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Q8FTH8

- THIED_COREF

UniProt

Q8FTH8 - THIED_COREF

Protein

Thiamine biosynthesis multifunctional protein ThiED

Gene

thiED

Organism
Corynebacterium efficiens (strain DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395)
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi
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    • History
      Entry version 86 (01 Oct 2014)
      Sequence version 1 (01 Mar 2003)
      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 sitei263 – 2631HydroxymethylpyrimidineBy 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

    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:thiED
    Ordered Locus Names:CE1591
    OrganismiCorynebacterium efficiens (strain DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395)
    Taxonomic identifieri196164 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeCorynebacteriaceaeCorynebacterium
    ProteomesiUP000001409: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 739739Thiamine biosynthesis multifunctional protein ThiEDPRO_0000192038Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi196164.CE1591.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8FTH8.
    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
    Regioni226 – 481256Hydroxymethylpyrimidine/phosphomethylpyrimidine kinaseAdd
    BLAST
    Regioni527 – 739213Thiaminase-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

    HOGENOMiHOG000225275.
    KOiK14153.
    OMAiRHELEFF.
    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.

    Q8FTH8-1 [UniParc]FASTAAdd to Basket

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    MTDFSLYLVT DPHLGGGPER VAGIVEDAIN GGVTVVQLRD KDADEQTFRE    50
    HAMELKRVCD RLGVPLFLND RFAVAAELSC HVHIGQGDLP YVQARRQLPG 100
    HLMIGLTIET MDQLETVIAD CTRAGIALPD VVGLGPVQAT DTKPDAPQAV 150
    GVDGVAAMAK VARAHGIASV AIGGVGLANA ADLARTGVDG LCVVSAIMAA 200
    PSPAEAAREL LDVWEAGRRV AQPRVLTIAG TDPTGGAGVQ ADLKSIAAAG 250
    GFGMSVITAL VAQNTHGVTG VHTPPADFLD EQLESVFSDV TVDAVKLGML 300
    GRADTVRQVT GWLRTRPHGP VILDPVMVAT SGDSLLDPDA TEALLELATV 350
    VDVITPNIPE LAVLCGEQPA PSFDAAIEQA RRFATDVGTT VIVKGGHLTG 400
    PRADNAVVYP DGSVHMVANP RVDTTNSHGT GCSLSAALAT RMGAGHPVDK 450
    ALDWATRWLN EALRGADALQ VGSGSGPVDH FAVTRRLLRA ADATPWPHLR 500
    MGAPSDGIIT PSDTQSPAPA LAPAGPYTRA LWEATGDVLG EILDSGFIRG 550
    LGDGTLSREE FLFYIDQDAH YLRQYSRALA TLSSRAPDAP AQVDWATSAA 600
    ECITVEAELH RTYLNKGLAE TGVSAPSPVT MAYTDFLIAR SHADDYVVGA 650
    AAVLPCYWLY AEIGLILAKQ NHPEHPYTDW LDTYSGEGFL AGTVKAIARV 700
    EAAMAGAGPD QQRVAAQTYL SACVHEREFF DQATRQGWN 739
    Length:739
    Mass (Da):77,744
    Last modified:March 1, 2003 - v1
    Checksum:iD6631B0553929077
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BA000035 Genomic DNA. Translation: BAC18401.1.
    RefSeqiNP_738201.1. NC_004369.1.
    WP_006767589.1. NZ_GG700683.1.

    Genome annotation databases

    EnsemblBacteriaiBAC18401; BAC18401; BAC18401.
    GeneIDi1034064.
    KEGGicef:CE1591.
    PATRICi21489321. VBICorEff9312_1583.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BA000035 Genomic DNA. Translation: BAC18401.1 .
    RefSeqi NP_738201.1. NC_004369.1.
    WP_006767589.1. NZ_GG700683.1.

    3D structure databases

    ProteinModelPortali Q8FTH8.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 196164.CE1591.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai BAC18401 ; BAC18401 ; BAC18401 .
    GeneIDi 1034064.
    KEGGi cef:CE1591.
    PATRICi 21489321. VBICorEff9312_1583.

    Phylogenomic databases

    HOGENOMi HOG000225275.
    KOi K14153.
    OMAi RHELEFF.
    OrthoDBi EOG6XWV53.

    Enzyme and pathway databases

    UniPathwayi UPA00060 ; UER00138 .
    UPA00060 ; UER00141 .

    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. "Comparative complete genome sequence analysis of the amino acid replacements responsible for the thermostability of Corynebacterium efficiens."
      Nishio Y., Nakamura Y., Kawarabayasi Y., Usuda Y., Kimura E., Sugimoto S., Matsui K., Yamagishi A., Kikuchi H., Ikeo K., Gojobori T.
      Genome Res. 13:1572-1579(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395.

    Entry informationi

    Entry nameiTHIED_COREF
    AccessioniPrimary (citable) accession number: Q8FTH8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 24, 2004
    Last sequence update: March 1, 2003
    Last modified: October 1, 2014
    This is version 86 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    There is also a ThiE protein in this bacteria (AC Q8FP55).

    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