ID THIED_COREF Reviewed; 739 AA. AC Q8FTH8; DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2003, sequence version 1. DT 27-MAR-2024, entry version 132. DE RecName: Full=Thiamine biosynthesis multifunctional 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=thiED; OrderedLocusNames=CE1591; OS Corynebacterium efficiens (strain DSM 44549 / YS-314 / AJ 12310 / JCM 11189 OS / NBRC 100395). OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; OC Corynebacteriaceae; Corynebacterium. OX NCBI_TaxID=196164; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395; RX PubMed=12840036; DOI=10.1101/gr.1285603; RA Nishio Y., Nakamura Y., Kawarabayasi Y., Usuda Y., Kimura E., Sugimoto S., RA Matsui K., Yamagishi A., Kikuchi H., Ikeo K., Gojobori T.; RT "Comparative complete genome sequence analysis of the amino acid RT replacements responsible for the thermostability of Corynebacterium RT efficiens."; RL Genome Res. 13:1572-1579(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 -!- MISCELLANEOUS: There is also a ThiE protein in this bacteria (AC CC Q8FP55). CC -!- SIMILARITY: In the N-terminal section; belongs to the thiamine- CC phosphate synthase family. {ECO:0000305}. CC -!- SIMILARITY: In the central section; belongs to the ThiD family. CC {ECO:0000305}. CC -!- SIMILARITY: In the C-terminal section; belongs to the thiaminase-2 CC family. {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; BA000035; BAC18401.1; -; Genomic_DNA. DR RefSeq; WP_006767589.1; NZ_GG700683.1. DR AlphaFoldDB; Q8FTH8; -. DR SMR; Q8FTH8; -. DR STRING; 196164.gene:10742010; -. DR KEGG; cef:CE1591; -. DR eggNOG; COG0351; Bacteria. DR eggNOG; COG0352; Bacteria. DR eggNOG; COG0819; Bacteria. DR HOGENOM; CLU_020520_2_0_11; -. DR OrthoDB; 34166at2; -. DR UniPathway; UPA00060; UER00138. DR UniPathway; UPA00060; UER00141. DR Proteomes; UP000001409; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0008902; F:hydroxymethylpyrimidine kinase activity; IEA:UniProtKB-EC. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:UniProtKB-EC. 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; IEA:UniProtKB-UniRule. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR CDD; cd01169; HMPP_kinase; 1. DR CDD; cd19365; TenA_C-like; 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 Gene3D; 1.20.910.10; Heme oxygenase-like; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR016084; Haem_Oase-like_multi-hlx. DR InterPro; IPR004399; HMP/HMP-P_kinase_dom. DR InterPro; IPR013749; PM/HMP-P_kinase-1. DR InterPro; IPR029056; Ribokinase-like. DR InterPro; IPR004305; Thiaminase-2/PQQC. 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; PF03070; TENA_THI-4; 1. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF48613; Heme oxygenase-like; 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..739 FT /note="Thiamine biosynthesis multifunctional protein ThiED" FT /id="PRO_0000192038" FT REGION 1..210 FT /note="Thiamine-phosphate synthase" FT REGION 226..481 FT /note="Hydroxymethylpyrimidine/phosphomethylpyrimidine FT kinase" FT REGION 527..739 FT /note="Thiaminase-2" FT BINDING 37..41 FT /ligand="4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine" FT /ligand_id="ChEBI:CHEBI:57841" FT /evidence="ECO:0000250" FT BINDING 69 FT /ligand="4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine" FT /ligand_id="ChEBI:CHEBI:57841" FT /evidence="ECO:0000250" FT BINDING 70 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250" FT BINDING 88 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250" FT BINDING 107 FT /ligand="4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine" FT /ligand_id="ChEBI:CHEBI:57841" FT /evidence="ECO:0000250" FT BINDING 140..142 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 143 FT /ligand="4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine" FT /ligand_id="ChEBI:CHEBI:57841" FT /evidence="ECO:0000250" FT BINDING 174 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 194..195 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 263 FT /ligand="4-amino-5-hydroxymethyl-2-methylpyrimidine" FT /ligand_id="ChEBI:CHEBI:16892" FT /evidence="ECO:0000250" SQ SEQUENCE 739 AA; 77744 MW; D6631B0553929077 CRC64; MTDFSLYLVT DPHLGGGPER VAGIVEDAIN GGVTVVQLRD KDADEQTFRE HAMELKRVCD RLGVPLFLND RFAVAAELSC HVHIGQGDLP YVQARRQLPG HLMIGLTIET MDQLETVIAD CTRAGIALPD VVGLGPVQAT DTKPDAPQAV GVDGVAAMAK VARAHGIASV AIGGVGLANA ADLARTGVDG LCVVSAIMAA PSPAEAAREL LDVWEAGRRV AQPRVLTIAG TDPTGGAGVQ ADLKSIAAAG GFGMSVITAL VAQNTHGVTG VHTPPADFLD EQLESVFSDV TVDAVKLGML GRADTVRQVT GWLRTRPHGP VILDPVMVAT SGDSLLDPDA TEALLELATV VDVITPNIPE LAVLCGEQPA PSFDAAIEQA RRFATDVGTT VIVKGGHLTG PRADNAVVYP DGSVHMVANP RVDTTNSHGT GCSLSAALAT RMGAGHPVDK ALDWATRWLN EALRGADALQ VGSGSGPVDH FAVTRRLLRA ADATPWPHLR MGAPSDGIIT PSDTQSPAPA LAPAGPYTRA LWEATGDVLG EILDSGFIRG LGDGTLSREE FLFYIDQDAH YLRQYSRALA TLSSRAPDAP AQVDWATSAA ECITVEAELH RTYLNKGLAE TGVSAPSPVT MAYTDFLIAR SHADDYVVGA AAVLPCYWLY AEIGLILAKQ NHPEHPYTDW LDTYSGEGFL AGTVKAIARV EAAMAGAGPD QQRVAAQTYL SACVHEREFF DQATRQGWN //