Q38814 (THI4_ARATH) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 100.
History...
Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Thiamine thiazole synthase, chloroplastic Alternative name(s): Thiazole biosynthetic enzyme | ||||||||
| Gene names |
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| Organism | Arabidopsis thaliana (Mouse-ear cress) [Reference proteome] | ||||||||
| Taxonomic identifier | 3702 [NCBI] | ||||||||
| Taxonomic lineage | Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis![]() |
Protein attributes
| Sequence length | 349 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Involved in biosynthesis of the thiamine precursor thiazole. Catalyzes the conversion of NAD and glycine to adenosine diphosphate 5-(2-hydroxyethyl)-4-methylthiazole-2-carboxylic acid (ADT), an adenylated thiazole intermediate. The reaction includes an iron-dependent sulfide transfer from a conserved cysteine residue of the protein to a thiazole intermediate. The enzyme can only undergo a single turnover, which suggests it is a suicide enzyme. May have additional roles in adaptation to various stress conditions and in DNA damage tolerance. Ref.1 Ref.9 |
| Cofactor | Binds 1 iron ion per subunit By similarity. |
| Subunit structure | Homooctamer. Ref.18 |
| Subcellular location | Plastid › chloroplast. Mitochondrion Ref.6 Ref.7 Ref.8 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15. |
| Tissue specificity | Expressed at high levels in chloroplast-containing parenchymatic cells of leaves, inflorescence shoots and flowers, and at lower levels in the vascular system. In young plants, detected in roots and shoots including cotyledons, leaves and hypocotyls. Also observed in apical meristematic regions, siliques and embryos. Low expression in roots, limited to the vascular tissue. Ref.5 Ref.9 Ref.10 |
| Developmental stage | Expressed throughout develpoment. Ref.10 |
| Induction | Up-regulated by osmotic and salt stresses and by abscisic acid treatment. No effect of thiamine, salicylic acid or paraquat treatments. Down-regulated by dark incubation. Ref.9 Ref.10 Ref.17 |
| Post-translational modification | During the catalytic reaction, a sulfide is transferred from Cys-216 to a reaction intermediate, generating a dehydroalanine residue. HAMAP-Rule MF_03158 |
| Sequence similarities | Belongs to the THI4 family. |
Ontologies
Alternative products
| This entry describes 2 isoforms produced by alternative initiation. [Align] [Select] | ||||||
| Isoform chloroplastic (identifier: Q38814-1) This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry. | ||||||
| Isoform mitochondrial (identifier: Q38814-2) The sequence of this isoform differs from the canonical sequence as follows: 1-69: Missing. | ||||||
| Note: Mitochondrial precursor. Contains a mitochondrial presequence-like structure at its N-terminus. |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | |||||||||||||||||||||||||||||||||||||||||||||||||||||
Molecule processing | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Transit peptide | 1 – 55 | 55 | Chloroplast HAMAP-Rule MF_03158 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Chain | 56 – 349 | 294 | Thiamine thiazole synthase, chloroplastic HAMAP-Rule MF_03158 | PRO_0000034060 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
Regions | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Region | 114 – 115 | 2 | Substrate binding HAMAP-Rule MF_03158 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Region | 295 – 297 | 3 | Substrate binding HAMAP-Rule MF_03158 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Compositional bias | 86 – 89 | 4 | Poly-Val HAMAP-Rule MF_03158 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||
Sites | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Binding site | 94 | 1 | Substrate; via amide nitrogen | |||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Binding site | 122 | 1 | Substrate; via amide nitrogen | |||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Binding site | 187 | 1 | Substrate; via amide nitrogen and carbonyl oxygen | |||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Binding site | 218 | 1 | Substrate | |||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Binding site | 233 | 1 | Substrate | |||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Binding site | 285 | 1 | Substrate; via amide nitrogen | |||||||||||||||||||||||||||||||||||||||||||||||||||||||
