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Q9WZP7 (THIDN_THEMA) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 63. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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:TM_0790
OrganismThermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099) [Reference proteome] [HAMAP]
Taxonomic identifier243274 [NCBI]
Taxonomic lineageBacteriaThermotogaeThermotogalesThermotogaceaeThermotoga

Protein attributes

Sequence length398 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. Ref.2

Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole monophosphate (THZ-P) and 4-amino-5-hydroxymethyl pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate (TMP). Ref.2

Catalytic activity

ATP + 4-amino-5-hydroxymethyl-2-methylpyrimidine = ADP + 4-amino-5-phosphonooxymethyl-2-methylpyrimidine. Ref.2

ATP + 4-amino-2-methyl-5-phosphomethylpyrimidine = ADP + 4-amino-2-methyl-5-diphosphomethylpyrimidine. Ref.2

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

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 annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 398398Bifunctional thiamine biosynthesis protein ThiDN
PRO_0000415381

Regions

Region1 – 216216Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase
Region217 – 398182Thiamine-phosphate synthase

Sites

Binding site401Hydroxymethylpyrimidine/phosphomethylpyrimidine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9WZP7 [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: DCE6977F471BF649

FASTA39845,392
        10         20         30         40         50         60 
MVLVVAGFDP SGGAGIIQDV KVLSALGVKT HAVISALTVQ NENRVFSVNF RDWEEMRKEI 

        70         80         90        100        110        120 
EVLTPPRVIK VGLSAPETVK RLREMFPDSA IVWNVVLESS SGFGFQDPEE VKKFVEYADY 

       130        140        150        160        170        180 
VILNSEEAKK LGEYNNFIVT GGHEKGNTVK VKYRDFVFEI PRVPGEFHGT GCAFSSAVSG 

       190        200        210        220        230        240 
FLAMSYPVEE AIRSAMELLK KILERSSGVV ETEKLLRDWY RYDTLNTLDE ILPEFLEIGH 

       250        260        270        280        290        300 
LTVPEVGQNV SYALPWAKNE FEVGKFPGRI RLKEGKAVAV SCASFKDRSH TARMAVTMMR 

       310        320        330        340        350        360 
YHPHMRCVVN VRYEREYVER AKKRGLKVFH YDRSKEPKEV QEKEGQSMVW MIEQAIAELK 

       370        380        390 
SPPDVIYDEG WWGKEAMIRV FGRNPKEVLE KIKLMVRE 

« Hide

References

« Hide 'large scale' references
[1]"Evidence for lateral gene transfer between Archaea and Bacteria from genome sequence of Thermotoga maritima."
Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M., Cotton M.D., Pratt M.S. expand/collapse author list , Phillips C.A., Richardson D.L., Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.
Nature 399:323-329(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 43589 / MSB8 / DSM 3109 / JCM 10099.
[2]"Systematic discovery of analogous enzymes in thiamin biosynthesis."
Morett E., Korbel J.O., Rajan E., Saab-Rincon G., Olvera L., Olvera M., Schmidt S., Snel B., Bork P.
Nat. Biotechnol. 21:790-795(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS A THIAMINE-PHOSPHATE SYNTHASE VIA ITS C-TERMINAL DOMAIN, CATALYTIC ACTIVITY.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE000512 Genomic DNA. Translation: AAD35872.1.
PIRG72333.
RefSeqNP_228599.1. NC_000853.1.
YP_007977141.1. NC_021214.1.
YP_008990240.1. NC_023151.1.

3D structure databases

ProteinModelPortalQ9WZP7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING243274.TM0790.

Protocols and materials databases

DNASU898458.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAD35872; AAD35872; TM_0790.
GeneID898458.
KEGGtma:TM0790.
tmi:THEMA_00700.
tmm:Tmari_0791.
PATRIC23936500. VBITheMar51294_0802.

Phylogenomic databases

KOK00941.
OMAEGATIPW.
OrthoDBEOG6HMXB7.

Enzyme and pathway databases

BioCycTMAR243274:GC6P-817-MONOMER.
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. 2 hits.
[Graphical view]
SUPFAMSSF53613. SSF53613. 1 hit.
SSF53639. SSF53639. 1 hit.
ProtoNetSearch...

Entry information

Entry nameTHIDN_THEMA
AccessionPrimary (citable) accession number: Q9WZP7
Entry history
Integrated into UniProtKB/Swiss-Prot: January 25, 2012
Last sequence update: November 1, 1999
Last modified: July 9, 2014
This is version 63 of the entry and version 1 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

PATHWAY comments

Index of metabolic and biosynthesis pathways