ID THI4_UROFA Reviewed; 338 AA. AC Q9UVF8; DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 1. DT 03-AUG-2022, entry version 78. DE RecName: Full=Thiamine thiazole synthase {ECO:0000255|HAMAP-Rule:MF_03158}; DE EC=2.4.2.60 {ECO:0000255|HAMAP-Rule:MF_03158}; DE AltName: Full=Planta-induced protein 4; DE AltName: Full=Thiazole biosynthetic enzyme {ECO:0000255|HAMAP-Rule:MF_03158}; GN Name=THI2; Synonyms=PIG4; OS Uromyces fabae (Rust fungus). OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina; OC Pucciniomycetes; Pucciniales; Pucciniaceae; Uromyces. OX NCBI_TaxID=55588; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND TISSUE SPECIFICITY. RX PubMed=10830262; DOI=10.1094/mpmi.2000.13.6.629; RA Sohn J., Voegele R.T., Mendgen K., Hahn M.; RT "High level activation of vitamin B1 biosynthesis genes in haustoria of the RT rust fungus Uromyces fabae."; RL Mol. Plant Microbe Interact. 13:629-636(2000). CC -!- FUNCTION: Involved in biosynthesis of the thiamine precursor thiazole. CC Catalyzes the conversion of NAD and glycine to adenosine diphosphate 5- CC (2-hydroxyethyl)-4-methylthiazole-2-carboxylic acid (ADT), an CC adenylated thiazole intermediate. The reaction includes an iron- CC dependent sulfide transfer from a conserved cysteine residue of the CC protein to a thiazole intermediate. The enzyme can only undergo a CC single turnover, which suggests it is a suicide enzyme. May have CC additional roles in adaptation to various stress conditions and in DNA CC damage tolerance. {ECO:0000255|HAMAP-Rule:MF_03158, CC ECO:0000269|PubMed:10830262}. CC -!- CATALYTIC ACTIVITY: CC Reaction=[ADP-thiazole synthase]-L-cysteine + glycine + NAD(+) = [ADP- CC thiazole synthase]-dehydroalanine + ADP-5-ethyl-4-methylthiazole-2- CC carboxylate + 2 H(+) + 3 H2O + nicotinamide; Xref=Rhea:RHEA:55708, CC Rhea:RHEA-COMP:14264, Rhea:RHEA-COMP:14265, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17154, ChEBI:CHEBI:29950, CC ChEBI:CHEBI:57305, ChEBI:CHEBI:57540, ChEBI:CHEBI:90873, CC ChEBI:CHEBI:139151; EC=2.4.2.60; Evidence={ECO:0000255|HAMAP- CC Rule:MF_03158}; CC -!- COFACTOR: CC Name=Fe cation; Xref=ChEBI:CHEBI:24875; CC Evidence={ECO:0000255|HAMAP-Rule:MF_03158}; CC Note=Binds 1 Fe cation per subunit. {ECO:0000255|HAMAP-Rule:MF_03158}; CC -!- SUBUNIT: Homooctamer. {ECO:0000255|HAMAP-Rule:MF_03158}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03158}. CC Nucleus {ECO:0000255|HAMAP-Rule:MF_03158}. CC -!- TISSUE SPECIFICITY: Highly expressed in haustoria, and only in low CC amounts in intercellular hyphae. Found in the basal hyphae of the CC uredia, but not in the pedicels and only at very low levels in CC uredospores. {ECO:0000269|PubMed:10830262}. CC -!- PTM: During the catalytic reaction, a sulfide is transferred from Cys- CC 221 to a reaction intermediate, generating a dehydroalanine residue. CC {ECO:0000255|HAMAP-Rule:MF_03158}. CC -!- SIMILARITY: Belongs to the THI4 family. {ECO:0000255|HAMAP- CC Rule:MF_03158}. 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; AJ250427; CAB59856.1; -; Genomic_DNA. DR AlphaFoldDB; Q9UVF8; -. DR SMR; Q9UVF8; -. DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-UniRule. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0016763; F:pentosyltransferase activity; IEA:UniProtKB-UniRule. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-UniRule. DR GO; GO:0052837; P:thiazole biosynthetic process; IEA:UniProtKB-UniRule. DR Gene3D; 3.50.50.60; -; 1. DR HAMAP; MF_03158; THI4; 1. DR InterPro; IPR036188; FAD/NAD-bd_sf. DR InterPro; IPR027495; Sti35. DR InterPro; IPR002922; Thi4_fam. DR SUPFAM; SSF51905; SSF51905; 1. DR TIGRFAMs; TIGR00292; TIGR00292; 1. PE 2: Evidence at transcript level; KW Cytoplasm; Iron; Metal-binding; NAD; Nucleus; Thiamine biosynthesis; KW Transferase. FT CHAIN 1..338 FT /note="Thiamine thiazole synthase" FT /id="PRO_0000034057" FT REGION 1..43 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1..39 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 91 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03158" FT BINDING 112..113 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03158" FT BINDING 120 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03158" FT BINDING 185 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03158" FT BINDING 223 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03158" FT BINDING 238 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03158" FT BINDING 290 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03158" FT BINDING 300..302 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03158" FT MOD_RES 221 FT /note="2,3-didehydroalanine (Cys)" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03158" SQ SEQUENCE 338 AA; 36213 MW; C3F9611094861230 CRC64; MSPVATESMY KPTTINQTAH QQAMDPLKSK QQSNATVNKP AFKPEPAVNL TPIKFAPIKE HQVQRAMVRR YFQDMEERAI SDVIIVGAGS AGLSCAYALG TARPDLKITI LESNVAPGGG CWLGGQLMSA MVCRKPADEF LDQVGVPYED EGNFVVVKHA ALFTSTVLSK VLAMPNVKMF NATACEDLII KPCPINPGVQ RIAGCVTNWT LVSLNHDHQS CMDPSTITAP LVCSFAGHDG PFGAFCVKRV ASAGLSEGLG DMRPLDMERA EDHIANKTRE ILPGLIVGGM ELSEFDGSAR MGPTFGAMLL SGKRAAEVAL QSLDRVKIEE GEVVGLAK //