Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Thiamine thiazole synthase, chloroplastic

Gene

THI1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

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. Acts as a positive regulator for the abscisic acid-induced activation of slow type anion channels during stomatal closure by repressing CPK33 kinase activity.UniRule annotation4 Publications

Cofactori

Fe cationUniRule annotationNote: Binds 1 Fe cation per subunit.UniRule annotation

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei94Substrate; via amide nitrogen1
Binding sitei122Substrate; via amide nitrogen1
Binding sitei187Substrate; via amide nitrogen and carbonyl oxygen1
Binding sitei218Substrate1
Binding sitei233Substrate1
Binding sitei285Substrate; via amide nitrogen1

GO - Molecular functioni

  • iron ion binding Source: GO_Central
  • protein domain specific binding Source: CAFA
  • protein homodimerization activity Source: TAIR
  • zinc ion binding Source: TAIR

GO - Biological processi

  • cellular response to DNA damage stimulus Source: TAIR
  • oxazole or thiazole biosynthetic process Source: TAIR
  • response to cold Source: TAIR
  • thiamine biosynthetic process Source: TAIR
  • thiazole biosynthetic process Source: GO_Central

Keywordsi

Biological processThiamine biosynthesis
LigandIron, Metal-binding, NAD

Enzyme and pathway databases

BioCyciMetaCyc:AT5G54770-MONOMER

Names & Taxonomyi

Protein namesi
Recommended name:
Thiamine thiazole synthase, chloroplasticUniRule annotation
Alternative name(s):
Thiazole biosynthetic enzymeUniRule annotation
Gene namesi
Name:THI1UniRule annotation
Synonyms:ARA6, THI4
Ordered Locus Names:At5g54770
ORF Names:MBG8.3
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 5

Organism-specific databases

AraportiAT5G54770
TAIRilocus:2160130 AT5G54770

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Chloroplast Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertion Graphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell membrane, Chloroplast, Membrane, Mitochondrion, Plastid

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi1M → I: No chloroplastic isoform produced. 1 Publication1
Mutagenesisi70M → I: No mitochondrial isoform produced. 1 Publication1
Mutagenesisi77D → G: No effect. 1 Publication1
Mutagenesisi85D → G: No effect. 1 Publication1
Mutagenesisi121G → V: Disrupts thiamine biosynthesis. 1 Publication1
Mutagenesisi124W → L: No effect. 1 Publication1
Mutagenesisi172K → M: No effect. 1 Publication1
Mutagenesisi184A → V in tz-201; disrupts thiamine biosynthesis, decreases the overall protein stability and the speed of the catalytic activity, but has no effect on the octomeric structure. 3 Publications1
Mutagenesisi211H → F: Disrupts thiamine biosynthesis and DNA damage tolerance activity. 1 Publication1
Mutagenesisi266E → G: Disrupts thiamine biosynthesis. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 55ChloroplastAdd BLAST55
ChainiPRO_000003406056 – 349Thiamine thiazole synthase, chloroplasticAdd BLAST294

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2162,3-didehydroalanine (Cys)1 Publication1

Post-translational modificationi

During the catalytic reaction, a sulfide is transferred from Cys-216 to a reaction intermediate, generating a dehydroalanine residue (PubMed:22031445, PubMed:24637331). Not phosphorylated in vitro by CPK33 (PubMed:26662273).3 Publications

Proteomic databases

PaxDbiQ38814
PRIDEiQ38814

PTM databases

iPTMnetiQ38814

Expressioni

Tissue specificityi

Expressed at high levels in chloroplast-containing parenchymatic cells of leaves, inflorescence shoots and flowers, and at lower levels in the vascular system (PubMed:8771789). In young plants, detected in roots and shoots including cotyledons, leaves and hypocotyls (PubMed:12941878). Also observed in apical meristematic regions, siliques and embryos (PubMed:15897230). Low expression in roots, limited to the vascular tissue (PubMed:15897230). Broadly expressed in roots, cotyledons, leaves, hypocotyls, inflorescences, siliques, and strongly in guard cells (PubMed:26662273).4 Publications

Developmental stagei

Expressed throughout develpoment.1 Publication

Inductioni

Up-regulated by osmotic stress, sugar deprivation, high salinity, and hypoxia (PubMed:15897230, PubMed:22214485). Up-regulated by abscisic acid treatment and drought stress (PubMed:22214485, PubMed:26662273). No effect of thiamine, salicylic acid or paraquat treatments (PubMed:12941878, PubMed:22214485). Down-regulated by dark incubation (PubMed:12941878).4 Publications

Gene expression databases

ExpressionAtlasiQ38814 baseline and differential
GenevisibleiQ38814 AT

Interactioni

Subunit structurei

Homooctomer (PubMed:16912043, PubMed:24637331). Interacts with RBCX1 and RBCX1 (PubMed:21922322). Interacts with CPK33 (PubMed:26662273).4 Publications

