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Q57688

- THIDN_METJA

UniProt

Q57688 - THIDN_METJA

Protein

Bifunctional thiamine biosynthesis protein ThiDN

Gene

thiDN

Organism
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 77 (01 Oct 2014)
      Sequence version 2 (25 Jan 2012)
      Previous versions | rss
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    Functioni

    Catalyzes the phosphorylation of hydroxymethylpyrimidine phosphate (HMP-P) to HMP-PP, and of HMP to HMP-P.By similarity
    Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole monophosphate (THZ-P) and 4-amino-5-hydroxymethyl pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate (TMP).By similarity

    Catalytic activityi

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

    Pathwayi

    Cofactor biosynthesis; thiamine diphosphate biosynthesis; 4-amino-2-methyl-5-diphosphomethylpyrimidine from 5-amino-1-(5-phospho-D-ribosyl)imidazole.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei41 – 411Hydroxymethylpyrimidine/phosphomethylpyrimidineBy similarity

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. hydroxymethylpyrimidine kinase activity Source: UniProtKB-EC
    3. phosphomethylpyrimidine kinase activity Source: UniProtKB-EC
    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, Nucleotide-binding

    Enzyme and pathway databases

    UniPathwayiUPA00060; UER00141.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Bifunctional thiamine biosynthesis protein ThiDN
    Including the following 2 domains:
    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
    Thiamine-phosphate synthase ThiN (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:thiDN
    Ordered Locus Names:MJ0236
    OrganismiMethanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii)
    Taxonomic identifieri243232 [NCBI]
    Taxonomic lineageiArchaeaEuryarchaeotaMethanococciMethanococcalesMethanocaldococcaceaeMethanocaldococcus
    ProteomesiUP000000805: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 417417Bifunctional thiamine biosynthesis protein ThiDNPRO_0000106755Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi243232.MJ0236.

    Structurei

    Secondary structure

    1
    417
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi240 – 25516
    Beta strandi269 – 2724
    Helixi279 – 2813
    Beta strandi282 – 2876
    Beta strandi289 – 2913
    Beta strandi295 – 2995
    Beta strandi303 – 3053
    Helixi309 – 31911
    Beta strandi327 – 3315
    Helixi335 – 3417
    Turni342 – 3443
    Beta strandi347 – 3493
    Helixi352 – 3543
    Helixi361 – 37313
    Beta strandi378 – 3825
    Beta strandi391 – 3988
    Helixi399 – 41416

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2PHPX-ray2.03A/B/D/E236-416[»]
    ProteinModelPortaliQ57688.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ57688.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 235235Hydroxymethylpyrimidine/phosphomethylpyrimidine kinaseAdd
    BLAST
    Regioni236 – 417182Thiamine-phosphate synthaseAdd
    BLAST

    Sequence similaritiesi

    In the N-terminal section; belongs to the ThiD family.Curated
    In the C-terminal section; belongs to the ThiN family.Curated

    Phylogenomic databases

    eggNOGiCOG1992.
    KOiK00941.

    Family and domain databases

    Gene3Di3.40.1190.20. 1 hit.
    3.40.225.10. 1 hit.
    InterProiIPR001303. Aldolase_II/adducin_N.
    IPR013749. PM/HMP-P_kinase-1.
    IPR029056. Ribokinase-like.
    IPR019293. ThiN.
    [Graphical view]
    PfamiPF10120. Aldolase_2. 1 hit.
    PF08543. Phos_pyr_kin. 1 hit.
    [Graphical view]
    SUPFAMiSSF53613. SSF53613. 1 hit.
    SSF53639. SSF53639. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q57688-1 [UniParc]FASTAAdd to Basket

    « Hide

    MVILAIGGYD PTSGAGISAD IKTAHTLGVY CPTITTSVIP QNNKMVYEKF    50
    DLPEENIKNQ FKAVFEEFDI EYVKTGVLTK PAIDTLLKYI DKYDLKVICD 100
    PVLASTTKFS FVDEKLMEKY IELFNKSFLI TPNKEEYKKI MEFIKNNNLM 150
    IRNDLYILAT GIDDILMKNF KPIKTFKGFR VDKEVHGTGC VYSTAITAFL 200
    SKGYDLEEAI KEAKRFVLSS VIYAKKSKFG YNSNPTYINK EKVIKNLSYA 250
    IYLLKKMNFT LIPEVGSNIA ESLPFPKDFK DVAALTGRII KNKLGGFYIV 300
    GDIEFGASEH IAKIILSASK FNPEIRACMN IKYDGGLIKL LKDKFAVSSF 350
    DRKEEPPNVS TMEWGTKIAC EKFGGVPDII YDRGGEGKEP MIRVLGRDAI 400
    EVVKKVEVIQ KIYNTLM 417
    Length:417
    Mass (Da):47,056
    Last modified:January 25, 2012 - v2
    Checksum:i810246AD46805E27
    GO

    Sequence cautioni

    The sequence AAB98222.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L77117 Genomic DNA. Translation: AAB98222.1. Different initiation.
    PIRiE64329.
    RefSeqiNP_247207.1. NC_000909.1.

    Genome annotation databases

    EnsemblBacteriaiAAB98222; AAB98222; MJ_0236.
    GeneIDi1451089.
    KEGGimja:MJ_0236.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L77117 Genomic DNA. Translation: AAB98222.1 . Different initiation.
    PIRi E64329.
    RefSeqi NP_247207.1. NC_000909.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2PHP X-ray 2.03 A/B/D/E 236-416 [» ]
    ProteinModelPortali Q57688.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 243232.MJ0236.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAB98222 ; AAB98222 ; MJ_0236 .
    GeneIDi 1451089.
    KEGGi mja:MJ_0236.

    Phylogenomic databases

    eggNOGi COG1992.
    KOi K00941.

    Enzyme and pathway databases

    UniPathwayi UPA00060 ; UER00141 .

    Miscellaneous databases

    EvolutionaryTracei Q57688.

    Family and domain databases

    Gene3Di 3.40.1190.20. 1 hit.
    3.40.225.10. 1 hit.
    InterProi IPR001303. Aldolase_II/adducin_N.
    IPR013749. PM/HMP-P_kinase-1.
    IPR029056. Ribokinase-like.
    IPR019293. ThiN.
    [Graphical view ]
    Pfami PF10120. Aldolase_2. 1 hit.
    PF08543. Phos_pyr_kin. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53613. SSF53613. 1 hit.
    SSF53639. SSF53639. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440.
    2. "Crystal structure of the C-terminal domain of protein MJ0236 (Y236_METJA)."
      New York structural genomix research consortium (NYSGXRC)
      Submitted (FEB-2009) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (2.03 ANGSTROMS) OF 236-416.

    Entry informationi

    Entry nameiTHIDN_METJA
    AccessioniPrimary (citable) accession number: Q57688
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: January 25, 2012
    Last modified: October 1, 2014
    This is version 77 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

    3D-structure, Complete proteome, Multifunctional enzyme, Reference proteome

    Documents

    1. Methanococcus jannaschii
      Methanococcus jannaschii: entries and gene names
    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