ID   CCPR2_CANAL             Reviewed;         291 AA.
AC   Q59X94; A0A1D8PN10;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2017, sequence version 2.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Putative heme-binding peroxidase;
DE            EC=1.11.1.-;
GN   Name=CCP2; OrderedLocusNames=CAALFM_C500810CA;
GN   ORFNames=CaO19.584, CaO19.8216;
OS   Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=237561;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA   Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA   Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA   Scherer S.;
RT   "The diploid genome sequence of Candida albicans.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA   van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA   Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA   Chibana H., Nantel A., Magee P.T.;
RT   "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT   on the eight chromosomes.";
RL   Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA   Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT   "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT   specific measurements and provides a simple model for repeat and indel
RT   structure.";
RL   Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
CC   -!- FUNCTION: Destroys radicals which are normally produced within the
CC       cells and which are toxic to biological systems. {ECO:0000250}.
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   -!- SIMILARITY: Belongs to the peroxidase family. Cytochrome c peroxidase
CC       subfamily. {ECO:0000305}.
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DR   EMBL; CP017627; AOW29523.1; -; Genomic_DNA.
DR   RefSeq; XP_714211.2; XM_709118.2.
DR   AlphaFoldDB; Q59X94; -.
DR   SMR; Q59X94; -.
DR   STRING; 237561.Q59X94; -.
DR   PeroxiBase; 2345; CalCcP01.
DR   GeneID; 3644127; -.
DR   KEGG; cal:CAALFM_C500810CA; -.
DR   CGD; CAL0000198101; orf19.8216.
DR   VEuPathDB; FungiDB:C5_00810C_A; -.
DR   eggNOG; ENOG502QR1E; Eukaryota.
DR   HOGENOM; CLU_036959_0_1_1; -.
DR   InParanoid; Q59X94; -.
DR   OMA; KMTKNYP; -.
DR   OrthoDB; 1228462at2759; -.
DR   BRENDA; 1.11.1.B10; 1096.
DR   PRO; PR:Q59X94; -.
DR   Proteomes; UP000000559; Chromosome 5.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004601; F:peroxidase activity; IBA:GO_Central.
DR   GO; GO:0034599; P:cellular response to oxidative stress; IBA:GO_Central.
DR   GO; GO:0042744; P:hydrogen peroxide catabolic process; IBA:GO_Central.
DR   GO; GO:0000302; P:response to reactive oxygen species; IBA:GO_Central.
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   PANTHER; PTHR31356; PTHR31356; 1.
DR   Pfam; PF00141; peroxidase; 1.
DR   PRINTS; PR00459; ASPEROXIDASE.
DR   PRINTS; PR00458; PEROXIDASE.
DR   SUPFAM; SSF48113; SSF48113; 1.
DR   PROSITE; PS00436; PEROXIDASE_2; 1.
DR   PROSITE; PS50873; PEROXIDASE_4; 1.
PE   3: Inferred from homology;
KW   Heme; Iron; Metal-binding; Oxidoreductase; Peroxidase; Reference proteome.
FT   CHAIN           1..291
FT                   /note="Putative heme-binding peroxidase"
FT                   /id="PRO_0000055584"
FT   ACT_SITE        61
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00297,
FT                   ECO:0000255|PROSITE-ProRule:PRU10012"
FT   ACT_SITE        201
FT                   /note="Tryptophan radical intermediate"
FT                   /evidence="ECO:0000250"
FT   BINDING         185
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            57
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
SQ   SEQUENCE   291 AA;  32950 MW;  DAD1F4DF2B21040F CRC64;
     MIRSYIRNII LAILSPLLTT PPPLILPPPY EKIIQEITTV LSINNYDDGS LAPIILRLAW
     HCCATYDMTT NTGGSNGATM RFVPEITDEG NYGLDIARAA LEPIKQRYPA ISYADLWTLA
     GKVAIEYMGG PTIIWKSGRV DYTNDRCTPS NGLLPFADKD ANHIRKTFTR LGYNDQQTVA
     LIGAHGVGRC HKRFSGWEGK WTRTPKTFSN QFYVVLLNET WSQGEVPETG KTQYFNADKS
     LIMLNTDMEL IRDKSYLHWV EIYAKDEPKF FHDFSSAFAK LLELGIKRET L