PF20628

Dyp-type peroxidase, C-terminal

Pfam entry
Member databasePfam
Pfam typedomain
Short nameDyp_perox_C
ClanDim_A_B_barrel
AuthorTIGRFAMs; Finn RD;0000-0001-8626-2148 Chuguransky S;0000-0002-0520-0736
Sequence Ontology0000417

Description

Dyp-type (dye-decolorizing) peroxidases are a family of heme proteins found in a wide range of bacteria and fungi
[1, 4]
. They have a wide substrate specificity and lack homology to most other peroxidases, with the ability to function well under much lower pH conditions compared with the other plant peroxidases
[4, 3, 2]
. They consist of two domains that adopt a ferredoxin-like fold
[4, 2]
, connected by a loop. This entry represents the C-terminal domain, which possess a large hydrophobic cavity for heme binding
[4, 3, 2]
.

References

1.Efficient heterologous expression in Aspergillus oryzae of a unique dye-decolorizing peroxidase, DyP, of Geotrichum candidum Dec 1. Sugano Y, Nakano R, Sasaki K, Shoda M. Appl. Environ. Microbiol. 66, 1754-8, (2000). View articlePMID: 10742277

2.Distal heme pocket residues of B-type dye-decolorizing peroxidase: arginine but not aspartate is essential for peroxidase activity. Singh R, Grigg JC, Armstrong Z, Murphy ME, Eltis LD. J. Biol. Chem. 287, 10623-30, (2012). View articlePMID: 22308037

3.Crystal structures of two novel dye-decolorizing peroxidases reveal a beta-barrel fold with a conserved heme-binding motif. Zubieta C, Krishna SS, Kapoor M, Kozbial P, McMullan D, Axelrod HL, Miller MD, Abdubek P, Ambing E, Astakhova T, Carlton D, Chiu HJ, Clayton T, Deller MC, Duan L, Elsliger MA, Feuerhelm J, Grzechnik SK, Hale J, Hampton E, Han GW, Jaroszewski L, Jin KK, Klock HE, Knuth MW, Kumar A, Marciano D, Morse AT, Nigoghossian E, Okach L, Oommachen S, Reyes R, Rife CL, Schimmel P, van den Bedem H, Weekes D, White A, Xu Q, Hodgson KO, Wooley J, Deacon AM, Godzik A, Lesley SA, Wilson IA. Proteins 69, 223-33, (2007). View articlePMID: 17654545

4.Crystal structure and biochemical features of EfeB/YcdB from Escherichia coli O157: ASP235 plays divergent roles in different enzyme-catalyzed processes. Liu X, Du Q, Wang Z, Zhu D, Huang Y, Li N, Wei T, Xu S, Gu L. J Biol Chem 286, 14922-31, (2011). PMID: 21324904

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