THI41_MAIZE
ID THI41_MAIZE Reviewed; 354 AA.
AC Q41738;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Thiamine thiazole synthase 1, chloroplastic {ECO:0000255|HAMAP-Rule:MF_03158};
DE EC=2.4.2.60 {ECO:0000255|HAMAP-Rule:MF_03158};
DE AltName: Full=Thiazole biosynthetic enzyme 1 {ECO:0000255|HAMAP-Rule:MF_03158};
DE Flags: Precursor;
GN Name=THI1-1 {ECO:0000255|HAMAP-Rule:MF_03158};
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
RC TISSUE=Seedling;
RX PubMed=8541506; DOI=10.1007/bf00041170;
RA Belanger F.C., Leustek T., Chu B., Kriz A.L.;
RT "Evidence for the thiamine biosynthetic pathway in higher-plant plastids
RT and its developmental regulation.";
RL Plant Mol. Biol. 29:809-821(1995).
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:8541506}.
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: Plastid, chloroplast {ECO:0000255|HAMAP-
CC Rule:MF_03158, ECO:0000269|PubMed:8541506}.
CC -!- TISSUE SPECIFICITY: Highest expression in developing embryos and green
CC leaves and a very low level expression seen in endosperm, roots,
CC etiolated shoots and immature ears.
CC -!- DEVELOPMENTAL STAGE: During embryo development, expression increases
CC from 15-21 days after pollination and decreases slightly at day 24 and
CC this level is maintained until day 36.
CC -!- PTM: During the catalytic reaction, a sulfide is transferred from Cys-
CC 222 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}.
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DR EMBL; U17350; AAA96738.1; -; mRNA.
DR PIR; S61419; S61419.
DR RefSeq; NP_001105696.1; NM_001112226.1.
DR AlphaFoldDB; Q41738; -.
DR SMR; Q41738; -.
DR STRING; 4577.GRMZM2G018375_P01; -.
DR PRIDE; Q41738; -.
DR EnsemblPlants; Zm00001eb356910_T003; Zm00001eb356910_P003; Zm00001eb356910.
DR GeneID; 542714; -.
DR Gramene; Zm00001eb356910_T003; Zm00001eb356910_P003; Zm00001eb356910.
DR KEGG; zma:542714; -.
DR MaizeGDB; 128724; -.
DR eggNOG; KOG2960; Eukaryota.
DR OMA; MWGGGMM; -.
DR OrthoDB; 1111148at2759; -.
DR Proteomes; UP000007305; Chromosome 8.
DR ExpressionAtlas; Q41738; baseline and differential.
DR Genevisible; Q41738; ZM.
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:cellular response to DNA damage stimulus; 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; 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 Chloroplast; Iron; Metal-binding; NAD; Plastid; Reference proteome;
KW Thiamine biosynthesis; Transferase; Transit peptide.
FT TRANSIT 1..45
FT /note="Chloroplast"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03158"
FT CHAIN 46..354
FT /note="Thiamine thiazole synthase 1, chloroplastic"
FT /id="PRO_0000034062"
FT BINDING 100
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03158"
FT BINDING 120..121
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03158"
FT BINDING 128
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03158"
FT BINDING 193
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03158"
FT BINDING 224
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03158"
FT BINDING 239
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03158"
FT BINDING 291
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03158"
FT BINDING 301..303
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03158"
FT MOD_RES 222
FT /note="2,3-didehydroalanine (Cys)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03158"
SQ SEQUENCE 354 AA; 37105 MW; 1D27B449CB9294DE CRC64;
MATAAASSLL KSSFAGSRLP AATRTTPASL VVATGPRGAG AGPICASMSM SSSNPPYDLT
SFRFSPIKES IVSREMTRRY MTDMITYADT DVVIVGAGSA GLSCAYELSK DPAVSIAIVE
QSVSPGGGAW LGGQLFSAMV VRKPAHLFLD ELGVAYDEAE DYVVIKHAAL FTSTVMSLLL
ARPNVKLFNA VAVEDLIVRG GRVGGVVTNW ALVSMNHDTQ SCMDPNVMEA KVVVSSCGHD
GPFGATGVKR LQDIGMISAV PGMKALDMNT AEDEIVRLTR EVVPGMIVTG MEVAEIDGAP
RMGPTFGAMM ISGQKAAHLA LKALGRPNAV DGTMSPPLRE ELMIAYKDDE VVDA
