ID THIDN_THEMA Reviewed; 398 AA. AC Q9WZP7; DT 25-JAN-2012, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 02-SEP-2026, entry version 117. DE RecName: Full=Bifunctional thiamine biosynthesis protein ThiDN; DE Includes: DE RecName: Full=Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase; DE EC=2.7.1.49 {ECO:0000250|UniProtKB:P76422}; DE EC=2.7.4.7 {ECO:0000250|UniProtKB:P76422}; DE AltName: Full=Hydroxymethylpyrimidine kinase; DE Short=HMP kinase; DE AltName: Full=Hydroxymethylpyrimidine phosphate kinase; DE Short=HMP-P kinase; DE Short=HMP-phosphate kinase; DE Short=HMPP kinase; DE Includes: DE RecName: Full=Thiamine-phosphate synthase ThiN; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3 {ECO:0000269|PubMed:12794638}; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiDN; OrderedLocusNames=TM_0790; OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 OS / MSB8). OC Bacteria; Thermotogati; Thermotogota; Thermotogae; Thermotogales; OC Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H., RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A., RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M., RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F., RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] RP FUNCTION AS A THIAMINE-PHOSPHATE SYNTHASE VIA ITS C-TERMINAL DOMAIN, AND RP CATALYTIC ACTIVITY. RX PubMed=12794638; DOI=10.1038/nbt834; RA Morett E., Korbel J.O., Rajan E., Saab-Rincon G., Olvera L., Olvera M., RA Schmidt S., Snel B., Bork P.; RT "Systematic discovery of analogous enzymes in thiamin biosynthesis."; RL Nat. Biotechnol. 21:790-795(2003). CC -!- FUNCTION: Catalyzes the phosphorylation of hydroxymethylpyrimidine CC phosphate (HMP-P) to HMP-PP, and of HMP to HMP-P. CC {ECO:0000250|UniProtKB:P76422}. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 4-amino-5-hydroxymethyl pyrimidine CC pyrophosphate (HMP-PP) to form thiamine monophosphate (TMP). CC {ECO:0000269|PubMed:12794638}. CC -!- CATALYTIC ACTIVITY: CC Reaction=4-amino-5-hydroxymethyl-2-methylpyrimidine + ATP = 4-amino-2- CC methyl-5-(phosphooxymethyl)pyrimidine + ADP + H(+); CC Xref=Rhea:RHEA:23096, ChEBI:CHEBI:15378, ChEBI:CHEBI:16892, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:58354, ChEBI:CHEBI:456216; CC EC=2.7.1.49; Evidence={ECO:0000250|UniProtKB:P76422}; CC -!- CATALYTIC ACTIVITY: CC Reaction=4-amino-2-methyl-5-(phosphooxymethyl)pyrimidine + ATP = 4- CC amino-2-methyl-5-(diphosphooxymethyl)pyrimidine + ADP; CC Xref=Rhea:RHEA:19893, ChEBI:CHEBI:30616, ChEBI:CHEBI:57841, CC ChEBI:CHEBI:58354, ChEBI:CHEBI:456216; EC=2.7.4.7; CC Evidence={ECO:0000250|UniProtKB:P76422}; CC -!- CATALYTIC ACTIVITY: CC Reaction=2-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-ylidene]ethyl CC phosphate + 4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine + 2 CC H(+) = thiamine phosphate + CO2 + diphosphate; Xref=Rhea:RHEA:47844, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:33019, CC ChEBI:CHEBI:37575, ChEBI:CHEBI:57841, ChEBI:CHEBI:62899; EC=2.5.1.3; CC Evidence={ECO:0000269|PubMed:12794638}; CC -!- CATALYTIC ACTIVITY: CC Reaction=2-(2-carboxy-4-methylthiazol-5-yl)ethyl phosphate + 4-amino-2- CC methyl-5-(diphosphooxymethyl)pyrimidine + 2 H(+) = thiamine phosphate CC + CO2 + diphosphate; Xref=Rhea:RHEA:47848, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:16526, ChEBI:CHEBI:33019, ChEBI:CHEBI:37575, CC ChEBI:CHEBI:57841, ChEBI:CHEBI:62890; EC=2.5.1.3; CC Evidence={ECO:0000269|PubMed:12794638}; CC -!