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Protein

Thiamine pyrophosphokinase

Gene

THI80

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Essential protein, it is the only enzyme in yeast capable of synthesizing thiamine pyrophosphate (TPP).

Catalytic activityi

ATP + thiamine = AMP + thiamine diphosphate.

Pathwayi

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. kinase activity Source: UniProtKB-KW
  3. thiamine binding Source: InterPro
  4. thiamine diphosphokinase activity Source: SGD

GO - Biological processi

  1. thiamine diphosphate biosynthetic process Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciYEAST:YOR143C-MONOMER.
ReactomeiREACT_251690. Vitamin B1 (thiamin) metabolism.
UniPathwayiUPA00060; UER00597.

Names & Taxonomyi

Protein namesi
Recommended name:
Thiamine pyrophosphokinase (EC:2.7.6.2)
Short name:
TPK
Short name:
Thiamine kinase
Gene namesi
Name:THI80
Ordered Locus Names:YOR143C
ORF Names:YOR3373C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome XV

Organism-specific databases

CYGDiYOR143c.
SGDiS000005669. THI80.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 319318Thiamine pyrophosphokinasePRO_0000072513Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP35202.
PaxDbiP35202.

Expressioni

Inductioni

Expression requires the positive regulatory factors THI2 and THI3. Incompletely repressed by exogenous thiamine pyrophosphokinase.

Gene expression databases

GenevestigatoriP35202.

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

BioGridi34540. 11 interactions.
DIPiDIP-5324N.
IntActiP35202. 5 interactions.
MINTiMINT-520646.
STRINGi4932.YOR143C.

Structurei

Secondary structure

1
319
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 74Combined sources
Beta strandi10 – 123Combined sources
Beta strandi23 – 275Combined sources
Helixi28 – 303Combined sources
Beta strandi37 – 437Combined sources
Helixi52 – 6110Combined sources
Beta strandi63 – 686Combined sources
Helixi71 – 788Combined sources
Helixi83 – 864Combined sources
Beta strandi92 – 965Combined sources
Helixi103 – 1119Combined sources
Beta strandi115 – 1184Combined sources
Beta strandi122 – 1243Combined sources
Helixi126 – 13914Combined sources
Helixi141 – 1477Combined sources
Turni153 – 1553Combined sources
Helixi156 – 1583Combined sources
Turni161 – 1633Combined sources
Helixi164 – 17310Combined sources
Helixi178 – 1803Combined sources
Beta strandi184 – 19512Combined sources
Helixi196 – 21217Combined sources
Beta strandi216 – 2216Combined sources
Beta strandi223 – 2308Combined sources
Beta strandi235 – 2384Combined sources
Helixi241 – 2477Combined sources
Beta strandi248 – 2547Combined sources
Beta strandi260 – 27819Combined sources
Turni279 – 2824Combined sources
Beta strandi285 – 2884Combined sources
Beta strandi292 – 30211Combined sources
Beta strandi304 – 3107Combined sources
Helixi312 – 3154Combined sources
Helixi316 – 3183Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1IG0X-ray1.80A/B1-319[»]
ProteinModelPortaliP35202.
SMRiP35202. Positions 1-319.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP35202.

Family & Domainsi

Sequence similaritiesi

Belongs to the thiamine pyrophosphokinase family.Curated

Phylogenomic databases

eggNOGiCOG1564.
GeneTreeiENSGT00390000016016.
HOGENOMiHOG000248374.
InParanoidiP35202.
KOiK00949.
OMAiSEECIEN.
OrthoDBiEOG7ZKSPD.

Family and domain databases

Gene3Di2.60.120.320. 1 hit.
3.40.50.10240. 2 hits.
InterProiIPR016966. Thiamin_pyrophosphokinase_euk.
IPR007373. Thiamin_PyroPKinase_B1-bd.
IPR007371. TPK_catalytic.
[Graphical view]
PfamiPF04265. TPK_B1_binding. 1 hit.
PF04263. TPK_catalytic. 1 hit.
[Graphical view]
PIRSFiPIRSF031057. Thiamin_pyrophosphokinase. 1 hit.
SMARTiSM00983. TPK_B1_binding. 1 hit.
[Graphical view]
SUPFAMiSSF63862. SSF63862. 1 hit.
SSF63999. SSF63999. 1 hit.

Sequencei

Sequence statusi: Complete.