GO - Molecular functioni

  • protein domain specific binding Source: CAFA
  • protein homodimerization activity Source: TAIR

Protein-protein interaction databases

BioGridi20811, 6 interactors
IntActiQ38814, 1 interactor
STRINGi3702.AT5G54770.1

Structurei

Secondary structure

1349
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi63 – 81Combined sources19
Beta strandi83 – 89Combined sources7
Helixi93 – 103Combined sources11
Beta strandi110 – 118Combined sources9
Turni121 – 124Combined sources4
Beta strandi133 – 136Combined sources4
Turni137 – 139Combined sources3
Helixi140 – 146Combined sources7
Beta strandi154 – 160Combined sources7
Helixi162 – 174Combined sources13
Beta strandi179 – 183Combined sources5
Beta strandi185 – 193Combined sources9
Beta strandi196 – 204Combined sources9
Helixi205 – 208Combined sources4
Turni211 – 213Combined sources3
Beta strandi220 – 229Combined sources10
Beta strandi233 – 235Combined sources3
Turni236 – 239Combined sources4
Helixi240 – 247Combined sources8
Beta strandi250 – 252Combined sources3
Beta strandi258 – 260Combined sources3
Helixi262 – 272Combined sources11
Beta strandi274 – 277Combined sources4
Beta strandi280 – 282Combined sources3
Helixi285 – 291Combined sources7
Helixi301 – 317Combined sources17
Turni323 – 326Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1RP0X-ray1.60A/B49-328[»]
ProteinModelPortaliQ38814
SMRiQ38814
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ38814

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni114 – 115Substrate binding2
Regioni295 – 297Substrate binding3

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi86 – 89Poly-Val4

Sequence similaritiesi

Belongs to the THI4 family.UniRule annotation

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG2960 Eukaryota
COG1635 LUCA
HOGENOMiHOG000106048
InParanoidiQ38814
KOiK03146
OMAiMWGGGMM
OrthoDBiEOG09360HDE
PhylomeDBiQ38814

Family and domain databases

Gene3Di3.50.50.60, 1 hit
HAMAPiMF_03158 THI4, 1 hit
InterProiView protein in InterPro
IPR036188 FAD/NAD-bd_sf
IPR027495 Sti35
IPR002922 Thi4_fam
SUPFAMiSSF51905 SSF51905, 1 hit
TIGRFAMsiTIGR00292 TIGR00292, 1 hit

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative initiation. AlignAdd to basket

Isoform chloroplastic (identifier: Q38814-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MAAIASTLSL SSTKPQRLFD SSFHGSAISA APISIGLKPR SFSVRATTAG
60 70 80 90 100
YDLNAFTFDP IKESIVSREM TRRYMTDMIT YAETDVVVVG AGSAGLSAAY
110 120 130 140 150
EISKNPNVQV AIIEQSVSPG GGAWLGGQLF SAMIVRKPAH LFLDEIGVAY
160 170 180 190 200
DEQDTYVVVK HAALFTSTIM SKLLARPNVK LFNAVAAEDL IVKGNRVGGV
210 220 230 240 250
VTNWALVAQN HHTQSCMDPN VMEAKIVVSS CGHDGPFGAT GVKRLKSIGM
260 270 280 290 300
IDHVPGMKAL DMNTAEDAIV RLTREVVPGM IVTGMEVAEI DGAPRMGPTF
310 320 330 340
GAMMISGQKA GQLALKALGL PNAIDGTLVG NLSPELVLAA ADSAETVDA
Length:349
Mass (Da):36,664
Last modified:November 1, 1996 - v1
Checksum:iF872AB061A23CB22
GO
Isoform mitochondrial (identifier: Q38814-2) [UniParc]FASTAAdd to basket

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.1 Publication
Show »
Length:280
Mass (Da):29,362
Checksum:iF7CBEDD149301E40
GO

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0445331 – 69Missing in isoform mitochondrial. CuratedAdd BLAST69

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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
PIRiS71191
RefSeqiNP_200288.1, NM_124858.4 [Q38814-1]
UniGeneiAt.24888

Genome annotation databases

EnsemblPlantsiAT5G54770.1; AT5G54770.1; AT5G54770 [Q38814-1]
GeneIDi835567
GrameneiAT5G54770.1; AT5G54770.1; AT5G54770 [Q38814-1]
KEGGiath:AT5G54770

Keywords - Coding sequence diversityi

Alternative initiation

Similar proteinsi

Entry informationi

Entry nameiTHI4_ARATH
AccessioniPrimary (citable) accession number: Q38814
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: April 25, 2018
This is version 139 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Cookie policy

We would like to use anonymized google analytics cookies to gather statistics on how uniprot.org is used in aggregate. Learn more

UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health