Literature summary extracted from

Miethke, M.; Hou, J.; Marahiel, M.
The siderophore-interacting protein YqjH acts as a ferric reductase in different iron assimilation pathways of Escherichia coli (2011), Biochemistry, 50, 10951-10964.

Cloned(Commentary)

EC Number	Cloned (Comment)	Organism
1.16.1.9	expressed in Escherichia coli BL21 cells	Escherichia coli

Protein Variants

EC Number	Protein Variants	Comment	Organism
1.16.1.9	K55A	the mutant shows strongly reduced activity compared to the wild type enzyme	Escherichia coli
1.16.1.9	R130A	the mutant shows strongly reduced activity compared to the wild type enzyme	Escherichia coli
1.16.1.9	R246A	the variant is rather unstable, showing precipitate formation and cofactor release during protein concentration	Escherichia coli

KM Value [mM]

EC Number	KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
1.16.1.9	0.0004	-	Fe(III)-enterobactin	wild type enzyme, in 50 mM Tris-HCl (pH 8.0) and 100 mM NaCl at 25°C	Escherichia coli
1.16.1.9	0.0014	-	Fe(III)-vibriobactin	wild type enzyme, in 50 mM Tris-HCl (pH 8.0) and 100 mM NaCl at 25°C	Escherichia coli
1.16.1.9	0.0018	-	Fe(III)-(N-2,3-dihydroxybenzoyl-L-serine)3	wild type enzyme, in 50 mM Tris-HCl (pH 8.0) and 100 mM NaCl at 25°C	Escherichia coli
1.16.1.9	0.0042	-	Fe(III)-(N-2,3-dihydroxybenzoyl-Gly-Thr)3	wild type enzyme, in 50 mM Tris-HCl (pH 8.0) and 100 mM NaCl at 25°C	Escherichia coli
1.16.1.9	0.0059	-	Fe(III)-enterobactin	mutant enzyme R130A, in 50 mM Tris-HCl (pH 8.0) and 100 mM NaCl at 25°C	Escherichia coli
1.16.1.9	0.0078	-	Fe(III)-enterobactin	mutant enzyme K55A, in 50 mM Tris-HCl (pH 8.0) and 100 mM NaCl at 25°C	Escherichia coli
1.16.1.9	0.0134	-	Fe(III)-dicitrate	wild type enzyme, in 50 mM Tris-HCl (pH 8.0) and 100 mM NaCl at 25°C	Escherichia coli
1.16.1.9	0.036	-	Fe(III)-(N-2,3-dihydroxybenzoyl-L-serine)3	mutant enzyme R130A in 50 mM Tris-HCl (pH 8.0) and 100 mM NaCl at 25°C	Escherichia coli
1.16.1.9	0.04	-	Fe(III)-(N-2,3-dihydroxybenzoyl-L-serine)3	mutant enzyme K55A, in 50 mM Tris-HCl (pH 8.0) and 100 mM NaCl at 25°C	Escherichia coli
1.16.1.9	0.048	-	Fe(III)-aerobactin	wild type enzyme, in 50 mM Tris-HCl (pH 8.0) and 100 mM NaCl at 25°C	Escherichia coli
1.16.1.9	0.051	-	Fe(III)-dicitrate	mutant enzyme K55A, in 50 mM Tris-HCl (pH 8.0) and 100 mM NaCl at 25°C	Escherichia coli
1.16.1.9	0.066	-	Fe(III)-dicitrate	mutant enzyme R130A, in 50 mM Tris-HCl (pH 8.0) and 100 mM NaCl at 25°C	Escherichia coli

Organism

EC Number	Organism	UniProt	Comment	Textmining
1.16.1.9	Escherichia coli	-	-	-

Purification (Commentary)

EC Number	Purification (Comment)	Organism
1.16.1.9	Strep-Tactin column chromatography	Escherichia coli

Substrates and Products (Substrate)

