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Protein

Thiamine-phosphate synthase

Gene

thiE

Organism
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

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 sitei68HMP-PPUniRule annotation1
Metal bindingi69MagnesiumUniRule annotation1
Metal bindingi88MagnesiumUniRule annotation1
Binding sitei106HMP-PPUniRule annotation1
Binding sitei135HMP-PPUniRule annotation1
Binding sitei162THZ-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:PF1334
OrganismiPyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
Taxonomic identifieri186497 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaePyrococcus
Proteomesi
  • UP000001013 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001570741 – 207Thiamine-phosphate synthaseAdd BLAST207

Proteomic databases

PRIDEiQ8U192.

Interactioni

Protein-protein interaction databases

STRINGi186497.PF1334.

Structurei

Secondary structure

1207
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi3 – 6Combined sources4
Beta strandi8 – 12Combined sources5
Turni15 – 17Combined sources3
Helixi20 – 29Combined sources10
Beta strandi33 – 37Combined sources5
Helixi44 – 60Combined sources17
Beta strandi64 – 69Combined sources6
Helixi71 – 77Combined sources7
Beta strandi80 – 84Combined sources5
Helixi91 – 97Combined sources7
Beta strandi101 – 109Combined sources9
Helixi110 – 119Combined sources10
Beta strandi122 – 127Combined sources6
Helixi142 – 152Combined sources11
Beta strandi157 – 162Combined sources6
Turni165 – 167Combined sources3
Helixi168 – 172Combined sources5
Turni173 – 175Combined sources3
Beta strandi177 – 182Combined sources6
Helixi183 – 186Combined sources4
Beta strandi188 – 190Combined sources3
Helixi191 – 206Combined sources16

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1XI3X-ray1.70A/B2-207[»]
ProteinModelPortaliQ8U192.
SMRiQ8U192.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8U192.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni36 – 40HMP-PP bindingUniRule annotation5
Regioni132 – 134THZ-P bindingUniRule annotation3
Regioni182 – 183THZ-P bindingUniRule annotation2

Sequence similaritiesi

Belongs to the thiamine-phosphate synthase family.UniRule annotation

Phylogenomic databases

eggNOGiarCOG01089. Archaea.
COG0352. LUCA.
HOGENOMiHOG000155781.
KOiK00788.
OMAiAWLQYRN.

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.

Q8U192-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNLRNKLKLY VITDRRLKPE VESVREALEG GATAIQMRIK NAPTREMYEI
60 70 80 90 100
GKTLRQLTRE YDALFFVDDR VDVALAVDAD GVQLGPEDMP IEVAKEIAPN
110 120 130 140 150
LIIGASVYSL EEALEAEKKG ADYLGAGSVF PTKTKEDARV IGLEGLRKIV
160 170 180 190 200
ESVKIPVVAI GGINKDNARE VLKTGVDGIA VISAVMGAED VRKATEELRK

IVEEVLG
Length:207
Mass (Da):22,590
Last modified:June 1, 2002 - v1
Checksum:i7776F777009AE858
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE009950 Genomic DNA. Translation: AAL81458.1.
RefSeqiWP_011012480.1. NC_003413.1.

Genome annotation databases

EnsemblBacteriaiAAL81458; AAL81458; PF1334.
GeneIDi1469209.
KEGGipfu:PF1334.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE009950 Genomic DNA. Translation: AAL81458.1.
RefSeqiWP_011012480.1. NC_003413.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1XI3X-ray1.70A/B2-207[»]
ProteinModelPortaliQ8U192.
SMRiQ8U192.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi186497.PF1334.

Proteomic databases

PRIDEiQ8U192.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAL81458; AAL81458; PF1334.
GeneIDi1469209.
KEGGipfu:PF1334.

Phylogenomic databases

eggNOGiarCOG01089. Archaea.
COG0352. LUCA.
HOGENOMiHOG000155781.
KOiK00788.
OMAiAWLQYRN.

Enzyme and pathway databases

UniPathwayiUPA00060; UER00141.

Miscellaneous databases

EvolutionaryTraceiQ8U192.

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_PYRFU
AccessioniPrimary (citable) accession number: Q8U192
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 19, 2002
Last sequence update: June 1, 2002
Last modified: November 2, 2016
This is version 97 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.