FUNCTION: Destroys radicals which are normally produced within the cells and which are toxic to biological systems (By similarity).
CATALYTIC ACTIVITY: 2 ferrocytochrome c + H₂O₂ = 2 ferricytochrome c + 2 H₂O.
COFACTOR: Binds 1 heme B (iron-protoporphyrin IX) group per subunit (By similarity).
SUBUNIT: Forms a one-to-one complex with cytochrome c (By similarity).
SUBCELLULAR LOCATION: Mitochondrion matrix (By similarity).
SIMILARITY: Belongs to the peroxidase family. Cytochrome c peroxidase subfamily.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AACQ01000027; EAL01077.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AACQ01000026; EAL01211.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

XP_719937.1; -.
XP_720067.1; -.

3D structure databases

ModBase

Q5AEN1.

Protein family/group databases

PeroxiBase

3406; CalCcP02.

Organism-specific databases

CGD

CAL0003960; CCP1.

Ontologies

GO:0005759;	Cellular component: mitochondrial matrix (inferred from electronic annotation from UniProtKB-SubCell).
GO:0004130;	Molecular function: cytochrome-c peroxidase activity (inferred from electronic annotation from EC).
QuickGo view.

Family and domain databases

InterPro

IPR002207; Asc_perxdse.
IPR002016; Haem_peroxidase_pln/fun/bac.
Graphical view of domain structure.

Pfam

PF00141; peroxidase; 1.
Pfam graphical view of domain structure.

PRINTS

PR00459; ASPEROXIDASE.
PR00458; PEROXIDASE.

PROSITE

PS00435; PEROXIDASE_1; FALSE_NEG.
PS00436; PEROXIDASE_2; FALSE_NEG.
PS50873; PEROXIDASE_4; 1.
PROSITE graphical view of domain structure (profiles).

BLOCKS

Q5AEN1.

Genome annotation databases

GeneID

3638289; -.
3638350; -.

KEGG

cal:CaO19_238; -.
cal:CaO19_7868; -.

Other

ProtoNet

Q5AEN1.

UniRef

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

Keywords

Heme; Iron; Metal-binding; Mitochondrion; Oxidoreductase; Peroxidase; Transit peptide.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`TRANSIT`	`1 ?`		`Mitochondrion (Potential).`
`CHAIN`	`? 366`		`Cytochrome c peroxidase, mitochondrial.`	`PRO_0000045287`
`ACT_SITE`	`123 123`		`Proton acceptor (By similarity).`
`ACT_SITE`	`263 263`		`Tryptophan radical intermediate (By similarity).`
`METAL`	`247 247`		`Iron (heme axial ligand).`
`SITE`	`119 119`	`1`	`Transition state stabilizer (By similarity).`
`VARIANT`	`58 58`	`1`	`E -> G (in allele CaO19.7868).`

Sequence information

Length: 366 AA [This is the length of the unprocessed precursor]

Molecular weight: 40754 Da [This is the MW of the unprocessed precursor]

CRC64: 826D6ED25355E801 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MATFAPHISK ITKSSTKFNY GRIAKTFLGV AGSAAIATYF YNNGNPFNNN NNNNNNNEGS 

        70         80         90        100        110        120 
KNAAKALFGA SAGANVKIAK VPEGKSASDY QKVYNDIATK ISENLEFDEN AGYYGQLLRL 

       130        140        150        160        170        180 
AWHTSGTYDK SDNSGGSYGG TMIFAPEEFD PENAGLQVGR EFLMEFLVKY PWISRGDLWT 

       190        200        210        220        230        240 
LGGVAAVQES GGPKIEWRPG RVDDNTASKV PPNGRLPDAS KDGKYVKDLF ARMGFNERET 

       250        260        270        280        290        300 
VALLGAHVLG RCHKHNSGYD GPWGPSFNQF TNVFYTTLLG DWHVKKWDGK KQYEDDETGE 

       310        320        330        340        350        360 
FMMLPTDMAL KEESYFLKYV KMYADDQDLF FKDFAKAFSK LISNGIKYPA DSKPILFKTL 


DEQDEE

Q5AEN1 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	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