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InterPro: IPR000866 Alkyl hydroperoxide reductase/ Thiol specific antioxidant/ Mal allergen

Protein matchesHelp
UniProtKB
Matches:
8100 proteins
AccessionHelp IPR000866 Alkyl_hydroperoxide_Rdtase
TypeHelp Domain
SignaturesHelp
InterPro RelationshipsHelp
Parent IPR017936 Thioredoxin-like
Found in IPR012335 Thioredoxin fold
IPR013478 Methylamine dehydrogenase accessory protein MauD
IPR017559 Peroxiredoxin
GO Term annotationHelp
Function GO:0016209 antioxidant activity
GO:0016491 oxidoreductase activity
InterPro annotation
BioMart Logo Entry Details in BioMart
AbstractHelp

Peroxiredoxins (Prxs) are a ubiquitous family of antioxidant enzymes that also control cytokine-induced peroxide levels which mediate signal transduction in mammalian cells. Prxs can be regulated by changes to phosphorylation, redox and possibly oligomerisation states. Prxs are divided into three classes: typical 2-Cys Prxs; atypical 2-Cys Prxs; and 1-Cys Prxs. All Prxs share the same basic catalytic mechanism, in which an active-site cysteine (the peroxidatic cysteine) is oxidised to a sulphenic acid by the peroxide substrate. The recycling of the sulphenic acid back to a thiol is what distinguishes the three enzyme classes. Using crystal structures, a detailed catalytic cycle has been derived for typical 2-Cys Prxs, including a model for the redox-regulated oligomeric state proposed to control enzyme activity [1].

Alkyl hydroperoxide reductase (AhpC) is responsible for directly reducing organic hyperoxides in its reduced dithiol form. Thiol specific antioxidant (TSA) is a physiologically important antioxidant which constitutes an enzymatic defence against sulphur-containing radicals. This family contains AhpC and TSA, as well as related proteins.

Some of the proteins in this family are allergens. Allergies are hypersensitivity reactions of the immune system to specific substances called allergens (such as pollen, stings, drugs, or food) that, in most people, result in no symptoms. A nomenclature system has been established for antigens (allergens) that cause IgE-mediated atopic allergies in humans [WHO/IUIS Allergen Nomenclature Subcommittee, King T.P., Hoffmann D., Loewenstein H., Marsh D.G., Platts-Mills T.A.E., Thomas W. Bull. World Health Organ. 72:797-806(1994)]. This nomenclature system is defined by a designation that is composed of the first three letters of the genus; a space; the first letter of the species name; a space and an arabic number. In the event that two species names have identical designations, they are discriminated from one another by adding one or more letters (as necessary) to each species designation.

The allergens in this family include allergens with the following designations: Asp f 3, Mal f 2 and Mal f 3.

Structural linksHelp
PDB - click here
SCOP: c.47.1.10
CATH: 3.40.30.10
Database linksHelp
Enzyme: EC:1.11.1.15
PANDIT: PF00578
Blocks: IPB000866
Pfam Clan: CL0172.13

Taxonomic coverageHelp

Overlapping InterPro entriesHelp
IPR000866 Numbers of overlapping proteins Average numbers of overlapping amino acids

Example proteinsHelp
O08709 Peroxiredoxin-6

P30041 Peroxiredoxin-6

P40553 Peroxiredoxin DOT5

Q21824 Probable peroxiredoxin prdx-3

Q9V3P0 Peroxiredoxin 1

More proteins


Example Proteins Key


InterPro entry accession number/name and structure databases Colour code
IPR017936 Thioredoxin-like
IPR000866 Alkyl hydroperoxide reductase/ Thiol specific antioxidant/ Mal allergen
IPR012335 Thioredoxin fold
IPR019479 Peroxiredoxin, C-terminal
IPR012336 Thioredoxin-like fold
SWISS-MODEL
PDB Chain
ModBase
CATH Domain
SCOP Domain

PublicationsHelp
1. Wood ZA, Schroder E, Robin Harris J, Poole LB.
Structure, mechanism and regulation of peroxiredoxins.
Trends Biochem. Sci. 28 32-40 2003 [PubMed: 12517450]
http://dx.doi.org/10.1016/S0968-0004(02)00003-8

Additional ReadingHelp
Nakamura T, Yamamoto T, Abe M, Matsumura H, Hagihara Y, Goto T, Yamaguchi T, Inoue T.
Oxidation of archaeal peroxiredoxin involves a hypervalent sulfur intermediate.
Proc. Natl. Acad. Sci. U.S.A. 105 2008 6238-42 [PubMed: 18436649]
http://dx.doi.org/10.1073/pnas.0709822105
Jonsson TJ, Johnson LC, Lowther WT.
Structure of the sulphiredoxin-peroxiredoxin complex reveals an essential repair embrace.
Nature 451 2008 98-101 [PubMed: 18172504]
http://dx.doi.org/10.1038/nature06415
Vedadi M, Lew J, Artz J, Amani M, Zhao Y, Dong A, Wasney GA, Gao M, Hills T, Brokx S, Qiu W, Sharma S, Diassiti A, Alam Z, Melone M, Mulichak A, Wernimont A, Bray J, Loppnau P, Plotnikova O, Newberry K, Sundararajan E, Houston S, Walker J, Tempel W, Bochkarev A, Kozieradzki I, Edwards A, Arrowsmith C, Roos D, Kain K, Hui R.
Genome-scale protein expression and structural biology of Plasmodium falciparum and related Apicomplexan organisms.
Mol. Biochem. Parasitol. 151 2007 100-10 [PubMed: 17125854]
http://dx.doi.org/10.1016/j.molbiopara.2006.10.011
Nakamura T, Yamamoto T, Inoue T, Matsumura H, Kobayashi A, Hagihara Y, Uegaki K, Ataka M, Kai Y, Ishikawa K.
Crystal structure of thioredoxin peroxidase from aerobic hyperthermophilic archaeon Aeropyrum pernix K1.
Proteins 62 2006 822-6 [PubMed: 16342268]
http://dx.doi.org/10.1002/prot.20796
Chae HZ, Robison K, Poole LB, Church G, Storz G, Rhee SG.
Cloning and sequencing of thiol-specific antioxidant from mammalian brain: alkyl hydroperoxide reductase and thiol-specific antioxidant define a large family of antioxidant enzymes.
Proc. Natl. Acad. Sci. U.S.A. 91 1994 7017-21 [PubMed: 8041738]
http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=EBI&pubmedid=8041738
Boucher IW, McMillan PJ, Gabrielsen M, Akerman SE, Brannigan JA, Schnick C, Brzozowski AM, Wilkinson AJ, Muller S.
Structural and biochemical characterization of a mitochondrial peroxiredoxin from Plasmodium falciparum.
Mol. Microbiol. 61 2006 948-59 [PubMed: 16879648]
http://dx.doi.org/10.1111/j.1365-2958.2006.05303.x
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InterPro 23.1