Literature summary extracted from

Axelrod, H.L.; McMullan, D.; Krishna, S.S.; Miller, M.D.; Elsliger, M.; Abdubek, P.; Ambing, E.; Astakhova, T.; Carlton, D.; Chiu, H.; Clayton, T.; Duan, L.; Feuerhelm, J.; Grzechnik, S.K.; Hale, J.; Han, G.W.; Haugen, J.; Jaroszewski, L.; Jin, K.K.; Klock, H.E.; Knuth, M.W.; Koesema, E.; Morse, A.T.; Nigoghossian, E.; Okach, L.; Oommachen, S.; Paulsen, J.; Quijano, K.; Reyes, R.; Rife, C.L.; van den Bedem, H.; Weekes, D.; White, A.; Wolf, G.; Xu, Q.; Hodgson, K.O.; Wooley, J.; Deacon. A.M.; Godzik, A.; Lesley, S.A.; Wilson, I.A.
Crystal structure of AICAR transformylase IMP cyclohydrolase (TM1249) from Thermotoga maritima at 1.88 ANG. resolution (2008), Proteins Struct. Funct. Bioinform., 71, 1042-1049.

Cloned(Commentary)

EC Number	Cloned (Comment)	Organism
2.1.2.3	into the plasmid pMH4 for expression in the Escherichia coli strain GeneHogs	Thermotoga maritima
3.5.4.10	expression of His-tagged enzyme in Escherichia coli	Thermotoga maritima

EC Number	Crystallization (Comment)	Organism
2.1.2.3	the three-dimensional structure of TM1249 is determined to 1.88 A resolution by molecular replacement	Thermotoga maritima
3.5.4.10	20 mg/ml purified recombinant enzyme in 20 mM Tris, pH 7.9, 150 mM NaCl, 0.25 mM TCEP, nanodroplet vapor diffusion method, the crystallization solution contains 20% w/v PEG 6000 and 0.1 M citrate pH 5.0, 10% v/v PEG 200 as a cryoprotectant, X-ray diffraction structure determination and anaylsis at 1.88 A resolution, modelling	Thermotoga maritima

EC Number	Metals/Ions	Comment	Organism	Structure
2.1.2.3	K+	the refined structure includes two K+ ions in the asymmetric unit	Thermotoga maritima

EC Number	Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
2.1.2.3	49700	-	monomer, residues 1-452	Thermotoga maritima
3.5.4.10	49700	-	1 * 49700, enzyme comprising residues 1-452, i.e. the IMP cyclohydrolase part of the bifunctional enzyme, SDS-PAGE	Thermotoga maritima

EC Number	Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
2.1.2.3	10-formyltetrahydrofolate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide	Thermotoga maritima	-	tetrahydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide	-	?
3.5.4.10	additional information	Thermotoga maritima	the TM1249 gene or gene purH of Thermotoga maritima encodes a bifunctional enzyme with 5-aminoimidazole-4-carboxamide ribonucleotide transformylase, AICAR Tfase, EC 2.1.2.3, and inosine 5'-monophosphate cyclohydrolase, IMPCH, EC 3.5.4.10, activities. These activities represent the final two steps of the de novo purine biosynthesis pathway, overview	?	-	?

EC Number	Organism	UniProt	Comment	Textmining
2.1.2.3	Thermotoga maritima	-	-	-
3.5.4.10	Thermotoga maritima	Q9X0X6	gene TM1249 or purH	-

EC Number	Purification (Comment)	Organism
2.1.2.3	using a nickel-chelating resin and a Resource Q column	Thermotoga maritima
3.5.4.10	recombinant His-tagged enzyme from Escherichia coli by nickel affinity and anion exchange chromatography	Thermotoga maritima

EC Number	Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.
2.1.2.3	10-formyltetrahydrofolate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide	-	Thermotoga maritima	tetrahydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide	-	?
3.5.4.10	5-formaminoimidazole-4-carboxamide ribonucleotide	the IMPCH domain catalyzes the intramolecular cyclization of 5-formyl-AICAR, FAICAR, to IMP	Thermotoga maritima	IMP + H2O	-	?
3.5.4.10	additional information	the TM1249 gene or gene purH of Thermotoga maritima encodes a bifunctional enzyme with 5-aminoimidazole-4-carboxamide ribonucleotide transformylase, AICAR Tfase, EC 2.1.2.3, and inosine 5'-monophosphate cyclohydrolase, IMPCH, EC 3.5.4.10, activities. These activities represent the final two steps of the de novo purine biosynthesis pathway, overview	Thermotoga maritima	?	-	?

EC Number	Subunits	Comment	Organism
2.1.2.3	dimer	-	Thermotoga maritima
3.5.4.10	monomer	1 * 49700, enzyme comprising residues 1-452, i.e. the IMP cyclohydrolase part of the bifunctional enzyme, SDS-PAGE	Thermotoga maritima

EC Number	Synonyms	Comment	Organism
2.1.2.3	5-aminoimidazole-4-carboxamide ribonucleotide transformylase	-	Thermotoga maritima
2.1.2.3	AICAR TFase	-	Thermotoga maritima
2.1.2.3	AICAR transformylase	-	Thermotoga maritima
2.1.2.3	PurH	-	Thermotoga maritima
2.1.2.3	TM1249	-	Thermotoga maritima
3.5.4.10	AICAR transformylase/inosine 5'-monophosphate cyclohydrolase	-	Thermotoga maritima
3.5.4.10	IMPCH	-	Thermotoga maritima
3.5.4.10	inosine 5'-monophosphate cyclohydrolase	-	Thermotoga maritima

EC Number	Cofactor	Comment	Organism	Structure
2.1.2.3	10-formyltetrahydrofolate	-	Thermotoga maritima

EC Number	Organism	Comment	pI Value Maximum	pI Value
2.1.2.3	Thermotoga maritima	calculated isoelectric point	-	5.49
3.5.4.10	Thermotoga maritima	sequence calculation	-	5.49