ID   THI4_POPEU              Reviewed;          48 AA.
AC   P84548;
DT   21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-JUN-2005, sequence version 1.
DT   03-AUG-2022, entry version 43.
DE   RecName: Full=Thiamine thiazole synthase, chloroplastic;
DE            EC=2.4.2.60;
DE   AltName: Full=Thiazole biosynthetic enzyme;
DE   Flags: Fragments;
GN   Name=THI1;
OS   Populus euphratica (Euphrates poplar).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Malpighiales; Salicaceae; Saliceae; Populus.
OX   NCBI_TaxID=75702;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   TISSUE=Leaf;
RX   PubMed=16740589; DOI=10.1093/aob/mcl106;
RA   Ferreira S., Hjernoe K., Larsen M., Wingsle G., Larsen P., Fey S.,
RA   Roepstorff P., Pais M.S.;
RT   "Proteome profiling of Populus euphratica Oliv. upon heat stress.";
RL   Ann. Bot. 98:361-377(2006).
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 (By similarity). {ECO:0000250}.
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; Evidence={ECO:0000250};
CC       Note=Binds 1 Fe cation per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Homooctamer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the THI4 family. {ECO:0000255}.
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DR   AlphaFoldDB; P84548; -.
DR   SMR; P84548; -.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.50.50.60; -; 1.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
PE   1: Evidence at protein level;
KW   Chloroplast; Direct protein sequencing; Iron; Metal-binding; NAD; Plastid;
KW   Thiamine biosynthesis; Transferase.
FT   CHAIN           <1..>48
FT                   /note="Thiamine thiazole synthase, chloroplastic"
FT                   /id="PRO_0000153942"
FT   BINDING         18
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         40
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   NON_CONS        11..12
FT                   /evidence="ECO:0000305"
FT   NON_CONS        27..28
FT                   /evidence="ECO:0000305"
FT   NON_TER         1
FT   NON_TER         48
SQ   SEQUENCE   48 AA;  5125 MW;  62A1E696F7679E47 CRC64;
     FQPIKESIVS RLFNAVAAED LIVKGGREIV PGMIVTGMEV AEIDGAPR