|PROSITE documentation PDOC51324|
The ~100-residue ERV/ALR sulfhydryl oxidase domain is a versatile module adapted for catalysis of disulfide bond formation in various organelles and biological settings. The ERV/ALR sulfhydryl oxidase domain has a Cys-X-X-Cys dithiol/disulfide motif adjacent to a bound FAD cofactor, enabling transfer of electrons from thiol substrates to non-thiol electron acceptors. ERV/ALR family members differ in their N- or C-terminal extensions, which typically contain at least one additional disulfide bond, the hypothesized 'shuttle' disulfide. In yeast ERV1, a mitochondrial enzyme, the shuttle disulfide is N-terminal to the catalytic core; in yeast ERV2, present in the endoplasmic reticulum, it is C-terminal. The N- and C-terminal extensions can be entire domains, such as the thioredoxin-like domains (see <PDOC00172>) or short segments that do not seem to be distinct domains. Proteins of the ERV/ALR family are encoded by all eukaryotes and cytoplasmic DNA viruses (poxviruses, African swine fever virus, iridoviruses, and Paramecium bursaria Chlorella virus 1) [1,2,3,4,5].
The ERV/ALR sulfhydryl oxidase domain contains a four-helix bundle (helices α1-α4) and an additional single turn of helix (α5) packed perpendicular to the bundle (see <PDB:1JRA>) [3,4]. The FAD prosthetic group is housed at the mouth of the 4-helix bundle and communicates with the pair of juxtaposed cysteine residues that form the proximal redox active site .
Some proteins known to contain an ERV/ALR sulfhydryl oxidase domain are listed below:
The profile we developed covers the entire ERV/ALR sulfhydryl oxidase domain.Last update:
July 2007 / First entry.
PROSITE method (with tools and information) covered by this documentation:
|1||Authors||Hoober K.L. Glynn N.M. Burnside J. Coppock D.L. Thorpe C.|
|Title||Homology between egg white sulfhydryl oxidase and quiescin Q6 defines a new class of flavin-linked sulfhydryl oxidases.|
|Source||J. Biol. Chem. 274:31759-31762(1999).|
|2||Authors||Senkevich T.G. White C.L. Koonin E.V. Moss B.|
|Title||A viral member of the ERV1/ALR protein family participates in a cytoplasmic pathway of disulfide bond formation.|
|Source||Proc. Natl. Acad. Sci. U.S.A. 97:12068-12073(2000).|
|3||Authors||Gross E. Sevier C.S. Vala A. Kaiser C.A. Fass D.|
|Title||A new FAD-binding fold and intersubunit disulfide shuttle in the thiol oxidase Erv2p.|
|Source||Nat. Struct. Biol. 9:61-67(2002).|
|4||Authors||Vitu E. Bentzur M. Lisowsky T. Kaiser C.A. Fass D.|
|Title||Gain of function in an ERV/ALR sulfhydryl oxidase by molecular engineering of the shuttle disulfide.|
|Source||J. Mol. Biol. 362:89-101(2006).|
|5||Authors||Wang W. Winther J.R. Thorpe C.|
|Title||Erv2p: characterization of the redox behavior of a yeast sulfhydryl oxidase.|