ID A6UPD2_METVS Unreviewed; 315 AA. AC A6UPD2; DT 21-AUG-2007, integrated into UniProtKB/TrEMBL. DT 21-AUG-2007, sequence version 1. DT 02-SEP-2026, entry version 76. 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=Mevan_0447 {ECO:0000313|EMBL:ABR54354.1}; OS Methanococcus vannielii (strain ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148 OS / SB). OC Archaea; Methanobacteriati; Methanobacteriota; Methanomada group; OC Methanococci; Methanococcales; Methanococcaceae; Methanococcus. OX NCBI_TaxID=406327 {ECO:0000313|EMBL:ABR54354.1, ECO:0000313|Proteomes:UP000001107}; RN [1] {ECO:0000313|EMBL:ABR54354.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SB {ECO:0000313|EMBL:ABR54354.1}; 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., Anderson I., RA Sieprawska-Lupa M., Whitman W.B., Richardson P.; RT "Complete sequence of Methanococcus vannielii SB."; 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; CP000742; ABR54354.1; -; Genomic_DNA. DR RefSeq; WP_011972257.1; NC_009634.1. DR AlphaFoldDB; A6UPD2; -. DR STRING; 406327.Mevan_0447; -. DR GeneID; 5325368; -. DR KEGG; mvn:Mevan_0447; -. DR eggNOG; arCOG00638; Archaea. DR HOGENOM; CLU_046964_2_0_2; -. DR OrthoDB; 45909at2157; -. DR UniPathway; UPA00060; UER00142. DR Proteomes; UP000001107; 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:ABR54354.1}; 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:UP000001107}; KW Thiamine biosynthesis {ECO:0000256|HAMAP-Rule:MF_02128}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_02128, ECO:0000313|EMBL:ABR54354.1}. FT DOMAIN 25..134 FT /note="PurM-like N-terminal" FT /evidence="ECO:0000259|Pfam:PF00586" FT BINDING 27 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="3" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02128" FT BINDING 27 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="4" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02128" FT BINDING 41 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="4" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02128" FT BINDING 42 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02128" FT BINDING 43 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02128" FT BINDING 43 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02128" FT BINDING 50 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02128" FT BINDING 71 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02128" FT BINDING 71 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="3" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02128" FT BINDING 71 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="4" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02128" FT BINDING 117..118 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02128" FT BINDING 118 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02128" FT BINDING 141 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02128" FT BINDING 214 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="3" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02128" FT BINDING 216 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02128" FT BINDING 217 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="5" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02128" FT BINDING 264 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02128" FT BINDING 311 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02128" SQ SEQUENCE 315 AA; 34967 MW; 06BC684122E3645F CRC64; MNEFDIINII SKNISYKNGV ERGIGDDCAV FKLENQHLVI TTDMMFRSTH FPEILTPFQI GMRIVTANVS DIAAMCAKPL GMVISMGFDK PDLKFIDEMS KGMNFISKEY GCPIVGGDTN KSKELTLSGT AFGITNNPIY RGGNLGNEIC ITGTIGRVFC ALKILEMSKN GIIDKLKFEK LIEEFPEIIK KLSEPKARVL EGISLNNVVT SCSDISDGLS KDLNHVGFFE IYSKELLKAV PKDVVEFSEK FDINLIDIAL NSGEEFELLF TVKDFKNAKK VLKGINTVTK FGKVVESGKT VDGNNITFEG YVHKW //