ID D9S3Q7_THEOJ Unreviewed; 375 AA.
AC D9S3Q7;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE SubName: Full=Thiamin pyrophosphokinase catalytic region {ECO:0000313|EMBL:ADL08034.1};
GN OrderedLocusNames=Toce_1278 {ECO:0000313|EMBL:ADL08034.1};
OS Thermosediminibacter oceani (strain ATCC BAA-1034 / DSM 16646 /
OS JW/IW-1228P).
OC Bacteria; Bacillota; Clostridia; Thermosediminibacterales;
OC Thermosediminibacteraceae; Thermosediminibacter.
OX NCBI_TaxID=555079 {ECO:0000313|EMBL:ADL08034.1, ECO:0000313|Proteomes:UP000000272};
RN [1] {ECO:0000313|EMBL:ADL08034.1, ECO:0000313|Proteomes:UP000000272}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1034 / DSM 16646 / JW/IW-1228P
RC {ECO:0000313|Proteomes:UP000000272};
RX PubMed=21304740;
RA Pitluck S., Yasawong M., Munk C., Nolan M., Lapidus A., Lucas S.,
RA Glavina Del Rio T., Tice H., Cheng J.F., Bruce D., Detter C., Tapia R.,
RA Han C., Goodwin L., Liolios K., Ivanova N., Mavromatis K., Mikhailova N.,
RA Pati A., Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J.,
RA Jeffries C.D., Rohde M., Spring S., Sikorski J., Goker M., Woyke T.,
RA Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C.,
RA Klenk H.P.;
RT "Complete genome sequence of Thermosediminibacter oceani type strain
RT (JW/IW-1228P).";
RL Stand. Genomic Sci. 3:108-116(2010).
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DR EMBL; CP002131; ADL08034.1; -; Genomic_DNA.
DR RefSeq; WP_013276073.1; NC_014377.1.
DR AlphaFoldDB; D9S3Q7; -.
DR STRING; 555079.Toce_1278; -.
DR KEGG; toc:Toce_1278; -.
DR eggNOG; COG4825; Bacteria.
DR HOGENOM; CLU_046690_0_0_9; -.
DR OrthoDB; 9804377at2; -.
DR Proteomes; UP000000272; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:InterPro.
DR Gene3D; 3.40.50.10240; Thiamin pyrophosphokinase, catalytic domain; 1.
DR InterPro; IPR047795; Put_SteA-like.
DR InterPro; IPR022215; SteA-like_C.
DR InterPro; IPR007371; TPK_catalytic.
DR InterPro; IPR036759; TPK_catalytic_sf.
DR NCBIfam; NF040608; division_SteA; 1.
DR Pfam; PF12555; SteA-like_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}; Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000000272};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 335..357
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 194..227
FT /note="Thiamin pyrophosphokinase catalytic"
FT /evidence="ECO:0000259|Pfam:PF04263"
FT DOMAIN 321..371
FT /note="SteA-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF12555"
SQ SEQUENCE 375 AA; 41413 MW; E295A4BA44D7D4A2 CRC64;
MGAVGRAVVD RKTKKLLQRL KPGEIAVIYH KDIDELAAKN LVKSKVKGVI NFQPSMSGRF
FNQGPAMLLD AGIPVVDVSE EELFDSIRDG DIVQIKENGE ITVNGRFLCK GVILSQDLIS
SKLEEAKANF EKELEKFAVN TLEYIRREKT LLSSDYTVPR LKTDMHRKHV MVVVRGKDYR
EDLLTLRSYI EEIKPVLIGV DGGADALLEF GLKPNVIIGD MDSISDKGLM CGAEIVVHAY
PDGRAPGLDR VKKLGLDYHI MPVTGTSEDA ALLLAYHSGA DLIVAVGTHN NIIDFLEKGR
QGMASTFLVR LKVGHILIDA KGVNKLYKGG IKINYIAALF VAAFFPIFIL GTTSPAFRHL
LRLILLKVKL MIGFL
//
