THI4_ARATH
ID THI4_ARATH Reviewed; 349 AA.
AC Q38814;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Thiamine thiazole synthase, chloroplastic {ECO:0000255|HAMAP-Rule:MF_03158};
DE EC=2.4.2.60 {ECO:0000269|PubMed:8790291};
DE AltName: Full=Thiazole biosynthetic enzyme {ECO:0000255|HAMAP-Rule:MF_03158};
DE Flags: Precursor;
GN Name=THI1 {ECO:0000255|HAMAP-Rule:MF_03158}; Synonyms=ARA6, THI4;
GN OrderedLocusNames=At5g54770; ORFNames=MBG8.3;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM CHLOROPLASTIC), FUNCTION, AND CATALYTIC
RP ACTIVITY.
RC STRAIN=cv. Columbia;
RX PubMed=8790291; DOI=10.1007/bf00042231;
RA Machado C.R., de Oliveira R.L., Boiteux S., Praekelt U.M., Meacock P.A.,
RA Menck C.F.;
RT "Thi1, a thiamine biosynthetic gene in Arabidopsis thaliana, complements
RT bacterial defects in DNA repair.";
RL Plant Mol. Biol. 31:585-593(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9330910; DOI=10.1093/dnares/4.3.215;
RA Sato S., Kotani H., Nakamura Y., Kaneko T., Asamizu E., Fukami M.,
RA Miyajima N., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. I. Sequence
RT features of the 1.6 Mb regions covered by twenty physically assigned P1
RT clones.";
RL DNA Res. 4:215-230(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM CHLOROPLASTIC).
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP TISSUE SPECIFICITY.
RX PubMed=8771789; DOI=10.1046/j.1365-313x.1996.10020361.x;
RA Ribeiro A., Praekelt U., Akkermans A.D.L., Meacock P.A., van Kammen A.,
RA Bisseling T., Pawlowski K.;
RT "Identification of agthi1, whose product is involved in biosynthesis of the
RT thiamine precursor thiazole, in actinorhizal nodules of Alnus glutinosa.";
RL Plant J. 10:361-368(1996).
RN [6]
RP SUBCELLULAR LOCATION, AND ALTERNATIVE INITIATION.
RX PubMed=11575719; DOI=10.1023/a:1011628510711;
RA Chabregas S.M., Luche D.D., Farias L.P., Ribeiro A.F., van Sluys M.A.,
RA Menck C.F., Silva-Filho M.C.;
RT "Dual targeting properties of the N-terminal signal sequence of Arabidopsis
RT thaliana THI1 protein to mitochondria and chloroplasts.";
RL Plant Mol. Biol. 46:639-650(2001).
RN [7]
RP ALTERNATIVE INITIATION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF MET-1 AND
RP MET-70.
RX PubMed=12482914; DOI=10.1242/jcs.00228;
RA Chabregas S.M., Luche D.D., Van Sluys M.A., Menck C.F., Silva-Filho M.C.;
RT "Differential usage of two in-frame translational start codons regulates
RT subcellular localization of Arabidopsis thaliana THI1.";
RL J. Cell Sci. 116:285-291(2003).
RN [8]
RP FUNCTION, MUTAGENESIS OF ALA-184, INDUCTION, AND TISSUE SPECIFICITY.
RX PubMed=12941878; DOI=10.1093/pcp/pcg104;
RA Papini-Terzi F.S., Galhardo R.S., Farias L.P., Menck C.F., Van Sluys M.A.;
RT "Point mutation is responsible for Arabidopsis tz-201 mutant phenotype
RT affecting thiamin biosynthesis.";
RL Plant Cell Physiol. 44:856-860(2003).
RN [9]
RP DEVELOPMENTAL STAGE, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=15897230; DOI=10.1093/jxb/eri168;
RA Ribeiro D.T., Farias L.P., de Almeida J.D., Kashiwabara P.M., Ribeiro A.F.,
RA Silva-Filho M.C., Menck C.F., Van Sluys M.A.;
RT "Functional characterization of the thi1 promoter region from Arabidopsis
RT thaliana.";
RL J. Exp. Bot. 56:1797-1804(2005).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RX PubMed=18431481; DOI=10.1371/journal.pone.0001994;
RA Zybailov B., Rutschow H., Friso G., Rudella A., Emanuelsson O., Sun Q.,
RA van Wijk K.J.;
RT "Sorting signals, N-terminal modifications and abundance of the chloroplast
RT proteome.";
RL PLoS ONE 3:E1994-E1994(2008).
