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Q67T51 (THIME_SYMTH) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 70. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Thiamine biosynthesis bifunctional protein ThiM/ThiE

Including the following 2 domains:

  1. Hydroxyethylthiazole kinase
    EC=2.7.1.50
    Alternative name(s):
    4-methyl-5-beta-hydroxyethylthiazole kinase
    Short name=TH kinase
    Short name=Thz kinase
  2. Thiamine-phosphate synthase
    Short name=TMP-PPase
    Short name=TP synthase
    Short name=TPS
    EC=2.5.1.3
    Alternative name(s):
    Thiamine-phosphate pyrophosphorylase
    Short name=TMP pyrophosphorylase
Gene names
Name:thiM/thiE
Ordered Locus Names:STH157
OrganismSymbiobacterium thermophilum (strain T / IAM 14863) [Complete proteome] [HAMAP]
Taxonomic identifier292459 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesClostridiales Family XVIII. Incertae SedisSymbiobacterium

Protein attributes

Sequence length480 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

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. HAMAP-Rule MF_00097

Catalytic activity

ATP + 4-methyl-5-(2-hydroxyethyl)thiazole = ADP + 4-methyl-5-(2-phosphonooxyethyl)thiazole. HAMAP-Rule MF_00097

2-methyl-4-amino-5-hydroxymethylpyrimidine diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = diphosphate + thiamine phosphate. HAMAP-Rule MF_00097

Cofactor

Binds 1 magnesium ion per subunit By similarity. HAMAP-Rule MF_00097

Pathway

Cofactor biosynthesis; thiamine diphosphate biosynthesis; 4-methyl-5-(2-phosphoethyl)-thiazole from 5-(2-hydroxyethyl)-4-methylthiazole: step 1/1. HAMAP-Rule MF_00097

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 Thz kinase family.

In the C-terminal section; belongs to the thiamine-phosphate synthase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 480480Thiamine biosynthesis bifunctional protein ThiM/ThiE HAMAP-Rule MF_00097
PRO_0000383912

Regions

Region1 – 287287Hydroxyethylthiazole kinase HAMAP-Rule MF_00097
Region288 – 480193Thiamine-phosphate synthase HAMAP-Rule MF_00097
Region303 – 3075HMP-PP binding By similarity
Region400 – 4023THZ-P binding By similarity
Region451 – 4522THZ-P binding By similarity

Sites

Metal binding3361Magnesium By similarity
Metal binding3551Magnesium By similarity
Binding site4014-methyl-5-(2-hydroxyethyl)thiazole; via amide nitrogen By similarity
Binding site1161ATP By similarity
Binding site1641ATP By similarity
Binding site19114-methyl-5-(2-hydroxyethyl)thiazole; via amide nitrogen By similarity
Binding site3351HMP-PP By similarity
Binding site3741HMP-PP By similarity
Binding site4031HMP-PP By similarity
Binding site4311THZ-P; via amide nitrogen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q67T51 [UniParc].

Last modified October 11, 2004. Version 1.
Checksum: 0FEC441B02894F29

FASTA48048,683
        10         20         30         40         50         60 
MSTLPERVRE RRPLVHAITN CVTMEWVARG LLAAGARPVM ARDAAEAPVV AAAADALVLN 

        70         80         90        100        110        120 
LGTWSPGLQQ AMLEAGQVAA RRGIPVVLDP VGAGGTETRT RAALELLERV RVTAVRGNAG 

       130        140        150        160        170        180 
EILALAGRDG LVRGVDGPDG RPGPQTERAA RAVARRFGCL VAVTGATDLV TDGRRTLAVR 

       190        200        210        220        230        240 
AGHPLMSQVP GTGCLATALV AAALAAGTGA GPAGRDRPME DVDVVAEALL WAGWAGEQAA 

       250        260        270        280        290        300 
SAASGPGTFA AAFLDRLALR GPLPPGRIAP PLSERLSLYV LVSGATPPDV LEAVLQAGCR 

       310        320        330        340        350        360 
MIQFREKRLP LPAQLEAAAR VREACRRHGA LLVVNDRVDL ALAVGADGVH LGQEDLPVAA 

       370        380        390        400        410        420 
ARRILGPDAV IGATCETAGE ARAARDAGAD YIGAGPVYVT PSKPDAGEPY GPDVVRRVSE 

       430        440        450        460        470        480 
AADLPVVGIG GIGPGRAAPV IAAGAAGVAV ISAVLGAPDP GAAARAILDE VRRAKGEVSA 

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References

[1]"Genome sequence of Symbiobacterium thermophilum, an uncultivable bacterium that depends on microbial commensalism."
Ueda K., Yamashita A., Ishikawa J., Shimada M., Watsuji T., Morimura K., Ikeda H., Hattori M., Beppu T.
Nucleic Acids Res. 32:4937-4944(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: T / IAM 14863.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP006840 Genomic DNA. Translation: BAD39142.1.
RefSeqYP_073986.1. NC_006177.1.

3D structure databases

ProteinModelPortalQ67T51.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING292459.STH157.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAD39142; BAD39142; STH157.
GeneID2981020.
KEGGsth:STH157.
PATRIC23778373. VBISymThe116959_0158.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0352.
HOGENOMHOG000097679.
OMARECKEND.
OrthoDBEOG628F8M.

Enzyme and pathway databases

BioCycSTHE292459:GJMM-173-MONOMER.
UniPathwayUPA00060; UER00139.
UPA00060; UER00141.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
3.40.1190.20. 1 hit.
HAMAPMF_00097. TMP_synthase.
MF_00228. Thz_kinase.
InterProIPR013785. Aldolase_TIM.
IPR000417. Hyethyz_kinase.
IPR029056. Ribokinase-like.
IPR022998. ThiaminP_synth_SF.
IPR003733. TMP_synthase.
[Graphical view]
PfamPF02110. HK. 1 hit.
PF02581. TMP-TENI. 1 hit.
[Graphical view]
PRINTSPR01099. HYETHTZKNASE.
SUPFAMSSF51391. SSF51391. 1 hit.
SSF53613. SSF53613. 1 hit.
TIGRFAMsTIGR00693. thiE. 1 hit.
ProtoNetSearch...

Entry information

Entry nameTHIME_SYMTH
AccessionPrimary (citable) accession number: Q67T51
Entry history
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: October 11, 2004
Last modified: June 11, 2014
This is version 70 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