ID B4SFU6_PELPB Unreviewed; 363 AA. AC B4SFU6; DT 23-SEP-2008, integrated into UniProtKB/TrEMBL. DT 23-SEP-2008, sequence version 1. DT 04-NOV-2026, entry version 87. 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=Ppha_2612 {ECO:0000313|EMBL:ACF44773.1}; OS Pelodictyon phaeoclathratiforme (strain DSM 5477 / BU-1). OC Bacteria; Pseudomonadati; Chlorobiota; Chlorobiia; Chlorobiales; OC Chlorobiaceae; Chlorobium/Pelodictyon group; Pelodictyon. OX NCBI_TaxID=324925 {ECO:0000313|EMBL:ACF44773.1, ECO:0000313|Proteomes:UP000002724}; RN [1] {ECO:0000313|EMBL:ACF44773.1, ECO:0000313|Proteomes:UP000002724} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 5477 / BU-1 {ECO:0000313|Proteomes:UP000002724}; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., RA Bruce D., Goodwin L., Pitluck S., Schmutz J., Larimer F., Land M., RA Hauser L., Kyrpides N., Mikhailova N., Liu Z., Li T., Zhao F., Overmann J., RA Bryant D.A., Richardson P.; RT "Complete sequence of Pelodictyon phaeoclathratiforme BU-1."; RL Submitted (JUN-2008) 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 --------------------------------------------------------------------------- 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; CP001110; ACF44773.1; -; Genomic_DNA. DR AlphaFoldDB; B4SFU6; -. DR STRING; 324925.Ppha_2612; -. DR KEGG; pph:Ppha_2612; -. DR eggNOG; COG0611; Bacteria. DR HOGENOM; CLU_046964_1_1_10; -. DR OMA; AAAXEYL; -. DR UniPathway; UPA00060; UER00142. DR Proteomes; UP000002724; 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:SF0; 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:ACF44773.1}; 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:UP000002724}; KW Thiamine biosynthesis {ECO:0000256|ARBA:ARBA00022977, ECO:0000256|HAMAP- KW Rule:MF_02128}; Transferase {ECO:0000256|HAMAP-Rule:MF_02128}. FT DOMAIN 45..159 FT /note="PurM-like N-terminal" FT /evidence="ECO:0000259|Pfam:PF00586" FT BINDING 47 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="3" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02128" FT BINDING 47 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="4" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02128" FT BINDING 62 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="4" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02128" FT BINDING 63 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02128" FT BINDING 64 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02128" FT BINDING 64 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="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02128" FT BINDING 93 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02128" FT BINDING 93 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="3" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02128" FT BINDING 93 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="4" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02128" FT BINDING 123 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02128" FT BINDING 140..141 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02128" FT BINDING 141 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02128" FT BINDING 167 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02128" FT BINDING 252 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="3" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02128" FT BINDING 254 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02128" FT BINDING 255 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="5" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02128" FT BINDING 305 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02128" FT BINDING 358 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02128" SQ SEQUENCE 363 AA; 39415 MW; 090BC13892D206DA CRC64; MNFNLRKNMS YTAISGIGEF GLIDKIATLA NSTLPAVPEL LTGIGDDCAV FQPSAELLQV ATTDMLADQV HFDLLTTPLK HLGSKAISVN VSDICAMNAL PRYALISLAI PASFSIAMIE ELYQGMSHAA REYGLAIAGG DTSSSRSGLV IAISMMGEVS REQLVHRSGA KPGELLCITG ALGGATAGLK LLMREKEIML NHIENNESYS RSAMADLKEY SESIQQQLLP LARLDIVRFF HAHHIRPTSM IDISDGLSSD LQHLCRRSKI GAMIQEARIP ILGSTRRIAD ELQDDALTWA LTGGEDYQLL FTIPKEEYPA IADNKTIAVI GETTDVEEGV QLSDIYGMKI DLSSIRGFDH FSS //