ID A6UX09_META3 Unreviewed; 327 AA. AC A6UX09; DT 21-AUG-2007, integrated into UniProtKB/TrEMBL. DT 21-AUG-2007, sequence version 1. DT 02-SEP-2026, entry version 78. DE RecName: Full=Thiamine-monophosphate kinase {ECO:0000256|HAMAP-Rule:MF_02128}; DE Short=TMP kinase {ECO:0000256|HAMAP-Rule:MF_02128}; DE Short=Thiamine-phosphate kinase {ECO:0000256|HAMAP-Rule:MF_02128}; DE EC=2.7.4.16 {ECO:0000256|HAMAP-Rule:MF_02128}; GN Name=thiL {ECO:0000256|HAMAP-Rule:MF_02128}; GN OrderedLocusNames=Maeo_1455 {ECO:0000313|EMBL:ABR57031.1}; OS Methanococcus aeolicus (strain ATCC BAA-1280 / DSM 17508 / OCM 812 / OS Nankai-3). OC Archaea; Methanobacteriati; Methanobacteriota; Methanomada group; OC Methanococci; Methanococcales; Methanococcaceae; Methanococcus. OX NCBI_TaxID=419665 {ECO:0000313|EMBL:ABR57031.1, ECO:0000313|Proteomes:UP000001106}; RN [1] {ECO:0000313|EMBL:ABR57031.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Nankai-3 {ECO:0000313|EMBL:ABR57031.1}; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., RA Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., RA Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., RA Sieprawska-Lupa M., Whitman W.B., Richardson P.; RT "Complete sequence of Methanococcus aeolicus Nankai-3."; RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the ATP-dependent phosphorylation of thiamine- CC monophosphate (TMP) to form thiamine-pyrophosphate (TPP), the active CC form of vitamin B1. {ECO:0000256|HAMAP-Rule:MF_02128}. CC -!- CATALYTIC ACTIVITY: CC Reaction=thiamine phosphate + ATP = thiamine diphosphate + ADP; CC Xref=Rhea:RHEA:15913, ChEBI:CHEBI:30616, ChEBI:CHEBI:37575, CC ChEBI:CHEBI:58937, ChEBI:CHEBI:456216; EC=2.7.4.16; CC Evidence={ECO:0000256|HAMAP-Rule:MF_02128}; CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine diphosphate from thiamine phosphate: step 1/1. CC {ECO:0000256|HAMAP-Rule:MF_02128}. CC -!- MISCELLANEOUS: Reaction mechanism of ThiL seems to utilize a direct, CC inline transfer of the gamma-phosphate of ATP to TMP rather than a CC phosphorylated enzyme intermediate. {ECO:0000256|HAMAP-Rule:MF_02128}. CC -!- SIMILARITY: Belongs to the thiamine-monophosphate kinase family. CC {ECO:0000256|HAMAP-Rule:MF_02128}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_02128}. 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; CP000743; ABR57031.1; -; Genomic_DNA. DR RefSeq; WP_011974163.1; NC_009635.1. DR AlphaFoldDB; A6UX09; -. DR STRING; 419665.Maeo_1455; -. DR GeneID; 5326540; -. DR GeneID; 75304937; -. DR KEGG; mae:Maeo_1455; -. DR eggNOG; arCOG00638; Archaea. DR HOGENOM; CLU_046964_2_1_2; -. DR OrthoDB; 45909at2157; -. DR UniPathway; UPA00060; UER00142. DR Proteomes; UP000001106; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0009030; F:thiamine-phosphate kinase activity; IEA:UniProtKB-UniRule. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniRule. DR CDD; cd02194; ThiL; 1. DR Gene3D; 3.90.650.10; PurM-like C-terminal domain; 1. DR Gene3D; 3.30.1330.10; PurM-like, N-terminal domain; 1. DR HAMAP; MF_02128; TMP_kinase; 1. DR InterPro; IPR036676; PurM-like_C_sf. DR InterPro; IPR016188; PurM-like_N. DR InterPro; IPR036921; PurM-like_N_sf. DR InterPro; IPR006283; ThiL-like. DR NCBIfam; TIGR01379; thiL; 1. DR PANTHER; PTHR30270; THIAMINE-MONOPHOSPHATE KINASE; 1. DR PANTHER; PTHR30270:SF3; THIAMINE-MONOPHOSPHATE KINASE; 1. DR Pfam; PF00586; AIRS; 1. DR PIRSF; PIRSF005303; Thiam_monoph_kin; 1. DR SUPFAM; SSF56042; PurM C-terminal domain-like; 1. DR SUPFAM; SSF55326; PurM N-terminal domain-like; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_02128}; KW Kinase {ECO:0000256|HAMAP-Rule:MF_02128, ECO:0000313|EMBL:ABR57031.1}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_02128}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_02128}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_02128}; KW Reference proteome {ECO:0000313|Proteomes:UP000001106}; KW Thiamine biosynthesis {ECO:0000256|HAMAP-Rule:MF_02128}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_02128, ECO:0000313|EMBL:ABR57031.1}. FT DOMAIN 27..138 FT /note="PurM-like N-terminal" FT /evidence="ECO:0000259|Pfam:PF00586" FT BINDING 29 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="3" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02128" FT BINDING 29 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="4" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02128" FT BINDING 44 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="4" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02128" FT BINDING 45 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02128" FT BINDING 46 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02128" FT BINDING 46 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02128" FT BINDING 53 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02128" FT BINDING 74 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02128" FT BINDING 74 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="3" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02128" FT BINDING 74 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="4" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02128" FT BINDING 120..121 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02128" FT BINDING 121 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02128" FT BINDING 144 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02128" FT BINDING 216 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="3" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02128" FT BINDING 218 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02128" FT BINDING 219 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="5" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02128" FT BINDING 266 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02128" FT BINDING 318 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02128" SQ SEQUENCE 327 AA; 36869 MW; B051F3BC3F098B2C CRC64; MDELNIIKII QNNLKYKGSS HVVKSIGDDC AVVGMGENNY LTITTDMMFR SSHFPNILSP FQIGHRVITA NLSDIASMGA KPLGIVVSMG FNNPSKKFIE ELTKGINYAT ELYCCPIIGG DTNKSKELTL CGTAFGIASN PLYRYNGNVG DDIVITNDIG KVYCAFKILE MIETDKKHNN LIEEYSEIME KLYMPIAQVK MGLLLNKYNY ASSCCDISDG LGKELFYMGN FEVKSKKLIN AMPKIVIEFC NRFNLNPVEV ALNSGEEWEL LFTTNKYDKI NNILNKYDNT KIIKLKKIGK IIDKGHYLDD EILHTSGYVH KWSDKNE //