ID CCPR_YEAST Reviewed; 361 AA. AC P00431; D6VXC7; Q6Q5M9; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1994, sequence version 2. DT 27-MAR-2024, entry version 229. DE RecName: Full=Cytochrome c peroxidase, mitochondrial; DE Short=CCP; DE EC=1.11.1.5; DE Flags: Precursor; GN Name=CCP1; Synonyms=CCP, CPO; OrderedLocusNames=YKR066C; OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=559292; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=6294090; DOI=10.1016/s0021-9258(18)33392-1; RA Kaput J., Goltz S., Blobel G.; RT "Nucleotide sequence of the yeast nuclear gene for cytochrome c peroxidase RT precursor. Functional implications of the pre sequence for protein RT transport into mitochondria."; RL J. Biol. Chem. 257:15054-15058(1982). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=DBY939; RA Piattoni M., Miyazaki W., Jayaraman K., Kaput J.; RT "Isolation and sequence analysis of a second allele of the yeast nuclear RT gene cytochrome C peroxidase."; RL Submitted (OCT-1991) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=8196765; DOI=10.1038/369371a0; RA Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V., RA Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P., RA Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L., RA Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A., RA Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H., RA Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L., RA Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M., RA Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H., RA Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J., RA Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H., RA Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J., RA Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S., RA Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F., RA Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R., RA Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W., RA Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M., RA Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C., RA Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H., RA Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L., RA van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S., RA von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M., RA Becker I., Mewes H.-W.; RT "Complete DNA sequence of yeast chromosome XI."; RL Nature 369:371-378(1994). RN [4] RP GENOME REANNOTATION. RC STRAIN=ATCC 204508 / S288c; RX PubMed=24374639; DOI=10.1534/g3.113.008995; RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.; RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now."; RL G3 (Bethesda) 4:389-398(2014). RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=17322287; DOI=10.1101/gr.6037607; RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J., RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., RA LaBaer J.; RT "Approaching a complete repository of sequence-verified protein-encoding RT clones for Saccharomyces cerevisiae."; RL Genome Res. 17:536-543(2007). RN [6] RP PROTEIN SEQUENCE OF 68-361. RX PubMed=6257176; DOI=10.1016/0003-9861(80)90219-2; RA Takio K., Titani K., Ericsson L.H., Yonetani T.; RT "Primary structure of yeast cytochrome c peroxidase. II. The complete amino RT acid sequence."; RL Arch. Biochem. Biophys. 