CCPR_YEAST
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 03-AUG-2022, entry version 221.
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}.
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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; 70.
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; P00431; -.
DR PRIDE; P00431; -.
DR EnsemblFungi; YKR066C_mRNA; YKR066C; YKR066C.
DR GeneID; 853940; -.
DR KEGG; sce:YKR066C; -.
DR SGD; S000001774; CCP1.
DR VEuPathDB; FungiDB:YKR066C; -.
DR eggNOG; ENOG502QR1E; Eukaryota.
DR HOGENOM; CLU_036959_1_1_1; -.
DR InParanoid; P00431; -.
DR OMA; NGPKQYE; -.
DR BioCyc; YEAST:YKR066C-MON; -.
DR BRENDA; 1.11.1.5; 984.
DR SABIO-RK; P00431; -.
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 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; PTHR31356; 1.
DR Pfam; PF00141; peroxidase; 1.
DR PRINTS; PR00459; ASPEROXIDASE.
DR PRINTS; PR00458; PEROXIDASE.
DR SUPFAM; SSF48113; SSF48113; 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
