Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P41835 (THI6_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 124. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Thiamine biosynthetic bifunctional enzyme

Including the following 2 domains:

  1. Thiamine-phosphate synthase
    Short name=TP synthase
    Short name=TPS
    EC=2.5.1.3
    Alternative name(s):
    Thiamine-phosphate pyrophosphorylase
    Short name=TMP pyrophosphorylase
    Short name=TMP-PPase
  2. Hydroxyethylthiazole kinase
    EC=2.7.1.50
    Alternative name(s):
    4-methyl-5-beta-hydroxyethylthiazole kinase
    Short name=TH kinase
    Short name=THZ kinase
Gene names
Name:THI6
Ordered Locus Names:YPL214C
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length540 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Essential for thiamine biosynthesis. The kinase activity is involved in the salvage synthesis of TH-P from the thiazole. HAMAP-Rule MF_00097

Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate (TMP) By similarity. HAMAP-Rule MF_00097

Catalytic activity

2-methyl-4-amino-5-hydroxymethylpyrimidine diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = diphosphate + thiamine phosphate. HAMAP-Rule MF_00097

ATP + 4-methyl-5-(2-hydroxyethyl)thiazole = ADP + 4-methyl-5-(2-phosphonooxyethyl)thiazole. HAMAP-Rule MF_00097

Cofactor

Binds 1 magnesium ion per subunit By similarity. HAMAP-Rule MF_00097

Pathway

Cofactor biosynthesis; thiamine diphosphate biosynthesis; 4-methyl-5-(2-phosphoethyl)-thiazole from 5-(2-hydroxyethyl)-4-methylthiazole: step 1/1. HAMAP-Rule MF_00097

Cofactor biosynthesis; thiamine diphosphate biosynthesis; thiamine phosphate from 4-amino-2-methyl-5-diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)-thiazole: step 1/1.

Subunit structure

Homooctamer.

Sequence similarities

In the N-terminal section; belongs to the thiamine-phosphate synthase family.

In the C-terminal section; belongs to the Thz kinase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 540540Thiamine biosynthetic bifunctional enzyme HAMAP-Rule MF_00097
PRO_0000157090

Regions

Region1 – 238238Thiamine-phosphate synthase HAMAP-Rule MF_00097
Region43 – 475HMP-PP binding By similarity
Region143 – 1453THZ-P binding By similarity
Region209 – 2102THZ-P binding By similarity
Region239 – 540302Hydroxyethylthiazole kinase HAMAP-Rule MF_00097

Sites

Active site4651Proton acceptor; for hydroxyethylthiazole kinase activity By similarity
Metal binding761Magnesium By similarity
Metal binding951Magnesium By similarity
Binding site751HMP-PP By similarity
Binding site1141HMP-PP By similarity
Binding site1461HMP-PP By similarity
Binding site1811THZ-P; via amide nitrogen By similarity
Binding site29014-methyl-5-(2-hydroxyethyl)thiazole; via amide nitrogen By similarity
Binding site3651ATP By similarity
Binding site4151ATP By similarity
Binding site46214-methyl-5-(2-hydroxyethyl)thiazole; via amide nitrogen By similarity

Natural variations

Natural variant3701E → K in THI6-3; possesses TMP-PPASE activity only.
Natural variant4761G → D in THI6-2; both enzyme activities greatly decreased.
Natural variant5101G → D in THI6-1; both enzyme activities greatly decreased.

Sequences

Sequence LengthMass (Da)Tools
P41835 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: F34FA1E0B76E3930

FASTA54058,059
        10         20         30         40         50         60 
MVFTKEEVDY SLYLVTDSTM LPPGTTLCSQ VEAGLKNGVT LVQIREKDIE TKNFVAEALE 

        70         80         90        100        110        120 
VQKICKKYNV PLIINDRIDV AMAIDADGVH VGQDDMPIPM VRKLLGPSKI LGWSVGKPSE 

       130        140        150        160        170        180 
VETLAKWGPD MVDYIGVGTL FPTSTKKNPK KSPMGPQGAI AILDALEEFK ATWCRTVGIG 