RN [11]
RP DIDEHYDROALANINE FORMATION AT CYS-216.
RX PubMed=22031445; DOI=10.1038/nature10503;
RA Chatterjee A., Abeydeera N.D., Bale S., Pai P.J., Dorrestein P.C.,
RA Russell D.H., Ealick S.E., Begley T.P.;
RT "Saccharomyces cerevisiae THI4p is a suicide thiamine thiazole synthase.";
RL Nature 478:542-546(2011).
RN [12]
RP INTERACTION WITH RBCX1 AND RBCX2.
RX PubMed=21922322; DOI=10.1007/s11103-011-9823-8;
RA Kolesinski P., Piechota J., Szczepaniak A.;
RT "Initial characteristics of RbcX proteins from Arabidopsis thaliana.";
RL Plant Mol. Biol. 77:447-459(2011).
RN [13]
RP INDUCTION.
RX PubMed=22214485; DOI=10.1186/1471-2229-12-2;
RA Rapala-Kozik M., Wolak N., Kujda M., Banas A.K.;
RT "The upregulation of thiamine (vitamin B1) biosynthesis in Arabidopsis
RT thaliana seedlings under salt and osmotic stress conditions is mediated by
RT abscisic acid at the early stages of this stress response.";
RL BMC Plant Biol. 12:2-2(2012).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22092075; DOI=10.1021/pr200917t;
RA Aryal U.K., Krochko J.E., Ross A.R.;
RT "Identification of phosphoproteins in Arabidopsis thaliana leaves using
RT polyethylene glycol fractionation, immobilized metal-ion affinity
RT chromatography, two-dimensional gel electrophoresis and mass
RT spectrometry.";
RL J. Proteome Res. 11:425-437(2012).
RN [15]
RP FUNCTION, SUBUNIT, MUTAGENESIS OF ALA-184, AND DIDEHYDROALANINE FORMATION
RP AT CYS-216.
RX PubMed=24637331; DOI=10.1016/j.bbapap.2014.03.005;
RA Garcia A.F., Dyszy F., Munte C.E., Demarco R., Beltramini L.M., Oliva G.,
RA Costa-Filho A.J., Araujo A.P.;
RT "THI1, a protein involved in the biosynthesis of thiamin in Arabidopsis
RT thaliana: structural analysis of THI1(A140V) mutant.";
RL Biochim. Biophys. Acta 1844:1094-1103(2014).
RN [16]
RP FUNCTION, TISSUE SPECIFICITY, INDUCTION BY ABSCISIC ACID AND DROUGHT,
RP SUBCELLULAR LOCATION, INTERACTION WITH CPK33, AND LACK OF PHOSPHORYLATION.
RX PubMed=26662273; DOI=10.1104/pp.15.01649;
RA Li C.L., Wang M., Wu X.M., Chen D.H., Lv H.J., Shen J.L., Qiao Z.,
RA Zhang W.;
RT "THI1, a thiamine thiazole synthase, interacts with Ca2+-dependent protein
RT kinase CPK33 and modulates the S-type anion channels and stomatal closure
RT in Arabidopsis.";
RL Plant Physiol. 170:1090-1104(2016).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 49-328 IN COMPLEX WITH ADT,
RP SUBUNIT, AND MUTAGENESIS OF ASP-77; ASP-85; GLY-121; TRP-124; LYS-172;
RP ALA-184; HIS-211 AND GLU-266.
RX PubMed=16912043; DOI=10.1074/jbc.m604469200;
RA Godoi P.H., Galhardo R.S., Luche D.D., Van Sluys M.A., Menck C.F.,
RA Oliva G.;
RT "Structure of the thiazole biosynthetic enzyme THI1 from Arabidopsis
RT thaliana.";
RL J. Biol. Chem. 281:30957-30966(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. Acts as a positive regulator for the abscisic acid-
CC induced activation of slow type anion channels during stomatal closure
CC by repressing CPK33 kinase activity. {ECO:0000255|HAMAP-Rule:MF_03158,
CC ECO:0000269|PubMed:12941878, ECO:0000269|PubMed:24637331,
CC ECO:0000269|PubMed:26662273, ECO:0000269|PubMed:8790291}.
