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Q38814

- THI4_ARATH

UniProt

Q38814 - THI4_ARATH

Protein

Thiamine thiazole synthase, chloroplastic

Gene

THI1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 111 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    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.2 PublicationsUniRule annotation

    Cofactori

    Binds 1 iron ion per subunit.UniRule annotation

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei94 – 941Substrate; via amide nitrogen
    Binding sitei122 – 1221Substrate; via amide nitrogen
    Binding sitei187 – 1871Substrate; via amide nitrogen and carbonyl oxygen
    Binding sitei218 – 2181Substrate
    Binding sitei233 – 2331Substrate
    Binding sitei285 – 2851Substrate; via amide nitrogen

    GO - Molecular functioni

    1. protein homodimerization activity Source: TAIR
    2. zinc ion binding Source: TAIR

    GO - Biological processi

    1. cellular response to DNA damage stimulus Source: TAIR
    2. oxazole or thiazole biosynthetic process Source: TAIR
    3. response to cold Source: TAIR
    4. thiamine biosynthetic process Source: TAIR
    5. thiazole biosynthetic process Source: UniProtKB-HAMAP

    Keywords - Biological processi

    Thiamine biosynthesis

    Keywords - Ligandi

    Iron, 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
    ProteomesiUP000006548: Chromosome 5

    Organism-specific databases

    TAIRiAT5G54770.

    Subcellular locationi

    GO - Cellular componenti

    1. chloroplast Source: TAIR
    2. chloroplast envelope Source: TAIR
    3. chloroplast stroma Source: TAIR
    4. cytosol Source: UniProtKB-HAMAP
    5. mitochondrion Source: TAIR
    6. stromule Source: TAIR
    7. thylakoid Source: TAIR

    Keywords - Cellular componenti

    Chloroplast, Mitochondrion, Plastid

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi1 – 11M → I: No chloroplastic isoform produced. 1 Publication
    Mutagenesisi70 – 701M → I: No mitochondrial isoform produced. 1 Publication
    Mutagenesisi77 – 771D → G: No effect. 1 Publication
    Mutagenesisi85 – 851D → G: No effect. 1 Publication
    Mutagenesisi121 – 1211G → V: Disrupts thiamine biosynthesis. 1 Publication
    Mutagenesisi124 – 1241W → L: No effect. 1 Publication
    Mutagenesisi172 – 1721K → M: No effect. 1 Publication
    Mutagenesisi184 – 1841A → V in tz-201; disrupts thiamine biosynthesis. 2 Publications
    Mutagenesisi211 – 2111H → F: Disrupts thiamine biosynthesis and DNA damage tolerance activity. 1 Publication
    Mutagenesisi266 – 2661E → G: Disrupts thiamine biosynthesis. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 5555ChloroplastAdd
    BLAST
    Chaini56 – 349294Thiamine thiazole synthase, chloroplasticPRO_0000034060Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei216 – 21612,3-didehydroalanine (Cys)

    Post-translational modificationi

    During the catalytic reaction, a sulfide is transferred from Cys-216 to a reaction intermediate, generating a dehydroalanine residue.

    Proteomic databases

    PaxDbiQ38814.
    PRIDEiQ38814.

    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. 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.3 Publications

    Developmental stagei

    Expressed throughout develpoment.1 Publication

    Inductioni

    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.3 Publications

    Gene expression databases

    GenevestigatoriQ38814.

    Interactioni

    Subunit structurei

    Homooctamer.1 PublicationUniRule annotation

    Protein-protein interaction databases

    BioGridi20811. 3 interactions.
    IntActiQ38814. 1 interaction.
    MINTiMINT-8071157.
    STRINGi3702.AT5G54770.1-P.