203:615-629(1980). RN [7] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 253-332. RX PubMed=6286684; DOI=10.1016/s0021-9258(18)33950-4; RA Goltz S., Kaput J., Blobel G.; RT "Isolation of the yeast nuclear gene encoding the mitochondrial protein, RT cytochrome c peroxidase."; RL J. Biol. Chem. 257:11186-11190(1982). RN [8] RP MUTAGENESIS OF TRP-258. RX PubMed=2851317; DOI=10.1021/bi00417a008; RA Mauro J.M., Fishel L.A., Hazzard J.T., Meyer T.E., Tollin G., RA Cusanovich M.A., Kraut J.; RT "Tryptophan-191-->phenylalanine, a proximal-side mutation in yeast RT cytochrome c peroxidase that strongly affects the kinetics of RT ferrocytochrome c oxidation."; RL Biochemistry 27:6243-6256(1988). RN [9] RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]. RX PubMed=14562106; DOI=10.1038/nature02046; RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., RA O'Shea E.K., Weissman J.S.; RT "Global analysis of protein expression in yeast."; RL Nature 425:737-741(2003). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-220, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200; RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.; RT "A multidimensional chromatography technology for in-depth phosphoproteome RT analysis."; RL Mol. Cell. Proteomics 7:1389-1396(2008). RN [11] RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE RP ANALYSIS]. RX PubMed=22984289; DOI=10.1074/mcp.m112.021105; RA Voegtle F.N., Burkhart J.M., Rao S., Gerbeth C., Hinrichs J., RA Martinou J.C., Chacinska A., Sickmann A., Zahedi R.P., Meisinger C.; RT "Intermembrane space proteome of yeast mitochondria."; RL Mol. Cell. Proteomics 11:1840-1852(2012). RN [12] RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS). RX PubMed=6092361; DOI=10.1016/s0021-9258(18)90651-4; RA Finzel B.C., Poulos T.L., Kraut J.; RT "Crystal structure of yeast cytochrome c peroxidase refined at 1.7-A RT resolution."; RL J. Biol. Chem. 259:13027-13036(1984). RN [13] RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF MUTANTS. RX PubMed=2169873; DOI=10.1021/bi00483a003; RA Wang J.M., Mauro M., Edwards S.L., Oatley S.J., Fishel L.A., Ashford V.A., RA Xuong N.-H., Kraut J.; RT "X-ray structures of recombinant yeast cytochrome c peroxidase and three RT heme-cleft mutants prepared by site-directed mutagenesis."; RL Biochemistry 29:7160-7173(1990). RN [14] RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS). RX PubMed=8384877; DOI=10.1021/bi00064a014; RA Goodin D.B., McRee D.E.; RT "The Asp-His-Fe triad of cytochrome c peroxidase controls the reduction RT potential, electronic structure, and coupling of the tryptophan free RT radical to the heme."; RL Biochemistry 32:3313-3324(1993). RN [15] RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS). RX PubMed=8673607; DOI=10.1038/nsb0796-626; RA Fitzgerald M.M., Musah R.A., McRee