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P40386

- THI6_SCHPO

UniProt

P40386 - THI6_SCHPO

Protein

Probable thiamine biosynthetic bifunctional enzyme

Gene

thi4

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 111 (01 Oct 2014)
      Sequence version 1 (01 Feb 1995)
      Previous versions | rss
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    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).By similarity

    Catalytic activityi

    2-methyl-4-amino-5-hydroxymethylpyrimidine diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = diphosphate + thiamine phosphate.
    ATP + 4-methyl-5-(2-hydroxyethyl)thiazole = ADP + 4-methyl-5-(2-phosphonooxyethyl)thiazole.

    Cofactori

    Binds 1 magnesium ion per subunit.By similarity

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei72 – 721HMP-PPBy similarity
    Metal bindingi73 – 731MagnesiumBy similarity
    Metal bindingi92 – 921MagnesiumBy similarity
    Binding sitei111 – 1111HMP-PPBy similarity
    Binding sitei140 – 1401HMP-PPBy similarity
    Binding sitei173 – 1731THZ-P; via amide nitrogenBy similarity
    Binding sitei281 – 28114-methyl-5-(2-hydroxyethyl)thiazole; via amide nitrogenBy similarity
    Binding sitei355 – 3551ATPBy similarity
    Binding sitei403 – 4031ATPBy similarity
    Binding sitei430 – 43014-methyl-5-(2-hydroxyethyl)thiazole; via amide nitrogenBy similarity
    Active sitei433 – 4331Proton acceptor; for hydroxyethylthiazole kinase activityBy similarity

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. hydroxyethylthiazole kinase activity Source: UniProtKB-EC
    3. metal ion binding Source: UniProtKB-KW
    4. thiamine-phosphate diphosphorylase activity Source: UniProtKB-EC

    GO - Biological processi

    1. thiamine biosynthetic process Source: UniProtKB-KW
    2. thiamine diphosphate biosynthetic process Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Kinase, Transferase

    Keywords - Biological processi

    Thiamine biosynthesis

    Keywords - Ligandi

    ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    UniPathwayiUPA00060; UER00139.
    UPA00060; UER00141.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Probable thiamine biosynthetic bifunctional enzyme
    Including the following 2 domains:
    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
    Hydroxyethylthiazole kinase (EC:2.7.1.50)
    Alternative name(s):
    4-methyl-5-beta-hydroxyethylthiazole kinase
    Short name:
    TH kinase
    Short name:
    THZ kinase
    Gene namesi
    Name:thi4
    ORF Names:SPAC23H4.10c
    OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
    Taxonomic identifieri284812 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
    ProteomesiUP000002485: Chromosome I

    Organism-specific databases

    PomBaseiSPAC23H4.10c.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: PomBase
    2. cytosol Source: PomBase

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 518518Probable thiamine biosynthetic bifunctional enzymePRO_0000157089Add
    BLAST

    Proteomic databases

    MaxQBiP40386.

    Expressioni

    Inductioni

    Repressed by thiamine and 5-(2-hydroxyethyl)-4-methylthiazole.

    Interactioni

    Protein-protein interaction databases

    BioGridi278362. 7 interactions.
    MINTiMINT-4689729.
    STRINGi4896.SPAC23H4.10c-1.

    Structurei

    3D structure databases

    ProteinModelPortaliP40386.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 229229Thiamine-phosphate synthaseAdd
    BLAST
    Regioni40 – 445HMP-PP bindingBy similarity
    Regioni137 – 1393THZ-P bindingBy similarity
    Regioni199 – 2002THZ-P bindingBy similarity
    Regioni230 – 518289Hydroxyethylthiazole kinaseAdd
    BLAST

    Sequence similaritiesi

    In the N-terminal section; belongs to the thiamine-phosphate synthase family.Curated
    In the C-terminal section; belongs to the Thz kinase family.Curated

    Phylogenomic databases

    eggNOGiCOG0352.
    HOGENOMiHOG000214306.
    KOiK14154.
    OMAiNLVVQNF.
    OrthoDBiEOG7KDFMZ.
    PhylomeDBiP40386.

    Family and domain databases

    Gene3Di3.20.20.70. 1 hit.
    3.40.1190.20. 1 hit.
    HAMAPiMF_00097. TMP_synthase.
    MF_00228. Thz_kinase.
    InterProiIPR013785. Aldolase_TIM.
    IPR000417. Hyethyz_kinase.
    IPR029056. Ribokinase-like.
    IPR022998. ThiaminP_synth_SF.
    IPR003733. TMP_synthase.
    [Graphical view]
    PfamiPF02110. HK. 1 hit.
    PF02581. TMP-TENI. 1 hit.
    [Graphical view]
    PRINTSiPR01099. HYETHTZKNASE.
    SUPFAMiSSF51391. SSF51391. 1 hit.
    SSF53613. SSF53613. 1 hit.
    TIGRFAMsiTIGR00693. thiE. 1 hit.
    TIGR00694. thiM. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P40386-1 [UniParc]FASTAAdd to Basket

