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Q9UZQ5 (THIE_PYRAB) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 82. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:PYRAB10900
ORF Names:PAB1645
OrganismPyrococcus abyssi (strain GE5 / Orsay) [Complete proteome] [HAMAP]
Taxonomic identifier272844 [NCBI]
Taxonomic lineageArchaea › Euryarchaeota › Thermococci › Thermococcales › Thermococcaceae › Pyrococcus

Protein attributes

Sequence length207 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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 termComplete 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_0000157073

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

Sequences

Sequence LengthMass (Da)Tools
Q9UZQ5 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: F53ACEEF7F8A82D4

FASTA20722,537
        10         20         30         40         50         60 
MGFREKLKLY VITDRRLKPE VKSVRQALEG GATSIQLRIK DASTKEMYEV GKEIRRLTQE 

        70         80         90        100        110        120 
YDALFFVDDR IDVALAVNAD GVQLGPEDMP IEVAREIAPN LIIGASVYSL EEALEAEKKG 

       130        140        150        160        170        180 
ADYLGAGSVF PTKTKRDVRV IRIEGLREIV EAVSIPVVAI GGINVENVKQ VLSAGVDGIA 

       190        200 
VVSAVMGASD VKKATEELRK IIEEVLG

« Hide

References

[1]"An integrated analysis of the genome of the hyperthermophilic archaeon Pyrococcus abyssi."
Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O., Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J., Weissenbach J., Zivanovic Y., Forterre P.
Mol. Microbiol. 47:1495-1512(2003) [PubMed: 12622808] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: GE5 / Orsay.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AJ248286 Genomic DNA. Translation: CAB50001.1.
PIRD75087.
RefSeqNP_126770.1. NC_000868.1.

3D structure databases

ProteinModelPortalQ9UZQ5.
SMRQ9UZQ5. Positions 3-207.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBPYRT00000003607; EBPYRP00000003538; EBPYRG00000003607.
GeneID1496448.
GenomeReviewsGene locus PYRAB10900 in contig AL096836_GR.
KEGGpab:PAB1645.
NMPDRfig|272844.1.peg.1141.

Organism-specific databases

CMRSearch...

Phylogenomic databases

GeneTreeEBGT00050000022349.
HOGENOMHBG754477.
OMAVSAICHA.
PhylomeDBQ9UZQ5.
ProtClustDBPRK00043.

Enzyme and pathway databases

BioCycPABY272844:PAB1645-MONOMER.

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_PYRAB
AccessionPrimary (citable) accession number: Q9UZQ5
Entry history
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: May 1, 2000
Last modified: January 25, 2012
This is version 82 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

SIMILARITY comments

Index of protein domains and families

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