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Q8U192 (THIE_PYRFU) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 67. 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:
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
Gene names
Name:thiE
Ordered Locus Names:PF1334
OrganismPyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
Taxonomic identifier186497 [NCBI]
Taxonomic lineageArchaea › Euryarchaeota › Thermococci › Thermococcales › Thermococcaceae › Pyrococcus

Protein attributes

Sequence length207 AA.
Sequence statusComplete.
Protein existenceEvidence at protein 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 MF_00097

Catalytic activity

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

Cofactor

Binds 1 magnesium ion per subunit By similarity. HAMAP MF_00097

Pathway

Cofactor biosynthesis; thiamine diphosphate biosynthesis; thiamine phosphate from 4-amino-2-methyl-5-diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)-thiazole: step 1/1. HAMAP MF_00097

Sequence similarities

Belongs to the thiamine-phosphate synthase family.

Ontologies

Keywords
   Biological processThiamine biosynthesis
   LigandMagnesium
Metal-binding
   Molecular functionTransferase
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological processthiamine biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionmetal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

thiamine-phosphate diphosphorylase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 207207Thiamine-phosphate synthase
PRO_0000157074

Regions

Region36 – 405HMP-PP binding By similarity
Region132 – 1343THZ-P binding By similarity
Region182 – 1832THZ-P binding By similarity

Sites

Metal binding691Magnesium By similarity
Metal binding881Magnesium By similarity
Binding site681HMP-PP By similarity
Binding site1061HMP-PP By similarity
Binding site1351HMP-PP By similarity
Binding site1621THZ-P; via amide nitrogen By similarity

Secondary structure

1 ........................................ 207
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q8U192 [UniParc].

Last modified June 1, 2002. Version 1.
Checksum: 7776F777009AE858

FASTA20722,590
        10         20         30         40         50         60 
MNLRNKLKLY VITDRRLKPE VESVREALEG GATAIQMRIK NAPTREMYEI GKTLRQLTRE 

        70         80         90        100        110        120 
YDALFFVDDR VDVALAVDAD GVQLGPEDMP IEVAKEIAPN LIIGASVYSL EEALEAEKKG 

       130        140        150        160        170        180 
ADYLGAGSVF PTKTKEDARV IGLEGLRKIV ESVKIPVVAI GGINKDNARE VLKTGVDGIA 

       190        200 
VISAVMGAED VRKATEELRK IVEEVLG

« Hide

References

[1]"Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P. horikoshii inferred from complete genomic sequences."
Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M., DiRuggiero J., Robb F.T.
Genetics 152:1299-1305(1999) [PubMed: 10430560] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 43587 / DSM 3638 / JCM 8422 / Vc1.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE009950 Genomic DNA. Translation: AAL81458.1.
RefSeqNP_579063.1. NC_003413.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1XI3X-ray1.70A/B2-207[»]
ProteinModelPortalQ8U192.
SMRQ8U192. Positions 2-207.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBPYRT00000004326; EBPYRP00000004187; EBPYRG00000004326.
GeneID1469209.
GenomeReviewsGene locus PF1334 in contig AE009950_GR.
KEGGpfu:PF1334.
NMPDRfig|186497.1.peg.1380.

Phylogenomic databases

GeneTreeEBGT00050000022349.
HOGENOMHBG754477.
OMAVSAICHA.
PhylomeDBQ8U192.
ProtClustDBPRK00043.

Family and domain databases

HAMAPMF_00097. TMP_synthase.
[Tree]
InterProIPR013785. Aldolase_TIM.
IPR022998. ThiaminP_synth_SF.
IPR003733. TMP_synthase.
[Graphical view]
Gene3DG3DSA:3.20.20.70. Aldolase_TIM. 1 hit.
KOK00788.
PfamPF02581. TMP-TENI. 1 hit.
[Graphical view]
SUPFAMSSF51391. TMP_synthase. 1 hit.
TIGRFAMsTIGR00693. ThiE. 1 hit.
ProtoNetSearch...

Entry information

Entry nameTHIE_PYRFU
AccessionPrimary (citable) accession number: Q8U192
Entry history
Integrated into UniProtKB/Swiss-Prot: October 19, 2002
Last sequence update: June 1, 2002
Last modified: January 25, 2012
This is version 67 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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