ID   CCPR_MAGO7              Reviewed;         362 AA.
AC   A4QVH4; G4MS72;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   15-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Cytochrome c peroxidase, mitochondrial;
DE            Short=CCP;
DE            EC=1.11.1.5;
DE   Flags: Precursor;
GN   Name=CCP1; ORFNames=MGG_04545;
OS   Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast
OS   fungus) (Pyricularia oryzae).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Magnaporthales; Pyriculariaceae; Pyricularia.
OX   NCBI_TaxID=242507;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=70-15 / ATCC MYA-4617 / FGSC 8958;
RX   PubMed=15846337; DOI=10.1038/nature03449;
RA   Dean R.A., Talbot N.J., Ebbole D.J., Farman M.L., Mitchell T.K.,
RA   Orbach M.J., Thon M.R., Kulkarni R., Xu J.-R., Pan H., Read N.D.,
RA   Lee Y.-H., Carbone I., Brown D., Oh Y.Y., Donofrio N., Jeong J.S.,
RA   Soanes D.M., Djonovic S., Kolomiets E., Rehmeyer C., Li W., Harding M.,
RA   Kim S., Lebrun M.-H., Bohnert H., Coughlan S., Butler J., Calvo S.E.,
RA   Ma L.-J., Nicol R., Purcell S., Nusbaum C., Galagan J.E., Birren B.W.;
RT   "The genome sequence of the rice blast fungus Magnaporthe grisea.";
RL   Nature 434:980-986(2005).
CC   -!- FUNCTION: Destroys radicals which are normally produced within the
CC       cells and which are toxic to biological systems. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 Fe(II)-[cytochrome c] + 2 H(+) + H2O2 = 2 Fe(III)-
CC         [cytochrome c] + 2 H2O; Xref=Rhea:RHEA:16581, Rhea:RHEA-COMP:10350,
CC         Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16240, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034; EC=1.11.1.5;
CC   -!- COFACTOR:
CC       Name=heme b; Xref=ChEBI:CHEBI:60344;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU00297};
CC       Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
CC       {ECO:0000255|PROSITE-ProRule:PRU00297};
CC   -!- SUBUNIT: Forms a one-to-one complex with cytochrome c. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peroxidase family. Cytochrome c peroxidase
CC       subfamily. {ECO:0000305}.
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DR   EMBL; CM001231; EHA58330.1; -; Genomic_DNA.
DR   RefSeq; XP_003710942.1; XM_003710894.1.
DR   AlphaFoldDB; A4QVH4; -.
DR   SMR; A4QVH4; -.
DR   STRING; 318829.MGG_04545T0; -.
DR   EnsemblFungi; MGG_04545T0; MGG_04545T0; MGG_04545.
DR   GeneID; 2677767; -.
DR   KEGG; mgr:MGG_04545; -.
DR   VEuPathDB; FungiDB:MGG_04545; -.
DR   eggNOG; ENOG502QR1E; Eukaryota.
DR   HOGENOM; CLU_036959_1_1_1; -.
DR   InParanoid; A4QVH4; -.
DR   OMA; NGPKQYE; -.
DR   OrthoDB; 1228462at2759; -.
DR   PHI-base; PHI:5187; -.
DR   Proteomes; UP000009058; Chromosome 1.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0004130; F:cytochrome-c peroxidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0034599; P:cellular response to oxidative stress; IEA:InterPro.
DR   InterPro; IPR044831; Ccp1-like.
DR   InterPro; IPR002016; Haem_peroxidase.
DR   InterPro; IPR010255; Haem_peroxidase_sf.
DR   InterPro; IPR002207; Peroxidase_I.
DR   InterPro; IPR019794; Peroxidases_AS.
DR   InterPro; IPR019793; Peroxidases_heam-ligand_BS.
DR   PANTHER; PTHR31356; PTHR31356; 1.
DR   Pfam; PF00141; peroxidase; 1.
DR   PRINTS; PR00459; ASPEROXIDASE.
DR   PRINTS; PR00458; PEROXIDASE.
DR   SUPFAM; SSF48113; SSF48113; 1.
DR   PROSITE; PS00435; PEROXIDASE_1; 1.
DR   PROSITE; PS00436; PEROXIDASE_2; 1.
DR   PROSITE; PS50873; PEROXIDASE_4; 1.
PE   3: Inferred from homology;
KW   Heme; Iron; Metal-binding; Mitochondrion; Oxidoreductase; Peroxidase;
KW   Reference proteome; Transit peptide.
FT   TRANSIT         1..40
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           41..362
FT                   /note="Cytochrome c peroxidase, mitochondrial"
FT                   /id="PRO_0000363407"
FT   ACT_SITE        121
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00297,
FT                   ECO:0000255|PROSITE-ProRule:PRU10012"
FT   ACT_SITE        260
FT                   /note="Tryptophan radical intermediate"
FT                   /evidence="ECO:0000250"
FT   BINDING         244
FT                   /ligand="heme b"
FT                   /ligand_id="ChEBI:CHEBI:60344"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT   SITE            117
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
SQ   SEQUENCE   362 AA;  39861 MW;  3E51FC022B61220A CRC64;
     MASASRQILR AASRASTRTA FAPAASRGLA ARTIAGRRFY SSSSEPAKAS SSNLGWIAGA
     LAAAAAGAGY WYTQNGGAAT LTKPEFKDYQ TVYNDIASRL EENPDYDDGS YGPVLVRLAW
     HASGTYDKET GTGGSNGATM RFSPEGGHGA NAGLKAARDF LEPIKAKYPW ITYSDLWILG
     GVCAIQEMLG PKIPYRPGRS DKDAAACTPD GRLPDAAQRQ DHVRNIFYRM GFNDQEIVAL
     AGAHALGRCH TDRSGFDGPW TFSPTVLTND YFKLLLNEKW EYKKWDGPKQ YVDSKTKSLM
     MLPADMCLIE DKKFKEWTKK YADDNDLFFK DFSAAVLKLF ELGVPFAEGT ENQRWIFKPT
     SE