- CATALYTIC ACTIVITY: CC Reaction=4-methyl-5-(2-phosphooxyethyl)-thiazole + 4-amino-2-methyl-5- CC (diphosphooxymethyl)pyrimidine + H(+) = thiamine phosphate + CC diphosphate; Xref=Rhea:RHEA:22328, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:33019, ChEBI:CHEBI:37575, ChEBI:CHEBI:57841, CC ChEBI:CHEBI:58296; EC=2.5.1.3; CC Evidence={ECO:0000269|PubMed:12794638}; CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; 4- CC amino-2-methyl-5-diphosphomethylpyrimidine from 5-amino-1-(5-phospho-D- CC ribosyl)imidazole. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5-diphosphomethylpyrimidine CC and 4-methyl-5-(2-phosphoethyl)-thiazole: step 1/1. CC -!- SIMILARITY: In the N-terminal section; belongs to the ThiD family. CC {ECO:0000305}. CC -!- SIMILARITY: In the C-terminal section; belongs to the ThiN family. CC {ECO:0000305}. 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; AE000512; AAD35872.1; -; Genomic_DNA. DR PIR; G72333; G72333. DR RefSeq; WP_004080887.1; NC_000853.1. DR AlphaFoldDB; Q9WZP7; -. DR SMR; Q9WZP7; -. DR FunCoup; Q9WZP7; 341. DR STRING; 243274.TM_0790; -. DR PaxDb; 243274-TM_0790; -. DR DNASU; 898458; -. DR EnsemblBacteria; AAD35872; AAD35872; TM_0790. DR KEGG; tma:TM0790; -. DR KEGG; tmi:THEMA_00700; -. DR KEGG; tmm:Tmari_0791; -. DR KEGG; tmw:THMA_0809; -. DR eggNOG; COG0351; Bacteria. DR eggNOG; COG1992; Bacteria. DR InParanoid; Q9WZP7; -. DR OrthoDB; 9810880at2; -. DR UniPathway; UPA00060; UER00141. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0008902; F:hydroxymethylpyrimidine kinase activity; IBA:GO_Central. DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IBA:GO_Central. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR CDD; cd01169; HMPP_kinase; 1. DR FunFam; 3.40.225.10:FF:000015; Phosphomethylpyrimidine kinase (Hmp-phosphate kinase); 1. DR Gene3D; 3.40.1190.20; -; 2. DR Gene3D; 3.40.225.10; Class II aldolase/adducin N-terminal domain; 1. DR InterPro; IPR036409; Aldolase_II/adducin_N_sf. DR InterPro; IPR004399; HMP/HMP-P_kinase_dom. DR InterPro; IPR013749; PM/HMP-P_kinase-1. DR InterPro; IPR029056; Ribokinase-like. DR InterPro; IPR019293; ThiN-like. DR PANTHER; PTHR20858:SF17; HYDROXYMETHYLPYRIMIDINE_PHOSPHOMETHYLPYRIMIDINE KINASE THI20-RELATED; 1. DR PANTHER; PTHR20858; PHOSPHOMETHYLPYRIMIDINE KINASE; 1. DR Pfam; PF08543; Phos_pyr_kin; 1. DR Pfam; PF10120; ThiN; 1. DR SUPFAM; SSF53639; AraD/HMP-PK domain-like; 1. DR SUPFAM; SSF53613; Ribokinase-like; 1. PE 1: Evidence at protein level; KW ATP-binding; Kinase; Multifunctional enzyme; Nucleotide-binding; KW Reference proteome; Thiamine biosynthesis; Transferase. FT CHAIN 1..398 FT /note="Bifunctional thiamine biosynthesis protein ThiDN" FT /id="PRO_0000415381" FT REGION 1..216 FT /note="Hydroxymethylpyrimidine/phosphomethylpyrimidine FT kinase" FT REGION 217..398 FT /note="Thiamine-phosphate synthase" FT BINDING 40 FT /ligand="4-amino-5-hydroxymethyl-2-methylpyrimidine" FT /ligand_id="ChEBI:CHEBI:16892" FT /evidence="ECO:0000250" SQ SEQUENCE 398 AA; 45392 MW; DCE6977F471BF649 CRC64; MVLVVAGFDP SGGAGIIQDV KVLSALGVKT HAVISALTVQ NENRVFSVNF RDWEEMRKEI EVLTPPRVIK VGLSAPETVK RLREMFPDSA IVWNVVLESS SGFGFQDPEE VKKFVEYADY VILNSEEAKK LGEYNNFIVT GGHEKGNTVK VKYRDFVFEI PRVPGEFHGT GCAFSSAVSG FLAMSYPVEE AIRSAMELLK KILERSSGVV ETEKLLRDWY RYDTLNTLDE ILPEFLEIGH LTVPEVGQNV SYALPWAKNE FEVGKFPGRI RLKEGKAVAV SCASFKDRSH TARMAVTMMR YHPHMRCVVN VRYEREYVER AKKRGLKVFH YDRSKEPKEV QEKEGQSMVW MIEQAIAELK SPPDVIYDEG WWGKEAMIRV FGRNPKEVLE KIKLMVRE //