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 05-OCT-2016, entry version 63. DE RecName: Full=Thiamine thiazole synthase {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 RT of the rust fungus Uromyces fabae."; RL Mol. Plant Microbe Interact. 13:629-636(2000). CC -!- FUNCTION: Involved in biosynthesis of the thiamine precursor CC thiazole. Catalyzes the conversion of NAD and glycine to adenosine CC diphosphate 5-(2-hydroxyethyl)-4-methylthiazole-2-carboxylic acid CC (ADT), an adenylated thiazole intermediate. The reaction includes CC an iron-dependent sulfide transfer from a conserved cysteine CC residue of the protein to a thiazole intermediate. The enzyme can CC only undergo a single turnover, which suggests it is a suicide CC enzyme. May have additional roles in adaptation to various stress CC conditions and in DNA damage tolerance. {ECO:0000255|HAMAP- CC Rule:MF_03158, ECO:0000269|PubMed:10830262}. 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- CC 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 CC Cys-221 to a reaction intermediate, generating a dehydroalanine CC residue. {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 ProteinModelPortal; Q9UVF8; -. DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-HAMAP. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro. DR GO; GO:0006950; P:response to stress; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0052837; P:thiazole biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.50.50.60; -; 1. DR HAMAP; MF_03158; THI4; 1. DR InterPro; IPR023753; FAD/NAD-binding_dom. 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. FT CHAIN 1 338 Thiamine thiazole synthase. FT /FTId=PRO_0000034057. FT REGION 112 113 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_03158}. FT REGION 300 302 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_03158}. FT BINDING 91 91 Substrate; via amide nitrogen. FT {ECO:0000255|HAMAP-Rule:MF_03158}. FT BINDING 120 120 Substrate; via amide nitrogen. FT {ECO:0000255|HAMAP-Rule:MF_03158}. FT BINDING 185 185 Substrate; via amide nitrogen and FT carbonyl oxygen. {ECO:0000255|HAMAP- FT Rule:MF_03158}. FT BINDING 223 223 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_03158}. FT BINDING 238 238 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_03158}. FT BINDING 290 290 Substrate; via amide nitrogen. FT {ECO:0000255|HAMAP-Rule:MF_03158}. FT MOD_RES 221 221 2,3-didehydroalanine (Cys). FT {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 //