ID   CCPR2_DEBHA             Reviewed;         428 AA.
AC   Q6BIB1;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 3.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Putative heme-binding peroxidase;
DE            EC=1.11.1.-;
GN   OrderedLocusNames=DEHA2G12166g;
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   -!- 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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAG90546.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CR382139; CAG90546.2; ALT_INIT; Genomic_DNA.
DR   RefSeq; XP_462060.2; XM_462060.1.
DR   AlphaFoldDB; Q6BIB1; -.
DR   SMR; Q6BIB1; -.
DR   STRING; 4959.XP_462060.2; -.
DR   PeroxiBase; 2619; DhCcP01.
DR   EnsemblFungi; CAG90546; CAG90546; DEHA2G12166g.
DR   GeneID; 2904971; -.
DR   KEGG; dha:DEHA2G12166g; -.
DR   eggNOG; ENOG502QR1E; Eukaryota.
DR   HOGENOM; CLU_501624_0_0_1; -.
DR   InParanoid; Q6BIB1; -.
DR   OrthoDB; 1228462at2759; -.
DR   Proteomes; UP000000599; Chromosome G.
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; 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   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..428
FT                   /note="Putative heme-binding peroxidase"
FT                   /id="PRO_0000055586"
FT   REGION          1..33
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        188
FT                   /note="Proton acceptor"
FT   ACT_SITE        328
FT                   /note="Tryptophan radical intermediate"
FT                   /evidence="ECO:0000250"
FT   BINDING         312
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            184
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
SQ   SEQUENCE   428 AA;  48399 MW;  52A290AC7B0A3FA9 CRC64;
     MTAIQKPVVA KREAPKAEVN PTVSRSTQTE TIKPTKERTV SVFSPPVFNF AANSFAQSVS
     NEYKHASPKR IKLDNSRVQV PSIVKPKQDK PRPPAIVTKP RVINIEFPNK QKSGFKLLIR
     PKHEPSIKKQ KQGIEVLSTS NTKRITKSIS VDDVEYVEKV KHAIKQVLPK PDYDDGSLGP
     VILRLAWHCC ATYNKFTGNG GSNGSTMRFV PEITDDGNSG LDIARSALEP IKQKFPDITY
     SDLWTLAGKI SIQEMGGPKI PWRCGRVDCI DDRYVPPNGR LPFAYKNANH IRETFGRMGF
     NDRETVSLLG AHGLGRCHKR FSGWEGKWTE NPTSFSNDFY KVLLDEEWSL GTVPETGKEQ
     YYNKDKSLIM LNTDIELIRD PHFLHFVKLY SQHQATFFQD FANAFGKLLE LGIERDSNGN
     VLPKNEFY