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A8A1W9 (THIM_ECOHS) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 43. 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:EcHS_A2240
OrganismEscherichia coli O9:H4 (strain HS) [Complete proteome] [HAMAP]
Taxonomic identifier331112 [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_1000058759

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
A8A1W9 [UniParc].

Last modified October 23, 2007. Version 1.
Checksum: 720774031BA7AC4B

FASTA26227,339
        10         20         30         40         50         60 
MQVDLLGSAQ SAHALHLFHQ HSPLVHCMTN DVVQTFTANT LLALGASPAM VIETEEASQF 

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

       130        140        150        160        170        180 
PAAIRGNASE IMALAGIANG GRGVDTTDAA ANAIPAAQTL ARETGAIVVV TGEMDYVTDG 

       190        200        210        220        230        240 
HRIIGIHGGD PLMTKVVGTG CALSAVVAAC CALPGDTLEN VASACHWMKQ AGERAVARSE 

       250        260 
GPGSFVPHFL DALWQLTQEV QA 

« Hide

References

[1]"The pangenome structure of Escherichia coli: comparative genomic analysis of E. coli commensal and pathogenic isolates."
Rasko D.A., Rosovitz M.J., Myers G.S.A., Mongodin E.F., Fricke W.F., Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R., Henderson I.R., Sperandio V., Ravel J.
J. Bacteriol. 190:6881-6893(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: HS.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000802 Genomic DNA. Translation: ABV06523.1.
RefSeqYP_001458906.1. NC_009800.1.

3D structure databases

ProteinModelPortalA8A1W9.
SMRA8A1W9. Positions 5-261.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING331112.EcHS_A2240.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABV06523; ABV06523; EcHS_A2240.
GeneID5591930.
KEGGecx:EcHS_A2240.
PATRIC18314458. VBIEscCol77814_2192.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2145.
HOGENOMHOG000114352.
KOK00878.
OMASPVMAHA.
OrthoDBEOG628F8M.
ProtClustDBPRK09355.

Enzyme and pathway databases

BioCycECOL331112:GHHI-2227-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.
TIGRFAMsTIGR00694. thiM. 1 hit.
ProtoNetSearch...

Entry information

Entry nameTHIM_ECOHS
AccessionPrimary (citable) accession number: A8A1W9
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: October 23, 2007
Last modified: March 19, 2014
This is version 43 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