Literature summary for 1.1.1.2 extracted from

Larson, S.; Jones, J.; McPherson, A.
The structure of an iron-containing alcohol dehydrogenase from a hyperthermophilic archaeon in two chemical states (2019), Acta Crystallogr. Sect. F, 75, 217-226 .

Cloned(Commentary)

Cloned (Comment)	Organism
gene A3L14_07690, recombinant enzyme expression in Escherichia coli strain Rosetta2	Thermococcus thioreducens

Crystallization (Commentary)

Crystallization (Comment)	Organism
purified enzyme in unit cells belonging to space groups P21, P212121 and P43212 (monoclinic, orthorhombic, and tetragonal crystals), vapour diffusion method, mixing of 0.0012 ml of 10 mg/ml protein in 50 mM Tris, pH 7.5, and 50 mM NaCl, with 600 nl of reservoir solution containing 8% PEG 4000, pH 4.2-4.5, in a protein:reservoir ratio of 2:1 (1:1 for the tetragonal crystals), at 20°C, X-ray diffraction structure determination and analysis at 2.4 A, 2.1 A, and 1.9 A resolution, respectively, modeling by molecular replacement using the FeADH from Thermotoga maritima as a template	Thermococcus thioreducens

Crystallization (Comment)

Organism

purified enzyme in unit cells belonging to space groups P21, P212121 and P43212 (monoclinic, orthorhombic, and tetragonal crystals), vapour diffusion method, mixing of 0.0012 ml of 10 mg/ml protein in 50 mM Tris, pH 7.5, and 50 mM NaCl, with 600 nl of reservoir solution containing 8% PEG 4000, pH 4.2-4.5, in a protein:reservoir ratio of 2:1 (1:1 for the tetragonal crystals), at 20°C, X-ray diffraction structure determination and analysis at 2.4 A, 2.1 A, and 1.9 A resolution, respectively, modeling by molecular replacement using the FeADH from Thermotoga maritima as a template

Thermococcus thioreducens

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Fe2+	required, the iron is internally sequestered, and is bound entirely by amino acids from one domain: three histidines and one aspartic acid. The monoclinic and orthorhombic asymmetric units one molecule contained iron and an NADP molecule, while the other do not. The tetragonal crystals lack both iron and NADP+	Thermococcus thioreducens

Organism

Organism	UniProt	Comment	Textmining
Thermococcus thioreducens	A0A0Q2QQL1	-	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant enzyme from Escherichia coli strain Rosetta2 by heat treatment for 30 min at 75°C, the supernatant is further purified by cation exchange and anion exchange chromatography, ultrafiltration, and gel filtration	Thermococcus thioreducens

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
1,4-butanediol + NADP+	-	Thermococcus thioreducens	4-hydroxybutanal + NADPH + H+	-	r

Subunits

Subunits	Comment	Organism
dimer	x * 41500, SDS-PAGE	Thermococcus thioreducens

Synonyms

Synonyms	Comment	Organism
A3L14_07690	-	Thermococcus thioreducens
FeADH	-	Thermococcus thioreducens
iron-containing alcohol dehydrogenase	-	Thermococcus thioreducens

Cofactor

Cofactor	Comment	Organism
additional information	the coenzyme is in an extended conformation, a feature that is common to the large superfamily of NADH-dependent dehydrogenases that share a classical nucleotide-binding domain. A long broad tunnel passes entirely through the enzyme between the two domains, completely encapsulating the coenzyme	Thermococcus thioreducens
NADP+	-	Thermococcus thioreducens
NADPH	-	Thermococcus thioreducens