EC Number	Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
1.16.1.9	Fe(III)-(N-2,3-dihydroxybenzoyl-Gly-Thr)3 + NADPH + H+	-	Escherichia coli	Fe(II) + (2,3-dihydroxybenzoyl-Gly-Thr)3 + NADP+	-	?
1.16.1.9	Fe(III)-(N-2,3-dihydroxybenzoyl-L-serine)3 + NADPH + H+	-	Escherichia coli	Fe(II) + (2,3-dihydroxybenzoyl-L-serine)3 + NADP+	-	?
1.16.1.9	Fe(III)-aerobactin + NADPH + H+	-	Escherichia coli	Fe(II) + aerobactin + NADP+	-	?
1.16.1.9	Fe(III)-bacillibactin + NADPH + H+	-	Escherichia coli	Fe(II) + bacillibacitin + NADP+	-	?
1.16.1.9	Fe(III)-dicitrate + NADPH + H+	-	Escherichia coli	Fe(II) + citrate + NADP+	-	?
1.16.1.9	Fe(III)-enterobactin + NADPH + H+	-	Escherichia coli	Fe(II) + enterobactin + NADP+	-	?
1.16.1.9	Fe(III)-vibriobactin + NADPH + H+	-	Escherichia coli	Fe(II) + vibriobactin + NADP+	-	?

Synonyms

EC Number	Synonyms	Comment	Organism
1.16.1.9	ferric siderophore reductase	-	Escherichia coli
1.16.1.9	YqjH	-	Escherichia coli

Cofactor

EC Number	Cofactor	Comment	Organism	Structure
1.16.1.9	FAD	-	Escherichia coli
1.16.1.9	NADPH	-	Escherichia coli

General Information

EC Number	General Information	Comment	Organism
1.16.1.9	malfunction	the absence of YqjH slows growth	Escherichia coli
1.16.1.9	metabolism	YqjH represents a redox factor that enhances the efficiency of ferric iron assimilation during siderophore-dependent iron homeostasis and enhances siderophore utilization in different iron acquisition pathways, including assimilation of low-potential ferric substrates that are not reduced by common cellular cofactors	Escherichia coli

kcat/KM [mM/s]

EC Number	kcat/KM Value [1/mMs^-1]	kcat/KM Value Maximum [1/mMs^-1]	Substrate	Comment	Organism	Structure
1.16.1.9	0.02	-	Fe(III)-aerobactin	wild type enzyme, in 50 mM Tris-HCl (pH 8.0) and 100 mM NaCl at 25°C	Escherichia coli
1.16.1.9	0.032	-	Fe(III)-enterobactin	mutant enzyme K55A, in 50 mM Tris-HCl (pH 8.0) and 100 mM NaCl at 25°C	Escherichia coli
1.16.1.9	0.076	-	Fe(III)-enterobactin	mutant enzyme R130A, in 50 mM Tris-HCl (pH 8.0) and 100 mM NaCl at 25°C	Escherichia coli
1.16.1.9	0.091	-	Fe(III)-(N-2,3-dihydroxybenzoyl-L-serine)3	mutant enzyme K55A, in 50 mM Tris-HCl (pH 8.0) and 100 mM NaCl at 25°C	Escherichia coli
1.16.1.9	0.132	-	Fe(III)-(N-2,3-dihydroxybenzoyl-L-serine)3	mutant enzyme R130A in 50 mM Tris-HCl (pH 8.0) and 100 mM NaCl at 25°C	Escherichia coli
1.16.1.9	0.139	-	Fe(III)-dicitrate	mutant enzyme R130A, in 50 mM Tris-HCl (pH 8.0) and 100 mM NaCl at 25°C	Escherichia coli
1.16.1.9	0.271	-	Fe(III)-dicitrate	mutant enzyme K55A, in 50 mM Tris-HCl (pH 8.0) and 100 mM NaCl at 25°C	Escherichia coli
1.16.1.9	1.268	-	Fe(III)-vibriobactin	wild type enzyme, in 50 mM Tris-HCl (pH 8.0) and 100 mM NaCl at 25°C	Escherichia coli
1.16.1.9	5.427	-	Fe(III)-dicitrate	wild type enzyme, in 50 mM Tris-HCl (pH 8.0) and 100 mM NaCl at 25°C	Escherichia coli
1.16.1.9	8.211	-	Fe(III)-enterobactin	wild type enzyme, in 50 mM Tris-HCl (pH 8.0) and 100 mM NaCl at 25°C	Escherichia coli
1.16.1.9	9.193	-	Fe(III)-(N-2,3-dihydroxybenzoyl-Gly-Thr)3	wild type enzyme, in 50 mM Tris-HCl (pH 8.0) and 100 mM NaCl at 25°C	Escherichia coli
1.16.1.9	23.35	-	Fe(III)-(N-2,3-dihydroxybenzoyl-L-serine)3	wild type enzyme, in 50 mM Tris-HCl (pH 8.0) and 100 mM NaCl at 25°C	Escherichia coli

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Release 2023.1 (January 2023)