ID   CCPR_GIBZE              Reviewed;         358 AA.
AC   Q4ING3;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2005, sequence version 1.
DT   16-JUN-2009, entry version 34.
DE   RecName: Full=Cytochrome c peroxidase, mitochondrial;
DE            Short=CCP;
DE            EC=1.11.1.5;
DE   Flags: Precursor;
GN   Name=CCP1; ORFNames=FG01245;
OS   Gibberella zeae (Fusarium graminearum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Hypocreomycetidae; Hypocreales; Nectriaceae;
OC   Gibberella.
OX   NCBI_TaxID=5518;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PH-1 / NRRL 31084;
RX   PubMed=17823352; DOI=10.1126/science.1143708;
RA   Cuomo C.A., Gueldener U., Xu J.-R., Trail F., Turgeon B.G.,
RA   Di Pietro A., Walton J.D., Ma L.-J., Baker S.E., Rep M., Adam G.,
RA   Antoniw J., Baldwin T., Calvo S.E., Chang Y.-L., DeCaprio D.,
RA   Gale L.R., Gnerre S., Goswami R.S., Hammond-Kosack K., Harris L.J.,
RA   Hilburn K., Kennell J.C., Kroken S., Magnuson J.K., Mannhaupt G.,
RA   Mauceli E.W., Mewes H.-W., Mitterbauer R., Muehlbauer G.,
RA   Muensterkoetter M., Nelson D., O'Donnell K., Ouellet T., Qi W.,
RA   Quesneville H., Roncero M.I.G., Seong K.-Y., Tetko I.V., Urban M.,
RA   Waalwijk C., Ward T.J., Yao J., Birren B.W., Kistler H.C.;
RT   "The Fusarium graminearum genome reveals a link between localized
RT   polymorphism and pathogen specialization.";
RL   Science 317:1400-1402(2007).
CC   -!- FUNCTION: Destroys radicals which are normally produced within the
CC       cells and which are toxic to biological systems (By similarity).
CC   -!- CATALYTIC ACTIVITY: 2 ferrocytochrome c + H(2)O(2) = 2
CC       ferricytochrome c + 2 H(2)O.
CC   -!- COFACTOR: Binds 1 heme B (iron-protoporphyrin IX) group per
CC       subunit (By similarity).
CC   -!- SUBUNIT: Forms a one-to-one complex with cytochrome c (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix (By similarity).
CC   -!- SIMILARITY: Belongs to the peroxidase family. Cytochrome c
CC       peroxidase subfamily.
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DR   EMBL; AACM01000062; EAA68106.1; -; Genomic_DNA.
DR   RefSeq; XP_381421.1; -.
DR   PeroxiBase; 2331; GzCcP02.
DR   GeneID; 2782242; -.
DR   KEGG; fgr:FG01245.1; -.
DR   BRENDA; 1.11.1.5; 74326.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0004130; F:cytochrome-c peroxidase activity; IEA:EC.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR   InterPro; IPR002207; Asc_perxdse.
DR   InterPro; IPR002016; Haem_peroxidase_pln/fun/bac.
DR   InterPro; IPR019794; Peroxidases_AS.
DR   InterPro; IPR019793; Peroxidases_heam-ligand_BS.
DR   Pfam; PF00141; peroxidase; 1.
DR   PRINTS; PR00459; ASPEROXIDASE.
DR   PRINTS; PR00458; PEROXIDASE.
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   Transit peptide.
FT   TRANSIT       1     36       Mitochondrion (Potential).
FT   CHAIN        37    358       Cytochrome c peroxidase, mitochondrial.
FT                                /FTId=PRO_0000045293.
FT   ACT_SITE    116    116       Proton acceptor (By similarity).
FT   ACT_SITE    255    255       Tryptophan radical intermediate (By
FT                                similarity).
FT   METAL       239    239       Iron (heme axial ligand).
FT   SITE        112    112       Transition state stabilizer (By
FT                                similarity).
SQ   SEQUENCE   358 AA;  40024 MW;  0AA34708745F0F01 CRC64;
     MASATRQFAR AATRATRNGF AIAPRQVIRQ QGRRYYSSEP AQKSSSAWIW LTGAAVAGGA
     GYYFYGNSAS SATAKVFNPS KEDYQKVYNE IAARLEEKDD YDDGSYGPVL VRLAWHASGT
     YDKETGTGGS NGATMRFAPE SDHGANAGLA AARDFLQPVK EKFPWITYSD LWILAGVCAI
     QEMLGPAIPY RPGRSDRDVS GCTPDGRLPD ASKRQDHLRG IFGRMGFNDQ EIVALSGAHA
     LGRCHTDRSG YSGPWTFSPT VLTNDYFRLL VEEKWQWKKW NGPAQYEDKS TKSLMMLPSD
     IALIEDKKFK PWVEKYAKDN DAFFKDFSNV VLRLFELGVP FAQGTENQRW TFKPTHQE
//