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Q8NQH1

- THIED_CORGL

UniProt

Q8NQH1 - THIED_CORGL

Protein

Thiamine biosynthesis multifunctional protein ThiED

Gene

theD

Organism
Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025)
Status
Reviewed - Annotation score: 5 out of 5- Protein inferred from homologyi
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    • History
      Entry version 89 (01 Oct 2014)
      Sequence version 2 (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 sitei69 – 691HMP-PPBy similarity
    Metal bindingi70 – 701MagnesiumBy similarity
    Metal bindingi88 – 881MagnesiumBy similarity
    Binding sitei107 – 1071HMP-PPBy similarity
    Binding sitei143 – 1431HMP-PPBy similarity
    Binding sitei174 – 1741THZ-P; via amide nitrogenBy similarity
    Binding sitei282 – 2821HydroxymethylpyrimidineBy 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

    BioCyciCGLU196627:GJDM-1450-MONOMER.
    UniPathwayiUPA00060; UER00138.
    UPA00060; UER00141.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Thiamine biosynthesis multifunctional 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:theD
    Synonyms:thiD1
    Ordered Locus Names:Cgl1463, cg1654
    OrganismiCorynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025)
    Taxonomic identifieri196627 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeCorynebacteriaceaeCorynebacterium
    ProteomesiUP000000582: Chromosome, UP000001009: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 763763Thiamine biosynthesis multifunctional protein ThiEDPRO_0000192039Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi196627.cg1654.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8NQH1.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 210210Thiamine-phosphate synthaseAdd
    BLAST
    Regioni37 – 415HMP-PP bindingBy similarity
    Regioni140 – 1423THZ-P bindingBy similarity
    Regioni194 – 1952THZ-P bindingBy similarity
    Regioni245 – 500256Hydroxymethylpyrimidine/phosphomethylpyrimidine kinaseAdd
    BLAST
    Regioni550 – 763214Thiaminase-2Add
    BLAST

    Sequence similaritiesi

    In the N-terminal section; belongs to the thiamine-phosphate synthase family.Curated
    In the central section; belongs to the ThiD family.Curated
    In the C-terminal section; belongs to the thiaminase-2 family.Curated

    Phylogenomic databases

    eggNOGiCOG0351.
    HOGENOMiHOG000225275.
    KOiK14153.
    OMAiGFWEMFP.
    OrthoDBiEOG6XWV53.

    Family and domain databases

    Gene3Di1.20.910.10. 1 hit.
    3.20.20.70. 1 hit.
    3.40.1190.20. 1 hit.
    HAMAPiMF_00097. TMP_synthase.
    InterProiIPR013785. Aldolase_TIM.
    IPR016084. Haem_Oase-like_multi-hlx.
    IPR004399. HMP/HMP-P_kinase.
    IPR013749. PM/HMP-P_kinase-1.
    IPR029056. Ribokinase-like.
    IPR004305. Thiaminase-2/PQQC.
    IPR022998. ThiaminP_synth_SF.
    IPR003733. TMP_synthase.
    [Graphical view]
    PfamiPF08543. Phos_pyr_kin. 1 hit.
    PF03070. TENA_THI-4. 1 hit.
    PF02581. TMP-TENI. 1 hit.
    [Graphical view]
    SUPFAMiSSF48613. SSF48613. 1 hit.
    SSF51391. SSF51391. 1 hit.
    SSF53613. SSF53613. 1 hit.
    TIGRFAMsiTIGR00097. HMP-P_kinase. 1 hit.
    TIGR00693. thiE. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q8NQH1-1 [UniParc]FASTAAdd to Basket

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    MTDFSLYLVT DPVLGGGPEK VAGIVDSAIS GGVSVVQLRD KNSGVEDVRA    50
    AAKELKELCD ARGVALVVND YLDIAVELGL HLHIGQGDTP YTQARELLPA 100
    HLELGLSIEN LDQLHAVIAQ CAETGVALPD VIGIGPVAST ATKPDAAPAL 150
    GVEGIAEIAA VAQDHGIASV AIGGVGLRNA AELAATPIDG LCVVSEIMTA 200
    ANPAAAATRL RTAFQPTFSP ETQTELSQTE LQGAFVNSPS APRVLSIAGT 250
    DPTGGAGIQA DLKSIAAGGG YGMCVVTSLV AQNTHGVNTI HTPPLTFLEE 300
    QLEAVFSDVT VDAIKLGMLG SADTVDLVAS WLGSHEHGPV VLDPVMIATS 350
    GDRLLDASAE ESLRRLAVHV DVVTPNIPEL AVLCDSAPAI TMDEAIAQAQ 400
    GFARTHDTIV IVKGGHLTGA LADNAVVRPD GSVFQVENLR VNTTNSHGTG 450
    CSLSASLATK IAAGESVEKA LEWSTRWLNE ALRHADHLAV GTGNGPVDHG 500
    HLARRMTHAA ETTPWAHLRA PRLDGATAAS FTTPSTVKSP APRIEPAGPF 550
    TRALWEASGD IIAGINSSDF ITMLGDGTLR RPEFDFYIDQ DAQYLAQYSR 600
    ALARLSSIAP DSHAQIEWAQ SAAECLVVEA ELHRSYMAGK EVSAPSHITM 650
    AYTDFLIART YTEDYVCGVA AVLPCYWLYA EIGLMLAEQN HDEHPYKDWL 700
    NTYSGEEFIA GTRAAIARLE KALENAGAEQ RVDAARAFLS ASVHEREFFD 750
    QATRHGWTMV GSS 763
    Length:763
    Mass (Da):80,355
    Last modified:May 24, 2004 - v2
    Checksum:iCA992321E884577F
    GO

    Sequence cautioni

    The sequence BAB98856.1 differs from that shown. Reason: Erroneous initiation.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BA000036 Genomic DNA. Translation: BAB98856.1. Different initiation.
    BX927152 Genomic DNA. Translation: CAF21472.1.
    RefSeqiNP_600680.3. NC_003450.3.
    WP_011014382.1. NC_006958.1.
    YP_225748.1. NC_006958.1.

    Genome annotation databases

    EnsemblBacteriaiBAB98856; BAB98856; BAB98856.
    CAF21472; CAF21472; cg1654.
    GeneIDi1019437.
    KEGGicgb:cg1654.
    cgl:NCgl1407.
    PATRICi21494969. VBICorGlu203724_1430.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BA000036 Genomic DNA. Translation: BAB98856.1 . Different initiation.
    BX927152 Genomic DNA. Translation: CAF21472.1 .
    RefSeqi NP_600680.3. NC_003450.3.
    WP_011014382.1. NC_006958.1.
    YP_225748.1. NC_006958.1.

    3D structure databases

    ProteinModelPortali Q8NQH1.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 196627.cg1654.

    Protocols and materials databases

    DNASUi 3345397.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai BAB98856 ; BAB98856 ; BAB98856 .
    CAF21472 ; CAF21472 ; cg1654 .
    GeneIDi 1019437.
    KEGGi cgb:cg1654.
    cgl:NCgl1407.
    PATRICi 21494969. VBICorGlu203724_1430.

    Phylogenomic databases

    eggNOGi COG0351.
    HOGENOMi HOG000225275.
    KOi K14153.
    OMAi GFWEMFP.
    OrthoDBi EOG6XWV53.

    Enzyme and pathway databases

    UniPathwayi UPA00060 ; UER00138 .
    UPA00060 ; UER00141 .
    BioCyci CGLU196627:GJDM-1450-MONOMER.

    Family and domain databases

    Gene3Di 1.20.910.10. 1 hit.
    3.20.20.70. 1 hit.
    3.40.1190.20. 1 hit.
    HAMAPi MF_00097. TMP_synthase.
    InterProi IPR013785. Aldolase_TIM.
    IPR016084. Haem_Oase-like_multi-hlx.
    IPR004399. HMP/HMP-P_kinase.
    IPR013749. PM/HMP-P_kinase-1.
    IPR029056. Ribokinase-like.
    IPR004305. Thiaminase-2/PQQC.
    IPR022998. ThiaminP_synth_SF.
    IPR003733. TMP_synthase.
    [Graphical view ]
    Pfami PF08543. Phos_pyr_kin. 1 hit.
    PF03070. TENA_THI-4. 1 hit.
    PF02581. TMP-TENI. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48613. SSF48613. 1 hit.
    SSF51391. SSF51391. 1 hit.
    SSF53613. SSF53613. 1 hit.
    TIGRFAMsi TIGR00097. HMP-P_kinase. 1 hit.
    TIGR00693. thiE. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "The Corynebacterium glutamicum genome: features and impacts on biotechnological processes."
      Ikeda M., Nakagawa S.
      Appl. Microbiol. Biotechnol. 62:99-109(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.

    Entry informationi

    Entry nameiTHIED_CORGL
    AccessioniPrimary (citable) accession number: Q8NQH1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 24, 2004
    Last sequence update: May 24, 2004
    Last modified: October 1, 2014
    This is version 89 of the entry and version 2 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