    Structurei

    Secondary structure

    1
    349
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi63 – 8119
    Beta strandi83 – 897
    Helixi93 – 10311
    Beta strandi110 – 1189
    Turni121 – 1244
    Beta strandi133 – 1364
    Turni137 – 1393
    Helixi140 – 1467
    Beta strandi154 – 1607
    Helixi162 – 17413
    Beta strandi179 – 1835
    Beta strandi185 – 1939
    Beta strandi196 – 2049
    Helixi205 – 2084
    Turni211 – 2133
    Beta strandi220 – 22910
    Beta strandi233 – 2353
    Turni236 – 2394
    Helixi240 – 2478
    Beta strandi250 – 2523
    Beta strandi258 – 2603
    Helixi262 – 27211
    Beta strandi274 – 2774
    Beta strandi280 – 2823
    Helixi285 – 2917
    Helixi301 – 31717
    Turni323 – 3264

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1RP0X-ray1.60A/B49-328[»]
    ProteinModelPortaliQ38814.
    SMRiQ38814. Positions 51-328.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ38814.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni114 – 1152Substrate binding
    Regioni295 – 2973Substrate binding

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi86 – 894Poly-Val

    Sequence similaritiesi

    Belongs to the THI4 family.UniRule annotation

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG1635.
    HOGENOMiHOG000106048.
    InParanoidiQ38814.
    KOiK03146.
    OMAiLMNATAV.
    PhylomeDBiQ38814.

    Family and domain databases

    HAMAPiMF_03158. THI4.
    InterProiIPR027495. Sti35.
    IPR002922. Thi4_fam.
    [Graphical view]
    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. Align

    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

    MAAIASTLSL SSTKPQRLFD SSFHGSAISA APISIGLKPR SFSVRATTAG    50
    YDLNAFTFDP IKESIVSREM TRRYMTDMIT YAETDVVVVG AGSAGLSAAY 100
    EISKNPNVQV AIIEQSVSPG GGAWLGGQLF SAMIVRKPAH LFLDEIGVAY 150
    DEQDTYVVVK HAALFTSTIM SKLLARPNVK LFNAVAAEDL IVKGNRVGGV 200
    VTNWALVAQN HHTQSCMDPN VMEAKIVVSS CGHDGPFGAT GVKRLKSIGM 250
    IDHVPGMKAL DMNTAEDAIV RLTREVVPGM IVTGMEVAEI DGAPRMGPTF 300
    GAMMISGQKA GQLALKALGL PNAIDGTLVG NLSPELVLAA ADSAETVDA 349
    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.

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

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 6969Missing in isoform mitochondrial. CuratedVSP_044533Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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_124858.3. [Q38814-1]
    UniGeneiAt.24888.

    Genome annotation databases

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

    Keywords - Coding sequence diversityi

    Alternative initiation

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    PIRi S71191.
    RefSeqi NP_200288.1. NM_124858.3. [Q38814-1 ]
    UniGenei At.24888.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1RP0 X-ray 1.60 A/B 49-328 [» ]
    ProteinModelPortali Q38814.
    SMRi Q38814. Positions 51-328.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 20811. 3 interactions.
    IntActi Q38814. 1 interaction.
    MINTi MINT-8071157.
    STRINGi 3702.AT5G54770.1-P.

    Proteomic databases

    PaxDbi Q38814.
    PRIDEi Q38814.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi AT5G54770.1 ; AT5G54770.1 ; AT5G54770 . [Q38814-1 ]
    GeneIDi 835567.
    KEGGi ath:AT5G54770.

    Organism-specific databases

    TAIRi AT5G54770.

    Phylogenomic databases

    eggNOGi COG1635.
    HOGENOMi HOG000106048.
    InParanoidi Q38814.
    KOi K03146.
    OMAi LMNATAV.
    PhylomeDBi Q38814.

    Enzyme and pathway databases

    BioCyci MetaCyc:AT5G54770-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei Q38814.

    Gene expression databases

    Genevestigatori Q38814.

    Family and domain databases

    HAMAPi MF_03158. THI4.
    InterProi IPR027495. Sti35.
    IPR002922. Thi4_fam.
    [Graphical view ]
    TIGRFAMsi TIGR00292. TIGR00292. 1 hit.
    ProtoNeti Search...

    Publicationsi

    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.
      , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., 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].
    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. Cited for: DEVELOPMENTAL STAGE, TISSUE SPECIFICITY, INDUCTION.
    11. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    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].
    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].
    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].
    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].
      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.

    Entry informationi

    Entry nameiTHI4_ARATH
    AccessioniPrimary (citable) accession number: Q38814
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 111 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Arabidopsis thaliana
      Arabidopsis thaliana: entries and gene names
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3