CCPR_DEBHA
ID CCPR_DEBHA Reviewed; 360 AA.
AC Q6BKY9;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Cytochrome c peroxidase, mitochondrial;
DE Short=CCP;
DE EC=1.11.1.5;
DE Flags: Precursor;
GN Name=CCP1; OrderedLocusNames=DEHA2F17754g;
OS Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX NCBI_TaxID=284592;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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 {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the peroxidase family. Cytochrome c peroxidase
CC subfamily. {ECO:0000305}.
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DR EMBL; CR382138; CAG89515.1; -; Genomic_DNA.
DR RefSeq; XP_461132.1; XM_461132.1.
DR AlphaFoldDB; Q6BKY9; -.
DR SMR; Q6BKY9; -.
DR STRING; 4959.XP_461132.1; -.
DR PeroxiBase; 3061; DhCcP02.
DR EnsemblFungi; CAG89515; CAG89515; DEHA2F17754g.
DR GeneID; 2904292; -.
DR KEGG; dha:DEHA2F17754g; -.
DR VEuPathDB; FungiDB:DEHA2F17754g; -.
DR eggNOG; ENOG502QR1E; Eukaryota.
DR HOGENOM; CLU_036959_1_1_1; -.
DR InParanoid; Q6BKY9; -.
DR OMA; NGPKQYE; -.
DR OrthoDB; 1228462at2759; -.
DR Proteomes; UP000000599; Chromosome F.
DR GO; GO:0005739; C:mitochondrion; 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 PANTHER; PTHR31356; PTHR31356; 1.
DR Pfam; PF00141; peroxidase; 1.
DR PRINTS; PR00459; ASPEROXIDASE.
DR PRINTS; PR00458; PEROXIDASE.
DR SUPFAM; SSF48113; SSF48113; 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..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..360
FT /note="Cytochrome c peroxidase, mitochondrial"
FT /id="PRO_0000045291"
FT ACT_SITE 118
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT ACT_SITE 258
FT /note="Tryptophan radical intermediate"
FT /evidence="ECO:0000250"
FT BINDING 242
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 SITE 114
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
SQ SEQUENCE 360 AA; 40439 MW; 98033D6DF83F33C0 CRC64;
MSTAAFKRQS VPLSKLFQSY GKNNSQSKYG GYFLATLIGS GILATSYFNN NKNGNTPSNN
HKKLLAGSGI VNTAAIPKGK SIKDYQSLYN EIAEKVRDQD DADDGAGRYG LLTRLAWHTS
GTYKKEDNTG GSYGGTMIYK PESTDGENSG LNHGRDFLQE FKDKYSWLSH GDLWTLGGVV
AVQECGGPKI KWRPGRQDIS DKTRVPENGR LPDASKDADY VKGVFGRMGF NERETVCLIG
AHCLGKCHKE NTNYDGPWGP SFNMFTNDFF VRLLQNWHVK KWDGKKQYED DETNSFMMLP
TDMALKEDSS FLKYVKMYAD DEKLFFSDFA KNFSTLLELG VTFPDSIKPT EFKTLDEQDK
