1.16.98.B1: mitochondrial amidoxime reducing component

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For detailed information about mitochondrial amidoxime reducing component, go to the full flat file.

Reaction

2 [Fe(II)-cytochrome b5] + 2 H+ +

Synonyms

B4114_1419, mARC1, mARC2, mitochondrial amidoxime reducing component 2, mitochondrial amidoxime-reducing component 1, Moco sulfurase C-terminal domain protein, MOSC domain-containing protein, MTARC1, MTARC2, YiiM

ECTree

     1 Oxidoreductases

         1.16 Oxidizing metal ions

             1.16.98 With other, known, physiological acceptors

                1.16.98.B1 mitochondrial amidoxime reducing component

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Results	in table
3	AA Sequence
3	Cloned(Commentary)
4	Cofactor
3	Crystallization (Commentary)
31	Disease/ Diagnostics
3	General Information
14	KM Value [mM]
3	Localization
4	Metals/Ions
3	Molecular Weight [Da]
1	Natural Substrates/ Products (Substrates)
10	Organism
1	Reaction
10	Reference
5	Source Tissue
21	Specific Activity [micromol/min/mg]
19	Substrates and Products (Substrate)
5	Subunits
13	Synonyms
1	Systematic Name

Crystallization

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Crystallization on EC 1.16.98.B1 - mitochondrial amidoxime reducing component

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CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

comparison of structures of Geobacillus stearothermophilus and Escherichia coli YiiM proteins. Both consist of a beta-barrel and two alpha-helix bundles and feature a cavity surrounded by the three modules. The cavity is characterized by positive electrostatic potentials and high sequence conservation. In silico docking of molybdenum cofactor

Escherichia coli

-

762452

comparison of structures of Geobacillus stearothermophilus and Escherichia coli YiiM proteins. Both consist of a beta-barrel and two alpha-helix bundles and feature a cavity surrounded by the three modules. The cavity is characterized by positive electrostatic potentials and high sequence conservation

Geobacillus stearothermophilus

A0A150NEL9

762452

structure of the fusion protein comprising T4 lysozyme and N-terminally truncated human mARC1, to 1.78 A resolution. Residue D209 seems to have a Moco-independent impact on mARC enzymatic activity. F237 is the central amino acid of a hydrophobic core between the large beta-barrel and helices alpha4, alpha7, and alpha8, securing the 3D arrangement of the Moco binding site

Homo sapiens

Q5VT66

762276