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 Evidence={ECO:0000269|PubMed:8790291};
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: Homooctomer (PubMed:16912043, PubMed:24637331). Interacts with
CC RBCX1 and RBCX1 (PubMed:21922322). Interacts with CPK33
CC (PubMed:26662273). {ECO:0000269|PubMed:16912043,
CC ECO:0000269|PubMed:21922322, ECO:0000269|PubMed:24637331,
CC ECO:0000269|PubMed:26662273}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:12482914, ECO:0000269|PubMed:18431481,
CC ECO:0000269|PubMed:26662273}. Mitochondrion
CC {ECO:0000269|PubMed:12482914}. Cell membrane
CC {ECO:0000269|PubMed:26662273}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=chloroplastic;
CC IsoId=Q38814-1; Sequence=Displayed;
CC Name=mitochondrial;
CC IsoId=Q38814-2; Sequence=VSP_044533;
CC -!- TISSUE SPECIFICITY: Expressed at high levels in chloroplast-containing
CC parenchymatic cells of leaves, inflorescence shoots and flowers, and at
CC lower levels in the vascular system (PubMed:8771789). In young plants,
CC detected in roots and shoots including cotyledons, leaves and
CC hypocotyls (PubMed:12941878). Also observed in apical meristematic
CC regions, siliques and embryos (PubMed:15897230). Low expression in
CC roots, limited to the vascular tissue (PubMed:15897230). Broadly
CC expressed in roots, cotyledons, leaves, hypocotyls, inflorescences,
CC siliques, and strongly in guard cells (PubMed:26662273).
CC {ECO:0000269|PubMed:12941878, ECO:0000269|PubMed:15897230,
CC ECO:0000269|PubMed:26662273, ECO:0000269|PubMed:8771789}.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout develpoment.
CC {ECO:0000269|PubMed:15897230}.
CC -!- INDUCTION: Up-regulated by osmotic stress, sugar deprivation, high
CC salinity, and hypoxia (PubMed:15897230, PubMed:22214485). Up-regulated
CC by abscisic acid treatment and drought stress (PubMed:22214485,
CC PubMed:26662273). No effect of thiamine, salicylic acid or paraquat
CC treatments (PubMed:12941878, PubMed:22214485). Down-regulated by dark
CC incubation (PubMed:12941878). {ECO:0000269|PubMed:12941878,
CC ECO:0000269|PubMed:15897230, ECO:0000269|PubMed:22214485,
CC ECO:0000269|PubMed:26662273}.
CC -!- PTM: During the catalytic reaction, a sulfide is transferred from Cys-
CC 216 to a reaction intermediate, generating a dehydroalanine residue
CC (PubMed:22031445, PubMed:24637331). Not phosphorylated in vitro by
CC CPK33 (PubMed:26662273). {ECO:0000269|PubMed:22031445,
CC ECO:0000269|PubMed:24637331, ECO:0000269|PubMed:26662273}.
CC -!- MISCELLANEOUS: [Isoform mitochondrial]: Mitochondrial precursor.
CC Contains a mitochondrial presequence-like structure at its N-terminus.
CC {ECO:0000269|PubMed:12482914}.
CC -!- SIMILARITY: Belongs to the THI4 family. {ECO:0000255|HAMAP-
CC Rule:MF_03158}.
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DR EMBL; U17589; AAC97124.1; -; mRNA.
DR EMBL; AB005232; BAB08756.1; -; Genomic_DNA.
DR EMBL; CP002688; AED96539.1; -; Genomic_DNA.
DR EMBL; AF419604; AAL31936.1; -; mRNA.
DR EMBL; AF428355; AAL16285.1; -; mRNA.
DR EMBL; AF428385; AAL16153.1; -; mRNA.
DR EMBL; AY054216; AAL06876.1; -; mRNA.
DR EMBL; AY058094; AAL24202.1; -; mRNA.
DR EMBL; AY143082; AAN12914.1; -; mRNA.
DR PIR; S71191; S71191.
DR RefSeq; NP_200288.1; NM_124858.4. [Q38814-1]
DR PDB; 1RP0; X-ray; 1.60 A; A/B=49-328.
DR PDBsum; 1RP0; -.
