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P39594 (THIE_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 114. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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
Synonyms:thiC, ywbK
Ordered Locus Names:BSU38290
ORF Names:ipa-26d
OrganismBacillus subtilis (strain 168) [Reference proteome] [HAMAP]
Taxonomic identifier224308 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length222 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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). 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. Ref.3 Ref.4

Catalytic activity

2-methyl-4-amino-5-hydroxymethylpyrimidine diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = diphosphate + thiamine phosphate. Ref.3

Cofactor

Binds 1 magnesium ion per subunit. Ref.3

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

Subunit structure

Monomer.

Induction

Is weakly repressed by THZ and not at all by thiamine. Ref.3

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.

Sequence similarities

Belongs to the thiamine-phosphate synthase family.

Biophysicochemical properties

Kinetic parameters:

KM=0.7 µM for HMP-PP Ref.3

KM=1.2 µM for THZ-P

Vmax=0.7 µmol/min/mg enzyme

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 222222Thiamine-phosphate synthase HAMAP-Rule MF_00097
PRO_0000156995

Regions

Region44 – 485HMP-PP binding HAMAP-Rule MF_00097
Region143 – 1453THZ-P binding HAMAP-Rule MF_00097
Region195 – 1962THZ-P binding HAMAP-Rule MF_00097

Sites

Metal binding801Magnesium
Metal binding991Magnesium
Binding site791HMP-PP
Binding site1171HMP-PP
Binding site1461HMP-PP
Binding site1751THZ-P; via amide nitrogen

Experimental info

Mutagenesis1171S → A: 8000-fold reduction in catalytic activity. Ref.4

Secondary structure

............................................. 222
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P39594 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: BF09EB73866F4FB4

FASTA22223,681
        10         20         30         40         50         60 
MTRISREMMK ELLSVYFIMG SNNTKADPVT VVQKALKGGA TLYQFREKGG DALTGEARIK 

        70         80         90        100        110        120 
FAEKAQAACR EAGVPFIVND DVELALNLKA DGIHIGQEDA NAKEVRAAIG DMILGVSAHT 

       130        140        150        160        170        180 
MSEVKQAEED GADYVGLGPI YPTETKKDTR AVQGVSLIEA VRRQGISIPI VGIGGITIDN 

       190        200        210        220 
AAPVIQAGAD GVSMISAISQ AEDPESAARK FREEIQTYKT GR 

« Hide

References

« Hide 'large scale' references
[1]"Bacillus subtilis genome project: cloning and sequencing of the 97 kb region from 325 degrees to 333 degrees."
Glaser P., Kunst F., Arnaud M., Coudart M.P., Gonzales W., Hullo M.-F., Ionescu M., Lubochinsky B., Marcelino L., Moszer I., Presecan E., Santana M., Schneider E., Schweizer J., Vertes A., Rapoport G., Danchin A.
Mol. Microbiol. 10:371-384(1993) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X73124 Genomic DNA. Translation: CAA51582.1.
AL009126 Genomic DNA. Translation: CAB15855.1.
PIRS39681.
RefSeqNP_391708.1. NC_000964.3.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalP39594.
SMRP39594. Positions 1-222.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING224308.BSU38290.

Proteomic databases

PaxDbP39594.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAB15855; CAB15855; BSU38290.
GeneID937316.
KEGGbsu:BSU38290.
PATRIC18979704. VBIBacSub10457_4014.

Organism-specific databases

GenoListBSU38290. [Micado]

Phylogenomic databases

eggNOGCOG0352.
HOGENOMHOG000155781.
KOK00788.
OMAQFREKGP.
OrthoDBEOG6W19NW.
PhylomeDBP39594.

Enzyme and pathway databases

BioCycBSUB:BSU38290-MONOMER.
MetaCyc:BSU38290-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...

Other

EvolutionaryTraceP39594.

Entry information

Entry nameTHIE_BACSU
AccessionPrimary (citable) accession number: P39594
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: July 9, 2014
This is version 114 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList