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Protein

Thiamine thiazole synthase

Gene

THI4

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
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.UniRule annotation7 Publications

Miscellaneous

Expressed at high levels in the early stationary phase of batch cultures growing on molasses, an industrial medium.

Cofactori

Fe cationNote: Binds 1 Fe cation per subunit.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei76Substrate; via amide nitrogen1
Binding sitei105Substrate; via amide nitrogen1
Binding sitei170Substrate; via amide nitrogen and carbonyl oxygen1
Binding sitei207Substrate1
Binding sitei237Substrate1
Binding sitei291Substrate; via amide nitrogen1

GO - Molecular functioni

GO - Biological processi

  • cellular response to DNA damage stimulus Source: EnsemblPlants
  • mitochondrial genome maintenance Source: SGD
  • response to cold Source: EnsemblPlants
  • thiamine biosynthetic process Source: SGD
  • thiazole biosynthetic process Source: SGD

Keywordsi

Biological processThiamine biosynthesis
LigandIron, Metal-binding, NAD

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER3O-153
YEAST:MONOMER3O-153
BRENDAi2.8.1.10 984

Names & Taxonomyi

Protein namesi
Recommended name:
Thiamine thiazole synthaseUniRule annotation
Alternative name(s):
Thiazole biosynthetic enzymeUniRule annotation
Gene namesi
Name:THI4UniRule annotation
Synonyms:ESP35, MOL1
Ordered Locus Names:YGR144W
ORF Names:G6620
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome VII

Organism-specific databases

EuPathDBiFungiDB:YGR144W
SGDiS000003376 THI4

Subcellular locationi

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

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi97E → A or Q: No activity. 1 Publication1
Mutagenesisi200H → N: Partially active, trapping the enzyme at an advanced intermediate, just before the sulfide transfer reaction. 1 Publication1
Mutagenesisi204C → A: Partially active, trapping the enzyme at an advanced intermediate, just before the sulfide transfer reaction. 1 Publication1
Mutagenesisi205C → S: Partially active, with very weak activity toward NAD. 1 Publication1
Mutagenesisi207D → A: No activity. 1 Publication1
Mutagenesisi237H → A or N: No activity. 1 Publication1
Mutagenesisi238D → A: Partially active, with very weak activity toward NAD. 1 Publication1
Mutagenesisi301R → A or Q: No activity. 1 Publication1
Mutagenesisi304P → A: No activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000340581 – 326Thiamine thiazole synthaseAdd BLAST326

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2052,3-didehydroalanine (Cys)1 Publication1

Post-translational modificationi

During the catalytic reaction, a sulfide is transferred from Cys-205 to a reaction intermediate, generating a dehydroalanine residue.1 Publication

Proteomic databases

PaxDbiP32318
PRIDEiP32318

Expressioni

Inductioni

Repressed by thiamine.2 Publications

Interactioni

Subunit structurei

Homooctamer.UniRule annotation1 Publication

GO - Molecular functioni

Protein-protein interaction databases

BioGridi3339282 interactors.
DIPiDIP-1703N
IntActiP32318 5 interactors.
MINTiP32318
STRINGi4932.YGR144W

Structurei

Secondary structure

1326
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi17 – 19Combined sources3
Turni25 – 29Combined sources5
Helixi45 – 62Combined sources18
Beta strandi65 – 71Combined sources7
Helixi75 – 87Combined sources13
Beta strandi93 – 96Combined sources4
Beta strandi98 – 101Combined sources4
Turni104 – 107Combined sources4
Beta strandi116 – 119Combined sources4
Turni120 – 122Combined sources3
Helixi123 – 128Combined sources6
Beta strandi137 – 143Combined sources7
Helixi145 – 157Combined sources13
Beta strandi162 – 165Combined sources4
Beta strandi168 – 178Combined sources11
Beta strandi180 – 183Combined sources4
Beta strandi185 – 193Combined sources9
Helixi194 – 197Combined sources4
Turni198 – 201Combined sources4
Beta strandi209 – 214Combined sources6
Beta strandi220 – 222Combined sources3
Beta strandi230 – 233Combined sources4
Beta strandi239 – 241Combined sources3
Helixi244 – 252Combined sources9
Helixi266 – 276Combined sources11
Beta strandi286 – 288Combined sources3
Helixi291 – 297Combined sources7
Helixi307 – 325Combined sources19

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3FPZX-ray1.82A/B1-326[»]
4Y4LX-ray2.00A/B/C/D1-326[»]
ProteinModelPortaliP32318
SMRiP32318
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP32318

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni97 – 98Substrate binding2
Regioni301 – 303Substrate binding3

Sequence similaritiesi

Belongs to the THI4 family.UniRule annotation

Phylogenomic databases

HOGENOMiHOG000106048
InParanoidiP32318
KOiK03146
OMAiMWGGGMM
OrthoDBiEOG092C3CAV

Family and domain databases

Gene3Di3.50.50.601 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

Sequencei

Sequence statusi: Complete.

P32318-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSATSTATST SASQLHLNST PVTHCLSDIV KKEDWSDFKF APIRESTVSR
60 70 80 90 100
AMTSRYFKDL DKFAVSDVII VGAGSSGLSA AYVIAKNRPD LKVCIIESSV
110 120 130 140 150
APGGGSWLGG QLFSAMVMRK PAHLFLQELE IPYEDEGDYV VVKHAALFIS
160 170 180 190 200
TVLSKVLQLP NVKLFNATCV EDLVTRPPTE KGEVTVAGVV TNWTLVTQAH
210 220 230 240 250
GTQCCMDPNV IELAGYKNDG TRDLSQKHGV ILSTTGHDGP FGAFCAKRIV
260 270 280 290 300
DIDQNQKLGG MKGLDMNHAE HDVVIHSGAY AGVDNMYFAG MEVAELDGLN
310 320
RMGPTFGAMA LSGVHAAEQI LKHFAA
Length:326
Mass (Da):34,991
Last modified:October 1, 1993 - v1
Checksum:i843790F2CE00BF02
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X61669 Genomic DNA Translation: CAA43843.1
Z72929 Genomic DNA Translation: CAA97157.1
Z72930 Genomic DNA Translation: CAA97159.1
X85807 Genomic DNA Translation: CAA59802.1
BK006941 Genomic DNA Translation: DAA08235.1
PIRiS25321
RefSeqiNP_011660.1, NM_001181273.1

Genome annotation databases

EnsemblFungiiYGR144W; YGR144W; YGR144W
GeneIDi853047
KEGGisce:YGR144W

Similar proteinsi

Entry informationi

Entry nameiTHI4_YEAST
AccessioniPrimary (citable) accession number: P32318
Secondary accession number(s): D6VUS4
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: March 28, 2018
This is version 144 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome