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P61422

- THIED_GEOSL

UniProt

P61422 - THIED_GEOSL

Protein

Thiamine biosynthesis bifunctional protein ThiED

Gene

thiDE

Organism
Geobacter sulfurreducens (strain ATCC 51573 / DSM 12127 / PCA)
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi
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    • History
      Entry version 83 (01 Oct 2014)
      Sequence version 1 (24 May 2004)
      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
    Catalyzes the phosphorylation of hydroxymethylpyrimidine phosphate (HMP-P) to HMP-PP, and of HMP to HMP-P.By similarity

    Catalytic activityi

    2-methyl-4-amino-5-hydroxymethylpyrimidine diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = diphosphate + thiamine phosphate.
    ATP + 4-amino-5-hydroxymethyl-2-methylpyrimidine = ADP + 4-amino-5-phosphonooxymethyl-2-methylpyrimidine.
    ATP + 4-amino-2-methyl-5-phosphomethylpyrimidine = ADP + 4-amino-2-methyl-5-diphosphomethylpyrimidine.

    Cofactori

    Binds 1 magnesium ion per subunit.By similarity

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei82 – 821HMP-PPBy similarity
    Metal bindingi83 – 831MagnesiumBy similarity
    Metal bindingi102 – 1021MagnesiumBy similarity
    Binding sitei121 – 1211HMP-PPBy similarity
    Binding sitei150 – 1501HMP-PPBy similarity
    Binding sitei177 – 1771THZ-P; via amide nitrogenBy similarity
    Binding sitei266 – 2661HydroxymethylpyrimidineBy similarity

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. hydroxymethylpyrimidine kinase activity Source: UniProtKB-EC
    3. metal ion binding Source: UniProtKB-KW
    4. phosphomethylpyrimidine kinase activity Source: UniProtKB-EC
    5. 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

    BioCyciGSUL243231:GH27-611-MONOMER.
    UniPathwayiUPA00060; UER00138.
    UPA00060; UER00141.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Thiamine biosynthesis bifunctional protein ThiED
    Including the following 2 domains:
    Thiamine-phosphate synthase (EC:2.5.1.3)
    Short name:
    TMP-PPase
    Short name:
    TP synthase
    Short name:
    TPS
    Alternative name(s):
    Thiamine-phosphate pyrophosphorylase
    Short name:
    TMP pyrophosphorylase
    Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase (EC:2.7.1.49, EC:2.7.4.7)
    Alternative name(s):
    Hydroxymethylpyrimidine kinase
    Short name:
    HMP kinase
    Hydroxymethylpyrimidine phosphate kinase
    Short name:
    HMP-P kinase
    Short name:
    HMP-phosphate kinase
    Short name:
    HMPP kinase
    Gene namesi
    Name:thiDE
    Ordered Locus Names:GSU0605
    OrganismiGeobacter sulfurreducens (strain ATCC 51573 / DSM 12127 / PCA)
    Taxonomic identifieri243231 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaDeltaproteobacteriaDesulfuromonadalesGeobacteraceaeGeobacter
    ProteomesiUP000000577: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 490490Thiamine biosynthesis bifunctional protein ThiEDPRO_0000192040Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi243231.GSU0605.

    Structurei

    3D structure databases

    ProteinModelPortaliP61422.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 213213Thiamine-phosphate synthaseAdd
    BLAST
    Regioni50 – 545HMP-PP bindingBy similarity
    Regioni147 – 1493THZ-P bindingBy similarity
    Regioni197 – 1982THZ-P bindingBy similarity
    Regioni229 – 490262Hydroxymethylpyrimidine/phosphomethylpyrimidine 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 ThiD family.Curated

    Phylogenomic databases

    eggNOGiCOG0351.
    HOGENOMiHOG000134175.
    KOiK14153.
    OMAiYLAQGEP.
    OrthoDBiEOG6XWV53.

    Family and domain databases

    Gene3Di3.20.20.70. 1 hit.
    3.40.1190.20. 1 hit.
    HAMAPiMF_00097. TMP_synthase.
    InterProiIPR013785. Aldolase_TIM.
    IPR004399. HMP/HMP-P_kinase.
    IPR013749. PM/HMP-P_kinase-1.
    IPR029056. Ribokinase-like.
    IPR022998. ThiaminP_synth_SF.
    IPR003733. TMP_synthase.
    [Graphical view]
    PfamiPF08543. Phos_pyr_kin. 1 hit.
    PF02581. TMP-TENI. 1 hit.
    [Graphical view]
    SUPFAMiSSF51391. SSF51391. 1 hit.
    SSF53613. SSF53613. 1 hit.
    TIGRFAMsiTIGR00097. HMP-P_kinase. 1 hit.
    TIGR00693. thiE. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P61422-1 [UniParc]FASTAAdd to Basket

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    MASNGHTLRL VINRDKHDSV IRGLYLVTDH DDNLIPRVEA AIDGGARVVQ    50
    YRNKNQDRES RLALGLELRE LCRRRSIPFI VNDDLEMAVS LKADGLHLGQ 100
    GDGDPREARR VLGPGKIIGV STHTLSEALE AQAAGVDYIG LGAMFPSRSK 150
    EVEHVAGSEL LAAIRSSISI PIVAIGGITR DNGASVIDAG ADAVAVISAV 200
    LSHPDPALAA TEIALLFNRR APFPRGSVLT VAGSDSGGGA GIQADLKTVT 250
    LLGSYGSSVL TALTAQNTRG VSGIHGVPPA FVADQLDAVF SDIPVDVVKT 300
    GMLFSAETIV AIAAKLTEYR RRMVVVDPVM VAKGGANLID RGAVSVLKER 350
    LFPLAYLVTP NIPEAERLTG ANISDEESMR EAARRLHRLG ARNVLLKGGH 400
    LLAGDSVDIL FDGAAFHRFV SPRILSKNTH GTGCTFASAI ATYLAQGDPL 450
    REAIARAKRY ITAAIRLAQP LGRGHGPVNH ILAAEDVRDR 490
    Length:490
    Mass (Da):51,910
    Last modified:May 24, 2004 - v1
    Checksum:i924B153FCD5E83D4
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE017180 Genomic DNA. Translation: AAR33936.1.
    RefSeqiNP_951663.1. NC_002939.5.

    Genome annotation databases

    EnsemblBacteriaiAAR33936; AAR33936; GSU0605.
    GeneIDi2687129.
    KEGGigsu:GSU0605.
    PATRICi22023961. VBIGeoSul17553_0603.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE017180 Genomic DNA. Translation: AAR33936.1 .
    RefSeqi NP_951663.1. NC_002939.5.

    3D structure databases

    ProteinModelPortali P61422.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 243231.GSU0605.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAR33936 ; AAR33936 ; GSU0605 .
    GeneIDi 2687129.
    KEGGi gsu:GSU0605.
    PATRICi 22023961. VBIGeoSul17553_0603.

    Phylogenomic databases

    eggNOGi COG0351.
    HOGENOMi HOG000134175.
    KOi K14153.
    OMAi YLAQGEP.
    OrthoDBi EOG6XWV53.

    Enzyme and pathway databases

    UniPathwayi UPA00060 ; UER00138 .
    UPA00060 ; UER00141 .
    BioCyci GSUL243231:GH27-611-MONOMER.

    Family and domain databases

    Gene3Di 3.20.20.70. 1 hit.
    3.40.1190.20. 1 hit.
    HAMAPi MF_00097. TMP_synthase.
    InterProi IPR013785. Aldolase_TIM.
    IPR004399. HMP/HMP-P_kinase.
    IPR013749. PM/HMP-P_kinase-1.
    IPR029056. Ribokinase-like.
    IPR022998. ThiaminP_synth_SF.
    IPR003733. TMP_synthase.
    [Graphical view ]
    Pfami PF08543. Phos_pyr_kin. 1 hit.
    PF02581. TMP-TENI. 1 hit.
    [Graphical view ]
    SUPFAMi SSF51391. SSF51391. 1 hit.
    SSF53613. SSF53613. 1 hit.
    TIGRFAMsi TIGR00097. HMP-P_kinase. 1 hit.
    TIGR00693. thiE. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 51573 / DSM 12127 / PCA.

    Entry informationi

    Entry nameiTHIED_GEOSL
    AccessioniPrimary (citable) accession number: P61422
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 24, 2004
    Last sequence update: May 24, 2004
    Last modified: October 1, 2014
    This is version 83 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, Multifunctional enzyme, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3