ID THIED_GEOSL Reviewed; 490 AA. AC P61422; DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot. DT 24-MAY-2004, sequence version 1. DT 27-MAR-2024, entry version 122. DE RecName: Full=Thiamine biosynthesis bifunctional protein ThiED; DE Includes: DE RecName: Full=Thiamine-phosphate synthase; DE Short=TMP-PPase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3 {ECO:0000250|UniProtKB:P39594}; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; 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; GN Name=thiDE; OrderedLocusNames=GSU0605; OS Geobacter sulfurreducens (strain ATCC 51573 / DSM 12127 / PCA). OC Bacteria; Thermodesulfobacteriota; Desulfuromonadia; Geobacterales; OC Geobacteraceae; Geobacter. OX NCBI_TaxID=243231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51573 / DSM 12127 / PCA; RX PubMed=14671304; DOI=10.1126/science.1088727; RA Methe B.A., Nelson K.E., Eisen J.A., Paulsen I.T., Nelson W.C., RA Heidelberg J.F., Wu D., Wu M., Ward N.L., Beanan M.J., Dodson R.J., RA Madupu R., Brinkac L.M., Daugherty S.C., DeBoy R.T., Durkin A.S., RA Gwinn M.L., Kolonay J.F., Sullivan S.A., Haft D.H., Selengut J., RA Davidsen T.M., Zafar N., White O., Tran B., Romero C., Forberger H.A., RA Weidman J.F., Khouri H.M., Feldblyum T.V., Utterback T.R., Van Aken S.E., RA Lovley D.R., Fraser C.M.; RT "Genome of Geobacter sulfurreducens: metal reduction in subsurface RT environments."; RL Science 302:1967-1969(2003). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl pyrimidine CC pyrophosphate (HMP-PP) to form thiamine monophosphate (TMP). CC {ECO:0000250|UniProtKB:P39594}. 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 -!- 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(+) = CO2 + diphosphate + thiamine phosphate; 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:0000250|UniProtKB:P39594}; CC -!- CATALYTIC ACTIVITY: CC Reaction=2-(2-carboxy-4-methylthiazol-5-yl)ethyl phosphate + 4-amino-2- CC methyl-5-(diphosphooxymethyl)pyrimidine + 2 H(+) = CO2 + diphosphate CC + thiamine phosphate; 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:0000250|UniProtKB:P39594}; CC -!- CATALYTIC ACTIVITY: CC Reaction=4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine + 4-methyl- CC 5-(2-phosphooxyethyl)-thiazole + H(+) = diphosphate + thiamine CC phosphate; 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:0000250|UniProtKB:P39594}; 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 -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250}; CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; 4- CC amino-2-methyl-5-diphosphomethylpyrimidine from 5-amino-1-(5-phospho-D- CC ribosyl)imidazole: step 3/3. 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 thiamine- CC phosphate synthase family. {ECO:0000305}. CC -!- SIMILARITY: In the C-terminal section; belongs to the ThiD 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; AE017180; AAR33936.1; -; Genomic_DNA. DR RefSeq; NP_951663.1; NC_002939.5. DR RefSeq; WP_010941267.1; NC_002939.5. DR AlphaFoldDB; P61422; -. DR SMR; P61422; -. DR STRING; 243231.GSU0605; -. DR EnsemblBacteria; AAR33936; AAR33936; GSU0605. DR KEGG; gsu:GSU0605; -. DR PATRIC; fig|243231.5.peg.603; -. DR eggNOG; COG0351; Bacteria. DR eggNOG; COG0352; Bacteria. DR HOGENOM; CLU_020520_5_1_7; -. DR InParanoid; P61422; -. DR OrthoDB; 9810880at2; -. DR UniPathway; UPA00060; UER00138. DR UniPathway; UPA00060; UER00141. DR Proteomes; UP000000577; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0008902; F:hydroxymethylpyrimidine kinase activity; IBA:GO_Central. