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Q03CB3 (THIM_LACC3) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 52. 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:LSEI_0299
OrganismLactobacillus casei (strain ATCC 334) [Complete proteome] [HAMAP]
Taxonomic identifier321967 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliLactobacillalesLactobacillaceaeLactobacillus

Protein attributes

Sequence length280 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 – 280280Hydroxyethylthiazole kinase HAMAP-Rule MF_00228
PRO_0000383869

Sites

Binding site501Substrate; via amide nitrogen By similarity
Binding site1251ATP By similarity
Binding site1781ATP By similarity
Binding site2051Substrate; via amide nitrogen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q03CB3 [UniParc].

Last modified November 14, 2006. Version 1.
Checksum: 89F78893162A26E8

FASTA28029,780
        10         20         30         40         50         60 
MSKAITDVFY TAFKTALPLT SSPLVQCITN EITVESMANA LLYIDAKPVM ADDQREFPEF 

        70         80         90        100        110        120 
FAQSDALLLN LGHISEVRQQ NLLAAGKFAQ ATNQPTVIDL VGVSATQLRY DLGHQLLVNH 

       130        140        150        160        170        180 
PNVVKGNISE MRRFADLKST GRGVDGSQLD QSVTALGELA ASLQQLTQAF PTTTFLATGK 

       190        200        210        220        230        240 
IDLVVSAKGT WYLKNGVPQL DRFTGTGDIV GALIAALLGT GLDNDAAVVV AVSYFNCCGE 

       250        260        270        280 
VAAAQNRTGG LAAFREGTLN QLSLLAATAD WLQMVKGEAL 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000423 Genomic DNA. Translation: ABJ69159.1.
RefSeqYP_805601.1. NC_008526.1.

3D structure databases

ProteinModelPortalQ03CB3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING321967.LSEI_0299.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABJ69159; ABJ69159; LSEI_0299.
GeneID4419766.
KEGGlca:LSEI_0299.
PATRIC22204324. VBILacCas62221_0323.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2145.
HOGENOMHOG000114352.
KOK00878.
OMALPLMATH.
OrthoDBEOG628F8M.
ProtClustDBCLSK559900.

Enzyme and pathway databases

BioCycLCAS321967:GH4S-299-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 nameTHIM_LACC3
AccessionPrimary (citable) accession number: Q03CB3
Entry history
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: November 14, 2006
Last modified: February 19, 2014
This is version 52 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