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    MKRQIDYSLY LVTSSSLIAP GSTIERQVEE GILGGVTLVQ HREKDISTKC    50
    FVERAKRLSE ICKKYDVPFL INDRIDVALA VGADGVHIGQ DDMDCALARK 100
    ILGDDAIIGV STNNIEEIEK AAADGADYVG IGSIYETNTK DVKDRLIGIT 150
    GLRKILEHVS KMHCQLGTVA IAGLNSSNIQ RVIYLSEANG KRIDGIALVS 200
    AIMCSITPRE TAKELRNLIA TPPCFAQARS SLTTPKDLLN QIPAALQKLK 250
    DFTPLIHHLT NAVAKNFSAN VTLAAYGSPT MGESYDEVAD FAKAPGALVL 300
    NIGILENTKT YIHAAQVNND LARPVILDPV AVGATTARSK VINTLLNYAY 350
    YDIIKGNEGE IMNLAGEQGL MRGVDSISQH TLAARITAVH RLAVERRCVV 400
    AMSGAVDVIS DGNSTYVIKN GNPLLGQITA SGCSLGSVMG VTASICQNDK 450
    LLAAITATLL YNIASELAVE AKNSCGDLLV QGPGTFIPIF VDKLHQLINE 500
    TIKGNVDWIE RAKLEKAE 518
    Length:518
    Mass (Da):55,566
    Last modified:February 1, 1995 - v1
    Checksum:iB8836D2BD67C79AA
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X78824 Genomic DNA. Translation: CAA55402.1.
    CU329670 Genomic DNA. Translation: CAB11664.1.
    PIRiS44183.
    RefSeqiNP_593396.1. NM_001018828.2.

    Genome annotation databases

    EnsemblFungiiSPAC23H4.10c.1; SPAC23H4.10c.1:pep; SPAC23H4.10c.
    GeneIDi2541872.
    KEGGispo:SPAC23H4.10c.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X78824 Genomic DNA. Translation: CAA55402.1 .
    CU329670 Genomic DNA. Translation: CAB11664.1 .
    PIRi S44183.
    RefSeqi NP_593396.1. NM_001018828.2.

    3D structure databases

    ProteinModelPortali P40386.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 278362. 7 interactions.
    MINTi MINT-4689729.
    STRINGi 4896.SPAC23H4.10c-1.

    Proteomic databases

    MaxQBi P40386.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii SPAC23H4.10c.1 ; SPAC23H4.10c.1:pep ; SPAC23H4.10c .
    GeneIDi 2541872.
    KEGGi spo:SPAC23H4.10c.

    Organism-specific databases

    PomBasei SPAC23H4.10c.

    Phylogenomic databases

    eggNOGi COG0352.
    HOGENOMi HOG000214306.
    KOi K14154.
    OMAi NLVVQNF.
    OrthoDBi EOG7KDFMZ.
    PhylomeDBi P40386.

    Enzyme and pathway databases

    UniPathwayi UPA00060 ; UER00139 .
    UPA00060 ; UER00141 .

    Miscellaneous databases

    NextBioi 20802959.

    Family and domain databases

    Gene3Di 3.20.20.70. 1 hit.
    3.40.1190.20. 1 hit.
    HAMAPi MF_00097. TMP_synthase.
    MF_00228. Thz_kinase.
    InterProi IPR013785. Aldolase_TIM.
    IPR000417. Hyethyz_kinase.
    IPR029056. Ribokinase-like.
    IPR022998. ThiaminP_synth_SF.
    IPR003733. TMP_synthase.
    [Graphical view ]
    Pfami PF02110. HK. 1 hit.
    PF02581. TMP-TENI. 1 hit.
    [Graphical view ]
    PRINTSi PR01099. HYETHTZKNASE.
    SUPFAMi SSF51391. SSF51391. 1 hit.
    SSF53613. SSF53613. 1 hit.
    TIGRFAMsi TIGR00693. thiE. 1 hit.
    TIGR00694. thiM. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Cloning, nucleotide sequence, and regulation of Schizosaccharomyces pombe thi4, a thiamine biosynthetic gene."
      Zurlinden A., Schweingruber M.E.
      J. Bacteriol. 176:6631-6635(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: 972 / ATCC 24843.
    2. "The genome sequence of Schizosaccharomyces pombe."
      Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.
      , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
      Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: 972 / ATCC 24843.

    Entry informationi

    Entry nameiTHI6_SCHPO
    AccessioniPrimary (citable) accession number: P40386
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1995
    Last sequence update: February 1, 1995
    Last modified: October 1, 2014
    This is version 111 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Multifunctional enzyme, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. Schizosaccharomyces pombe
      Schizosaccharomyces pombe: entries and gene names
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3