Literature summary extracted from
Coquille, S.; Roux, C.; Mehta, A.; Begley, T.P.; Fitzpatrick, T.B.; Thore, S.
High-resolution crystal structure of the eukaryotic HMP-P synthase (THIC) from Arabidopsis thaliana (2013), J. Struct. Biol., 184, 438-444.
Cloned(Commentary)
EC Number |
Cloned (Comment) |
Organism |
---|
4.1.99.17 |
gene thiC, recombinant expression of His-tagged N-terminally truncated mutant DELTAN71-AtTHIC in Escherichia coli strain BL21(DE3) |
Arabidopsis thaliana |
Crystallization (Commentary)
EC Number |
Crystallization (Comment) |
Organism |
---|
4.1.99.17 |
purified recombinant His-tagged DELTAN71-AtTHIC mutant, by a proteolysis assay (especially alpha-chymotrypsin) coupled with the sitting drop vapor diffusion technique at 18°C, using 0.01 M cobalt (II) chloride hexahydrate, 0.1 M sodium acetate trihydrate, pH 4.6, 1 M 1,6-hexanediol, X-ray diffraction structure determination and analysis at 1.6 A resolution |
Arabidopsis thaliana |
Protein Variants
EC Number |
Protein Variants |
Comment |
Organism |
---|
4.1.99.17 |
additional information |
generation of an N-terminally truncated version of Arabidopsis thaliana THIC, lacking the first 71 amino acids, a chloroplastidial targeting peptide. The truncated AtTHIC is functionally active |
Arabidopsis thaliana |
Localization
EC Number |
Localization |
Comment |
Organism |
GeneOntology No. |
Textmining |
---|
4.1.99.17 |
chloroplast |
- |
Arabidopsis thaliana |
9507 |
- |
Metals/Ions
EC Number |
Metals/Ions |
Comment |
Organism |
Structure |
---|
4.1.99.17 |
Co2+ |
a metal ion with octahedral coordination (two strictly conserved histidine residues (H426 and H490) and four water molecules) at the same location as a zinc ion in the bacterial enzyme, and a metal ion with multiple coordinated water molecules in the close vicinity of the substrate binding sites, binding structures, overview |
Arabidopsis thaliana |
|
4.1.99.17 |
Fe2+ |
the enzyme contains a [4Fe-4S] cluster |
Arabidopsis thaliana |
|
Molecular Weight [Da]
EC Number |
Molecular Weight [Da] |
Molecular Weight Maximum [Da] |
Comment |
Organism |
---|
4.1.99.17 |
65451 |
- |
2 * 65451, recombinant His-tagged DELTAN71-AtTHIC mutant, mass spectrometry and crystal structure |
Arabidopsis thaliana |
4.1.99.17 |
130000 |
- |
recombinant His-tagged DELTAN71-AtTHIC mutant, gel filtration |
Arabidopsis thaliana |
Natural Substrates/ Products (Substrates)
EC Number |
Natural Substrates |
Organism |
Comment (Nat. Sub.) |
Natural Products |
Comment (Nat. Pro.) |
Rev. |
Reac. |
---|
4.1.99.17 |
5-amino-1-(5-phospho-D-ribosyl)imidazole + S-adenosyl-L-methionine |
Arabidopsis thaliana |
- |
4-amino-2-methyl-5-phosphomethylpyrimidine + 5'-deoxyadenosine + L-methionine + formate + CO |
- |
? |
|
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
4.1.99.17 |
Arabidopsis thaliana |
O82392 |
gene thiC |
- |
Purification (Commentary)
EC Number |
Purification (Comment) |
Organism |
---|
4.1.99.17 |
recombinant His-tagged N-terminally truncated mutant DELTAN71-AtTHIC from Escherichia coli strain BL21(DE3) by nickel affinity chromatography |
Arabidopsis thaliana |
Substrates and Products (Substrate)
EC Number |
Substrates |
Comment Substrates |
Organism |
Products |
Comment (Products) |
Rev. |
Reac. |
---|
4.1.99.17 |
5-amino-1-(5-phospho-D-ribosyl)imidazole + S-adenosyl-L-methionine |
- |
Arabidopsis thaliana |
4-amino-2-methyl-5-phosphomethylpyrimidine + 5'-deoxyadenosine + L-methionine + formate + CO |
- |
? |
|
4.1.99.17 |
5-amino-1-(5-phospho-D-ribosyl)imidazole + S-adenosyl-L-methionine |
the enzyme uses an iron-sulfur cluster as well as a 5'-deoxyadenosyl radical as cofactors to rearrange the 5-amino-imidazole ribonucleotide (AIR) substrate to the pyrimidine ring |
Arabidopsis thaliana |
4-amino-2-methyl-5-phosphomethylpyrimidine + 5'-deoxyadenosine + L-methionine + formate + CO |
- |
? |
|
Subunits
EC Number |
Subunits |
Comment |
Organism |
---|
4.1.99.17 |
dimer |
2 * 65451, recombinant His-tagged DELTAN71-AtTHIC mutant, mass spectrometry and crystal structure |
Arabidopsis thaliana |
4.1.99.17 |
More |
enzyme three-dimensional structure analysis, overview |
Arabidopsis thaliana |
Synonyms
EC Number |
Synonyms |
Comment |
Organism |
---|
4.1.99.17 |
HMP-P synthase |
- |
Arabidopsis thaliana |
4.1.99.17 |
thiC |
- |
Arabidopsis thaliana |
Cofactor
EC Number |
Cofactor |
Comment |
Organism |
Structure |
---|
4.1.99.17 |
S-adenosyl-L-methionine |
a S-adenosyl-L-methionine radical enzyme |
Arabidopsis thaliana |
|
General Information
EC Number |
General Information |
Comment |
Organism |
---|
4.1.99.17 |
metabolism |
the enzyme is important in thiamine diphosphate, vitamin B1, biosynthesis, an essential cofactor for key cellular metabolic enzymes in all forms of life |
Arabidopsis thaliana |
4.1.99.17 |
additional information |
enzyme three-dimensional structure analysis and comparison, overview |
Arabidopsis thaliana |