D.E., Goodin D.B.; RT "A ligand-gated, hinged loop rearrangement opens a channel to a buried RT artificial protein cavity."; RL Nat. Struct. Biol. 3:626-631(1996). RN [16] RP X-RAY CRYSTALLOGRAPHY (1.93 ANGSTROMS). RX PubMed=10722697; DOI=10.1074/jbc.275.12.8582; RA Hirst J., Goodin D.B.; RT "Unusual oxidative chemistry of N(omega)-hydroxyarginine and N- RT hydroxyguanidine catalyzed at an engineered cavity in a heme peroxidase."; RL J. Biol. Chem. 275:8582-8591(2000). RN [17] RP X-RAY CRYSTALLOGRAPHY (2.56 ANGSTROMS). RX PubMed=11170452; DOI=10.1021/bi002089r; RA Hirst J., Wilcox S.K., Williams P.A., Blankenship J., McRee D.E., RA Goodin D.B.; RT "Replacement of the axial histidine ligand with imidazole in cytochrome c RT peroxidase. 1. Effects on structure."; RL Biochemistry 40:1265-1273(2001). CC -!- FUNCTION: Destroys radicals which are normally produced within the CC cells and which are toxic to biological systems. 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 Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.; CC -!- SUBUNIT: Forms a one-to-one complex with cytochrome c. CC -!- INTERACTION: CC P00431; P00044: CYC1; NbExp=4; IntAct=EBI-4389, EBI-5393; CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix. Mitochondrion intermembrane CC space {ECO:0000269|PubMed:22984289}. CC -!- MISCELLANEOUS: Present with 6730 molecules/cell in log phase SD medium. CC {ECO:0000269|PubMed:14562106}. CC -!- SIMILARITY: Belongs to the peroxidase family. Cytochrome c peroxidase CC subfamily. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; J01468; AAA88709.1; -; Genomic_DNA. DR EMBL; X62422; CAA44288.1; -; Genomic_DNA. DR EMBL; Z28291; CAA82145.1; -; Genomic_DNA. DR EMBL; AY557921; AAS56247.1; -; Genomic_DNA. DR EMBL; J01321; AAA88710.1; -; Genomic_DNA. DR EMBL; BK006944; DAA09217.1; -; Genomic_DNA. DR PIR; S19064; OPBYC. DR RefSeq; NP_012992.1; NM_001179856.1. DR PDB; 1A2F; X-ray; 2.10 A; A=71-361. DR PDB; 1A2G; X-ray; 2.10 A; A=71-361. DR PDB; 1AA4; X-ray; 2.10 A; A=71-361. DR PDB; 1AC4; X-ray; 2.10 A; A=71-361. DR PDB; 1AC8; X-ray; 2.10 A; A=71-361. DR PDB; 1AEB; X-ray; 2.10 A; A=71-361. DR PDB; 1AED; X-ray; 2.10 A; A=71-361. DR PDB; 1AEE; X-ray; 2.10 A; A=71-361. DR PDB; 1AEF; X-ray; 2.10 A; A=71-361. DR PDB; 1AEG; X-ray; 2.10 A; A=71-361. DR PDB; 1AEH; X-ray; 2.10 A; A=71-361. DR PDB; 1AEJ; X-ray; 2.10 A; A=71-361. DR PDB; 1AEK; X-ray; 2.10 A; A=71-361. DR PDB; 1AEM; X-ray; 2.10 A; A=71-361. DR PDB; 1AEN; X-ray; 2.10 A; A=71-361. DR PDB; 1AEO; X-ray; 2.10 A; A=71-361. DR PDB; 1AEQ; X-ray; 2.10 A; A=71-361. DR PDB; 1AES; X-ray; 2.10 A; A=71-361. DR PDB; 1AET; X-ray; 2.10 A; A=71-361. DR PDB; 1AEU; X-ray; 2.10 A; A=71-361. DR PDB; 1AEV; X-ray; 2.10 A; A=71-361. DR PDB; 1BEJ; X-ray; 2.40 A; A=71-361. DR PDB; 1BEK; X-ray; 2.20 A; A=71-361. DR PDB; 1BEM; X-ray; 2.20 A; A=71-361. DR PDB; 1BEP; X-ray; 2.20 A; A=71-361. DR PDB; 1BEQ; X-ray; 2.16 A; A=71-361. DR PDB; 1BES; X-ray; 2.00 A; A=71-361. DR PDB; 1BJ9; X-ray; 2.20 A; A=71-361. DR PDB; 1BVA; X-ray; 1.89 A; A=71-361. DR PDB; 1CCA; X-ray; 1.80 A; A=68-361. DR PDB; 1CCB; X-ray; 