ID B2RIK2_PORG3 Unreviewed; 346 AA. AC B2RIK2; DT 01-JUL-2008, integrated into UniProtKB/TrEMBL. DT 01-JUL-2008, sequence version 1. DT 02-SEP-2026, entry version 89. 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=PGN_0678 {ECO:0000313|EMBL:BAG33197.1}; OS Porphyromonas gingivalis (strain ATCC 33277 / DSM 20709 / CIP 103683 / JCM OS 12257 / NCTC 11834 / 2561). OC Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales; OC Porphyromonadaceae; Porphyromonas. OX NCBI_TaxID=431947 {ECO:0000313|EMBL:BAG33197.1, ECO:0000313|Proteomes:UP000008842}; RN [1] {ECO:0000313|EMBL:BAG33197.1, ECO:0000313|Proteomes:UP000008842} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33277 / DSM 20709 / CIP 103683 / JCM 12257 / NCTC 11834 / RC 2561 {ECO:0000313|Proteomes:UP000008842}; RX PubMed=18524787; DOI=10.1093/dnares/dsn013; RA Naito M., Hirakawa H., Yamashita A., Ohara N., Shoji M., Yukitake H., RA Nakayama K., Toh H., Yoshimura F., Kuhara S., Hattori M., Hayashi T., RA Nakayama K.; RT "Determination of the genome sequence of Porphyromonas gingivalis strain RT ATCC 33277 and genomic comparison with strain W83 revealed extensive genome RT rearrangements in P. gingivalis."; RL DNA Res. 15:215-225(2008). 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; AP009380; BAG33197.1; -; Genomic_DNA. DR RefSeq; WP_012457692.1; NC_010729.1. DR AlphaFoldDB; B2RIK2; -. DR GeneID; 29255901; -. DR KEGG; pgn:PGN_0678; -. DR eggNOG; COG0611; Bacteria. DR HOGENOM; CLU_046964_1_0_10; -. DR OrthoDB; 9802811at2; -. DR BioCyc; PGIN431947:G1G2V-744-MONOMER; -. DR UniPathway; UPA00060; UER00142. DR Proteomes; UP000008842; 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; IPR010918; PurM-like_C_dom. 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 Pfam; PF02769; AIRS_C; 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:BAG33197.1}; 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:UP000008842}; KW Thiamine biosynthesis {ECO:0000256|ARBA:ARBA00022977, ECO:0000256|HAMAP- KW Rule:MF_02128}; Transferase {ECO:0000256|HAMAP-Rule:MF_02128}. FT DOMAIN 34..147 FT /note="PurM-like N-terminal" FT /evidence="ECO:0000259|Pfam:PF00586" FT DOMAIN 211..277 FT /note="PurM-like C-terminal" FT /evidence="ECO:0000259|Pfam:PF02769" FT BINDING 36 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="3" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02128" FT BINDING 36 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="4" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02128" FT BINDING 51 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="4" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02128" FT BINDING 52 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02128" FT BINDING 53 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02128" FT BINDING 53 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02128" FT BINDING 60 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02128" FT BINDING 82 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02128" FT BINDING 82 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="3" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02128" FT BINDING 82 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="4" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02128" FT BINDING 112 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02128" FT BINDING 129..130 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02128" FT BINDING 130 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02128" FT BINDING 156 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02128" FT BINDING 233 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="3" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02128" FT BINDING 235 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02128" FT BINDING 236 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="5" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02128" FT BINDING 286 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02128" FT BINDING 338 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02128" SQ SEQUENCE 346 AA; 37628 MW; 6EE781164B221E51 CRC64; MKRTEISSLG EFGLIRHLTD CVRLKNPGTL KGIGDDAAVI SFDEGMKALV TTDMLLEGIH FDLTYTPLKH LGYKSAIVNF SDIYAMNGTP RQLTVSIGVS ARFSVEDIEQ IYQGILTACD VYGVDLVGGD TSASLTGLCL SLTCIGEARE EEIVYRSGAK PTDLICVSGD LGAAYMGLQL LEREKAVYQG EKDFAPDFAG HEYILERQLK PEARKDIVEK LRSAGIKPTA MMDISDGLSS ELLHIAHAGK VGIRIYDDKL PIDYQTAAMA EEFNMNLSTA ALNGGEDYEL LFTVPLTRLD DIQRIEGIHL IGHITEEADG HLLVARDGTE ITLVAQGWNA AKALNG //