AC MF_03158; DC Protein; auto TR HAMAP; MF_03158; -; 1; level=0 XX Names: THI4 XX ID THI4 case DE RecName: Full=Thiamine thiazole synthase, chloroplastic; DE AltName: Full=Thiazole biosynthetic enzyme; DE EC=2.4.2.60; else DE RecName: Full=Thiamine thiazole synthase; DE AltName: Full=Thiazole biosynthetic enzyme; DE EC=2.4.2.60; end case case GN Name=THI4; else case GN Name=thiA; else case GN Name=THI1; end case XX 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. 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; CC -!- COFACTOR: CC Name=Fe cation; Xref=ChEBI:CHEBI:24875; CC Note=Binds 1 Fe cation per subunit.; CC -!- SUBUNIT: Homooctamer. case CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast. else CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. end case CC -!- PTM: During the catalytic reaction, a sulfide is transferred from CC #{Cys-205} to a reaction intermediate, generating a dehydroalanine CC residue. case and not CC -!- MISCELLANEOUS: This protein may be expected to contain an N-terminal CC transit peptide but none has been predicted. end case CC -!- SIMILARITY: Belongs to the THI4 family. XX DR PRINTS; PR00368; FADPNR; 1; trigger=no DR NCBIfam; TIGR00292; TIGR00292; 1; trigger=no case DR General; TransitC; -; 0-1; trigger=yes end case XX case KW Chloroplast KW Plastid else KW Cytoplasm KW Nucleus end case KW Iron KW Metal-binding KW NAD KW Thiamine biosynthesis KW Transferase XX GO GO:0005506; F:iron ion binding GO GO:0016763; F:pentosyltransferase activity GO GO:0005829; C:cytosol case GO GO:0009570; C:chloroplast stroma end case GO GO:0009228; P:thiamine biosynthetic process GO GO:0052837; P:thiazole biosynthetic process XX FT From: THI4_YEAST (P32318) FT BINDING 97..98 FT /ligand="substrate" FT Condition: E-x FT BINDING 301..303 FT /ligand="substrate" FT Condition: R-M-x FT BINDING 76 FT /ligand="substrate" FT BINDING 105 FT /ligand="substrate" FT BINDING 170 FT /ligand="substrate" FT BINDING 207 FT /ligand="substrate" FT Condition: D FT BINDING 237 FT /ligand="substrate" FT Condition: H FT BINDING 291 FT /ligand="substrate" FT MOD_RES 205 FT /note="2,3-didehydroalanine (Cys)" FT Condition: C XX Size: 283-383; Related: None; Template: P32318; Q38814; Q1K6I4; Scope: Eukaryota Fusion: Nter: None Cter: None Duplicate: in 9HYPO, MAIZE, ORYSJ, PHYPA, POPTR, PSEMZ, SELML, SORBI, SOYBN, VITVI, VOLCA Plasmid: None Comments: None XX # Revision 1.12 2023/06/01 //