2.10 A; A=68-361. DR PDB; 1CCC; X-ray; 2.00 A; A=68-361. DR PDB; 1CCE; X-ray; 2.30 A; A=71-361. DR PDB; 1CCG; X-ray; 2.10 A; A=71-361. DR PDB; 1CCI; X-ray; 2.40 A; A=71-361. DR PDB; 1CCJ; X-ray; 2.10 A; A=71-361. DR PDB; 1CCK; X-ray; 2.10 A; A=71-361. DR PDB; 1CCL; X-ray; 2.00 A; A=71-361. DR PDB; 1CCP; X-ray; 2.20 A; A=68-361. DR PDB; 1CMP; X-ray; 1.90 A; A=71-361. DR PDB; 1CMQ; X-ray; 2.30 A; A=71-361. DR PDB; 1CMT; X-ray; 2.10 A; A=71-361. DR PDB; 1CMU; X-ray; 2.10 A; A=71-361. DR PDB; 1CPD; X-ray; 2.20 A; A=68-361. DR PDB; 1CPE; X-ray; 2.20 A; A=68-361. DR PDB; 1CPF; X-ray; 2.20 A; A=68-361. DR PDB; 1CPG; X-ray; 2.20 A; A=71-361. DR PDB; 1CYF; X-ray; 2.35 A; A=68-361. DR PDB; 1DCC; X-ray; 2.20 A; A=68-361. DR PDB; 1DJ1; X-ray; 1.93 A; A=71-361. DR PDB; 1DJ5; X-ray; 1.93 A; A=71-361. DR PDB; 1DS4; X-ray; 2.02 A; A=71-361. DR PDB; 1DSE; X-ray; 2.00 A; A=71-361. DR PDB; 1DSG; X-ray; 2.56 A; A=71-361. DR PDB; 1DSO; X-ray; 2.03 A; A=71-361. DR PDB; 1DSP; X-ray; 2.03 A; A=71-361. DR PDB; 1EBE; X-ray; 2.20 A; A=68-361. DR PDB; 1JCI; X-ray; 1.90 A; A=68-361. DR PDB; 1JDR; X-ray; 1.50 A; A=68-361. DR PDB; 1KOK; X-ray; 1.70 A; A=68-361. DR PDB; 1KRJ; X-ray; 2.00 A; A=68-361. DR PDB; 1KXM; X-ray; 1.74 A; A=71-361. DR PDB; 1KXN; X-ray; 1.80 A; A=71-361. DR PDB; 1MK8; X-ray; 1.65 A; A=68-361. DR PDB; 1MKQ; X-ray; 1.64 A; A=68-361. DR PDB; 1MKR; X-ray; 1.58 A; A=68-361. DR PDB; 1ML2; X-ray; 1.65 A; A=68-361. DR PDB; 1RYC; X-ray; 1.80 A; A=71-361. DR PDB; 1S6V; X-ray; 1.88 A; A/C=68-361. DR PDB; 1S73; X-ray; 1.53 A; A=68-361. DR PDB; 1SBM; X-ray; 1.69 A; A=68-361. DR PDB; 1SDQ; X-ray; 1.69 A; A=68-361. DR PDB; 1SOG; X-ray; 1.85 A; A=68-361. DR PDB; 1STQ; X-ray; 1.82 A; A=68-361. DR PDB; 1U74; X-ray; 2.40 A; A/C=68-361. DR PDB; 1U75; X-ray; 2.55 A; A/C=68-361. DR PDB; 1Z53; X-ray; 1.13 A; A=68-361. DR PDB; 1ZBY; X-ray; 1.20 A; A=68-361. DR PDB; 1ZBZ; X-ray; 1.29 A; A=68-361. DR PDB; 2ANZ; X-ray; 1.75 A; A=71-361. DR PDB; 2AQD; X-ray; 1.35 A; A=71-361. DR PDB; 2AS1; X-ray; 1.55 A; A=71-361. DR PDB; 2AS2; X-ray; 1.45 A; A=71-361. DR PDB; 2AS3; X-ray; 1.40 A; A=71-361. DR PDB; 2AS4; X-ray; 1.30 A; A=71-361. DR PDB; 2AS6; X-ray; 1.45 A; A=71-361. DR PDB; 2B0Z; X-ray; 2.70 A; A=68-361. DR PDB; 2B10; X-ray; 2.80 A; A/C=68-361. DR PDB; 2B11; X-ray; 2.30 A; A/C=68-361. DR PDB; 2B12; X-ray; 3.02 A; A=68-361. DR PDB; 2BCN; X-ray; 1.70 A; A/C=68-361. DR PDB; 2CCP; X-ray; 2.20 A; A=68-361. DR PDB; 2CEP; X-ray; 2.20 A; A=68-361. DR PDB; 2CYP; X-ray; 1.70 A; A=68-361. DR PDB; 2EUN; X-ray; 1.70 A; A=71-361. DR PDB; 2EUO; X-ray; 1.45 A; A=71-361. DR PDB; 2EUP; X-ray; 1.40 A; A=71-361. DR PDB; 2EUQ; X-ray; 1.30 A; A=71-361. DR PDB; 2EUR; X-ray; 1.39 A; A=71-361. DR PDB; 2EUS; X-ray; 1.55 A; A=71-361. DR PDB; 2EUT; X-ray; 1.12 A; A=71-361. DR PDB; 2EUU; X-ray; 1.45 A; A=71-361. DR PDB; 2GB8; NMR; -; A=68-361. DR PDB; 2IA8; X-ray; 1.48 A; A=71-361. DR PDB; 2ICV; X-ray; 1.60 A; A=71-361. DR PDB; 2JTI; NMR; -; A=68-361. DR PDB; 2N18; NMR; -; A=68-361. DR PDB; 2PCB; X-ray; 2.80 A; A/C=68-361. DR PDB; 2PCC; X-ray; 2.30 A; A/C=68-361. DR PDB; 2RBT; X-ray; 1.24 