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InterPro: IPR017559 Peroxiredoxin

Protein matches Help

UniProtKB

Matches:

690 proteins

Overview:	sorted by AC,	sorted by name,	of known structure,	proteins with splice variants
Detailed:	sorted by AC,	sorted by name,	of known structure	proteins with splice variants
Table:	For all matching proteins,	of known structure
Architectures
Accession List
Matches in BioMart

Accession

IPR017559 Peroxiredoxin

Type

Family

Signatures Help

Database	ID	Name	Proteins
TIGRFAMs	TIGR03137	AhpC	690
Signatures in BioMart

InterPro Relationships Help

Contains

IPR000866 Alkyl hydroperoxide reductase/ Thiol specific antioxidant/ Mal allergen
IPR012335 Thioredoxin fold
IPR017936 Thioredoxin-like
IPR019479 Peroxiredoxin, C-terminal

GO Term annotation Help

Process

GO:0055114 oxidation reduction

Function

GO:0051920 peroxiredoxin activity

InterPro annotation

Entry Details in BioMart

Abstract

This peroxiredoxin (AhpC, alkylhydroperoxide reductase subunit C) is one subunit of a two-subunit complex with subunit F(IPR012081). Usually these are found as an apparent operon. The gene has been characterised in Bacteroides fragilis [1] where it is important in oxidative stress defence. This gene contains two invariant cysteine residues, one near the N terminus and one near the C terminus, each followed immediately by a proline residue.

Structural links Help

PDB - click here

SCOP: c.47.1.10

CATH: 3.40.30.10

Database links Help

Enzyme: EC:1.11.1.15

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR017559

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

P0A251 Alkyl hydroperoxide reductase subunit C

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
IPR017559	Peroxiredoxin
IPR012336	Thioredoxin-like fold
	PDB Chain
	ModBase
	SCOP Domain
	CATH Domain

Publications Open in usermanual
1.	Rocha ER, Smith CJ. Role of the alkyl hydroperoxide reductase (ahpCF) gene in oxidative stress defense of the obligate Anaerobe bacteroides fragilis. J. Bacteriol. 181 5701-10 1999 [PubMed: 10482511] http://ukpmc.ac.uk/articlerender.cgi?tool=EBI&pubmedid=10482511

Additional Reading Open in usermanual
	Kitano K, Kita A, Hakoshima T, Niimura Y, Miki K. Crystal structure of decameric peroxiredoxin (AhpC) from Amphibacillus xylanus. Proteins 59 2005 644-7 [PubMed: 15770647] http://dx.doi.org/10.1002/prot.20412
	Parsonage D, Youngblood DS, Sarma GN, Wood ZA, Karplus PA, Poole LB. Analysis of the link between enzymatic activity and oligomeric state in AhpC, a bacterial peroxiredoxin. Biochemistry 44 2005 10583-92 [PubMed: 16060667] http://dx.doi.org/10.1021/bi050448i
	Kitano K, Niimura Y, Nishiyama Y, Miki K. Stimulation of peroxidase activity by decamerization related to ionic strength: AhpC protein from Amphibacillus xylanus. J. Biochem. 126 1999 313-9 [PubMed: 10423523]
	Wood ZA, Poole LB, Karplus PA. Peroxiredoxin evolution and the regulation of hydrogen peroxide signaling. Science 300 2003 650-3 [PubMed: 12714747] http://dx.doi.org/10.1126/science.1080405

InterPro 23.1