GenomeNet

Database: UniProt
Entry: P00431
LinkDB: P00431
Original site: P00431 
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   07-APR-2021, entry version 216.
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;
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;
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;
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)cytochrome
CC         c] + 2 H2O; Xref=Rhea:RHEA:16581, Rhea:RHEA-COMP:10350, Rhea:RHEA-
CC         COMP:14399, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16240,
CC         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; 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; 7CCP; -.
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; CAIQEMQ; -.
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; 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   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   METAL           242
FT                   /note="Iron (heme axial ligand)"
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:0007744|PDB:3E2O"
FT   TURN            100..102
FT                   /evidence="ECO:0007744|PDB:2IA8"
FT   HELIX           103..106
FT                   /evidence="ECO:0007744|PDB:3E2O"
FT   HELIX           110..121
FT                   /evidence="ECO:0007744|PDB:3E2O"
FT   TURN            126..128
FT                   /evidence="ECO:0007744|PDB:3E2O"
FT   STRAND          131..133
FT                   /evidence="ECO:0007744|PDB:3E2O"
FT   HELIX           137..139
FT                   /evidence="ECO:0007744|PDB:3E2O"
FT   HELIX           141..144
FT                   /evidence="ECO:0007744|PDB:3E2O"
FT   HELIX           147..149
FT                   /evidence="ECO:0007744|PDB:3E2O"
FT   TURN            150..152
FT                   /evidence="ECO:0007744|PDB:3E2O"
FT   HELIX           153..165
FT                   /evidence="ECO:0007744|PDB:3E2O"
FT   STRAND          167..169
FT                   /evidence="ECO:0007744|PDB:2B0Z"
FT   HELIX           171..185
FT                   /evidence="ECO:0007744|PDB:3E2O"
FT   HELIX           202..204
FT                   /evidence="ECO:0007744|PDB:3E2O"
FT   TURN            208..210
FT                   /evidence="ECO:0007744|PDB:1MKR"
FT   HELIX           218..226
FT                   /evidence="ECO:0007744|PDB:3E2O"
FT   TURN            227..229
FT                   /evidence="ECO:0007744|PDB:3E2O"
FT   HELIX           232..239
FT                   /evidence="ECO:0007744|PDB:3E2O"
FT   HELIX           240..243
FT                   /evidence="ECO:0007744|PDB:3E2O"
FT   STRAND          244..247
FT                   /evidence="ECO:0007744|PDB:3E2O"
FT   HELIX           249..252
FT                   /evidence="ECO:0007744|PDB:3E2O"
FT   STRAND          256..260
FT                   /evidence="ECO:0007744|PDB:3E2O"
FT   STRAND          262..264
FT                   /evidence="ECO:0007744|PDB:3M23"
FT   HELIX           268..275
FT                   /evidence="ECO:0007744|PDB:3E2O"
FT   STRAND          278..282
FT                   /evidence="ECO:0007744|PDB:3E2O"
FT   STRAND          284..286
FT                   /evidence="ECO:0007744|PDB:2PCC"
FT   STRAND          288..292
FT                   /evidence="ECO:0007744|PDB:3E2O"
FT   TURN            293..295
FT                   /evidence="ECO:0007744|PDB:1CMT"
FT   STRAND          296..298
FT                   /evidence="ECO:0007744|PDB:1CMT"
FT   HELIX           300..307
FT                   /evidence="ECO:0007744|PDB:3E2O"
FT   HELIX           309..319
FT                   /evidence="ECO:0007744|PDB:3E2O"
FT   HELIX           322..338
FT                   /evidence="ECO:0007744|PDB:3E2O"
FT   STRAND          345..347
FT                   /evidence="ECO:0007744|PDB:2BCN"
FT   HELIX           356..359
FT                   /evidence="ECO:0007744|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
//
DBGET integrated database retrieval system