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IBA:GO_Central. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-UniRule. DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR GO; GO:0009228; P:thiamine biosynthetic process; IBA:GO_Central. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR CDD; cd01169; HMPP_kinase; 1. DR CDD; cd00564; TMP_TenI; 1. DR Gene3D; 3.40.1190.20; -; 1. DR Gene3D; 3.20.20.70; Aldolase class I; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR004399; HMP/HMP-P_kinase_dom. DR InterPro; IPR013749; PM/HMP-P_kinase-1. DR InterPro; IPR029056; Ribokinase-like. DR InterPro; IPR036206; ThiamineP_synth_sf. DR InterPro; IPR022998; ThiamineP_synth_TenI. DR InterPro; IPR034291; TMP_synthase. DR NCBIfam; TIGR00097; HMP-P_kinase; 1. DR NCBIfam; TIGR00693; thiE; 1. DR PANTHER; PTHR20858; PHOSPHOMETHYLPYRIMIDINE KINASE; 1. DR PANTHER; PTHR20858:SF21; THIAMINE-PHOSPHATE SYNTHASE; 1. DR Pfam; PF08543; Phos_pyr_kin; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF53613; Ribokinase-like; 1. DR SUPFAM; SSF51391; Thiamin phosphate synthase; 1. PE 3: Inferred from homology; KW ATP-binding; Kinase; Magnesium; Metal-binding; Multifunctional enzyme; KW Nucleotide-binding; Reference proteome; Thiamine biosynthesis; Transferase. FT CHAIN 1..490 FT /note="Thiamine biosynthesis bifunctional protein ThiED" FT /id="PRO_0000192040" FT REGION 1..213 FT /note="Thiamine-phosphate synthase" FT REGION 229..490 FT /note="Hydroxymethylpyrimidine/phosphomethylpyrimidine FT kinase" FT BINDING 50..54 FT /ligand="4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine" FT /ligand_id="ChEBI:CHEBI:57841" FT /evidence="ECO:0000250" FT BINDING 82 FT /ligand="4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine" FT /ligand_id="ChEBI:CHEBI:57841" FT /evidence="ECO:0000250" FT BINDING 83 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250" FT BINDING 102 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250" FT BINDING 121 FT /ligand="4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine" FT /ligand_id="ChEBI:CHEBI:57841" FT /evidence="ECO:0000250" FT BINDING 147..149 FT /ligand="2-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)- FT ylidene]ethyl phosphate" FT /ligand_id="ChEBI:CHEBI:62899" FT /evidence="ECO:0000250" FT BINDING 150 FT /ligand="4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine" FT /ligand_id="ChEBI:CHEBI:57841" FT /evidence="ECO:0000250" FT BINDING 177 FT /ligand="2-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)- FT ylidene]ethyl phosphate" FT /ligand_id="ChEBI:CHEBI:62899" FT /evidence="ECO:0000250" FT BINDING 197..198 FT /ligand="2-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)- FT ylidene]ethyl phosphate" FT /ligand_id="ChEBI:CHEBI:62899" FT /evidence="ECO:0000250" FT BINDING 266 FT /ligand="4-amino-5-hydroxymethyl-2-methylpyrimidine" FT /ligand_id="ChEBI:CHEBI:16892" FT /evidence="ECO:0000250" SQ SEQUENCE 490 AA; 51910 MW; 924B153FCD5E83D4 CRC64; MASNGHTLRL VINRDKHDSV IRGLYLVTDH DDNLIPRVEA AIDGGARVVQ YRNKNQDRES RLALGLELRE LCRRRSIPFI VNDDLEMAVS LKADGLHLGQ GDGDPREARR VLGPGKIIGV STHTLSEALE AQAAGVDYIG LGAMFPSRSK EVEHVAGSEL LAAIRSSISI PIVAIGGITR DNGASVIDAG ADAVAVISAV LSHPDPALAA TEIALLFNRR APFPRGSVLT VAGSDSGGGA GIQADLKTVT LLGSYGSSVL TALTAQNTRG VSGIHGVPPA FVADQLDAVF SDIPVDVVKT GMLFSAETIV AIAAKLTEYR RRMVVVDPVM VAKGGANLID RGAVSVLKER LFPLAYLVTP NIPEAERLTG ANISDEESMR EAARRLHRLG ARNVLLKGGH LLAGDSVDIL FDGAAFHRFV SPRILSKNTH GTGCTFASAI ATYLAQGDPL REAIARAKRY ITAAIRLAQP LGRGHGPVNH ILAAEDVRDR //