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PROSITE documentation PDOC51324 [for PROSITE entry PS51324]

ERV/ALR sulfhydryl oxidase domain profile





Description

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 [5].

Some proteins known to contain an ERV/ALR sulfhydryl oxidase domain are listed below:

  • Yeast essential for respiration and viability proteins 1 and 2 (ERV1 and ERV2). ERV1 is required for mitochondrial biogenesis.
  • Mammalian Augmenter of Liver Regeneration (ALR), the homolog of ERV1.
  • Animal and plant quiescin-sulfhydryl oxidase (QSOX).
  • Poxviruses E10R protein, that promotes disulfide-bond formation in coat proteins assembling in the reducing environment of the cell cytosol.

The profile we developed covers the entire ERV/ALR sulfhydryl oxidase domain.

Last update:

July 2007 / First entry.

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Technical section

PROSITE method (with tools and information) covered by this documentation:

ERV_ALR, PS51324; ERV/ALR sulfhydryl oxidase domain profile  (MATRIX)


References

1AuthorsHoober K.L. Glynn N.M. Burnside J. Coppock D.L. Thorpe C.
TitleHomology between egg white sulfhydryl oxidase and quiescin Q6 defines a new class of flavin-linked sulfhydryl oxidases.
SourceJ. Biol. Chem. 274:31759-31762(1999).
PubMed ID10542195

2AuthorsSenkevich T.G. White C.L. Koonin E.V. Moss B.
TitleA viral member of the ERV1/ALR protein family participates in a cytoplasmic pathway of disulfide bond formation.
SourceProc. Natl. Acad. Sci. U.S.A. 97:12068-12073(2000).
PubMed ID11035794
DOI10.1073/pnas.210397997

3AuthorsGross E. Sevier C.S. Vala A. Kaiser C.A. Fass D.
TitleA new FAD-binding fold and intersubunit disulfide shuttle in the thiol oxidase Erv2p.
SourceNat. Struct. Biol. 9:61-67(2002).
PubMed ID11740506
DOI10.1038/nsb740

4AuthorsVitu E. Bentzur M. Lisowsky T. Kaiser C.A. Fass D.
TitleGain of function in an ERV/ALR sulfhydryl oxidase by molecular engineering of the shuttle disulfide.
SourceJ. Mol. Biol. 362:89-101(2006).
PubMed ID16893552
DOI10.1016/j.jmb.2006.06.070

5AuthorsWang W. Winther J.R. Thorpe C.
TitleErv2p: characterization of the redox behavior of a yeast sulfhydryl oxidase.
SourceBiochemistry 46:3246-3254(2007).
PubMed ID17298084
DOI10.1021/bi602499t



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