{PDOC51404}
{PS51404; DYP_PEROXIDASE}
{BEGIN}
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* DyP-type peroxidase family *
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Heme  peroxidases  were originally divided into two superfamilies, namely, the
animal  peroxidases  and  the  plant  peroxidases (class I, II and III), which
include   fungal   (class   II)   and  bacterial  peroxidases.  The  DyP  (for
dye-decolorizing   peroxidase)  family  constitutes  a  novel  class  of  heme
peroxidase.  Because  these  enzymes were derived from fungal sources, the DyP
family was thought to be structurally related to the class II secretory fungal
peroxidases.  However, the DyP family exhibits only low sequence similarity to
classical  fungal  peroxidases,  such as LiP and MnP, and does not contain the
conserved  proximal  and  distal histidines and an essential arginine found in
other plant peroxidase superfamily members.

DyP proteins have several characteristics that distinguish them from all other
peroxidases,  including  a  particularly wide substrate specificity, a lack of
homology  to  most  other  peroxidases, and the ability to function well under
much  lower  pH  conditions  compared with the other plant peroxidases [1]. In
terms   of   substrate   specificity,  DyP  degrades  the  typical  peroxidase
substrates,  but  also  degrades  hydroxyl-free  anthraquinone  (many dyes are
derived from anthraquinone compounds).

Crystal structures of DyP family members reveal two domains, each one adopting
a  ferredoxin-like  fold  (see  <PDB:  2GVK>)  [2]. The proteins consist of an
N-terminal  domain  and  a  C-terminal  domain  likely  to  be  related  by  a
duplication  of  an ancestral gene, as inferred from the conserved topology of
the domains. The heme iron is penta-coordinated, with the protein contributing
a  conserved  histidine ligand to the iron center. A conserved Asp most likely
acts as a proton donor/acceptor and takes the place of the catalytic histidine
used  by  plant  peroxidases.  This Asp substitution helps explain why the DyP
family is active at low pH [3].

The  profile  we  developed  covers  the  whole  conserved  region of DyP-type
peroxidases.

-Sequences known to belong to this class detected by the profile: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.
-Last update: August 2008 / First entry.

[ 1] Zubieta C., Krishna S.S., Kapoor M., Kozbial P., McMullan D.,
     Axelrod H.L., Miller M.D., Abdubek P., Ambing E., Astakhova T.,
     Carlton D., Chiu H.J., Clayton T., Deller M.C., Duan L.,
     Elsliger M.A., Feuerhelm J., Grzechnik S.K., Hale J., Hampton E.,
     Han G.W., Jaroszewski L., Jin K.K., Klock H.E., Knuth M.W., Kumar A.,
     Marciano D., Morse A.T., Nigoghossian E., Okach L., Oommachen S.,
     Reyes R., Rife C.L., Schimmel P., van den Bedem H., Weekes D.,
     White A., Xu Q., Hodgson K.O., Wooley J., Deacon A.M., Godzik A.,
     Lesley S.A., Wilson I.A.
     "Crystal structures of two novel dye-decolorizing peroxidases reveal a
     beta-barrel fold with a conserved heme-binding motif."
     Proteins 69:223-233(2007).
     PubMed=17654545; DOI=10.1002/prot.21550
[ 2] Zubieta C., Joseph R., Krishna S.S., McMullan D., Kapoor M.,
     Axelrod H.L., Miller M.D., Abdubek P., Acosta C., Astakhova T.,
     Carlton D., Chiu H.J., Clayton T., Deller M.C., Duan L., Elias Y.,
     Elsliger M.A., Feuerhelm J., Grzechnik S.K., Hale J., Han G.W.,
     Jaroszewski L., Jin K.K., Klock H.E., Knuth M.W., Kozbial P.,
     Kumar A., Marciano D., Morse A.T., Murphy K.D., Nigoghossian E.,
     Okach L., Oommachen S., Reyes R., Rife C.L., Schimmel P., Trout C.V.,
     van den Bedem H., Weekes D., White A., Xu Q., Hodgson K.O., Wooley J.,
     Deacon A.M., Godzik A., Lesley S.A., Wilson I.A.
     "Identification and structural characterization of heme binding in a
     novel dye-decolorizing peroxidase, TyrA."
     Proteins 69:234-243(2007).
     PubMed=17654547; DOI=10.1002/prot.21673
[ 3] Sugano Y., Muramatsu R., Ichiyanagi A., Sato T., Shoda M.
     "DyP, a unique dye-decolorizing peroxidase, represents a novel heme
     peroxidase family: ASP171 replaces the distal histidine of classical
     peroxidases."
     J. Biol. Chem. 282:36652-36658(2007).
     PubMed=17928290; DOI=10.1074/jbc.M706996200

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