|General category ||Metabolism|
|Detailed category ||Other enzymes|
Document: Function annotation of SCOP domain superfamilies
|Cross references ||IPR000028 SSF47571 Protein matches|
|Abstract ||Chloroperoxidase (CPO) is a versatile heme-containing enzyme that exhibits peroxidase, catalase and cytochrome P450-like
activities in addition to catalyzing halogenation reactions .
Despite functional similarities with other heme enzymes, CPO folds into a novel
tertiary structure dominated by eight helical segments. The catalytic base,
required to cleave the peroxide O-O bond, is glutamic acid
rather than histidine as in other peroxidases.|
PDBeMotif information about ligands, sequence and structure motifs
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Internal database links
Browse genome assignments for this superfamily. The SUPERFAMILY hidden Markov model library has been used to carry
out SCOP domain assignments to all genomes at the superfamily level.
Alignments of sequences to 2 models
in this superfamily are available by clicking on the 'Alignments' icon above. PDB sequences less than 40% identical
are shown by default, but any other sequence(s) may be aligned. Select PDB sequences, genome sequences, or paste in or upload your own sequences.
Browse and view proteins in genomes which have
different domain combinations including a Cloroperoxidase domain.
Examine the distribution of domain superfamilies, or families, across the major taxonomic kingdoms or genomes within a kingdom. This gives an immediate impression of how superfamilies, or families, are restricted to certain kingdoms of life.
Explore domain occurrence network where nodes represent genomes and edges are domain architectures (shared between genomes) containing the superfamily of interest.
There are 2 hidden Markov models representing the Cloroperoxidase superfamily. Information on how the models are built, and plots showing hydrophobicity, match emmission probabilities and insertion/deletion probabilities can be inspected.
Jump to [ Top of page · SCOP classification · InterPro annotation · PDBeMotif links · Functional annotation · Internal database links ]