2.7.4.7: phosphooxymethylpyrimidine kinase

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For detailed information about phosphooxymethylpyrimidine kinase, go to the full flat file.

Reaction

Synonyms

2-methyl-4-amino-5-hydroxymethylpyrimidine monophosphate kinase, CCC13826_0338, CcThiD2, HMP-P kinase, HMP/HMP phosphate kinase, HMPPK, HVO_2666, hydroxymethylpyrimidine phosphate kinase, hydroxymethylpyrimidine phosphokinase, kinase, phosphomethylpyrimidine (phosphorylating), More, phosphomethylpyrimidine kinase, StHMPPK, Suden_2055, TdThiD2, Thi20, Thi20p, Thi20p protein, Thi21p protein, thiamine phosphate synthase, ThiD, ThiD2, ThiD2 domain-containing protein, TTHA0680, TtHMPPK

ECTree

     2 Transferases

         2.7 Transferring phosphorus-containing groups

             2.7.4 Phosphotransferases with a phosphate group as acceptor

                2.7.4.7 phosphooxymethylpyrimidine kinase

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Results	in table
13889	AA Sequence
1	CAS Registry Number
9	Cloned(Commentary)
2	Crystallization (Commentary)
44	General Information
3	IC50 Value
4	Inhibitors
2	kcat/KM [mM/s]
7	KM Value [mM]
1	Localization
8	Metals/Ions
2	Molecular Weight [Da]
27	Natural Substrates/ Products (Substrates)
31	Organism
9	Pathway
14	PDB ID
8	pH Optimum
7	Protein Variants
10	Purification (Commentary)
8	Reaction
1	Reaction Type
30	Reference
3	Storage Stability
44	Substrates and Products (Substrate)
4	Subunits
65	Synonyms
1	Systematic Name
5	Temperature Optimum [°C]
4	Temperature Stability [°C]
5	Turnover Number [1/s]

Crystallization

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Crystallization on EC 2.7.4.7 - phosphooxymethylpyrimidine kinase

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CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

to 2.7 A resolution. Enzyme is composed of a ThiD-like N-terminal domain that catalyzes the phosphorylation of 4-amino-5-hydroxymethyl-2-methylpyrimidine and 4-amino-5-hydroxymethyl-2-methylpyrimidine phosphate and a TenA-like C-terminal domain with thiaminase activity. The structure reveals an overall dimeric organization in which N-terminal domains and C-terminal domains form ThiD-like and TenA-like local dimers. A relatively flexible linker region composed of a loop and a short helix joins the two domains. This linker region and a flexible N-terminal extension occupy the interface between the ThiD-like and TenA-like dimers. The N-terminal extension is composed of a single beta-strand that packs against and extends the length of the internal beta-sheet of the ThiD-like domain and a short alpha-helix

Saccharomyces cerevisiae

Q08224

718477

hanging drop vapor diffusion, 6 mg/ml HMPP kinase, hanging drops contain 0.002 mL protein solution and 0.002 ml reservoir solution, crystal without HMP are obtained using a reservoir solution containing 1.35 M MgSO4, 150 mM MES, pH 7.0, crystals with HMP are obtained with 1.4 M MgSO4 and 150 M MES, crystals of native HMP-P kinase diffract to 2.3 A resolution

Salmonella enterica subsp. enterica serovar Typhimurium

-

645187