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46  structures 2292  species 1  interaction 2596  sequences 9  architectures

Family: HK (PF02110)

Summary: Hydroxyethylthiazole kinase family

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This is the Wikipedia entry entitled "Hydroxyethylthiazole kinase". More...

Hydroxyethylthiazole kinase Edit Wikipedia article

hydroxyethylthiazole kinase
Identifiers
EC number 2.7.1.50
CAS number 9026-56-6
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Gene Ontology AmiGO / EGO
Hydroxyethylthiazole kinase family
PDB 1c3q EBI.jpg
crystal structure of native thiazole kinase in the monoclinic form
Identifiers
Symbol HK
Pfam PF02110
Pfam clan CL0118
InterPro IPR000417
SCOP 1c3q
SUPERFAMILY 1c3q

In enzymology, a hydroxyethylthiazole kinase (EC 2.7.1.50) is an enzyme that catalyzes the chemical reaction

ATP + 4-methyl-5-(2-hydroxyethyl)thiazole \rightleftharpoons ADP + 4-methyl-5-(2-phosphonooxyethyl)thiazole

Thus, the two substrates of this enzyme are ATP and 4-methyl-5-(2-hydroxyethyl)thiazole, whereas its two products are ADP and 4-methyl-5-(2-phosphonooxyethyl)thiazole.

This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:4-methyl-5-(2-hydroxyethyl)thiazole 2-phosphotransferase. Other names in common use include hydroxyethylthiazole kinase (phosphorylating), and 4-methyl-5-(beta-hydroxyethyl)thiazole kinase. This enzyme participates in thiamine metabolism. Thiamine pyrophosphate (TPP), a required cofactor for many enzymes in the cell, is synthesised de novo in Salmonella typhimurium.[1]

In Saccharomyces cerevisiae, hydroxyethylthiazole kinase expression is regulated at the mRNA level by intracellular thiamin pyrophosphate.[2]

Structural studies[edit]

As of late 2007, 6 structures have been solved for this class of enzymes, with PDB accession codes 1C3Q, 1EKK, 1EKQ, 1ESJ, 1ESQ, and 1V8A.

References[edit]

  1. ^ Petersen LA, Downs DM (August 1997). "Identification and characterization of an operon in Salmonella typhimurium involved in thiamine biosynthesis". J. Bacteriol. 179 (15): 4894–900. PMC 179339. PMID 9244280. 
  2. ^ Nosaka K, Nishimura H, Kawasaki Y, Tsujihara T, Iwashima A (December 1994). "Isolation and characterization of the THI6 gene encoding a bifunctional thiamin-phosphate pyrophosphorylase/hydroxyethylthiazole kinase from Saccharomyces cerevisiae". J. Biol. Chem. 269 (48): 30510–6. PMID 7982968. 

Further reading[edit]

  • Lewin LM and Brown GM (1961). "The biosynthesis of thiamine. III. Mechanism of enzymatic formation of the pyrophosphate ester of 2-methyl-4-amino-5-hydroxymethylpyrimidine". J. Biol. Chem. 236: 2768–2771. 

This article incorporates text from the public domain Pfam and InterPro IPR000417


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Internal database links

External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR000417

This entry represents the hydoxyethylthiazole kinase, ThiM, of a number of bacteria. It also represents the C-terminal domain of bifunctional thiamine biosynthesis proteins of Saccharomyces cerevisiae and Schizosaccharomyces pombe, in which the N-terminal domain corresponds to the bacterial thiamine-phosphate pyrophosphorylase (EC), ThiE.

Gene Ontology

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Domain organisation

Below is a listing of the unique domain organisations or architectures in which this domain is found. More...

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Pfam Clan

This family is a member of clan Ribokinase (CL0118), which contains the following 6 members:

ADP_PFK_GK Aldolase_2 Carb_kinase HK PfkB Phos_pyr_kin

Alignments

We store a range of different sequence alignments for families. As well as the seed alignment from which the family is built, we provide the full alignment, generated by searching the sequence database using the family HMM. We also generate alignments using four representative proteomes (RP) sets, the NCBI sequence database, and our metagenomics sequence database. More...

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We make a range of alignments for each Pfam-A family. You can see a description of each above. You can view these alignments in various ways but please note that some types of alignment are never generated while others may not be available for all families, most commonly because the alignments are too large to handle.

  Seed
(9)
Full
(2596)
Representative proteomes NCBI
(2628)
Meta
(261)
RP15
(163)
RP35
(312)
RP55
(412)
RP75
(490)
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Key: ✓ available, x not generated, not available.

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  Seed
(9)
Full
(2596)
Representative proteomes NCBI
(2628)
Meta
(261)
RP15
(163)
RP35
(312)
RP55
(412)
RP75
(490)
Alignment:
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Sequence:
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We make all of our alignments available in Stockholm format. You can download them here as raw, plain text files or as gzip-compressed files.

  Seed
(9)
Full
(2596)
Representative proteomes NCBI
(2628)
Meta
(261)
RP15
(163)
RP35
(312)
RP55
(412)
RP75
(490)
Raw Stockholm Download   Download   Download   Download   Download   Download   Download   Download  
Gzipped Download   Download   Download   Download   Download   Download   Download   Download  

You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.

External links

MyHits provides a collection of tools to handle multiple sequence alignments. For example, one can refine a seed alignment (sequence addition or removal, re-alignment or manual edition) and then search databases for remote homologs using HMMER3.

Pfam alignments:

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Trees

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Curation and family details

This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.

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Seed source: IPR000417
Previous IDs: none
Type: Domain
Author: Mian N, Bateman A
Number in seed: 9
Number in full: 2596
Average length of the domain: 239.80 aa
Average identity of full alignment: 38 %
Average coverage of the sequence by the domain: 87.31 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 20.1 20.1
Trusted cut-off 20.1 20.1
Noise cut-off 20.0 20.0
Model length: 246
Family (HMM) version: 10
Download: download the raw HMM for this family

Species distribution

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Interactions

There is 1 interaction for this family. More...

HK

Structures

For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the HK domain has been found. There are 46 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.

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