Summary: Chlorite dismutase
Chlorite dismutase Provide feedback
This family contains chlorite dismutase enzymes of bacterial and archaeal origin. This enzyme catalyses the disproportionation of chlorite into chloride and oxygen . Note that many family members are hypothetical proteins.
van Ginkel CG, Rikken GB, Kroon AG, Kengen SW; , Arch Microbiol 1996;166:321-326.: Purification and characterization of chlorite dismutase: a novel oxygen-generating enzyme. PUBMED:8929278 EPMC:8929278
This tab holds annotation information from the InterPro database.
InterPro entry IPR010644
Proteins in this family are putative heme-dependent peroxidases. This family also includes chlorite dismutase enzymes of bacterial and archaeal origin. Chlorite dismutase catalyses the disproportionation of chlorite into chloride and oxygen [PUBMED:8929278, PUBMED:20386942].
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This superfamily of proteins possess a Ferredoxin-like fold. Pairs of these assemble into a beta barrel. The function of this barrel is quite varied and includes Muconolactone isomerase as well as monooxygenases.
The clan contains the following 21 members:ABM AsnC_trans_reg Chlor_dismutase Cyclase_polyket Dabb Dehydratase_hem DUF1330 DUF1428 DUF3291 DUF4188 DUF718 Dyp_perox EthD MIase MmlI NapD NIPSNAP SchA_CurD SOR YCII ydhR
We make a range of alignments for each Pfam-A family:
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- Representative Proteomes (RPs) at 15%, 35%, 55% and 75% co-membership thresholds
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- alignment generated by searching the metagenomics sequence database using the family HMM
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Curation and family details
|Seed source:||Pfam-B_3770 (release 10.0)|
|Author:||Vella Briffa B|
|Number in seed:||133|
|Number in full:||353|
|Average length of the domain:||192.70 aa|
|Average identity of full alignment:||33 %|
|Average coverage of the sequence by the domain:||72.27 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 11927849 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||9|
|Download:||download the raw HMM for this family|
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There is 1 interaction for this family. More...
We determine these interactions using iPfam, which considers the interactions between residues in three-dimensional protein structures and maps those interactions back to Pfam families. You can find more information about the iPfam algorithm in the journal article that accompanies the website.
For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the Chlor_dismutase domain has been found. There are 112 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.
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