FUNCTION: Involved in redox regulation of the cell. Protects radical-sensitive enzymes from oxidative damage by a radical-generating system (By similarity).
CATALYTIC ACTIVITY: 2 R'-SH + ROOH = R'-S-S-R' + H₂O + ROH.
SUBUNIT: Homodimer; disulfide-linked, upon oxidation (By similarity). Binds MAP3K13 (By similarity).
SUBCELLULAR LOCATION: Mitochondrion (By similarity).
MISCELLANEOUS: The active site is the redox-active Cys-108 oxidized to Cys-SOH. Cys-SOH rapidly reacts with Cys-229-SH of the other subunit to form an intermolecular disulfide with a concomitant homodimer formation. The enzyme may be subsequently regenerated by reduction of the disulfide by thioredoxin (By similarity).
MISCELLANEOUS: Irreversibly inactivated by overoxidation of Cys-108 (to Cys-SO(3)H) upon oxidative stress (By similarity).
SIMILARITY: Belongs to the ahpC/TSA family.
SIMILARITY: Contains 1 thioredoxin domain.

Copyright

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Cross-references

Sequence databases

EMBL

CR857380; CAH89674.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

SMR

Q5REY3; 63-223.

ModBase

Q5REY3.

Protein family/group databases

PeroxiBase

4500; Ppy2CysPrx03.

Ontologies

GO:0051920;	Molecular function: peroxiredoxin activity (inferred from electronic annotation from EC).
QuickGo view.

Family and domain databases

InterPro

IPR000866; AhpC-TSA.
IPR012335; Thioredoxin_fold.
Graphical view of domain structure.

Gene3D

G3DSA:3.40.30.10; Thioredoxin_fold; 1.

Pfam

PF00578; AhpC-TSA; 1.
Pfam graphical view of domain structure.

PROSITE

PS51352; THIOREDOXIN_2; 1.
PROSITE graphical view of domain structure (profiles).

BLOCKS

Q5REY3.

Phylogenomic databases

HOVERGEN

Q5REY3; -.

Other

ProtoNet

Q5REY3.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Antioxidant; Mitochondrion; Oxidoreductase; Peroxidase; Redox-active center; Transit peptide.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`TRANSIT`	`1 62`	`62`	`Mitochondrion (By similarity).`
`CHAIN`	`63 256`	`194`	`Thioredoxin-dependent peroxide reductase, mitochondrial (By similarity).`	`PRO_0000256858`
`DOMAIN`	`63 221`	`159`	`Thioredoxin.`
`ACT_SITE`	`108 108`		`Cysteine sulfenic acid (-SOH) intermediate (By similarity).`
`DISULFID`	`108 108`		`Interchain (with C-229); in linked form (By similarity).`
`DISULFID`	`229 229`		`Interchain (with C-108); in linked form (By similarity).`

Sequence information

Length: 256 AA [This is the length of the unprocessed precursor]

Molecular weight: 27700 Da [This is the MW of the unprocessed precursor]

CRC64: BF425B99C7794406 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAAAVGRLLR ASVARGVSAI PWGISATAAL RPAACGRTSL TNLLCSGSSQ AKLFSTSSSY 

        70         80         90        100        110        120 
HAPAVTQHAP YFKGTAVVNG EFKDLSLDDF KGKYLVLFFY PLDFTFVCPT EIVAFSDKAN 

       130        140        150        160        170        180 
EFHDVNCEVV AVSVDSHFSH LAWINTPRKN GGLGHMNIAL LSDLTKQISR DYGVLLEGSG 

       190        200        210        220        230        240 
LALRGLFIID PNGVIKHLSV NDLPVGRSVE ETLRLVKAFQ YVETHGEVCP ANWTPDSPTI 

       250 
KPNPAASKEY FQKVNQ

Q5REY3 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools