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Q8NQH1 (THIED_CORGL) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 87. 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:theD
Synonyms:thiD1
Ordered Locus Names:Cgl1463, cg1654
OrganismCorynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025) [Reference proteome] [HAMAP]
Taxonomic identifier196627 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeCorynebacteriaceaeCorynebacterium

Protein attributes

Sequence length763 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 central section; belongs to the ThiD family.

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

Sequence caution

The sequence BAB98856.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 763763Thiamine biosynthesis multifunctional protein ThiED HAMAP-Rule MF_00097
PRO_0000192039

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
Region245 – 500256Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase HAMAP-Rule MF_00097
Region550 – 763214Thiaminase-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 site2821Hydroxymethylpyrimidine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8NQH1 [UniParc].

Last modified May 24, 2004. Version 2.
Checksum: CA992321E884577F

FASTA76380,355
        10         20         30         40         50         60 
MTDFSLYLVT DPVLGGGPEK VAGIVDSAIS GGVSVVQLRD KNSGVEDVRA AAKELKELCD 

        70         80         90        100        110        120 
ARGVALVVND YLDIAVELGL HLHIGQGDTP YTQARELLPA HLELGLSIEN LDQLHAVIAQ 

       130        140        150        160        170        180 
CAETGVALPD VIGIGPVAST ATKPDAAPAL GVEGIAEIAA VAQDHGIASV AIGGVGLRNA 

       190        200        210        220        230        240 
AELAATPIDG LCVVSEIMTA ANPAAAATRL RTAFQPTFSP ETQTELSQTE LQGAFVNSPS 

       250        260        270        280        290        300 
APRVLSIAGT DPTGGAGIQA DLKSIAAGGG YGMCVVTSLV AQNTHGVNTI HTPPLTFLEE 

       310        320        330        340        350        360 
QLEAVFSDVT VDAIKLGMLG SADTVDLVAS WLGSHEHGPV VLDPVMIATS GDRLLDASAE 

       370        380        390        400        410        420 
ESLRRLAVHV DVVTPNIPEL AVLCDSAPAI TMDEAIAQAQ GFARTHDTIV IVKGGHLTGA 

       430        440        450        460        470        480 
LADNAVVRPD GSVFQVENLR VNTTNSHGTG CSLSASLATK IAAGESVEKA LEWSTRWLNE 

       490        500        510        520        530        540 
ALRHADHLAV GTGNGPVDHG HLARRMTHAA ETTPWAHLRA PRLDGATAAS FTTPSTVKSP 

       550        560        570        580        590        600 
APRIEPAGPF TRALWEASGD IIAGINSSDF ITMLGDGTLR RPEFDFYIDQ DAQYLAQYSR 

       610        620        630        640        650        660 
ALARLSSIAP DSHAQIEWAQ SAAECLVVEA ELHRSYMAGK EVSAPSHITM AYTDFLIART 

       670        680        690        700        710        720 
YTEDYVCGVA AVLPCYWLYA EIGLMLAEQN HDEHPYKDWL NTYSGEEFIA GTRAAIARLE 

       730        740        750        760 
KALENAGAEQ RVDAARAFLS ASVHEREFFD QATRHGWTMV GSS 

« Hide

References

[1]"The Corynebacterium glutamicum genome: features and impacts on biotechnological processes."
Ikeda M., Nakagawa S.
Appl. Microbiol. Biotechnol. 62:99-109(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.
[2]"The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its impact on the production of L-aspartate-derived amino acids and vitamins."
Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A., Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A., Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F., Moeckel B. expand/collapse author list , Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O., Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.
J. Biotechnol. 104:5-25(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000036 Genomic DNA. Translation: BAB98856.1. Different initiation.
BX927152 Genomic DNA. Translation: CAF21472.1.
RefSeqNP_600680.3. NC_003450.3.
YP_225748.1. NC_006958.1.

3D structure databases

ProteinModelPortalQ8NQH1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING196627.cg1654.

Protocols and materials databases

DNASU3345397.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAB98856; BAB98856; BAB98856.
CAF21472; CAF21472; cg1654.
GeneID1019437.
KEGGcgb:cg1654.
cgl:NCgl1407.
PATRIC21494969. VBICorGlu203724_1430.

Phylogenomic databases

eggNOGCOG0351.
HOGENOMHOG000225275.
KOK14153.
OMAGFWEMFP.
OrthoDBEOG6XWV53.

Enzyme and pathway databases

BioCycCGLU196627:GJDM-1450-MONOMER.
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_CORGL
AccessionPrimary (citable) accession number: Q8NQH1
Entry history
Integrated into UniProtKB/Swiss-Prot: May 24, 2004
Last sequence update: May 24, 2004
Last modified: July 9, 2014
This is version 87 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

PATHWAY comments

Index of metabolic and biosynthesis pathways