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Literature summary for 1.8.1.2 extracted from

  • Askenasy, I.; Pennington, J.M.; Tao, Y.; Marshall, A.G.; Young, N.L.; Shang, W.; Stroupe, M.E.
    The N-terminal domain of Escherichia coli assimilatory NADPH-sulfite reductase hemoprotein is an oligomerization domain that mediates holoenzyme assembly (2015), J. Biol. Chem., 290, 19319-19333 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.8.1.2

Protein Variants

Protein Variants Comment Organism
R83S mutant is unable to bind flavoprotein SiRFP Escherichia coli

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
660
-
 PAGE, octamer of alpha subunit SiRFP Escherichia coli
800
-
 PAGE, holoenzyme Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli P17846 beta subunit, hemoprotein SiRHP
-

Subunits

Subunits Comment Organism
multimer octamer of alpha subunit SiRFP, plus 4 * * 64000, beta-subunit SiRHP, calculated Escherichia coli

Synonyms

Synonyms Comment Organism
CysI beta subunit, hemoprotein SiRHP Escherichia coli

Cofactor

Cofactor Comment Organism Structure
[4Fe-4S]-center
-
 Escherichia coli

General Information

General Information Comment Organism
metabolism the alpha8beta4 SiR holoenzyme assembles through the N-terminus of flavin-binding flavoprotein SiRFP and the NADPH binding domain of iron-containing hemoprotein SiRHP. Apo-SiRHP forms a homotetramer, also dependent on its N-terminus, that is unable to assemble with SiRFP Escherichia coli