Protein Family Models

Dyp-type (dye-decolorizing) peroxidases are a family of heme proteins found in a wide range of bacteria and fungi [1,2]. 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 [2,3,4]. They consist of two domains that adopt a ferredoxin-like fold [2,4], connected by a loop. This entry represents the C-terminal domain, which possess a large hydrophobic cavity for heme binding [2,3,4]. [1]. 10742277. 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 2000;66:1754-1758. [2]. 21324904. 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. 2011;286:14922-14931. [3]. 17654545. 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. 20. TRUNCATED at 1650 bytes (from Pfam)

Date:

2024-10-16

Dyp-type (dye-decolorizing) peroxidases are a family of heme proteins found in a wide range of bacteria and fungi [1,2]. 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 [2,3,4]. They consist of two domains that adopt a ferredoxin-like fold [2,4], connected by a loop. This entry represents the N-terminal domain [2,3,4]. [1]. 10742277. 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 2000;66:1754-1758. [2]. 21324904. 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. 2011;286:14922-14931. [3]. 17654545. 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. 2007;69:223-233. [4]. 22308037. Distal heme pocket residues o. TRUNCATED at 1650 bytes (from Pfam)

Date:

2024-10-16

Members of this family, including YwbN in Bacillus subtilis and EfeB from Escherichia coli, are heme-containing proteins with a Tat (twin-arginine translocation) signal sequence to support export with cofactor already bound. The family is homologous to the dye-decolorizing peroxidase Dyp. Members act as a deferrochelatase/peroxidase involved obtaining element iron from heme or from siderophores such as bacillobactin, for import into the cell.

Gene:

efeB

Date:

2022-10-20

A defined member of this superfamily is Dyp, a dye-decolorizing peroxidase that lacks a typical heme-binding region. A distinct, uncharacterized branch (TIGR01412) of this superfamily has a typical twin-arginine dependent signal sequence characteristic of exported proteins with bound redox cofactors.

Date:

2021-10-20