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Protein

Thiamine-phosphate synthase

Gene

thiE

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 5 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). Is also able to use the 2-methoxy analog MeO-HMP-PP, as substrate in vitro, but not the 2-trifluoromethyl analog CF(3)-HMP-PP.2 Publications

Catalytic activityi

2-methyl-4-amino-5-hydroxymethylpyrimidine diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = diphosphate + thiamine phosphate.1 Publication

Cofactori

Mg2+1 PublicationNote: Binds 1 Mg2+ ion per subunit.1 Publication

Kineticsi

  1. KM=0.7 µM for HMP-PP1 Publication
  2. KM=1.2 µM for THZ-P1 Publication

Vmax=0.7 µmol/min/mg enzyme1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei79 – 791HMP-PP
Metal bindingi80 – 801Magnesium
Metal bindingi99 – 991Magnesium
Binding sitei117 – 1171HMP-PP
Binding sitei146 – 1461HMP-PP
Binding sitei175 – 1751THZ-P; via amide nitrogen

GO - Molecular functioni

  1. magnesium ion binding Source: UniProtKB-HAMAP
  2. thiamine-phosphate diphosphorylase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. thiamine biosynthetic process Source: UniProtKB-HAMAP
  2. thiamine diphosphate biosynthetic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Thiamine biosynthesis

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciBSUB:BSU38290-MONOMER.
MetaCyc:BSU38290-MONOMER.
BRENDAi2.5.1.3. 658.
UniPathwayiUPA00060; UER00141.

Names & Taxonomyi

Protein namesi
Recommended name:
Thiamine-phosphate synthase (EC:2.5.1.3)
Short name:
TP synthase
Short name:
TPS
Alternative name(s):
Thiamine-phosphate pyrophosphorylase
Short name:
TMP pyrophosphorylase
Short name:
TMP-PPase
Gene namesi
Name:thiE
Synonyms:thiC, ywbK
Ordered Locus Names:BSU38290
ORF Names:ipa-26d
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
ProteomesiUP000001570 Componenti: Chromosome

Organism-specific databases

GenoListiBSU38290. [Micado]

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi117 – 1171S → A: 8000-fold reduction in catalytic activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 222222Thiamine-phosphate synthasePRO_0000156995Add
BLAST

Proteomic databases

PaxDbiP39594.

Expressioni

Inductioni

Is weakly repressed by THZ and not at all by thiamine.1 Publication

Interactioni

Subunit structurei

Monomer.1 Publication

Protein-protein interaction databases

STRINGi224308.BSU38290.

Structurei

Secondary structure

1
222
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi6 – 127Combined sources
Beta strandi15 – 195Combined sources
Helixi21 – 233Combined sources
Helixi28 – 3811Combined sources
Beta strandi41 – 455Combined sources
Helixi55 – 7218Combined sources
Beta strandi76 – 805Combined sources
Helixi82 – 887Combined sources
Beta strandi91 – 955Combined sources
Beta strandi97 – 993Combined sources
Helixi102 – 1098Combined sources
Beta strandi112 – 1187Combined sources
Helixi121 – 13010Combined sources
Beta strandi133 – 1375Combined sources
Beta strandi145 – 1484Combined sources
Helixi156 – 1638Combined sources
Beta strandi170 – 1756Combined sources
Turni178 – 1803Combined sources
Helixi182 – 1865Combined sources
Beta strandi190 – 1956Combined sources
Helixi196 – 1994Combined sources
Beta strandi201 – 2033Combined sources
Helixi204 – 22118Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1G4EX-ray1.60A/B1-222[»]
1G4PX-ray2.50A/B1-222[»]
1G4SX-ray1.70A/B1-222[»]
1G4TX-ray1.55A/B1-222[»]
1G67X-ray1.40A/B1-222[»]
1G69X-ray1.50A/B1-222[»]
1G6CX-ray1.40A/B1-222[»]
2TPSX-ray1.25A/B1-222[»]
3O15X-ray1.95A1-222[»]
3O16X-ray2.10A1-222[»]
ProteinModelPortaliP39594.
SMRiP39594. Positions 1-222.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP39594.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni44 – 485HMP-PP binding
Regioni143 – 1453THZ-P binding
Regioni195 – 1962THZ-P binding

Sequence similaritiesi

Belongs to the thiamine-phosphate synthase family.Curated

Phylogenomic databases

eggNOGiCOG0352.
HOGENOMiHOG000155781.
InParanoidiP39594.
KOiK00788.
OMAiVSAICHA.
OrthoDBiEOG6W19NW.
PhylomeDBiP39594.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_00097. TMP_synthase.
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.