Amino acid modifications | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Modified residue | 216 | 1 | 2,3-didehydroalanine (Cys) HAMAP-Rule MF_03158 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||
Natural variations | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Alternative sequence | 1 – 69 | 69 | Missing in isoform mitochondrial. | VSP_044533 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
Experimental info | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Mutagenesis | 1 | 1 | M → I: No chloroplastic isoform produced. Ref.7 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Mutagenesis | 70 | 1 | M → I: No mitochondrial isoform produced. Ref.7 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Mutagenesis | 77 | 1 | D → G: No effect. Ref.18 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Mutagenesis | 85 | 1 | D → G: No effect. Ref.18 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Mutagenesis | 121 | 1 | G → V: Disrupts thiamine biosynthesis. Ref.18 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Mutagenesis | 124 | 1 | W → L: No effect. Ref.18 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Mutagenesis | 172 | 1 | K → M: No effect. Ref.18 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Mutagenesis | 184 | 1 | A → V in tz-201; disrupts thiamine biosynthesis. Ref.9 Ref.18 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Mutagenesis | 211 | 1 | H → F: Disrupts thiamine biosynthesis and DNA damage tolerance activity. Ref.18 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Mutagenesis | 266 | 1 | E → G: Disrupts thiamine biosynthesis. Ref.18 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||
Secondary structure | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Helix Strand Turn | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 63 – 81 | 19 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 83 – 89 | 7 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 93 – 103 | 11 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 110 – 118 | 9 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Turn | 121 – 124 | 4 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 133 – 136 | 4 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Turn | 137 – 139 | 3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 140 – 146 | 7 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 154 – 160 | 7 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 162 – 174 | 13 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 179 – 183 | 5 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 185 – 193 | 9 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 196 – 204 | 9 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 205 – 208 | 4 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Turn | 211 – 213 | 3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 220 – 229 | 10 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 233 – 235 | 3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Turn | 236 – 239 | 4 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 240 – 247 | 8 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 250 – 252 | 3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 258 – 260 | 3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 262 – 272 | 11 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 274 – 277 | 4 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 280 – 282 | 3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 285 – 291 | 7 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 301 – 317 | 17 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Turn | 323 – 326 | 4 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Thi1, a thiamine biosynthetic gene in Arabidopsis thaliana, complements bacterial defects in DNA repair." Machado C.R., de Oliveira R.L., Boiteux S., Praekelt U.M., Meacock P.A., Menck C.F. Plant Mol. Biol. 31:585-593(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM CHLOROPLASTIC), FUNCTION. Strain: cv. Columbia. |
