Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P39594

- THIE_BACSU

UniProt

P39594 - THIE_BACSU

Protein

Thiamine-phosphate synthase

Gene

thiE

Organism
Bacillus subtilis (strain 168)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 115 (01 Oct 2014)
      Sequence version 1 (01 Feb 1995)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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

    Binds 1 magnesium 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

    Keywords - Molecular functioni

    Transferase

    Keywords - Biological processi

    Thiamine biosynthesis

    Keywords - Ligandi

    Magnesium, Metal-binding

    Enzyme and pathway databases

    BioCyciBSUB:BSU38290-MONOMER.
    MetaCyc:BSU38290-MONOMER.
    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: 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 – 127
    Beta strandi15 – 195
    Helixi21 – 233
    Helixi28 – 3811
    Beta strandi41 – 455
    Helixi55 – 7218
    Beta strandi76 – 805
    Helixi82 – 887
    Beta strandi91 – 955
    Beta strandi97 – 993
    Helixi102 – 1098
    Beta strandi112 – 1187
    Helixi121 – 13010
    Beta strandi133 – 1375
    Beta strandi145 – 1484
    Helixi156 – 1638
    Beta strandi170 – 1756
    Turni178 – 1803
    Helixi182 – 1865
    Beta strandi190 – 1956
    Helixi196 – 1994
    Beta strandi201 – 2033
    Helixi204 – 22118

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    KOiK00788.
    OMAiQFREKGP.
    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

    MTRISREMMK ELLSVYFIMG SNNTKADPVT VVQKALKGGA TLYQFREKGG    50
    DALTGEARIK FAEKAQAACR EAGVPFIVND DVELALNLKA DGIHIGQEDA 100
    NAKEVRAAIG DMILGVSAHT MSEVKQAEED GADYVGLGPI YPTETKKDTR 150
    AVQGVSLIEA VRRQGISIPI VGIGGITIDN AAPVIQAGAD GVSMISAISQ 200
    AEDPESAARK FREEIQTYKT GR 222
    Length:222
    Mass (Da):23,681
    Last modified:February 1, 1995 - v1
    Checksum:iBF09EB73866F4FB4
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X73124 Genomic DNA. Translation: CAA51582.1 .
    AL009126 Genomic DNA. Translation: CAB15855.1 .
    PIRi S39681.
    RefSeqi NP_391708.1. NC_000964.3.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1G4E X-ray 1.60 A/B 1-222 [» ]
    1G4P X-ray 2.50 A/B 1-222 [» ]
    1G4S X-ray 1.70 A/B 1-222 [» ]
    1G4T X-ray 1.55 A/B 1-222 [» ]
    1G67 X-ray 1.40 A/B 1-222 [» ]
    1G69 X-ray 1.50 A/B 1-222 [» ]
    1G6C X-ray 1.40 A/B 1-222 [» ]
    2TPS X-ray 1.25 A/B 1-222 [» ]
    3O15 X-ray 1.95 A 1-222 [» ]
    3O16 X-ray 2.10 A 1-222 [» ]
    ProteinModelPortali P39594.
    SMRi P39594. Positions 1-222.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 224308.BSU38290.

    Proteomic databases

    PaxDbi P39594.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAB15855 ; CAB15855 ; BSU38290 .
    GeneIDi 937316.
    KEGGi bsu:BSU38290.
    PATRICi 18979704. VBIBacSub10457_4014.

    Organism-specific databases

    GenoListi BSU38290. [Micado ]

    Phylogenomic databases

    eggNOGi COG0352.
    HOGENOMi HOG000155781.
    KOi K00788.
    OMAi QFREKGP.
    OrthoDBi EOG6W19NW.
    PhylomeDBi P39594.

    Enzyme and pathway databases

    UniPathwayi UPA00060 ; UER00141 .
    BioCyci BSUB:BSU38290-MONOMER.
    MetaCyc:BSU38290-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P39594.

    Family and domain databases

    Gene3Di 3.20.20.70. 1 hit.
    HAMAPi MF_00097. TMP_synthase.
    InterProi IPR013785. Aldolase_TIM.
    IPR022998. ThiaminP_synth_SF.
    IPR003733. TMP_synthase.
    [Graphical view ]
    Pfami PF02581. TMP-TENI. 1 hit.
    [Graphical view ]
    SUPFAMi SSF51391. SSF51391. 1 hit.
    TIGRFAMsi TIGR00693. thiE. 1 hit.
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 115 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