DR AlphaFoldDB; Q38814; -.
DR SMR; Q38814; -.
DR BioGRID; 20811; 7.
DR IntAct; Q38814; 1.
DR STRING; 3702.AT5G54770.1; -.
DR iPTMnet; Q38814; -.
DR MetOSite; Q38814; -.
DR PaxDb; Q38814; -.
DR PRIDE; Q38814; -.
DR ProteomicsDB; 234286; -. [Q38814-1]
DR EnsemblPlants; AT5G54770.1; AT5G54770.1; AT5G54770. [Q38814-1]
DR GeneID; 835567; -.
DR Gramene; AT5G54770.1; AT5G54770.1; AT5G54770. [Q38814-1]
DR KEGG; ath:AT5G54770; -.
DR Araport; AT5G54770; -.
DR TAIR; locus:2160130; AT5G54770.
DR eggNOG; KOG2960; Eukaryota.
DR HOGENOM; CLU_053727_1_0_1; -.
DR InParanoid; Q38814; -.
DR OMA; MWGGGMM; -.
DR PhylomeDB; Q38814; -.
DR BioCyc; MetaCyc:AT5G54770-MON; -.
DR BRENDA; 2.4.2.60; 399.
DR EvolutionaryTrace; Q38814; -.
DR PRO; PR:Q38814; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q38814; baseline and differential.
DR Genevisible; Q38814; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-UniRule.
DR GO; GO:0005739; C:mitochondrion; IDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0010319; C:stromule; IDA:TAIR.
DR GO; GO:0009579; C:thylakoid; HDA:TAIR.
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; IPI:CAFA.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:TAIR.
DR GO; GO:0008270; F:zinc ion binding; HDA:TAIR.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IMP:TAIR.
DR GO; GO:0018131; P:oxazole or thiazole biosynthetic process; IGI:TAIR.
DR GO; GO:0009409; P:response to cold; IEP:TAIR.
DR GO; GO:0009228; P:thiamine biosynthetic process; IGI:TAIR.
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 1: Evidence at protein level;
KW 3D-structure; Alternative initiation; Cell membrane; Chloroplast; Iron;
KW Membrane; Metal-binding; Mitochondrion; NAD; Plastid; Reference proteome;
KW Thiamine biosynthesis; Transferase; Transit peptide.
FT TRANSIT 1..45
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 46..349
FT /note="Thiamine thiazole synthase, chloroplastic"
FT /id="PRO_0000034060"
FT BINDING 94
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:16912043,
FT ECO:0007744|PDB:1RP0"
FT BINDING 114..115
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:16912043,
FT ECO:0007744|PDB:1RP0"
FT BINDING 122
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:16912043,
FT ECO:0007744|PDB:1RP0"
FT BINDING 187
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:16912043,
FT ECO:0007744|PDB:1RP0"
FT BINDING 218
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:16912043,
FT ECO:0007744|PDB:1RP0"
FT BINDING 233
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:16912043,
FT ECO:0007744|PDB:1RP0"
FT BINDING 285
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:16912043,
FT ECO:0007744|PDB:1RP0"
FT BINDING 295..297
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:16912043,
FT ECO:0007744|PDB:1RP0"
FT MOD_RES 216
FT /note="2,3-didehydroalanine (Cys)"
FT /evidence="ECO:0000269|PubMed:22031445"
FT VAR_SEQ 1..69
FT /note="Missing (in isoform mitochondrial)"
FT /evidence="ECO:0000305"
FT /id="VSP_044533"
FT MUTAGEN 1
FT /note="M->I: No chloroplastic isoform produced."
FT /evidence="ECO:0000269|PubMed:12482914"
FT MUTAGEN 70
FT /note="M->I: No mitochondrial isoform produced."
FT /evidence="ECO:0000269|PubMed:12482914"
FT MUTAGEN 77
FT /note="D->G: No effect."
FT /evidence="ECO:0000269|PubMed:16912043"
FT MUTAGEN 85
FT /note="D->G: No effect."
FT /evidence="ECO:0000269|PubMed:16912043"
FT MUTAGEN 121
FT /note="G->V: Disrupts thiamine biosynthesis."
FT /evidence="ECO:0000269|PubMed:16912043"
FT MUTAGEN 124
FT /note="W->L: No effect."
FT /evidence="ECO:0000269|PubMed:16912043"
FT MUTAGEN 172
FT /note="K->M: No effect."
FT /evidence="ECO:0000269|PubMed:16912043"
FT MUTAGEN 184
FT /note="A->V: In tz-201; disrupts thiamine biosynthesis,
FT decreases the overall protein stability and the speed of
FT the catalytic activity, but has no effect on the octomeric
FT structure."
FT /evidence="ECO:0000269|PubMed:12941878,
FT ECO:0000269|PubMed:16912043, ECO:0000269|PubMed:24637331"
FT MUTAGEN 211
FT /note="H->F: Disrupts thiamine biosynthesis and DNA damage
FT tolerance activity."
FT /evidence="ECO:0000269|PubMed:16912043"
FT MUTAGEN 266
FT /note="E->G: Disrupts thiamine biosynthesis."
FT /evidence="ECO:0000269|PubMed:16912043"
FT HELIX 63..81
FT /evidence="ECO:0007829|PDB:1RP0"
FT STRAND 83..89
FT /evidence="ECO:0007829|PDB:1RP0"
FT HELIX 93..103
FT /evidence="ECO:0007829|PDB:1RP0"
FT STRAND 110..118
FT /evidence="ECO:0007829|PDB:1RP0"
FT TURN 121..124
FT /evidence="ECO:0007829|PDB:1RP0"
FT STRAND 133..136
FT /evidence="ECO:0007829|PDB:1RP0"
FT TURN 137..139
FT /evidence="ECO:0007829|PDB:1RP0"
FT HELIX 140..146
FT /evidence="ECO:0007829|PDB:1RP0"
FT STRAND 154..160
FT /evidence="ECO:0007829|PDB:1RP0"
FT HELIX 162..174
FT /evidence="ECO:0007829|PDB:1RP0"
FT STRAND 179..183
FT /evidence="ECO:0007829|PDB:1RP0"
FT STRAND 185..193
FT /evidence="ECO:0007829|PDB:1RP0"
FT STRAND 196..204
FT /evidence="ECO:0007829|PDB:1RP0"
FT HELIX 205..208
FT /evidence="ECO:0007829|PDB:1RP0"
FT TURN 211..213
FT /evidence="ECO:0007829|PDB:1RP0"
FT STRAND 220..229
FT /evidence="ECO:0007829|PDB:1RP0"
FT STRAND 233..235
FT /evidence="ECO:0007829|PDB:1RP0"
FT TURN 236..239
FT /evidence="ECO:0007829|PDB:1RP0"
FT HELIX 240..247
FT /evidence="ECO:0007829|PDB:1RP0"
FT STRAND 250..252
FT /evidence="ECO:0007829|PDB:1RP0"
FT STRAND 258..260
FT /evidence="ECO:0007829|PDB:1RP0"
FT HELIX 262..272
FT /evidence="ECO:0007829|PDB:1RP0"
FT STRAND 274..277
FT /evidence="ECO:0007829|PDB:1RP0"
FT STRAND 280..282
FT /evidence="ECO:0007829|PDB:1RP0"
FT HELIX 285..291
FT /evidence="ECO:0007829|PDB:1RP0"
FT HELIX 301..317
FT /evidence="ECO:0007829|PDB:1RP0"
FT TURN 323..326
FT /evidence="ECO:0007829|PDB:1RP0"
SQ SEQUENCE 349 AA; 36664 MW; F872AB061A23CB22 CRC64;
MAAIASTLSL SSTKPQRLFD SSFHGSAISA APISIGLKPR SFSVRATTAG YDLNAFTFDP
IKESIVSREM TRRYMTDMIT YAETDVVVVG AGSAGLSAAY EISKNPNVQV AIIEQSVSPG
GGAWLGGQLF SAMIVRKPAH LFLDEIGVAY DEQDTYVVVK HAALFTSTIM SKLLARPNVK
LFNAVAAEDL IVKGNRVGGV VTNWALVAQN HHTQSCMDPN VMEAKIVVSS CGHDGPFGAT
GVKRLKSIGM IDHVPGMKAL DMNTAEDAIV RLTREVVPGM IVTGMEVAEI DGAPRMGPTF
GAMMISGQKA GQLALKALGL PNAIDGTLVG NLSPELVLAA ADSAETVDA
