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Protein

Thiamine-phosphate synthase

Gene

thiE

Organism
Mycobacterium leprae (strain TN)
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 sitei91HMP-PPUniRule annotation1
Metal bindingi92MagnesiumUniRule annotation1
Metal bindingi111MagnesiumUniRule annotation1
Binding sitei130HMP-PPUniRule annotation1
Binding sitei163HMP-PPUniRule annotation1
Binding sitei191THZ-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:ML0300
ORF Names:MLCB1450.23c
OrganismiMycobacterium leprae (strain TN)
Taxonomic identifieri272631 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacterium
Proteomesi
  • UP000000806 Componenti: Chromosome

Organism-specific databases

LepromaiML0300.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001570241 – 235Thiamine-phosphate synthaseAdd BLAST235

Interactioni

Protein-protein interaction databases

STRINGi272631.ML0300.

Structurei

3D structure databases

ProteinModelPortaliQ9ZBL5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni50 – 54HMP-PP bindingUniRule annotation5
Regioni160 – 162THZ-P bindingUniRule annotation3

Sequence similaritiesi

Belongs to the thiamine-phosphate synthase family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4107RZ7. Bacteria.
COG0352. LUCA.
HOGENOMiHOG000155781.
KOiK00788.
OMAiIIGVTTH.
OrthoDBiPOG091H01SL.

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.

Q9ZBL5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQEPHRQPAI CLSTRLAKAR LYLCTDARRE RGDLAQFVNA ALAGGVDIVQ
60 70 80 90 100
LRDKGSVGEQ QFGPLEARDA LAACEIFTDA TGRHDALFAV NDRADIARAA
110 120 130 140 150
GADVLHLGQG DLPPGVARQI VCRQMLIGLS THDRHQVAAA VAALDAGLVD
160 170 180 190 200
YFCVGPCWPT PTKPDRPAPG LELVRAAAEL AGDKPWFAIG GIDAQRLPDV
210 220 230
LHAGARRIVV VRAITAAADP RAAAEQLIST LTATS
Length:235
Mass (Da):24,846
Last modified:May 1, 1999 - v1
Checksum:i3447784202D3DD1C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL035159 Genomic DNA. Translation: CAA22707.1.
AL583918 Genomic DNA. Translation: CAC29808.1.
PIRiT44738.
RefSeqiNP_301336.1. NC_002677.1.
WP_010907660.1. NC_002677.1.

Genome annotation databases

EnsemblBacteriaiCAC29808; CAC29808; CAC29808.
GeneIDi908861.
KEGGimle:ML0300.
PATRICi18051036. VBIMycLep78757_0467.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL035159 Genomic DNA. Translation: CAA22707.1.
AL583918 Genomic DNA. Translation: CAC29808.1.
PIRiT44738.
RefSeqiNP_301336.1. NC_002677.1.
WP_010907660.1. NC_002677.1.

3D structure databases

ProteinModelPortaliQ9ZBL5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi272631.ML0300.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAC29808; CAC29808; CAC29808.
GeneIDi908861.
KEGGimle:ML0300.
PATRICi18051036. VBIMycLep78757_0467.

Organism-specific databases

LepromaiML0300.

Phylogenomic databases

eggNOGiENOG4107RZ7. Bacteria.
COG0352. LUCA.
HOGENOMiHOG000155781.
KOiK00788.
OMAiIIGVTTH.
OrthoDBiPOG091H01SL.

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_MYCLE
AccessioniPrimary (citable) accession number: Q9ZBL5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 1, 1999
Last modified: September 7, 2016
This is version 98 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

Complete proteome, Reference proteome

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.