IPR044528
Persulfide dioxygenase-like, MBL-fold metallo-hydrolase domain
InterPro entry
Short name | POD-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
GO terms
biological process
molecular function
cellular component
- None
Cross References
ENZYME
Contributing Member Database Entry
- CDD:cd07724
Representative structure
2gcu: X-Ray Structure of Gene Product from Arabidopsis Thaliana At1g53580