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

P35202-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSEECIENPE RIKIGTDLIN IRNKMNLKEL IHPNEDENST LLILNQKIDI
60 70 80 90 100
PRPLFYKIWK LHDLKVCADG AANRLYDYLD DDETLRIKYL PNYIIGDLDS
110 120 130 140 150
LSEKVYKYYR KNKVTIIKQT TQYSTDFTKC VNLISLHFNS PEFRSLISNK
160 170 180 190 200
DNLQSNHGIE LEKGIHTLYN TMTESLVFSK VTPISLLALG GIGGRFDQTV
210 220 230 240 250
HSITQLYTLS ENASYFKLCY MTPTDLIFLI KKNGTLIEYD PQFRNTCIGN
260 270 280 290 300
CGLLPIGEAT LVKETRGLKW DVKNWPTSVV TGRVSSSNRF VGDNCCFIDT
310
KDDIILNVEI FVDKLIDFL
Length:319
Mass (Da):36,616
Last modified:February 1, 1994 - v1
Checksum:iB82609E195D4D53F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D14417 Genomic DNA. Translation: BAA03312.1.
X94335 Genomic DNA. Translation: CAA64061.1.
Z75051 Genomic DNA. Translation: CAA99346.1.
BK006948 Genomic DNA. Translation: DAA10917.1.
PIRiA47499.
RefSeqiNP_014786.1. NM_001183562.1.

Genome annotation databases

EnsemblFungiiYOR143C; YOR143C; YOR143C.
GeneIDi854314.
KEGGisce:YOR143C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D14417 Genomic DNA. Translation: BAA03312.1.
X94335 Genomic DNA. Translation: CAA64061.1.
Z75051 Genomic DNA. Translation: CAA99346.1.
BK006948 Genomic DNA. Translation: DAA10917.1.
PIRiA47499.
RefSeqiNP_014786.1. NM_001183562.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1IG0X-ray1.80A/B1-319[»]
ProteinModelPortaliP35202.
SMRiP35202. Positions 1-319.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34540. 11 interactions.
DIPiDIP-5324N.
IntActiP35202. 5 interactions.
MINTiMINT-520646.
STRINGi4932.YOR143C.

Proteomic databases

MaxQBiP35202.
PaxDbiP35202.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYOR143C; YOR143C; YOR143C.
GeneIDi854314.
KEGGisce:YOR143C.

Organism-specific databases

CYGDiYOR143c.
SGDiS000005669. THI80.

Phylogenomic databases

eggNOGiCOG1564.
GeneTreeiENSGT00390000016016.
HOGENOMiHOG000248374.
InParanoidiP35202.
KOiK00949.
OMAiSEECIEN.
OrthoDBiEOG7ZKSPD.

Enzyme and pathway databases

UniPathwayiUPA00060; UER00597.
BioCyciYEAST:YOR143C-MONOMER.
ReactomeiREACT_251690. Vitamin B1 (thiamin) metabolism.

Miscellaneous databases

EvolutionaryTraceiP35202.
NextBioi976339.
PROiP35202.

Gene expression databases

GenevestigatoriP35202.

Family and domain databases

Gene3Di2.60.120.320. 1 hit.
3.40.50.10240. 2 hits.
InterProiIPR016966. Thiamin_pyrophosphokinase_euk.
IPR007373. Thiamin_PyroPKinase_B1-bd.
IPR007371. TPK_catalytic.
[Graphical view]
PfamiPF04265. TPK_B1_binding. 1 hit.
PF04263. TPK_catalytic. 1 hit.
[Graphical view]
PIRSFiPIRSF031057. Thiamin_pyrophosphokinase. 1 hit.
SMARTiSM00983. TPK_B1_binding. 1 hit.
[Graphical view]
SUPFAMiSSF63862. SSF63862. 1 hit.
SSF63999. SSF63999. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation and characterization of a thiamin pyrophosphokinase gene, THI80, from Saccharomyces cerevisiae."
    Nosaka K., Kaneko Y., Nishimura H., Iwashima A.
    J. Biol. Chem. 268:17440-17447(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV."
    Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A., Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B., Dang V.-D.
    , de Haan M., Delius H., Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U., Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B., Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A., Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.
    Nature 387:98-102(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  5. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  6. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  7. "The crystal structure of yeast thiamin pyrophosphokinase."
    Baker L.-J., Dorocke J.A., Harris R.A., Timm D.E.
    Structure 9:539-546(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).

Entry informationi

Entry nameiTHI80_YEAST
AccessioniPrimary (citable) accession number: P35202
Secondary accession number(s): D6W2K1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: March 4, 2015
This is version 131 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 3320 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
  4. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  5. Yeast chromosome XV
    Yeast (Saccharomyces cerevisiae) chromosome XV: entries and gene names

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.