       190        200        210        220        230        240 
GLHPDNIQRV LCQCVASNGK RSLDGISLVS DIMAAPDACA ATKRLRGLLD ATRYQFVECE 

       250        260        270        280        290        300 
LNNTFPTTTS IQNVISQVSN NRPLVQHITN KVHQNFGANV TLALGSSPIM SEIESEVSEL 

       310        320        330        340        350        360 
ARIPNASLLL NTGSVAPIEM LKAAINAYNE VNRPITFDPV GYSATETRLC LNNTLLTYGQ 

       370        380        390        400        410        420 
FACIKGNCSE ILSLAKLNNH KMKGVDSSSG KTNIDTLVRA TQIVAFQYRT VAVCTGEFDC 

       430        440        450        460        470        480 
VADGTFGGEY KLSSGTEGIT AEDLPCVIIE DGPIPIMGDI TASGCSLGST IASFIGGLDS 

       490        500        510        520        530        540 
TGKLFDAVVG AVLLYKSAGK LASTRCQGSG SFHVELIDAL YQLFHENKPE KWSASLKKFK 

« Hide

References

« Hide 'large scale' references
[1]"Isolation and characterization of the THI6 gene encoding a bifunctional thiamin-phosphate pyrophosphorylase/hydroxyethylthiazole kinase from Saccharomyces cerevisiae."
Nosaka K., Nishimura H., Kawasaki Y., Tsujihara T., Iwashima A.
J. Biol. Chem. 269:30510-30516(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ND5-5A.
[2]"The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI."
Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W., Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D., Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E., Churcher C.M. expand/collapse author list , Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H., DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N., Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K., Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M., Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A., Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D., Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S., Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B., Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A., Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R., Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A., Vo D.H., Hani J.
Nature 387:103-105(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[3]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D31908 Genomic DNA. Translation: BAA06703.1.
Z73570 Genomic DNA. Translation: CAA97929.1.
BK006949 Genomic DNA. Translation: DAA11222.1.
PIRA55145.
RefSeqNP_015110.1. NM_001184028.1.

3D structure databases

ProteinModelPortalP41835.
SMRP41835. Positions 3-536.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid35971. 44 interactions.
DIPDIP-1666N.
IntActP41835. 1 interaction.
MINTMINT-403731.
STRING4932.YPL214C.

Proteomic databases

MaxQBP41835.
PaxDbP41835.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYPL214C; YPL214C; YPL214C.
GeneID855887.
KEGGsce:YPL214C.

Organism-specific databases

CYGDYPL214c.
SGDS000006135. THI6.

Phylogenomic databases

eggNOGCOG0352.
HOGENOMHOG000214306.
KOK14154.
OMANLVVQNF.
OrthoDBEOG7KDFMZ.

Enzyme and pathway databases

BioCycMetaCyc:YPL214C-MONOMER.
YEAST:YPL214C-MONOMER.
UniPathwayUPA00060; UER00139.
UPA00060; UER00141.

Gene expression databases

GenevestigatorP41835.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
3.40.1190.20. 1 hit.
HAMAPMF_00097. TMP_synthase.
InterProIPR013785. Aldolase_TIM.
IPR000417. Hyethyz_kinase.
IPR029056. Ribokinase-like.
IPR022998. ThiaminP_synth_SF.
IPR003733. TMP_synthase.
[Graphical view]
PfamPF02110. HK. 1 hit.
PF02581. TMP-TENI. 1 hit.
[Graphical view]
PRINTSPR01099. HYETHTZKNASE.
SUPFAMSSF51391. SSF51391. 1 hit.
SSF53613. SSF53613. 1 hit.
TIGRFAMsTIGR00693. thiE. 1 hit.
TIGR00694. thiM. 1 hit.
ProtoNetSearch...

Other

NextBio980553.

Entry information

Entry nameTHI6_YEAST
AccessionPrimary (citable) accession number: P41835
Secondary accession number(s): D6W3F6
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: June 11, 2014
This is version 124 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome XVI

Yeast (Saccharomyces cerevisiae) chromosome XVI: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways