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A7FVR9 (THIM2_CLOB1) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 47. 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:
Hydroxyethylthiazole kinase 2

EC=2.7.1.50
Alternative name(s):
4-methyl-5-beta-hydroxyethylthiazole kinase 2
Short name=TH kinase 2
Short name=Thz kinase 2
Gene names
Name:thiM2
Ordered Locus Names:CLB_2193
OrganismClostridium botulinum (strain ATCC 19397 / Type A) [Complete proteome] [HAMAP]
Taxonomic identifier441770 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium

Protein attributes

Sequence length265 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

ATP + 4-methyl-5-(2-hydroxyethyl)thiazole = ADP + 4-methyl-5-(2-phosphonooxyethyl)thiazole. HAMAP-Rule MF_00228

Cofactor

Magnesium By similarity. HAMAP-Rule MF_00228

Pathway

Cofactor biosynthesis; thiamine diphosphate biosynthesis; 4-methyl-5-(2-phosphoethyl)-thiazole from 5-(2-hydroxyethyl)-4-methylthiazole: step 1/1. HAMAP-Rule MF_00228

Sequence similarities

Belongs to the Thz kinase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 265265Hydroxyethylthiazole kinase 2 HAMAP-Rule MF_00228
PRO_0000383838

Sites

Binding site391Substrate; via amide nitrogen By similarity
Binding site1151ATP By similarity
Binding site1681ATP By similarity
Binding site1951Substrate; via amide nitrogen By similarity

Sequences

Sequence LengthMass (Da)Tools
A7FVR9 [UniParc].

Last modified September 11, 2007. Version 1.
Checksum: F2F92C9C43F88AE8

FASTA26528,576
        10         20         30         40         50         60 
MQIRQSIKLK KPLIHYITNP ISINDCANII LAAGAKPIMA EHPLEVSEIT SVSKSLGVNL 

        70         80         90        100        110        120 
GNITDNKMKS MLISGKTAYE NKIPQVIDLV GVGCSKLRLD YAKKFISECH PNVIKGNMSE 

       130        140        150        160        170        180 
IKAIYGIKSS AKGIDVGACD IITKQNFDEN IEMIKRLSME TGSVVAATGV VDIISNGTYT 

       190        200        210        220        230        240 
YIISNGCEML SMITGTGCML TGLIASYISS ENILDGTVLA VALMGICGEL SQHAKGTGSF 

       250        260 
RNELTDNMFS ISDDIIIKKI RINSY 

« Hide

References

[1]"Analysis of the neurotoxin complex genes in Clostridium botulinum A1-A4 and B1 strains: BoNT/A3, /Ba4 and /B1 clusters are located within plasmids."
Smith T.J., Hill K.K., Foley B.T., Detter J.C., Munk A.C., Bruce D.C., Doggett N.A., Smith L.A., Marks J.D., Xie G., Brettin T.S.
PLoS ONE 2:E1271-E1271(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 19397 / Type A.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000726 Genomic DNA. Translation: ABS34423.1.
RefSeqYP_001384506.1. NC_009697.1.

3D structure databases

ProteinModelPortalA7FVR9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING441770.CLB_2193.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABS34423; ABS34423; CLB_2193.
GeneID5395818.
KEGGcba:CLB_2193.
PATRIC19358962. VBICloBot110701_2116.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2145.
HOGENOMHOG000114352.
KOK00878.
OMAFDENIEM.
OrthoDBEOG628F8M.
ProtClustDBCLSK972179.

Enzyme and pathway databases

BioCycCBOT441770:GH1E-2170-MONOMER.
UniPathwayUPA00060; UER00139.

Family and domain databases

HAMAPMF_00228. Thz_kinase.
InterProIPR000417. Hyethyz_kinase.
[Graphical view]
PfamPF02110. HK. 1 hit.
[Graphical view]
PIRSFPIRSF000513. Thz_kinase. 1 hit.
PRINTSPR01099. HYETHTZKNASE.
ProtoNetSearch...

Entry information

Entry nameTHIM2_CLOB1
AccessionPrimary (citable) accession number: A7FVR9
Entry history
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: September 11, 2007
Last modified: February 19, 2014
This is version 47 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