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B5YV51 (THIM_ECO5E) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 42. 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

EC=2.7.1.50
Alternative name(s):
4-methyl-5-beta-hydroxyethylthiazole kinase
Short name=TH kinase
Short name=Thz kinase
Gene names
Name:thiM
Ordered Locus Names:ECH74115_3083
OrganismEscherichia coli O157:H7 (strain EC4115 / EHEC) [Complete proteome] [HAMAP]
Taxonomic identifier444450 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length262 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 – 262262Hydroxyethylthiazole kinase HAMAP-Rule MF_00228
PRO_1000100412

Sites

Binding site501Substrate; via amide nitrogen By similarity
Binding site1251ATP By similarity
Binding site1711ATP By similarity
Binding site1981Substrate; via amide nitrogen By similarity

Sequences

Sequence LengthMass (Da)Tools
B5YV51 [UniParc].

Last modified November 25, 2008. Version 1.
Checksum: A28BF773FD2AD29F

FASTA26227,355
        10         20         30         40         50         60 
MQVDLLSSAQ SAHTLHLFHQ HSPLVHCMTN DVVQTFTANT LLALGASPAM VIETEEASQF 

        70         80         90        100        110        120 
AAIASALLIN VGTLTQPRAQ AMRAAVEQAK SSQTPWTLDP VAVGALDYRR HFCHELLSFK 

       130        140        150        160        170        180 
PAAIRGNASE IMALAGVANG GRGVDTTDAA VNAIPAAQTL ARETGAIVVV TGEVDYVTDG 

       190        200        210        220        230        240 
HRAVGIHGGD PLMTKVVGTG CALSAVVAAC CALPGDMLEN VASACHWMKQ AGERAVARSE 

       250        260 
GPGSFVPHFL DALWQLTQEV QA 

« Hide

References

[1]"Genomic anatomy of Escherichia coli O157:H7 outbreaks."
Eppinger M., Mammel M.K., Leclerc J.E., Ravel J., Cebula T.A.
Proc. Natl. Acad. Sci. U.S.A. 108:20142-20147(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: EC4115 / EHEC.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001164 Genomic DNA. Translation: ACI34772.1.
RefSeqYP_002271383.1. NC_011353.1.

3D structure databases

ProteinModelPortalB5YV51.
SMRB5YV51. Positions 4-261.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING444450.ECH74115_3083.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACI34772; ACI34772; ECH74115_3083.
GeneID6971519.
KEGGecf:ECH74115_3083.
PATRIC18366853. VBIEscCol74651_3084.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2145.
HOGENOMHOG000114352.
KOK00878.
OMAQTFTANV.
OrthoDBEOG628F8M.

Enzyme and pathway databases

BioCycECOL444450:GHOB-3076-MONOMER.
UniPathwayUPA00060; UER00139.

Family and domain databases

Gene3D3.40.1190.20. 1 hit.
HAMAPMF_00228. Thz_kinase.
InterProIPR000417. Hyethyz_kinase.
IPR029056. Ribokinase-like.
[Graphical view]
PfamPF02110. HK. 1 hit.
[Graphical view]
PIRSFPIRSF000513. Thz_kinase. 1 hit.
PRINTSPR01099. HYETHTZKNASE.
SUPFAMSSF53613. SSF53613. 1 hit.
TIGRFAMsTIGR00694. thiM. 1 hit.
ProtoNetSearch...

Entry information

Entry nameTHIM_ECO5E
AccessionPrimary (citable) accession number: B5YV51
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: November 25, 2008
Last modified: July 9, 2014
This is version 42 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