ID A0A0E0AKT3_9ORYZ Unreviewed; 352 AA.
AC A0A0E0AKT3;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE RecName: Full=Thiamine thiazole synthase, chloroplastic {ECO:0000256|HAMAP-Rule:MF_03158};
DE AltName: Full=Thiazole biosynthetic enzyme {ECO:0000256|HAMAP-Rule:MF_03158};
DE EC=2.4.2.60 {ECO:0000256|HAMAP-Rule:MF_03158};
GN Name=THI1 {ECO:0000256|HAMAP-Rule:MF_03158};
OS Oryza glumipatula.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=40148 {ECO:0000313|EnsemblPlants:OGLUM07G16600.1};
RN [1] {ECO:0000313|EnsemblPlants:OGLUM07G16600.1}
RP NUCLEOTIDE SEQUENCE.
RA Wing R.A., Panaud O., Oliveira A.C.;
RT "Oryza genome evolution.";
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:OGLUM07G16600.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (APR-2015) to UniProtKB.
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:0000256|HAMAP-Rule:MF_03158}.
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:0000256|HAMAP-
CC Rule:MF_03158};
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_03158};
CC Note=Binds 1 Fe cation per subunit. {ECO:0000256|HAMAP-Rule:MF_03158};
CC -!- SUBUNIT: Homooctamer. {ECO:0000256|HAMAP-Rule:MF_03158}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000256|HAMAP-
CC Rule:MF_03158}.
CC -!- PTM: During the catalytic reaction, a sulfide is transferred from Cys-
CC 218 to a reaction intermediate, generating a dehydroalanine residue.
CC {ECO:0000256|HAMAP-Rule:MF_03158}.
CC -!- SIMILARITY: Belongs to the THI4 family. {ECO:0000256|HAMAP-
CC Rule:MF_03158}.
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DR AlphaFoldDB; A0A0E0AKT3; -.
DR STRING; 40148.A0A0E0AKT3; -.
DR EnsemblPlants; OGLUM07G16600.1; OGLUM07G16600.1; OGLUM07G16600.
DR Gramene; OGLUM07G16600.1; OGLUM07G16600.1; OGLUM07G16600.
DR eggNOG; KOG2960; Eukaryota.
DR HOGENOM; CLU_053727_1_0_1; -.
DR Proteomes; UP000026961; Unassembled WGS sequence.
DR GO; GO:0009570; C:chloroplast stroma; IEA:UniProtKB-UniRule.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-UniRule.
DR GO; GO:0005739; C:mitochondrion; IEA:EnsemblPlants.
DR GO; GO:0010319; C:stromule; IEA:EnsemblPlants.
DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016763; F:pentosyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0019904; F:protein domain specific binding; IEA:EnsemblPlants.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:EnsemblPlants.
DR GO; GO:0006974; P:DNA damage response; IEA:EnsemblPlants.
DR GO; GO:0009409; P:response to cold; IEA:EnsemblPlants.
DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0052837; P:thiazole biosynthetic process; IEA:UniProtKB-UniRule.
DR Gene3D; 6.10.250.2840; -; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR HAMAP; MF_03158; THI4; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR027495; Sti35.
DR InterPro; IPR002922; Thi4_fam.
DR NCBIfam; TIGR00292; sulfide-dependent adenosine diphosphate thiazole synthase; 1.
DR PANTHER; PTHR43422; THIAMINE THIAZOLE SYNTHASE; 1.
DR PANTHER; PTHR43422:SF16; THIAMINE THIAZOLE SYNTHASE 1, CHLOROPLASTIC; 1.
DR Pfam; PF01946; Thi4; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 3: Inferred from homology;
KW Chloroplast {ECO:0000256|HAMAP-Rule:MF_03158};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|HAMAP-Rule:MF_03158};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_03158}; NAD {ECO:0000256|HAMAP-Rule:MF_03158};
KW Plastid {ECO:0000256|HAMAP-Rule:MF_03158};
KW Reference proteome {ECO:0000313|Proteomes:UP000026961};
KW Thiamine biosynthesis {ECO:0000256|ARBA:ARBA00022977, ECO:0000256|HAMAP-
KW Rule:MF_03158}; Transferase {ECO:0000256|HAMAP-Rule:MF_03158}.
FT BINDING 96
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03158"
FT BINDING 116..117
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03158"
FT BINDING 124
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03158"
FT BINDING 189
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03158"
FT BINDING 220
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03158"
FT BINDING 235
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03158"
FT BINDING 287
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03158"
FT BINDING 297..299
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03158"
FT MOD_RES 218
FT /note="2,3-didehydroalanine (Cys)"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03158"
SQ SEQUENCE 352 AA; 37012 MW; 2B14B957670C5254 CRC64;
MAAMATTASS LLKTSFAGAR LPAAARNPTV SVAPRTGGAI CNSISSSSST PPYDLNAIRF
SPIKESIVSR EMTRRYMTDM ITYADTDVVV VGAGSAGLSC AYELSKDPSV SVAVIEQSVS
PGGGAWLGGQ LFSAMVVRKP AHLFLDELGV AYDEQEDYVV IKHAALFTST VMSRLLARPN
VKLFNAVAVE DLIVKEGRVG GVVTNWALVS MNHDTQSCMD PNVMESRVVV SSCGHDGPFG
ATGVKRLQDI GMIDAVPGMR ALDMNTAEDE IVRLTREVVP GMIVTGMEVA EIDGAPRMGP
TFGAMMISGQ KAAHLALKAL GRPNAIDGTI KKAAAHPELI LASKDDGEIV DA
//
