10; -.
DR Proteomes; UP000005697; 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: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; IPR049442; Thi_PPkinase-like_C.
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; PF21275; Thi_PPkinase_C; 1.
DR Pfam; PF04263; TPK_catalytic; 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:EGC19580.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000005697};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EGC19580.1}.
FT DOMAIN 64..169
FT /note="Thiamin pyrophosphokinase catalytic"
FT /evidence="ECO:0000259|Pfam:PF04263"
FT DOMAIN 182..250
FT /note="Thiamin pyrophosphokinase-like substrate-binding"
FT /evidence="ECO:0000259|Pfam:PF21275"
SQ SEQUENCE 255 AA; 28661 MW; 97AC4DCC8D7B2309 CRC64;
MVFNNKTKES FSEAGDGHPV RYSFFSDETK GSLSKGTDES STERFSAVIL AAGDFPYHVL
PLRILREARN LVVCDGALAE LIEYEIEPAA VVGDGDSLSA GLKQRYAHIY HQISEQAFND
LTKATLFARS HLQMDAPTHI RPRFCYLGAT GKREDHTLGN ISLMLYYHRQ LGIDPVMVTD
YGWFVPASGT TRFASFPGQQ VSIYNATCKE LTSEGLKWDA YPFQELWQGT LNEALEDRFT
IHADGDYLIY RTHSI
//