| [2] | "Structural analysis of Arabidopsis thaliana chromosome 5. I. Sequence features of the 1.6 Mb regions covered by twenty physically assigned P1 clones." Sato S., Kotani H., Nakamura Y., Kaneko T., Asamizu E., Fukami M., Miyajima N., Tabata S. DNA Res. 4:215-230(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia. |
| [3] | The Arabidopsis Information Resource (TAIR) Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: cv. Columbia. |
| [4] | "Empirical analysis of transcriptional activity in the Arabidopsis genome." Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. Ecker J.R.Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM CHLOROPLASTIC). Strain: cv. Columbia. |
| [5] | "Identification of agthi1, whose product is involved in biosynthesis of the thiamine precursor thiazole, in actinorhizal nodules of Alnus glutinosa." Ribeiro A., Praekelt U., Akkermans A.D.L., Meacock P.A., van Kammen A., Bisseling T., Pawlowski K. Plant J. 10:361-368(1996) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY. |
| [6] | "Dual targeting properties of the N-terminal signal sequence of Arabidopsis thaliana THI1 protein to mitochondria and chloroplasts." Chabregas S.M., Luche D.D., Farias L.P., Ribeiro A.F., van Sluys M.A., Menck C.F., Silva-Filho M.C. Plant Mol. Biol. 46:639-650(2001) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, ALTERNATIVE INITIATION. |
| [7] | "Differential usage of two in-frame translational start codons regulates subcellular localization of Arabidopsis thaliana THI1." Chabregas S.M., Luche D.D., Van Sluys M.A., Menck C.F., Silva-Filho M.C. J. Cell Sci. 116:285-291(2003) [PubMed] [Europe PMC] [Abstract] Cited for: ALTERNATIVE INITIATION, SUBCELLULAR LOCATION, MUTAGENESIS OF MET-1 AND MET-70. |
| [8] | "Proteomic study of the Arabidopsis thaliana chloroplastic envelope membrane utilizing alternatives to traditional two-dimensional electrophoresis." Froehlich J.E., Wilkerson C.G., Ray W.K., McAndrew R.S., Osteryoung K.W., Gage D.A., Phinney B.S. J. Proteome Res. 2:413-425(2003) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY. |
| [9] | "Point mutation is responsible for Arabidopsis tz-201 mutant phenotype affecting thiamin biosynthesis." Papini-Terzi F.S., Galhardo R.S., Farias L.P., Menck C.F., Van Sluys M.A. Plant Cell Physiol. 44:856-860(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF ALA-184, INDUCTION, TISSUE SPECIFICITY. |
| [10] | "Functional characterization of the thi1 promoter region from Arabidopsis thaliana." Ribeiro D.T., Farias L.P., de Almeida J.D., Kashiwabara P.M., Ribeiro A.F., Silva-Filho M.C., Menck C.F., Van Sluys M.A. J. Exp. Bot. 56:1797-1804(2005) [PubMed] [Europe PMC] [Abstract] Cited for: DEVELOPMENTAL STAGE, TISSUE SPECIFICITY, INDUCTION. |
| [11] | "The oligomeric stromal proteome of Arabidopsis thaliana chloroplasts." Peltier J.-B., Cai Y., Sun Q., Zabrouskov V., Giacomelli L., Rudella A., Ytterberg A.J., Rutschow H., van Wijk K.J. Mol. Cell. Proteomics 5:114-133(2006) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY. |
| [12] | "The chloroplast lumen and stromal proteomes of Arabidopsis thaliana show differential sensitivity to short- and long-term exposure to low temperature." Goulas E., Schubert M., Kieselbach T., Kleczkowski L.A., Gardestroem P., Schroeder W., Hurry V. Plant J. 47:720-734(2006) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY. |
| [13] | "Sorting signals, N-terminal modifications and abundance of the chloroplast proteome." Zybailov B., Rutschow H., Friso G., Rudella A., Emanuelsson O., Sun Q., van Wijk K.J. PLoS ONE 3:E1994-E1994(2008) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY. |
| [14] | "AT_CHLORO, a comprehensive chloroplast proteome database with subplastidial localization and curated information on envelope proteins." Ferro M., Brugiere S., Salvi D., Seigneurin-Berny D., Court M., Moyet L., Ramus C., Miras S., Mellal M., Le Gall S., Kieffer-Jaquinod S., Bruley C., Garin J., Joyard J., Masselon C., Rolland N. Mol. Cell. Proteomics 9:1063-1084(2010) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY. |