A; X=71-361. DR PDB; 2RBU; X-ray; 1.80 A; X=71-361. DR PDB; 2RBV; X-ray; 1.39 A; X=71-361. DR PDB; 2RBW; X-ray; 1.50 A; X=71-361. DR PDB; 2RBX; X-ray; 1.50 A; X=71-361. DR PDB; 2RBY; X-ray; 1.50 A; X=71-361. DR PDB; 2RBZ; X-ray; 1.80 A; X=71-361. DR PDB; 2RC0; X-ray; 1.50 A; X=71-361. DR PDB; 2RC1; X-ray; 2.49 A; X=71-361. DR PDB; 2RC2; X-ray; 1.50 A; X=71-361. DR PDB; 2V23; X-ray; 1.80 A; A=68-361. DR PDB; 2V2E; X-ray; 1.68 A; A=71-361. DR PDB; 2X07; X-ray; 1.86 A; A=69-361. DR PDB; 2X08; X-ray; 2.01 A; A=69-361. DR PDB; 2XIL; X-ray; 1.68 A; A=71-361. DR PDB; 2XJ5; X-ray; 1.69 A; A=71-361. DR PDB; 2XJ8; X-ray; 1.69 A; A=71-361. DR PDB; 2Y5A; X-ray; 1.25 A; A=71-361. DR PDB; 2YCG; X-ray; 1.81 A; A=68-361. DR PDB; 3CCP; X-ray; 2.20 A; A=68-361. DR PDB; 3CCX; X-ray; 2.30 A; A=71-361. DR PDB; 3E2N; X-ray; 1.30 A; A=68-96, A=110-361. DR PDB; 3E2O; X-ray; 1.06 A; A=68-361. DR PDB; 3EXB; X-ray; 1.60 A; A=68-361. DR PDB; 3M23; X-ray; 1.40 A; A=71-361. DR PDB; 3M25; X-ray; 1.40 A; A=71-361. DR PDB; 3M26; X-ray; 1.40 A; A=71-361. DR PDB; 3M27; X-ray; 1.40 A; A=71-361. DR PDB; 3M28; X-ray; 1.40 A; A=71-361. DR PDB; 3M29; X-ray; 1.40 A; A=71-361. DR PDB; 3M2A; X-ray; 1.40 A; A=71-361. DR PDB; 3M2B; X-ray; 1.40 A; A=71-361. DR PDB; 3M2C; X-ray; 1.40 A; A=71-361. DR PDB; 3M2D; X-ray; 1.40 A; A=71-361. DR PDB; 3M2E; X-ray; 1.40 A; A=71-361. DR PDB; 3M2F; X-ray; 1.40 A; A=71-361. DR PDB; 3M2G; X-ray; 1.40 A; A=71-361. DR PDB; 3M2H; X-ray; 1.40 A; A=71-361. DR PDB; 3M2I; X-ray; 1.40 A; A=71-361. DR PDB; 3R98; Other; 2.40 A; A=69-361. DR PDB; 3R99; Other; 2.40 A; A=69-361. DR PDB; 4A6Z; X-ray; 1.61 A; A=68-361. DR PDB; 4A71; X-ray; 1.61 A; A=68-361. DR PDB; 4A78; X-ray; 2.01 A; A=68-361. DR PDB; 4A7M; X-ray; 1.71 A; A=68-361. DR PDB; 4CCP; X-ray; 2.20 A; A=68-361. DR PDB; 4CCX; X-ray; 1.90 A; A=71-361. DR PDB; 4CVI; Other; 2.10 A; A=70-361. DR PDB; 4CVJ; Other; 2.18 A; A=71-361. DR PDB; 4JB4; X-ray; 2.39 A; A/C=68-361. DR PDB; 4NFG; X-ray; 2.11 A; A=71-361. DR PDB; 4P4Q; X-ray; 2.01 A; A/C=68-361. DR PDB; 4XV4; X-ray; 1.69 A; A=71-361. DR PDB; 4XV5; X-ray; 1.65 A; A=71-361. DR PDB; 4XV6; X-ray; 1.55 A; A=71-361. DR PDB; 4XV7; X-ray; 1.62 A; A=71-361. DR PDB; 4XV8; X-ray; 1.57 A; A=71-361. DR PDB; 4XVA; X-ray; 2.66 A; A/C/E/G=69-361. DR PDB; 5CCP; X-ray; 2.20 A; A=68-361. DR PDB; 5CIB; X-ray; 3.01 A; A/C=68-361. DR PDB; 5CIC; X-ray; 2.10 A; A/C=68-361. DR PDB; 5CID; X-ray; 2.76 A; A/C=68-361. DR PDB; 5CIE; X-ray; 2.60 A; A/C=68-361. DR PDB; 5CIF; X-ray; 2.01 A; A/C=68-361. DR PDB; 5CIG; X-ray; 2.06 A; A/C=68-361. DR PDB; 5CIH; X-ray; 2.60 A; A/C=68-361. DR PDB; 5D6M; X-ray; 1.65 A; A=71-361. DR PDB; 5EJT; X-ray; 1.55 A; A=68-361. DR PDB; 5EJX; X-ray; 1.50 A; A=68-361. DR PDB; 6CCP; X-ray; 2.20 A; A=68-361. DR PDB; 6H08; X-ray; 1.90 A; A/B/C=71-361. DR PDB; 6P41; X-ray; 2.90 A; A/C=68-361. DR PDB; 6P42; X-ray; 2.90 A; A/C=68-361. DR PDB; 6P43; X-ray; 1.91 A; A/C=68-361. DR PDB; 6Y1T; X-ray; 1.50 A; A=71-361. DR PDB; 6Y2Y; X-ray; 1.70 A; A=71-361. DR PDB; 7BIU; X-ray; 1.06 A; A=70-361. DR PDB; 7CCP; X-ray; 2.20 A; A=68-361. DR PDBsum; 1A2F; -. DR PDBsum; 