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P40386 (THI6_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 110. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Probable 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:thi4
ORF Names:SPAC23H4.10c
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces

Protein attributes

Sequence length518 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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.

Induction

Repressed by thiamine and 5-(2-hydroxyethyl)-4-methylthiazole. HAMAP-Rule MF_00097

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 – 518518Probable thiamine biosynthetic bifunctional enzyme HAMAP-Rule MF_00097
PRO_0000157089

Regions

Region1 – 229229Thiamine-phosphate synthase HAMAP-Rule MF_00097
Region40 – 445HMP-PP binding By similarity
Region137 – 1393THZ-P binding By similarity
Region199 – 2002THZ-P binding By similarity
Region230 – 518289Hydroxyethylthiazole kinase HAMAP-Rule MF_00097

Sites

Active site4331Proton acceptor; for hydroxyethylthiazole kinase activity By similarity
Metal binding731Magnesium By similarity
Metal binding921Magnesium By similarity
Binding site721HMP-PP By similarity
Binding site1111HMP-PP By similarity
Binding site1401HMP-PP By similarity
Binding site1731THZ-P; via amide nitrogen By similarity
Binding site28114-methyl-5-(2-hydroxyethyl)thiazole; via amide nitrogen By similarity
Binding site3551ATP By similarity
Binding site4031ATP By similarity
Binding site43014-methyl-5-(2-hydroxyethyl)thiazole; via amide nitrogen By similarity

Sequences

Sequence LengthMass (Da)Tools
P40386 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: B8836D2BD67C79AA

FASTA51855,566
        10         20         30         40         50         60 
MKRQIDYSLY LVTSSSLIAP GSTIERQVEE GILGGVTLVQ HREKDISTKC FVERAKRLSE 

        70         80         90        100        110        120 
ICKKYDVPFL INDRIDVALA VGADGVHIGQ DDMDCALARK ILGDDAIIGV STNNIEEIEK 

       130        140        150        160        170        180 
AAADGADYVG IGSIYETNTK DVKDRLIGIT GLRKILEHVS KMHCQLGTVA IAGLNSSNIQ 

       190        200        210        220        230        240 
RVIYLSEANG KRIDGIALVS AIMCSITPRE TAKELRNLIA TPPCFAQARS SLTTPKDLLN 

       250        260        270        280        290        300 
QIPAALQKLK DFTPLIHHLT NAVAKNFSAN VTLAAYGSPT MGESYDEVAD FAKAPGALVL 

       310        320        330        340        350        360 
NIGILENTKT YIHAAQVNND LARPVILDPV AVGATTARSK VINTLLNYAY YDIIKGNEGE 

       370        380        390        400        410        420 
IMNLAGEQGL MRGVDSISQH TLAARITAVH RLAVERRCVV AMSGAVDVIS DGNSTYVIKN 

       430        440        450        460        470        480 
GNPLLGQITA SGCSLGSVMG VTASICQNDK LLAAITATLL YNIASELAVE AKNSCGDLLV 

       490        500        510 
QGPGTFIPIF VDKLHQLINE TIKGNVDWIE RAKLEKAE 

« Hide

References

« Hide 'large scale' references
[1]"Cloning, nucleotide sequence, and regulation of Schizosaccharomyces pombe thi4, a thiamine biosynthetic gene."
Zurlinden A., Schweingruber M.E.
J. Bacteriol. 176:6631-6635(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 972 / ATCC 24843.
[2]"The genome sequence of Schizosaccharomyces pombe."
Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. expand/collapse author list , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 972 / ATCC 24843.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X78824 Genomic DNA. Translation: CAA55402.1.
CU329670 Genomic DNA. Translation: CAB11664.1.
PIRS44183.
RefSeqNP_593396.1. NM_001018828.2.

3D structure databases

ProteinModelPortalP40386.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid278362. 7 interactions.
MINTMINT-4689729.
STRING4896.SPAC23H4.10c-1.

Proteomic databases

MaxQBP40386.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSPAC23H4.10c.1; SPAC23H4.10c.1:pep; SPAC23H4.10c.
GeneID2541872.
KEGGspo:SPAC23H4.10c.

Organism-specific databases

PomBaseSPAC23H4.10c.

Phylogenomic databases

eggNOGCOG0352.
HOGENOMHOG000214306.
KOK14154.
OMANLVVQNF.
OrthoDBEOG7KDFMZ.
PhylomeDBP40386.

Enzyme and pathway databases

UniPathwayUPA00060; UER00139.
UPA00060; UER00141.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
3.40.1190.20. 1 hit.
HAMAPMF_00097. TMP_synthase.
MF_00228. Thz_kinase.
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

NextBio20802959.

Entry information

Entry nameTHI6_SCHPO
AccessionPrimary (citable) accession number: P40386
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: June 11, 2014
This is version 110 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways