ID B9MRV6_CALBD Unreviewed; 371 AA.
AC B9MRV6;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE SubName: Full=Thiamin pyrophosphokinase catalytic region {ECO:0000313|EMBL:ACM60410.1};
GN OrderedLocusNames=Athe_1310 {ECO:0000313|EMBL:ACM60410.1};
OS Caldicellulosiruptor bescii (strain ATCC BAA-1888 / DSM 6725 / KCTC 15123 /
OS Z-1320) (Anaerocellum thermophilum).
OC Bacteria; Bacillota; Clostridia; Caldicellulosiruptorales;
OC Caldicellulosiruptoraceae; Caldicellulosiruptor.
OX NCBI_TaxID=521460 {ECO:0000313|EMBL:ACM60410.1, ECO:0000313|Proteomes:UP000007723};
RN [1] {ECO:0000313|Proteomes:UP000007723}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1888 / DSM 6725 / Z-1320
RC {ECO:0000313|Proteomes:UP000007723};
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA Goodwin L., Pitluck S., Sims D., Meincke L., Brettin T., Detter J.C.,
RA Han C., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G.,
RA Kataeva I., Adams M.W.W.;
RT "Complete sequence of chromosome of Anaerocellum thermophilum DSM 6725.";
RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP001393; ACM60410.1; -; Genomic_DNA.
DR AlphaFoldDB; B9MRV6; -.
DR STRING; 521460.Athe_1310; -.
DR KEGG; ate:Athe_1310; -.
DR eggNOG; COG4825; Bacteria.
DR HOGENOM; CLU_046690_0_0_9; -.
DR Proteomes; UP000007723; 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, ECO:0000313|EMBL:ACM60410.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 333..362
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 192..232
FT /note="Thiamin pyrophosphokinase catalytic"
FT /evidence="ECO:0000259|Pfam:PF04263"
FT DOMAIN 319..369
FT /note="SteA-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF12555"
SQ SEQUENCE 371 AA; 41665 MW; 5005729651268A2B CRC64;
MIKGKVRVDR RTKNLVRRLR PGEIPVIMHE DIDEVAAYSL LEKKVRVVIN CAKSFTGKFP
AVGAKILLAH DVIIIDNLGE DVFNRIREGD VVEIEDDKIF LNGNYLCIAK YLTKEEFESF
YQKSFKEMEN LLEDFIENTL EYAKKEKGFI LGQFEMPDIS TKIAGRHVLV VTRGSSFKKD
IKAIKGYITE VKPVVIAVDG AADALLEEKI RPNIIIGDMD SVSEESLYKC DEIIVHSYPN
GYAPGLRKIQ ALGLKAKTIA CPGTSEDVAL LLAYEKGAEL IVSVGSHSSM LDFLEKGRKG
MSSTFLVRLK IGSKLVDARG VSKLYTEKVS FKYIGVLLFS ALIPILAILM VTPPFQYFFY
LIQLKLRVIL R
//