1A2G; -. DR PDBsum; 1AA4; -. DR PDBsum; 1AC4; -. DR PDBsum; 1AC8; -. DR PDBsum; 1AEB; -. DR PDBsum; 1AED; -. DR PDBsum; 1AEE; -. DR PDBsum; 1AEF; -. DR PDBsum; 1AEG; -. DR PDBsum; 1AEH; -. DR PDBsum; 1AEJ; -. DR PDBsum; 1AEK; -. DR PDBsum; 1AEM; -. DR PDBsum; 1AEN; -. DR PDBsum; 1AEO; -. DR PDBsum; 1AEQ; -. DR PDBsum; 1AES; -. DR PDBsum; 1AET; -. DR PDBsum; 1AEU; -. DR PDBsum; 1AEV; -. DR PDBsum; 1BEJ; -. DR PDBsum; 1BEK; -. DR PDBsum; 1BEM; -. DR PDBsum; 1BEP; -. DR PDBsum; 1BEQ; -. DR PDBsum; 1BES; -. DR PDBsum; 1BJ9; -. DR PDBsum; 1BVA; -. DR PDBsum; 1CCA; -. DR PDBsum; 1CCB; -. DR PDBsum; 1CCC; -. DR PDBsum; 1CCE; -. DR PDBsum; 1CCG; -. DR PDBsum; 1CCI; -. DR PDBsum; 1CCJ; -. DR PDBsum; 1CCK; -. DR PDBsum; 1CCL; -. DR PDBsum; 1CCP; -. DR PDBsum; 1CMP; -. DR PDBsum; 1CMQ; -. DR PDBsum; 1CMT; -. DR PDBsum; 1CMU; -. DR PDBsum; 1CPD; -. DR PDBsum; 1CPE; -. DR PDBsum; 1CPF; -. DR PDBsum; 1CPG; -. DR PDBsum; 1CYF; -. DR PDBsum; 1DCC; -. DR PDBsum; 1DJ1; -. DR PDBsum; 1DJ5; -. DR PDBsum; 1DS4; -. DR PDBsum; 1DSE; -. DR PDBsum; 1DSG; -. DR PDBsum; 1DSO; -. DR PDBsum; 1DSP; -. DR PDBsum; 1EBE; -. DR PDBsum; 1JCI; -. DR PDBsum; 1JDR; -. DR PDBsum; 1KOK; -. DR PDBsum; 1KRJ; -. DR PDBsum; 1KXM; -. DR PDBsum; 1KXN; -. DR PDBsum; 1MK8; -. DR PDBsum; 1MKQ; -. DR PDBsum; 1MKR; -. DR PDBsum; 1ML2; -. DR PDBsum; 1RYC; -. DR PDBsum; 1S6V; -. DR PDBsum; 1S73; -. DR PDBsum; 1SBM; -. DR PDBsum; 1SDQ; -. DR PDBsum; 1SOG; -. DR PDBsum; 1STQ; -. DR PDBsum; 1U74; -. DR PDBsum; 1U75; -. DR PDBsum; 1Z53; -. DR PDBsum; 1ZBY; -. DR PDBsum; 1ZBZ; -. DR PDBsum; 2ANZ; -. DR PDBsum; 2AQD; -. DR PDBsum; 2AS1; -. DR PDBsum; 2AS2; -. DR PDBsum; 2AS3; -. DR PDBsum; 2AS4; -. DR PDBsum; 2AS6; -. DR PDBsum; 2B0Z; -. DR PDBsum; 2B10; -. DR PDBsum; 2B11; -. DR PDBsum; 2B12; -. DR PDBsum; 2BCN; -. DR PDBsum; 2CCP; -. DR PDBsum; 2CEP; -. DR PDBsum; 2CYP; -. DR PDBsum; 2EUN; -. DR PDBsum; 2EUO; -. DR PDBsum; 2EUP; -. DR PDBsum; 2EUQ; -. DR PDBsum; 2EUR; -. DR PDBsum; 2EUS; -. DR PDBsum; 2EUT; -. DR PDBsum; 2EUU; -. DR PDBsum; 2GB8; -. DR PDBsum; 2IA8; -. DR PDBsum; 2ICV; -. DR PDBsum; 2JTI; -. DR PDBsum; 2N18; -. DR PDBsum; 2PCB; -. DR PDBsum; 2PCC; -. DR PDBsum; 2RBT; -. DR PDBsum; 2RBU; -. DR PDBsum; 2RBV; -. DR PDBsum; 2RBW; -. DR PDBsum; 2RBX; -. DR PDBsum; 2RBY; -. DR PDBsum; 2RBZ; -. DR PDBsum; 2RC0; -. DR PDBsum; 2RC1; -. DR PDBsum; 2RC2; -. DR PDBsum; 2V23; -. DR PDBsum; 2V2E; -. DR PDBsum; 2X07; -. DR PDBsum; 2X08; -. DR PDBsum; 2XIL; -. DR PDBsum; 2XJ5; -. DR PDBsum; 2XJ8; -. DR PDBsum; 2Y5A; -. DR PDBsum; 2YCG; -. DR PDBsum; 3CCP; -. DR PDBsum; 3CCX; -. DR PDBsum; 3E2N; -. DR PDBsum; 3E2O; -. DR PDBsum; 3EXB; -. DR PDBsum; 3M23; -. DR PDBsum; 3M25; -. DR PDBsum; 3M26; -. DR PDBsum; 3M27; -. DR PDBsum; 3M28; -. DR PDBsum; 3M29; -. DR PDBsum; 3M2A; -. DR PDBsum; 3M2B; -. DR PDBsum; 3M2C; -. DR PDBsum; 3M2D; -. DR PDBsum; 3M2E; -. DR PDBsum; 3M2F; -. DR PDBsum; 3M2G; -. DR PDBsum; 3M2H; -. DR PDBsum; 3M2I; -. DR PDBsum; 3R98; -. DR PDBsum; 3R99; -. DR PDBsum; 4A6Z; -. DR PDBsum; 4A71; -. DR PDBsum; 4A78; -. DR PDBsum; 4A7M; -. DR PDBsum; 4CCP; -. DR PDBsum; 4CCX; -. DR