| [15] | "Megadalton complexes in the chloroplast stroma of Arabidopsis thaliana characterized by size exclusion chromatography, mass spectrometry, and hierarchical clustering." Olinares P.D., Ponnala L., van Wijk K.J. Mol. Cell. Proteomics 9:1594-1615(2010) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY. Strain: cv. Columbia. |
| [16] | "Saccharomyces cerevisiae THI4p is a suicide thiamine thiazole synthase." Chatterjee A., Abeydeera N.D., Bale S., Pai P.J., Dorrestein P.C., Russell D.H., Ealick S.E., Begley T.P. Nature 478:542-546(2011) [PubMed] [Europe PMC] [Abstract] Cited for: DIDEHYDROALANINE FORMATION AT CYS-216. |
| [17] | "The upregulation of thiamine (vitamin B1) biosynthesis in Arabidopsis thaliana seedlings under salt and osmotic stress conditions is mediated by abscisic acid at the early stages of this stress response." Rapala-Kozik M., Wolak N., Kujda M., Banas A.K. BMC Plant Biol. 12:2-2(2012) [PubMed] [Europe PMC] [Abstract] Cited for: INDUCTION. |
| [18] | "Structure of the thiazole biosynthetic enzyme THI1 from Arabidopsis thaliana." Godoi P.H., Galhardo R.S., Luche D.D., Van Sluys M.A., Menck C.F., Oliva G. J. Biol. Chem. 281:30957-30966(2006) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 49-328 IN COMPLEX WITH ADT, SUBUNIT, MUTAGENESIS OF ASP-77; ASP-85; GLY-121; TRP-124; LYS-172; ALA-184; HIS-211 AND GLU-266. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| EMBL GenBank DDBJ | U17589 mRNA. Translation: AAC97124.1. AB005232 Genomic DNA. Translation: BAB08756.1. CP002688 Genomic DNA. Translation: AED96539.1. AF419604 mRNA. Translation: AAL31936.1. AF428355 mRNA. Translation: AAL16285.1. AF428385 mRNA. Translation: AAL16153.1. AY054216 mRNA. Translation: AAL06876.1. AY058094 mRNA. Translation: AAL24202.1. AY143082 mRNA. Translation: AAN12914.1. | ||||||||||||
| IPI | IPI00541324. | ||||||||||||
| PIR | S71191. | ||||||||||||
| RefSeq | NP_200288.1. NM_124858.3. | ||||||||||||
| UniGene | At.24888. | ||||||||||||
3D structure databases | |||||||||||||
| PDBe RCSB PDB PDBj |
| ||||||||||||
| ProteinModelPortal | Q38814. | ||||||||||||
| SMR | Q38814. Positions 51-328. | ||||||||||||
| ModBase | Search... | ||||||||||||
Protein-protein interaction databases | |||||||||||||
| IntAct | Q38814. 1 interaction. | ||||||||||||
| STRING | 3702.AT5G54770.1-P. | ||||||||||||
Proteomic databases | |||||||||||||
| PaxDb | Q38814. | ||||||||||||
| PRIDE | Q38814. | ||||||||||||
Protocols and materials databases | |||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||
Genome annotation databases | |||||||||||||
| EnsemblPlants | AT5G54770.1; AT5G54770.1; AT5G54770. | ||||||||||||
| GeneID | 835567. | ||||||||||||
| KEGG | ath:AT5G54770. | ||||||||||||
Organism-specific databases | |||||||||||||
| TAIR | At5g54770. | ||||||||||||
Phylogenomic databases | |||||||||||||
| eggNOG | COG1635. | ||||||||||||
| HOGENOM | HOG000106048. | ||||||||||||
| InParanoid | Q38814. | ||||||||||||
| KO | K03146. | ||||||||||||
| OMA | CMDPNTI. | ||||||||||||
| PhylomeDB | Q38814. | ||||||||||||
| ProtClustDB | PLN02661. | ||||||||||||
Enzyme and pathway databases | |||||||||||||
| BioCyc | MetaCyc:AT5G54770-MONOMER. | ||||||||||||
Gene expression databases | |||||||||||||
| ArrayExpress | Q38814. | ||||||||||||
| Genevestigator | Q38814. | ||||||||||||
| GermOnline | AT5G54770. Arabidopsis thaliana. | ||||||||||||
Family and domain databases | |||||||||||||
| HAMAP | MF_03158. THI4. | ||||||||||||
| InterPro | IPR002922. Thi4_fam. [Graphical view] | ||||||||||||
| PANTHER | PTHR10617:SF54. PTHR10617:SF54. 1 hit. | ||||||||||||
| TIGRFAMs | TIGR00292. TIGR00292. 1 hit. | ||||||||||||
| ProtoNet | Search... | ||||||||||||
Other | |||||||||||||
| EvolutionaryTrace | Q38814. | ||||||||||||
Entry information
| Entry name | THI4_ARATH | ||||||||
| Accession | Primary (citable) accession number: Q38814 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Plant Protein Annotation Program | ||||||||
Relevant documents
| Arabidopsis thaliana Arabidopsis thaliana: entries and gene names |
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with
