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P61422 (THIED_GEOSL) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 81. 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 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:thiDE
Ordered Locus Names:GSU0605
OrganismGeobacter sulfurreducens (strain ATCC 51573 / DSM 12127 / PCA) [Reference proteome] [HAMAP]
Taxonomic identifier243231 [NCBI]
Taxonomic lineageBacteriaProteobacteriaDeltaproteobacteriaDesulfuromonadalesGeobacteraceaeGeobacter

Protein attributes

Sequence length490 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.

Sequence similarities

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

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 490490Thiamine biosynthesis bifunctional protein ThiED HAMAP-Rule MF_00097
PRO_0000192040

Regions

Region1 – 213213Thiamine-phosphate synthase HAMAP-Rule MF_00097
Region50 – 545HMP-PP binding By similarity
Region147 – 1493THZ-P binding By similarity
Region197 – 1982THZ-P binding By similarity
Region229 – 490262Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase HAMAP-Rule MF_00097

Sites

Metal binding831Magnesium By similarity
Metal binding1021Magnesium By similarity
Binding site821HMP-PP By similarity
Binding site1211HMP-PP By similarity
Binding site1501HMP-PP By similarity
Binding site1771THZ-P; via amide nitrogen By similarity
Binding site2661Hydroxymethylpyrimidine By similarity

Sequences

Sequence LengthMass (Da)Tools
P61422 [UniParc].

Last modified May 24, 2004. Version 1.
Checksum: 924B153FCD5E83D4

FASTA49051,910
        10         20         30         40         50         60 
MASNGHTLRL VINRDKHDSV IRGLYLVTDH DDNLIPRVEA AIDGGARVVQ YRNKNQDRES 

        70         80         90        100        110        120 
RLALGLELRE LCRRRSIPFI VNDDLEMAVS LKADGLHLGQ GDGDPREARR VLGPGKIIGV 

       130        140        150        160        170        180 
STHTLSEALE AQAAGVDYIG LGAMFPSRSK EVEHVAGSEL LAAIRSSISI PIVAIGGITR 

       190        200        210        220        230        240 
DNGASVIDAG ADAVAVISAV LSHPDPALAA TEIALLFNRR APFPRGSVLT VAGSDSGGGA 

       250        260        270        280        290        300 
GIQADLKTVT LLGSYGSSVL TALTAQNTRG VSGIHGVPPA FVADQLDAVF SDIPVDVVKT 

       310        320        330        340        350        360 
GMLFSAETIV AIAAKLTEYR RRMVVVDPVM VAKGGANLID RGAVSVLKER LFPLAYLVTP 

       370        380        390        400        410        420 
NIPEAERLTG ANISDEESMR EAARRLHRLG ARNVLLKGGH LLAGDSVDIL FDGAAFHRFV 

       430        440        450        460        470        480 
SPRILSKNTH GTGCTFASAI ATYLAQGDPL REAIARAKRY ITAAIRLAQP LGRGHGPVNH 

       490 
ILAAEDVRDR 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE017180 Genomic DNA. Translation: AAR33936.1.
RefSeqNP_951663.1. NC_002939.5.

3D structure databases

ProteinModelPortalP61422.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING243231.GSU0605.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAR33936; AAR33936; GSU0605.
GeneID2687129.
KEGGgsu:GSU0605.
PATRIC22023961. VBIGeoSul17553_0603.

Phylogenomic databases

eggNOGCOG0351.
HOGENOMHOG000134175.
KOK14153.
OMAYLAQGEP.
OrthoDBEOG6XWV53.

Enzyme and pathway databases

BioCycGSUL243231:GH27-611-MONOMER.
UniPathwayUPA00060; UER00138.
UPA00060; UER00141.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
3.40.1190.20. 1 hit.
HAMAPMF_00097. TMP_synthase.
InterProIPR013785. Aldolase_TIM.
IPR013749. HMP-P_kinase-1.
IPR004399. HMP-P_kinase-2.
IPR029056. Ribokinase-like.
IPR022998. ThiaminP_synth_SF.
IPR003733. TMP_synthase.
[Graphical view]
PfamPF08543. Phos_pyr_kin. 1 hit.
PF02581. TMP-TENI. 1 hit.
[Graphical view]
SUPFAMSSF51391. SSF51391. 1 hit.
SSF53613. SSF53613. 1 hit.
TIGRFAMsTIGR00097. HMP-P_kinase. 1 hit.
TIGR00693. thiE. 1 hit.
ProtoNetSearch...

Entry information

Entry nameTHIED_GEOSL
AccessionPrimary (citable) accession number: P61422
Entry history
Integrated into UniProtKB/Swiss-Prot: May 24, 2004
Last sequence update: May 24, 2004
Last modified: June 11, 2014
This is version 81 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