PDBsum; 4CVI; -. DR PDBsum; 4CVJ; -. DR PDBsum; 4JB4; -. DR PDBsum; 4NFG; -. DR PDBsum; 4P4Q; -. DR PDBsum; 4XV4; -. DR PDBsum; 4XV5; -. DR PDBsum; 4XV6; -. DR PDBsum; 4XV7; -. DR PDBsum; 4XV8; -. DR PDBsum; 4XVA; -. DR PDBsum; 5CCP; -. DR PDBsum; 5CIB; -. DR PDBsum; 5CIC; -. DR PDBsum; 5CID; -. DR PDBsum; 5CIE; -. DR PDBsum; 5CIF; -. DR PDBsum; 5CIG; -. DR PDBsum; 5CIH; -. DR PDBsum; 5D6M; -. DR PDBsum; 5EJT; -. DR PDBsum; 5EJX; -. DR PDBsum; 6CCP; -. DR PDBsum; 6H08; -. DR PDBsum; 6P41; -. DR PDBsum; 6P42; -. DR PDBsum; 6P43; -. DR PDBsum; 6Y1T; -. DR PDBsum; 6Y2Y; -. DR PDBsum; 7BIU; -. DR PDBsum; 7CCP; -. DR AlphaFoldDB; P00431; -. DR BMRB; P00431; -. DR SMR; P00431; -. DR BioGRID; 34197; 136. DR DIP; DIP-6251N; -. DR IntAct; P00431; 5. DR MINT; P00431; -. DR STRING; 4932.YKR066C; -. DR PeroxiBase; 2361; SceCcP01. DR iPTMnet; P00431; -. DR MaxQB; P00431; -. DR PaxDb; 4932-YKR066C; -. DR PeptideAtlas; P00431; -. DR EnsemblFungi; YKR066C_mRNA; YKR066C; YKR066C. DR GeneID; 853940; -. DR KEGG; sce:YKR066C; -. DR AGR; SGD:S000001774; -. DR SGD; S000001774; CCP1. DR VEuPathDB; FungiDB:YKR066C; -. DR eggNOG; ENOG502QR1E; Eukaryota. DR HOGENOM; CLU_036959_1_1_1; -. DR InParanoid; P00431; -. DR OMA; QRKWNGP; -. DR OrthoDB; 168803at2759; -. DR BioCyc; YEAST:YKR066C-MONOMER; -. DR BRENDA; 1.11.1.5; 984. DR SABIO-RK; P00431; -. DR BioGRID-ORCS; 853940; 7 hits in 10 CRISPR screens. DR EvolutionaryTrace; P00431; -. DR PRO; PR:P00431; -. DR Proteomes; UP000002311; Chromosome XI. DR RNAct; P00431; Protein. DR GO; GO:0005758; C:mitochondrial intermembrane space; IDA:SGD. DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell. DR GO; GO:0005739; C:mitochondrion; HDA:SGD. DR GO; GO:0004130; F:cytochrome-c peroxidase activity; IDA:SGD. 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; IMP:SGD. 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 CDD; cd00691; ascorbate_peroxidase; 1. DR Gene3D; 1.10.520.10; -; 1. DR Gene3D; 1.10.420.10; Peroxidase, domain 2; 1. 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 InterPro; IPR019793; Peroxidases_heam-ligand_BS. DR PANTHER; PTHR31356:SF58; CYTOCHROME C PEROXIDASE, MITOCHONDRIAL; 1. DR PANTHER; PTHR31356; THYLAKOID LUMENAL 29 KDA PROTEIN, CHLOROPLASTIC-RELATED; 1. DR Pfam; PF00141; peroxidase; 1. DR PRINTS; PR00459; ASPEROXIDASE. DR PRINTS; PR00458; PEROXIDASE. DR SUPFAM; SSF48113; Heme-dependent peroxidases; 1. DR PROSITE; PS00435; PEROXIDASE_1; 1. DR PROSITE; PS00436; PEROXIDASE_2; 1. DR PROSITE; PS50873; PEROXIDASE_4; 1. PE 1: Evidence at protein level; KW 3D-structure; Direct protein sequencing; Heme; Hydrogen peroxide; Iron; KW Metal-binding; Mitochondrion; Organic radical; Oxidoreductase; Peroxidase; KW Phosphoprotein; Reference proteome; Transit peptide. FT TRANSIT 1..67 FT /note="Mitochondrion" FT /evidence="ECO:0000269|PubMed:6257176" FT CHAIN 68..361 FT /note="Cytochrome c peroxidase, mitochondrial" FT /id="PRO_0000023634" FT ACT_SITE 119 FT /note="Proton acceptor" FT ACT_SITE 258 FT /note="Tryptophan radical intermediate" 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 115 FT /note="Transition state stabilizer" FT MOD_RES 220 FT /note="Phosphotyrosine" FT /evidence="ECO:0007744|PubMed:18407956" FT VARIANT 33 FT /note="A -> AA (in allele 2)" FT VARIANT 120 FT /note="T -> I (in allele 2)" FT VARIANT 219 FT /note="D -> G (in allele 2)" FT MUTAGEN 258 FT /note="W->F: Substantially diminished activity." FT /evidence="ECO:0000269|PubMed:2851317" FT CONFLICT 41 FT /note="Q -> H (in Ref. 3; AAA88709)" FT /evidence="ECO:0000305" FT CONFLICT 62 FT /note="A -> P (in Ref. 3; AAA88709)" FT /evidence="ECO:0000305" FT CONFLICT 145..146 FT /note="ND -> DN (in Ref. 6; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 231 FT /note="Missing (in Ref. 6; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 273 FT /note="L -> M (in Ref. 5; AAS56247)" FT /evidence="ECO:0000305" FT HELIX 83..99 FT /evidence="ECO:0007829|PDB:3E2O" FT TURN 100..102 FT /evidence="ECO:0007829|PDB:2IA8" FT HELIX 103..106 FT /evidence="ECO:0007829|PDB:3E2O" FT HELIX 110..121 FT /evidence="ECO:0007829|PDB:3E2O" FT TURN 126..128 FT /evidence="ECO:0007829|PDB:3E2O" FT STRAND 131..133 FT /evidence="ECO:0007829|PDB:3E2O" FT HELIX 137..139 FT /evidence="ECO:0007829|PDB:3E2O" FT HELIX 141..144 FT /evidence="ECO:0007829|PDB:3E2O" FT HELIX 147..149 FT /evidence="ECO:0007829|PDB:3E2O" FT TURN 150..152 FT /evidence="ECO:0007829|PDB:3E2O" FT HELIX 153..165 FT /evidence="ECO:0007829|PDB:3E2O" FT STRAND 167..169 FT /evidence="ECO:0007829|PDB:2B0Z" FT HELIX 171..185 FT /evidence="ECO:0007829|PDB:3E2O" FT HELIX 202..204 FT /evidence="ECO:0007829|PDB:3E2O" FT TURN 208..210 FT /evidence="ECO:0007829|PDB:1MKR" FT HELIX 218..226 FT /evidence="ECO:0007829|PDB:3E2O" FT TURN 227..229 FT /evidence="ECO:0007829|PDB:3E2O" FT HELIX 232..239 FT /evidence="ECO:0007829|PDB:3E2O" FT HELIX 240..243 FT /evidence="ECO:0007829|PDB:3E2O" FT STRAND 244..247 FT /evidence="ECO:0007829|PDB:3E2O" FT HELIX 249..252 FT /evidence="ECO:0007829|PDB:3E2O" FT STRAND 256..260 FT /evidence="ECO:0007829|PDB:3E2O" FT STRAND 262..264 FT /evidence="ECO:0007829|PDB:3M23" FT HELIX 268..275 FT /evidence="ECO:0007829|PDB:3E2O" FT STRAND 278..282 FT /evidence="ECO:0007829|PDB:3E2O" FT STRAND 284..286 FT /evidence="ECO:0007829|PDB:2PCC" FT STRAND 288..292 FT /evidence="ECO:0007829|PDB:3E2O" FT TURN 293..295 FT /evidence="ECO:0007829|PDB:1CMT" FT STRAND 296..298 FT /evidence="ECO:0007829|PDB:1CMT" FT HELIX 300..307 FT /evidence="ECO:0007829|PDB:3E2O" FT HELIX 309..319 FT /evidence="ECO:0007829|PDB:3E2O" FT HELIX 322..338 FT /evidence="ECO:0007829|PDB:3E2O" FT STRAND 345..347 FT /evidence="ECO:0007829|PDB:2BCN" FT HELIX 356..359 FT /evidence="ECO:0007829|PDB:3E2O" SQ SEQUENCE 361 AA; 40353 MW; A5D26385DA6F0A0B CRC64; MTTAVRLLPS LGRTAHKRSL YLFSAAAAAA AAATFAYSQS QKRSSSSPGG GSNHGWNNWG KAAALASTTP LVHVASVEKG RSYEDFQKVY NAIALKLRED DEYDNYIGYG PVLVRLAWHT SGTWDKHDNT GGSYGGTYRF KKEFNDPSNA GLQNGFKFLE PIHKEFPWIS SGDLFSLGGV TAVQEMQGPK IPWRCGRVDT PEDTTPDNGR LPDADKDADY VRTFFQRLNM NDREVVALMG AHALGKTHLK NSGYEGPWGA ANNVFTNEFY LNLLNEDWKL EKNDANNEQW DSKSGYMMLP TDYSLIQDPK YLSIVKEYAN DQDKFFKDFS KAFEKLLENG ITFPKDAPSP FIFKTLEEQG L //