D
IPR044528

Persulfide dioxygenase-like, MBL-fold metallo-hydrolase domain

InterPro entry
Short namePOD-like_MBL-fold
Overlapping
homologous
superfamilies
 
domain relationships

Description

Persulfide dioxygenase (PDO, also known as sulfur dioxygenase, SDO,
1.13.11.18
) is a non-heme iron-dependent oxygenase that catalyses the oxidation of glutathione persulfide (GSSH) to glutathione (GSH) and persulfite and play important and varied roles in all kingdoms, including sulfide detoxification
[3]
. These enzymes belong to the metallo-beta-lactamase (MBL) superfamily as they consist of the same structural fold of two β-sheets surrounded by α-helices, which supports the metal-binding feature. The PDOs share high sequence and structural similarity with glyoxalases II (classical di-zinc MBL hydrolase), specially at the metal-binding centre. PDOs have a Fe2 binding site and a secondary coordination sphere-based hydrogen bond network that is absent in glyoxalases II, in which the corresponding residues are involved in coordinating a second metal ion. This suggests that PDOs may evolve from a hydrolytic enzyme with two coordinated ions
[3]
. Based on sequence analysis, three subclasses of PDO were described: ETHE1, which is present in animals, plants, and bacteria (in the latter they are also called type 1 PDOs), persulfide dioxygenase A (PDOA, or type 2 PDOs), also known as sulfur dioxygenase A (SdoA), which is common in Proteobacteria, and Blh, which is an acronym for beta-lactamase-like hydrolase
[3]
. In humans, mutations in PDO ETHE1 cause a rare autosomal recessive metabolic disorder called ethylmalonic encephalopathy
[2]
. In Arabidopsis thaliana, ETHE1 is essential for embryo and endosperm development
[1]
.

This entry represents the MBL-fold metallo-hydrolase domain.

References

1.Arabidopsis ETHE1 encodes a sulfur dioxygenase that is essential for embryo and endosperm development. Holdorf MM, Owen HA, Lieber SR, Yuan L, Adams N, Dabney-Smith C, Makaroff CA. Plant Physiol 160, 226-36, (2012). PMID: 22786886

2.Crystal structure of human persulfide dioxygenase: structural basis of ethylmalonic encephalopathy. Pettinati I, Brem J, McDonough MA, Schofield CJ. Hum Mol Genet 24, 2458-69, (2015). PMID: 25596185

3.Characterizations of Two Bacterial Persulfide Dioxygenases of the Metallo-β-lactamase Superfamily. Sattler SA, Wang X, Lewis KM, DeHan PJ, Park CM, Xin Y, Liu H, Xian M, Xun L, Kang C. J Biol Chem 290, 18914-23, (2015). PMID: 26082492

GO terms

cellular component

  • None

Cross References

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