P39594-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTRISREMMK ELLSVYFIMG SNNTKADPVT VVQKALKGGA TLYQFREKGG
60 70 80 90 100
DALTGEARIK FAEKAQAACR EAGVPFIVND DVELALNLKA DGIHIGQEDA
110 120 130 140 150
NAKEVRAAIG DMILGVSAHT MSEVKQAEED GADYVGLGPI YPTETKKDTR
160 170 180 190 200
AVQGVSLIEA VRRQGISIPI VGIGGITIDN AAPVIQAGAD GVSMISAISQ
210 220
AEDPESAARK FREEIQTYKT GR
Length:222
Mass (Da):23,681
Last modified:February 1, 1995 - v1
Checksum:iBF09EB73866F4FB4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X73124 Genomic DNA. Translation: CAA51582.1.
AL009126 Genomic DNA. Translation: CAB15855.1.
PIRiS39681.
RefSeqiNP_391708.1. NC_000964.3.

Genome annotation databases

EnsemblBacteriaiCAB15855; CAB15855; BSU38290.
GeneIDi937316.
KEGGibsu:BSU38290.
PATRICi18979704. VBIBacSub10457_4014.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X73124 Genomic DNA. Translation: CAA51582.1.
AL009126 Genomic DNA. Translation: CAB15855.1.
PIRiS39681.
RefSeqiNP_391708.1. NC_000964.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1G4EX-ray1.60A/B1-222[»]
1G4PX-ray2.50A/B1-222[»]
1G4SX-ray1.70A/B1-222[»]
1G4TX-ray1.55A/B1-222[»]
1G67X-ray1.40A/B1-222[»]
1G69X-ray1.50A/B1-222[»]
1G6CX-ray1.40A/B1-222[»]
2TPSX-ray1.25A/B1-222[»]
3O15X-ray1.95A1-222[»]
3O16X-ray2.10A1-222[»]
ProteinModelPortaliP39594.
SMRiP39594. Positions 1-222.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224308.BSU38290.

Proteomic databases

PaxDbiP39594.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB15855; CAB15855; BSU38290.
GeneIDi937316.
KEGGibsu:BSU38290.
PATRICi18979704. VBIBacSub10457_4014.

Organism-specific databases

GenoListiBSU38290. [Micado]

Phylogenomic databases

eggNOGiCOG0352.
HOGENOMiHOG000155781.
InParanoidiP39594.
KOiK00788.
OMAiVSAICHA.
OrthoDBiEOG6W19NW.
PhylomeDBiP39594.

Enzyme and pathway databases

UniPathwayiUPA00060; UER00141.
BioCyciBSUB:BSU38290-MONOMER.
MetaCyc:BSU38290-MONOMER.
BRENDAi2.5.1.3. 658.

Miscellaneous databases

EvolutionaryTraceiP39594.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_00097. TMP_synthase.
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...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 168.
  2. "The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
    Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V.
    , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
    Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 168.
  3. "Characterization of the Bacillus subtilis thiC operon involved in thiamine biosynthesis."
    Zhang Y., Taylor S.V., Chiu H.-J., Begley T.P.
    J. Bacteriol. 179:3030-3035(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, KINETIC PARAMETERS, INDUCTION.
    Strain: 168 / CU1065.
  4. "Mechanistic studies on thiamin phosphate synthase: evidence for a dissociative mechanism."
    Reddick J.J., Nicewonger R., Begley T.P.
    Biochemistry 40:10095-10102(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBSTRATE SPECIFICITY, MUTAGENESIS OF SER-117, REACTION MECHANISM.
    Strain: 168 / CU1065.
  5. "Crystal structure of thiamin phosphate synthase from Bacillus subtilis at 1.25 A resolution."
    Chiu H.-J., Reddick J.J., Begley T.P., Ealick S.E.
    Biochemistry 38:6460-6470(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.25 ANGSTROMS) IN COMPLEX WITH THIAMINE PHOSPHATE AND MAGNESIUM PYROPHOSPHATE.
    Strain: 168 / CU1065.
  6. "Structural characterization of the enzyme-substrate, enzyme-intermediate, and enzyme-product complexes of thiamin phosphate synthase."
    Peapus D.H., Chiu H.J., Campobasso N., Reddick J.J., Begley T.P., Ealick S.E.
    Biochemistry 40:10103-10114(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF WILD-TYPE AND MUTANT ALA-117 IN COMPLEXES WITH SUBSTRATE; PRODUCTS AND INTERMEDIATES.
    Strain: 168 / CU1065.
  7. "Crystal structure and kinetic characterization of Bacillus subtilis thiamin phosphate synthase with a carboxylated thiazole phosphate."
    McCulloch K.M., Hanes J.W., Abdelwahed S., Mahanta N., Hazra A., Ishida K., Begley T.P., Ealick S.E.
    Submitted (JUL-2011) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS).

Entry informationi

Entry nameiTHIE_BACSU
AccessioniPrimary (citable) accession number: P39594
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: April 1, 2015
This is version 119 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

Thiamine phosphate synthase appears to proceed with a dissociative mechanism (SN1 like) in which the pyrimidine pyrophosphate dissociates to give a reactive pyrimidine intermediate which is then trapped by the thiazole moiety.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.