ID   CCPR_USTMA              Reviewed;         398 AA.
AC   Q4PBY6;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   16-JUN-2009, entry version 32.
DE   RecName: Full=Cytochrome c peroxidase, mitochondrial;
DE            Short=CCP;
DE            EC=1.11.1.5;
DE   Flags: Precursor;
GN   Name=CCP1; ORFNames=UM02377;
OS   Ustilago maydis (Smut fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Ustilago.
OX   NCBI_TaxID=5270;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=521;
RX   PubMed=17080091; DOI=10.1038/nature05248;
RA   Kaemper J., Kahmann R., Boelker M., Ma L.-J., Brefort T.,
RA   Saville B.J., Banuett F., Kronstad J.W., Gold S.E., Mueller O.,
RA   Perlin M.H., Woesten H.A.B., de Vries R., Ruiz-Herrera J.,
RA   Reynaga-Pena C.G., Snetselaar K., McCann M., Perez-Martin J.,
RA   Feldbruegge M., Basse C.W., Steinberg G., Ibeas J.I., Holloman W.,
RA   Guzman P., Farman M.L., Stajich J.E., Sentandreu R.,
RA   Gonzalez-Prieto J.M., Kennell J.C., Molina L., Schirawski J.,
RA   Mendoza-Mendoza A., Greilinger D., Muench K., Roessel N., Scherer M.,
RA   Vranes M., Ladendorf O., Vincon V., Fuchs U., Sandrock B., Meng S.,
RA   Ho E.C.H., Cahill M.J., Boyce K.J., Klose J., Klosterman S.J.,
RA   Deelstra H.J., Ortiz-Castellanos L., Li W., Sanchez-Alonso P.,
RA   Schreier P.H., Haeuser-Hahn I., Vaupel M., Koopmann E., Friedrich G.,
RA   Voss H., Schlueter T., Margolis J., Platt D., Swimmer C., Gnirke A.,
RA   Chen F., Vysotskaia V., Mannhaupt G., Gueldener U.,
RA   Muensterkoetter M., Haase D., Oesterheld M., Mewes H.-W.,
RA   Mauceli E.W., DeCaprio D., Wade C.M., Butler J., Young S.K.,
RA   Jaffe D.B., Calvo S.E., Nusbaum C., Galagan J.E., Birren B.W.;
RT   "Insights from the genome of the biotrophic fungal plant pathogen
RT   Ustilago maydis.";
RL   Nature 444:97-101(2006).
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; AACP01000083; EAK83415.1; -; Genomic_DNA.
DR   RefSeq; XP_758524.1; -.
DR   PeroxiBase; 2328; UmCcP02.
DR   GeneID; 3630421; -.
DR   KEGG; uma:UM02377.1; -.
DR   OMA; Q4PBY6; ATMRFAP.
DR   BRENDA; 1.11.1.5; 2320.
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   Complete proteome; Heme; Iron; Metal-binding; Mitochondrion;
KW   Oxidoreductase; Peroxidase; Transit peptide.
FT   TRANSIT       1     34       Mitochondrion (Potential).
FT   CHAIN        35    398       Cytochrome c peroxidase, mitochondrial.
FT                                /FTId=PRO_0000045296.
FT   ACT_SITE    145    145       Proton acceptor (By similarity).
FT   ACT_SITE    284    284       Tryptophan radical intermediate (By
FT                                similarity).
FT   METAL       268    268       Iron (heme axial ligand).
FT   SITE        141    141       Transition state stabilizer (By
FT                                similarity).
SQ   SEQUENCE   398 AA;  43162 MW;  81C9947C2D71B3D3 CRC64;
     MASLRTGLRV AQPLRASARN FATRPSIRSS VRHYSSPAPG SPPPPQPSSS SSTSKVLLTS
     VAIAAAAGGA FLAFGRDDKV SILGVGANGA NKFQGSKGSV GPATTSAHSK ADYQAVYNAI
     AEQLEANPDY DDGSYGPVLV RLAWHASGTY DKNSNTGGSN GATMRFAPES EHGANAGLGA
     ARDFMEKIHQ KFPWITYSDL WTLGGVAAIQ ELGGPKIPWR PGRKDATADK CTPDGRLPDG
     DKGPDHLRYI FYKMGFNDQE IVALSGAHAL GRCHTDRSGF DGPWTFAPTS FTNEYFNLLM
     NEKWNIRKWN GPPQFEDKST KSLMMLMTDM ALVQDPSFKK HVQRYAKSED EFFNDFRSAY
     AKLLELGVPA ENFKAFETKL DGGKPFEFAT SAEQENAN
//