Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Thiamine-phosphate synthase

Gene

thiE

Organism
Staphylococcus aureus (strain JH9)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

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).UniRule annotation

Catalytic activityi

4-amino-2-methyl-5-diphosphomethylpyrimidine + 2-((2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-ylidene)ethyl phosphate = diphosphate + thiamine phosphate + CO2.UniRule annotation
4-amino-2-methyl-5-diphosphomethylpyrimidine + 2-(2-carboxy-4-methylthiazol-5-yl)ethyl phosphate = diphosphate + thiamine phosphate + CO2.UniRule annotation
4-amino-2-methyl-5-diphosphomethylpyrimidine + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = diphosphate + thiamine phosphate.UniRule annotation

Cofactori

Mg2+UniRule annotationNote: Binds 1 Mg2+ ion per subunit.UniRule annotation

Pathwayi: thiamine diphosphate biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes thiamine phosphate from 4-amino-2-methyl-5-diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)-thiazole.UniRule annotation
Proteins known to be involved in this subpathway in this organism are:
  1. Thiamine-phosphate synthase (thiE)
This subpathway is part of the pathway thiamine diphosphate biosynthesis, which is itself part of Cofactor biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes thiamine phosphate from 4-amino-2-methyl-5-diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)-thiazole, the pathway thiamine diphosphate biosynthesis and in Cofactor biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei75HMP-PPUniRule annotation1
Metal bindingi76MagnesiumUniRule annotation1
Metal bindingi95MagnesiumUniRule annotation1
Binding sitei113HMP-PPUniRule annotation1
Binding sitei142HMP-PPUniRule annotation1
Binding sitei171THZ-P; via amide nitrogenUniRule annotation1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Thiamine biosynthesis

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

UniPathwayiUPA00060; UER00141.

Names & Taxonomyi

Protein namesi
Recommended name:
Thiamine-phosphate synthaseUniRule annotation (EC:2.5.1.3UniRule annotation)
Short name:
TP synthaseUniRule annotation
Short name:
TPSUniRule annotation
Alternative name(s):
Thiamine-phosphate pyrophosphorylaseUniRule annotation
Short name:
TMP pyrophosphorylaseUniRule annotation
Short name:
TMP-PPaseUniRule annotation
Gene namesi
Name:thiEUniRule annotation
Ordered Locus Names:SaurJH9_2128
OrganismiStaphylococcus aureus (strain JH9)
Taxonomic identifieri359786 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcaceaeStaphylococcus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_10000755781 – 213Thiamine-phosphate synthaseAdd BLAST213

Structurei

3D structure databases

ProteinModelPortaliA5IUN7.
SMRiA5IUN7.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni40 – 44HMP-PP bindingUniRule annotation5
Regioni139 – 141THZ-P bindingUniRule annotation3
Regioni191 – 192THZ-P bindingUniRule annotation2

Sequence similaritiesi

Belongs to the thiamine-phosphate synthase family.UniRule annotation

Phylogenomic databases

HOGENOMiHOG000155781.
KOiK00788.
OMAiQVREKHG.

Family and domain databases

CDDicd00564. TMP_TenI. 1 hit.
Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_00097. TMP_synthase. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR022998. ThiaminP_synth_SF.
IPR003733. TMP_synthase.
[Graphical view]
PfamiPF02581. TMP-TENI. 1 hit.
[Graphical view]
SUPFAMiSSF51391. SSF51391. 1 hit.
TIGRFAMsiTIGR00693. thiE. 1 hit.

Sequencei

Sequence statusi: Complete.

A5IUN7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFNQSYLNVY FICGTSDVPS HRTIHEVLEA ALKAGITLFQ FREKGESALK
60 70 80 90 100
GNDKLVLAKE LQHLCHQYDV PFIVNDDVSL AKEINADGIH VGQDDAKVKE
110 120 130 140 150
IAQYFTDKII GLSISDLDEY AKSDLTHVDY IGVGPIYPTP SKHDAHIPVG
160 170 180 190 200
PEMIATFKEM NPQLPIVAIG GINTNNVAPI VEAGANGISV ISAISKSENI
210
EKTVNRFKDF FNN
Length:213
Mass (Da):23,399
Last modified:June 26, 2007 - v1
Checksum:i8FEFB39D6EF82F94
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000703 Genomic DNA. Translation: ABQ49910.1.
RefSeqiWP_000483153.1. NC_009487.1.

Genome annotation databases

EnsemblBacteriaiABQ49910; ABQ49910; SaurJH9_2128.
GeneIDi28380324.
KEGGisaj:SaurJH9_2128.
PATRICi19542195. VBIStaAur42398_2245.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000703 Genomic DNA. Translation: ABQ49910.1.
RefSeqiWP_000483153.1. NC_009487.1.

3D structure databases

ProteinModelPortaliA5IUN7.
SMRiA5IUN7.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABQ49910; ABQ49910; SaurJH9_2128.
GeneIDi28380324.
KEGGisaj:SaurJH9_2128.
PATRICi19542195. VBIStaAur42398_2245.

Phylogenomic databases

HOGENOMiHOG000155781.
KOiK00788.
OMAiQVREKHG.

Enzyme and pathway databases

UniPathwayiUPA00060; UER00141.

Family and domain databases

CDDicd00564. TMP_TenI. 1 hit.
Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_00097. TMP_synthase. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR022998. ThiaminP_synth_SF.
IPR003733. TMP_synthase.
[Graphical view]
PfamiPF02581. TMP-TENI. 1 hit.
[Graphical view]
SUPFAMiSSF51391. SSF51391. 1 hit.
TIGRFAMsiTIGR00693. thiE. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiTHIE_STAA9
AccessioniPrimary (citable) accession number: A5IUN7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: June 26, 2007
Last modified: November 2, 2016
This is version 66 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.