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Q57688 (THIDN_METJA) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 75. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Bifunctional thiamine biosynthesis protein ThiDN

Including the following 2 domains:

  1. 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
  2. Thiamine-phosphate synthase ThiN
    Short name=TP synthase
    Short name=TPS
    EC=2.5.1.3
    Alternative name(s):
    Thiamine-phosphate pyrophosphorylase
    Short name=TMP pyrophosphorylase
    Short name=TMP-PPase
Gene names
Name:thiDN
Ordered Locus Names:MJ0236
OrganismMethanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii) [Reference proteome] [HAMAP]
Taxonomic identifier243232 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaMethanococciMethanococcalesMethanocaldococcaceaeMethanocaldococcus

Protein attributes

Sequence length417 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 activity

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.

Pathway

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

Cofactor biosynthesis; thiamine diphosphate biosynthesis; thiamine phosphate from 4-amino-2-methyl-5-diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)-thiazole: step 1/1.

Sequence similarities

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

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

Sequence caution

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 417417Bifunctional thiamine biosynthesis protein ThiDN
PRO_0000106755

Regions

Region1 – 235235Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase
Region236 – 417182Thiamine-phosphate synthase

Sites

Binding site411Hydroxymethylpyrimidine/phosphomethylpyrimidine By similarity

Secondary structure

................................ 417
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q57688 [UniParc].

Last modified January 25, 2012. Version 2.
Checksum: 810246AD46805E27

FASTA41747,056
        10         20         30         40         50         60 
MVILAIGGYD PTSGAGISAD IKTAHTLGVY CPTITTSVIP QNNKMVYEKF DLPEENIKNQ 

        70         80         90        100        110        120 
FKAVFEEFDI EYVKTGVLTK PAIDTLLKYI DKYDLKVICD PVLASTTKFS FVDEKLMEKY 

       130        140        150        160        170        180 
IELFNKSFLI TPNKEEYKKI MEFIKNNNLM IRNDLYILAT GIDDILMKNF KPIKTFKGFR 

       190        200        210        220        230        240 
VDKEVHGTGC VYSTAITAFL SKGYDLEEAI KEAKRFVLSS VIYAKKSKFG YNSNPTYINK 

       250        260        270        280        290        300 
EKVIKNLSYA IYLLKKMNFT LIPEVGSNIA ESLPFPKDFK DVAALTGRII KNKLGGFYIV 

       310        320        330        340        350        360 
GDIEFGASEH IAKIILSASK FNPEIRACMN IKYDGGLIKL LKDKFAVSSF DRKEEPPNVS 

       370        380        390        400        410 
TMEWGTKIAC EKFGGVPDII YDRGGEGKEP MIRVLGRDAI EVVKKVEVIQ KIYNTLM 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L77117 Genomic DNA. Translation: AAB98222.1. Different initiation.
PIRE64329.
RefSeqNP_247207.1. NC_000909.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2PHPX-ray2.03A/B/D/E236-416[»]
ProteinModelPortalQ57688.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING243232.MJ0236.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAB98222; AAB98222; MJ_0236.
GeneID1451089.
KEGGmja:MJ_0236.

Phylogenomic databases

eggNOGCOG1992.
KOK00941.

Enzyme and pathway databases

UniPathwayUPA00060; UER00141.

Family and domain databases

Gene3D3.40.1190.20. 1 hit.
3.40.225.10. 1 hit.
InterProIPR001303. Aldolase_II/adducin_N.
IPR013749. HMP-P_kinase-1.
IPR029056. Ribokinase-like.
IPR019293. ThiN.
[Graphical view]
PfamPF10120. Aldolase_2. 1 hit.
PF08543. Phos_pyr_kin. 1 hit.
[Graphical view]
SUPFAMSSF53613. SSF53613. 1 hit.
SSF53639. SSF53639. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceQ57688.

Entry information

Entry nameTHIDN_METJA
AccessionPrimary (citable) accession number: Q57688
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 25, 2012
Last modified: June 11, 2014
This is version 75 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

Methanococcus jannaschii

Methanococcus jannaschii: entries and gene names