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Q8FTH8 (THIED_COREF) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 84. 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:
Thiamine biosynthesis multifunctional protein ThiED

Including the following 2 domains:

  1. 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
  2. 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 names
Name:thiED
Ordered Locus Names:CE1591
OrganismCorynebacterium efficiens (strain DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395) [Complete proteome] [HAMAP]
Taxonomic identifier196164 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeCorynebacteriaceaeCorynebacterium

Protein attributes

Sequence length739 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

Catalyzes the phosphorylation of hydroxymethylpyrimidine phosphate (HMP-P) to HMP-PP, and of HMP to HMP-P By similarity. HAMAP-Rule MF_00097

Catalytic activity

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

ATP + 4-amino-5-hydroxymethyl-2-methylpyrimidine = ADP + 4-amino-5-phosphonooxymethyl-2-methylpyrimidine. HAMAP-Rule MF_00097

ATP + 4-amino-2-methyl-5-phosphomethylpyrimidine = ADP + 4-amino-2-methyl-5-diphosphomethylpyrimidine. HAMAP-Rule MF_00097

Cofactor

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

Pathway

Cofactor biosynthesis; thiamine diphosphate biosynthesis; 4-amino-2-methyl-5-diphosphomethylpyrimidine from 5-amino-1-(5-phospho-D-ribosyl)imidazole: step 3/3. 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.

Miscellaneous

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

Sequence similarities

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

In the central section; belongs to the ThiD family.

In the C-terminal section; belongs to the thiaminase-2 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 739739Thiamine biosynthesis multifunctional protein ThiED HAMAP-Rule MF_00097
PRO_0000192038

Regions

Region1 – 210210Thiamine-phosphate synthase HAMAP-Rule MF_00097
Region37 – 415HMP-PP binding By similarity
Region140 – 1423THZ-P binding By similarity
Region194 – 1952THZ-P binding By similarity
Region226 – 481256Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase HAMAP-Rule MF_00097
Region527 – 739213Thiaminase-2 HAMAP-Rule MF_00097

Sites

Metal binding701Magnesium By similarity
Metal binding881Magnesium By similarity
Binding site691HMP-PP By similarity
Binding site1071HMP-PP By similarity
Binding site1431HMP-PP By similarity
Binding site1741THZ-P; via amide nitrogen By similarity
Binding site2631Hydroxymethylpyrimidine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8FTH8 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: D6631B0553929077

FASTA73977,744
        10         20         30         40         50         60 
MTDFSLYLVT DPHLGGGPER VAGIVEDAIN GGVTVVQLRD KDADEQTFRE HAMELKRVCD 

        70         80         90        100        110        120 
RLGVPLFLND RFAVAAELSC HVHIGQGDLP YVQARRQLPG HLMIGLTIET MDQLETVIAD 

       130        140        150        160        170        180 
CTRAGIALPD VVGLGPVQAT DTKPDAPQAV GVDGVAAMAK VARAHGIASV AIGGVGLANA 

       190        200        210        220        230        240 
ADLARTGVDG LCVVSAIMAA PSPAEAAREL LDVWEAGRRV AQPRVLTIAG TDPTGGAGVQ 

       250        260        270        280        290        300 
ADLKSIAAAG GFGMSVITAL VAQNTHGVTG VHTPPADFLD EQLESVFSDV TVDAVKLGML 

       310        320        330        340        350        360 
GRADTVRQVT GWLRTRPHGP VILDPVMVAT SGDSLLDPDA TEALLELATV VDVITPNIPE 

       370        380        390        400        410        420 
LAVLCGEQPA PSFDAAIEQA RRFATDVGTT VIVKGGHLTG PRADNAVVYP DGSVHMVANP 

       430        440        450        460        470        480 
RVDTTNSHGT GCSLSAALAT RMGAGHPVDK ALDWATRWLN EALRGADALQ VGSGSGPVDH 

       490        500        510        520        530        540 
FAVTRRLLRA ADATPWPHLR MGAPSDGIIT PSDTQSPAPA LAPAGPYTRA LWEATGDVLG 

       550        560        570        580        590        600 
EILDSGFIRG LGDGTLSREE FLFYIDQDAH YLRQYSRALA TLSSRAPDAP AQVDWATSAA 

       610        620        630        640        650        660 
ECITVEAELH RTYLNKGLAE TGVSAPSPVT MAYTDFLIAR SHADDYVVGA AAVLPCYWLY 

       670        680        690        700        710        720 
AEIGLILAKQ NHPEHPYTDW LDTYSGEGFL AGTVKAIARV EAAMAGAGPD QQRVAAQTYL 

       730 
SACVHEREFF DQATRQGWN 

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References

[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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000035 Genomic DNA. Translation: BAC18401.1.
RefSeqNP_738201.1. NC_004369.1.

3D structure databases

ProteinModelPortalQ8FTH8.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING196164.CE1591.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAC18401; BAC18401; BAC18401.
GeneID1034064.
KEGGcef:CE1591.
PATRIC21489321. VBICorEff9312_1583.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000225275.
KOK14153.
OMARHELEFF.
OrthoDBEOG6XWV53.

Enzyme and pathway databases

UniPathwayUPA00060; UER00138.
UPA00060; UER00141.

Family and domain databases

Gene3D1.20.910.10. 1 hit.
3.20.20.70. 1 hit.
3.40.1190.20. 1 hit.
HAMAPMF_00097. TMP_synthase.
InterProIPR013785. Aldolase_TIM.
IPR016084. Haem_Oase-like_multi-hlx.
IPR013749. HMP-P_kinase-1.
IPR004399. HMP-P_kinase-2.
IPR029056. Ribokinase-like.
IPR004305. Thiaminase-2/PQQC.
IPR022998. ThiaminP_synth_SF.
IPR003733. TMP_synthase.
[Graphical view]
PfamPF08543. Phos_pyr_kin. 1 hit.
PF03070. TENA_THI-4. 1 hit.
PF02581. TMP-TENI. 1 hit.
[Graphical view]
SUPFAMSSF48613. SSF48613. 1 hit.
SSF51391. SSF51391. 1 hit.
SSF53613. SSF53613. 1 hit.
TIGRFAMsTIGR00097. HMP-P_kinase. 1 hit.
TIGR00693. thiE. 1 hit.
ProtoNetSearch...

Entry information

Entry nameTHIED_COREF
AccessionPrimary (citable) accession number: Q8FTH8
Entry history
Integrated into UniProtKB/Swiss-Prot: May 24, 2004
Last sequence update: March 1, 2003
Last modified: June 11, 2014
This is version 84 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