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A6QIT5 (THIE_STAAE) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 48. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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-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:NWMN_1995
OrganismStaphylococcus aureus (strain Newman) [Complete proteome] [HAMAP]
Taxonomic identifier426430 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesStaphylococcus

Protein attributes

Sequence length213 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-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

Cofactor

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

thiamine diphosphate biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Molecular_functionmagnesium ion binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

thiamine-phosphate diphosphorylase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 213213Thiamine-phosphate synthase HAMAP-Rule MF_00097
PRO_1000071284

Regions

Region40 – 445HMP-PP binding By similarity
Region139 – 1413THZ-P binding By similarity
Region191 – 1922THZ-P binding By similarity

Sites

Metal binding761Magnesium By similarity
Metal binding951Magnesium By similarity
Binding site751HMP-PP By similarity
Binding site1131HMP-PP By similarity
Binding site1421HMP-PP By similarity
Binding site1711THZ-P; via amide nitrogen By similarity

Sequences

Sequence LengthMass (Da)Tools
A6QIT5 [UniParc].

Last modified August 21, 2007. Version 1.
Checksum: 8FEFB39D6EF82F94

FASTA21323,399
        10         20         30         40         50         60 
MFNQSYLNVY FICGTSDVPS HRTIHEVLEA ALKAGITLFQ FREKGESALK GNDKLVLAKE 

        70         80         90        100        110        120 
LQHLCHQYDV PFIVNDDVSL AKEINADGIH VGQDDAKVKE IAQYFTDKII GLSISDLDEY 

       130        140        150        160        170        180 
AKSDLTHVDY IGVGPIYPTP SKHDAHIPVG PEMIATFKEM NPQLPIVAIG GINTNNVAPI 

       190        200        210 
VEAGANGISV ISAISKSENI EKTVNRFKDF FNN 

« Hide

References

[1]"Genome sequence of Staphylococcus aureus strain Newman and comparative analysis of staphylococcal genomes: polymorphism and evolution of two major pathogenicity islands."
Baba T., Bae T., Schneewind O., Takeuchi F., Hiramatsu K.
J. Bacteriol. 190:300-310(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Newman.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP009351 Genomic DNA. Translation: BAF68267.1.
RefSeqYP_001333029.1. NC_009641.1.

3D structure databases

ProteinModelPortalA6QIT5.
SMRA6QIT5. Positions 4-209.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING426430.NWMN_1995.

Proteomic databases

PRIDEA6QIT5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAF68267; BAF68267; NWMN_1995.
GeneID5332232.
KEGGsae:NWMN_1995.
PATRIC19587794. VBIStaAur133992_2182.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0352.
HOGENOMHOG000155781.
KOK00788.
OMAVSAICHA.
OrthoDBEOG6W19NW.
ProtClustDBPRK00043.

Enzyme and pathway databases

BioCycSAUR426430:GIXC-2059-MONOMER.
UniPathwayUPA00060; UER00141.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
HAMAPMF_00097. TMP_synthase.
InterProIPR013785. Aldolase_TIM.
IPR022998. ThiaminP_synth_SF.
IPR003733. TMP_synthase.
[Graphical view]
PfamPF02581. TMP-TENI. 1 hit.
[Graphical view]
SUPFAMSSF51391. SSF51391. 1 hit.
TIGRFAMsTIGR00693. thiE. 1 hit.
ProtoNetSearch...

Entry information

Entry nameTHIE_STAAE
AccessionPrimary (citable) accession number: A6QIT5
Entry history
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: August 21, 2007
Last modified: February 19, 2014
This is version 48 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways