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UniProtKB/Swiss-Prot entry P00431


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name CCPR_YEAST
Primary accession number P00431
Secondary accession number Q6Q5M9
Integrated into Swiss-Prot on July 21, 1986
Sequence was last modified on June 1, 1994 (Sequence version 2)
Annotations were last modified on    September 2, 2008 (Entry version 105)
Name and origin of the protein
Protein name Cytochrome c peroxidase, mitochondrial [Precursor]
Synonyms CCP
EC 1.11.1.5
Gene name
Name: CCP1
Synonyms: CCP, CPO
OrderedLocusNames: YKR066C
From
Saccharomyces cerevisiae (Baker's yeast) [TaxID: 4932] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=6294090 [NCBI, ExPASy, EBI, Israel, Japan]
Kaput J., Goltz S., Blobel G.;
"Nucleotide sequence of the yeast nuclear gene for cytochrome c peroxidase precursor. Functional implications of the pre sequence for protein transport into mitochondria.";
J. Biol. Chem. 257:15054-15058(1982).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=DBY939;
Piattoni M., Miyazaki W., Jayaraman K., Kaput J.;
"Isolation and sequence analysis of a second allele of the yeast nuclear gene cytochrome C peroxidase.";
Submitted (OCT-1991) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
DOI=10.1038/369371a0; PubMed=8196765 [NCBI, ExPASy, EBI, Israel, Japan]
Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V., Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P., Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L., Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A., Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H., Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L., Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M., Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H., Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J., Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H., Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J., Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S., Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F., Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R., Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W., Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M., Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C., Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H., Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L., van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S., von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M., Becker I., Mewes H.-W.;
"Complete DNA sequence of yeast chromosome XI.";
Nature 369:371-378(1994).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
DOI=10.1101/gr.6037607; PubMed=17322287 [NCBI, ExPASy, EBI, Israel, Japan]
Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J., Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J.;
"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae.";
Genome Res. 17:536-543(2007).
[5]
PROTEIN SEQUENCE OF 68-361.
DOI=10.1016/0003-9861(80)90219-2; PubMed=6257176 [NCBI, ExPASy, EBI, Israel, Japan]
Takio K., Titani K., Ericsson L.H., Yonetani T.;
"Primary structure of yeast cytochrome c peroxidase. II. The complete amino acid sequence.";
Arch. Biochem. Biophys. 203:615-629(1980).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 253-332.
PubMed=6286684 [NCBI, ExPASy, EBI, Israel, Japan]
Goltz S., Kaput J., Blobel G.;
"Isolation of the yeast nuclear gene encoding the mitochondrial protein, cytochrome c peroxidase.";
J. Biol. Chem. 257:11186-11190(1982).
[7]
MUTAGENESIS OF TRP-258.
DOI=10.1021/bi00417a008; PubMed=2851317 [NCBI, ExPASy, EBI, Israel, Japan]
Mauro J.M., Fishel L.A., Hazzard J.T., Meyer T.E., Tollin G., Cusanovich M.A., Kraut J.;
"Tryptophan-191-->phenylalanine, a proximal-side mutation in yeast cytochrome c peroxidase that strongly affects the kinetics of ferrocytochrome c oxidation.";
Biochemistry 27:6243-6256(1988).
[8]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
DOI=10.1038/nature02046; PubMed=14562106 [NCBI, ExPASy, EBI, Israel, Japan]
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-220, AND MASS SPECTROMETRY.
DOI=10.1074/mcp.M700468-MCP200; PubMed=18407956 [NCBI, ExPASy, EBI, Israel, Japan]
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
[10]
X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
PubMed=6092361 [NCBI, ExPASy, EBI, Israel, Japan]
Finzel B.C., Poulos T.L., Kraut J.;
"Crystal structure of yeast cytochrome c peroxidase refined at 1.7-A resolution.";
J. Biol. Chem. 259:13027-13036(1984).
[11]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF MUTANTS.
DOI=10.1021/bi00483a003; PubMed=2169873 [NCBI, ExPASy, EBI, Israel, Japan]
Wang J.M., Mauro M., Edwards S.L., Oatley S.J., Fishel L.A., Ashford V.A., Xuong N.-H., Kraut J.;
"X-ray structures of recombinant yeast cytochrome c peroxidase and three heme-cleft mutants prepared by site-directed mutagenesis.";
Biochemistry 29:7160-7173(1990).
[12]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
DOI=10.1021/bi00064a014; PubMed=8384877 [NCBI, ExPASy, EBI, Israel, Japan]
Goodin D.B., McRee D.E.;
"The Asp-His-Fe triad of cytochrome c peroxidase controls the reduction potential, electronic structure, and coupling of the tryptophan free radical to the heme.";
Biochemistry 32:3313-3324(1993).
[13]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
DOI=10.1038/nsb0796-626; PubMed=8673607 [NCBI, ExPASy, EBI, Israel, Japan]
Fitzgerald M.M., Musah R.A., McRee D.E., Goodin D.B.;
"A ligand-gated, hinged loop rearrangement opens a channel to a buried artificial protein cavity.";
Nat. Struct. Biol. 3:626-631(1996).
[14]
X-RAY CRYSTALLOGRAPHY (1.93 ANGSTROMS).
DOI=10.1074/jbc.275.12.8582; PubMed=10722697 [NCBI, ExPASy, EBI, Israel, Japan]
Hirst J., Goodin D.B.;
"Unusual oxidative chemistry of N(omega)-hydroxyarginine and N-hydroxyguanidine catalyzed at an engineered cavity in a heme peroxidase.";
J. Biol. Chem. 275:8582-8591(2000).
[15]
X-RAY CRYSTALLOGRAPHY (2.56 ANGSTROMS).
DOI=10.1021/bi002089r; PubMed=11170452 [NCBI, ExPASy, EBI, Israel, Japan]
Hirst J., Wilcox S.K., Williams P.A., Blankenship J., McRee D.E., Goodin D.B.;
"Replacement of the axial histidine ligand with imidazole in cytochrome c peroxidase. 1. Effects on structure.";
Biochemistry 40:1265-1273(2001).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
J01468; AAA88709.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X62422; CAA44288.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z28291; CAA82145.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY557921; AAS56247.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
J01321; AAA88710.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S19064; OPBYC.
RefSeq NP_012992.1; -.
3D structure databases
PDB
1A2F; X-ray; 2.10 A; A=71-361.[ExPASy / RCSB / EBI]
1A2G; X-ray; 2.10 A; A=71-361.[ExPASy / RCSB / EBI]
1AA4; X-ray; 2.10 A; A=71-361.[ExPASy / RCSB / EBI]
1AC4; X-ray; 2.10 A; A=71-361.[ExPASy / RCSB / EBI]
1AC8; X-ray; 2.10 A; A=71-361.[ExPASy / RCSB / EBI]
1AEB; X-ray; 2.10 A; A=71-361.[ExPASy / RCSB / EBI]
1AED; X-ray; 2.10 A; A=71-361.[ExPASy / RCSB / EBI]
1AEE; X-ray; 2.10 A; A=71-361.[ExPASy / RCSB / EBI]
1AEF; X-ray; 2.10 A; A=71-361.[ExPASy / RCSB / EBI]
1AEG; X-ray; 2.10 A; A=71-361.[ExPASy / RCSB / EBI]
1AEH; X-ray; 2.10 A; A=71-361.[ExPASy / RCSB / EBI]
1AEJ; X-ray; 2.10 A; A=71-361.[ExPASy / RCSB / EBI]
1AEK; X-ray; 2.10 A; A=71-361.[ExPASy / RCSB / EBI]
1AEM; X-ray; 2.10 A; A=71-361.[ExPASy / RCSB / EBI]
1AEN; X-ray; 2.10 A; A=71-361.[ExPASy / RCSB / EBI]
1AEO; X-ray; 2.10 A; A=71-361.[ExPASy / RCSB / EBI]
1AEQ; X-ray; 2.10 A; A=71-361.[ExPASy / RCSB / EBI]
1AES; X-ray; 2.10 A; A=71-361.[ExPASy / RCSB / EBI]
1AET; X-ray; 2.10 A; A=71-361.[ExPASy / RCSB / EBI]
1AEU; X-ray; 2.10 A; A=71-361.[ExPASy / RCSB / EBI]
1AEV; X-ray; 2.10 A; A=71-361.[ExPASy / RCSB / EBI]
1BEJ; X-ray; 2.40 A; A=71-361.[ExPASy / RCSB / EBI]
1BEK; X-ray; 2.20 A; A=71-361.[ExPASy / RCSB / EBI]
1BEM; X-ray; 2.20 A; A=71-361.[ExPASy / RCSB / EBI]
1BEP; X-ray; 2.20 A; A=71-361.[ExPASy / RCSB / EBI]
1BEQ; X-ray; 2.16 A; A=71-361.[ExPASy / RCSB / EBI]
1BES; X-ray; 2.00 A; A=71-361.[ExPASy / RCSB / EBI]
1BJ9; X-ray; 2.20 A; A=71-361.[ExPASy / RCSB / EBI]
1BVA; X-ray; 1.89 A; A=71-361.[ExPASy / RCSB / EBI]
1CCA; X-ray; 1.80 A; A=68-361.[ExPASy / RCSB / EBI]
1CCB; X-ray; 2.10 A; A=68-361.[ExPASy / RCSB / EBI]
1CCC; X-ray; 2.00 A; A=68-361.[ExPASy / RCSB / EBI]
1CCE; X-ray; 2.30 A; A=71-361.[ExPASy / RCSB / EBI]
1CCG; X-ray; 2.10 A; A=71-361.[ExPASy / RCSB / EBI]
1CCI; X-ray; 2.40 A; A=71-361.[ExPASy / RCSB / EBI]
1CCJ; X-ray; 2.10 A; A=71-361.[ExPASy / RCSB / EBI]
1CCK; X-ray; 2.10 A; A=71-361.[ExPASy / RCSB / EBI]
1CCL; X-ray; 2.00 A; A=71-361.[ExPASy / RCSB / EBI]
1CCP; X-ray; 2.20 A; A=68-361.[ExPASy / RCSB / EBI]
1CMP; X-ray; 1.90 A; A=71-361.[ExPASy / RCSB / EBI]
1CMQ; X-ray; 2.30 A; A=71-361.[ExPASy / RCSB / EBI]
1CMT; X-ray; 2.10 A; A=71-361.[ExPASy / RCSB / EBI]
1CMU; X-ray; 2.10 A; A=71-361.[ExPASy / RCSB / EBI]
1CPD; X-ray; 2.20 A; A=68-361.[ExPASy / RCSB / EBI]
1CPE; X-ray; 2.20 A; A=68-361.[ExPASy / RCSB / EBI]
1CPF; X-ray; 2.20 A; A=68-361.[ExPASy / RCSB / EBI]
1CPG; X-ray; 2.20 A; A=71-361.[ExPASy / RCSB / EBI]
1CYF; X-ray; 2.35 A; A=68-361.[ExPASy / RCSB / EBI]
1DCC; X-ray; 2.20 A; A=68-361.[ExPASy / RCSB / EBI]
1DJ1; X-ray; 1.93 A; A=71-361.[ExPASy / RCSB / EBI]
1DJ5; X-ray; 1.93 A; A=71-361.[ExPASy / RCSB / EBI]
1DS4; X-ray; 2.02 A; A=71-361.[ExPASy / RCSB / EBI]
1DSE; X-ray; 2.00 A; A=71-361.[ExPASy / RCSB / EBI]
1DSG; X-ray; 2.56 A; A=71-361.[ExPASy / RCSB / EBI]
1DSO; X-ray; 2.03 A; A=71-361.[ExPASy / RCSB / EBI]
1DSP; X-ray; 2.03 A; A=71-361.[ExPASy / RCSB / EBI]
1EBE; X-ray; 2.20 A; A=68-361.[ExPASy / RCSB / EBI]
1JCI; X-ray; 1.90 A; A=68-361.[ExPASy / RCSB / EBI]
1JDR; X-ray; 1.50 A; A=68-361.[ExPASy / RCSB / EBI]
1KOK; X-ray; 1.70 A; A=68-361.[ExPASy / RCSB / EBI]
1KRJ; X-ray; 2.00 A; A=68-361.[ExPASy / RCSB / EBI]
1KXM; X-ray; 1.74 A; A=71-361.[ExPASy / RCSB / EBI]
1KXN; X-ray; 1.80 A; A=71-361.[ExPASy / RCSB / EBI]
1MK8; X-ray; 1.65 A; A=68-361.[ExPASy / RCSB / EBI]
1MKQ; X-ray; 1.64 A; A=68-361.[ExPASy / RCSB / EBI]
1MKR; X-ray; 1.58 A; A=68-361.[ExPASy / RCSB / EBI]
1ML2; X-ray; 1.65 A; A=68-361.[ExPASy / RCSB / EBI]
1RYC; X-ray; 1.80 A; A=71-361.[ExPASy / RCSB / EBI]
1S6V; X-ray; 1.88 A; A/C=68-361.[ExPASy / RCSB / EBI]
1S73; X-ray; 1.53 A; A=68-361.[ExPASy / RCSB / EBI]
1SBM; X-ray; 1.69 A; A=68-361.[ExPASy / RCSB / EBI]
1SDQ; X-ray; 1.69 A; A=68-361.[ExPASy / RCSB / EBI]
1SOG; X-ray; 1.85 A; A=68-361.[ExPASy / RCSB / EBI]
1STQ; X-ray; 1.82 A; A=68-361.[ExPASy / RCSB / EBI]
1U74; X-ray; 2.40 A; A/C=68-361.[ExPASy / RCSB / EBI]
1U75; X-ray; 2.55 A; A/C=68-361.[ExPASy / RCSB / EBI]
1Z53; X-ray; 1.13 A; A=68-361.[ExPASy / RCSB / EBI]
1ZBY; X-ray; 1.20 A; A=68-361.[ExPASy / RCSB / EBI]
1ZBZ; X-ray; 1.29 A; A=68-361.[ExPASy / RCSB / EBI]
2ANZ; X-ray; 1.75 A; A=71-361.[ExPASy / RCSB / EBI]
2AQD; X-ray; 1.35 A; A=71-361.[ExPASy / RCSB / EBI]
2AS1; X-ray; 1.55 A; A=71-361.[ExPASy / RCSB / EBI]
2AS2; X-ray; 1.45 A; A=71-361.[ExPASy / RCSB / EBI]
2AS3; X-ray; 1.40 A; A=71-361.[ExPASy / RCSB / EBI]
2AS4; X-ray; 1.30 A; A=71-361.[ExPASy / RCSB / EBI]
2AS6; X-ray; 1.45 A; A=71-361.[ExPASy / RCSB / EBI]
2B0Z; X-ray; 2.70 A; A=68-361.[ExPASy / RCSB / EBI]
2B10; X-ray; 2.80 A; A/C=68-361.[ExPASy / RCSB / EBI]
2B11; X-ray; 2.30 A; A/C=68-361.[ExPASy / RCSB / EBI]
2B12; X-ray; 3.02 A; A=68-361.[ExPASy / RCSB / EBI]
2BCN; X-ray; 1.70 A; A/C=68-361.[ExPASy / RCSB / EBI]
2CCP; X-ray; 2.20 A; A=68-361.[ExPASy / RCSB / EBI]
2CEP; X-ray; 2.20 A; A=68-361.[ExPASy / RCSB / EBI]
2CYP; X-ray; 1.70 A; A=68-361.[ExPASy / RCSB / EBI]
2EUN; X-ray; 1.70 A; A=71-361.[ExPASy / RCSB / EBI]
2EUO; X-ray; 1.45 A; A=71-361.[ExPASy / RCSB / EBI]
2EUP; X-ray; 1.40 A; A=71-361.[ExPASy / RCSB / EBI]
2EUQ; X-ray; 1.30 A; A=71-361.[ExPASy / RCSB / EBI]
2EUR; X-ray; 1.39 A; A=71-361.[ExPASy / RCSB / EBI]
2EUS; X-ray; 1.55 A; A=71-361.[ExPASy / RCSB / EBI]
2EUT; X-ray; 1.12 A; A=71-361.[ExPASy / RCSB / EBI]
2EUU; X-ray; 1.45 A; A=71-361.[ExPASy / RCSB / EBI]
2GB8; NMR; -; A=68-361.[ExPASy / RCSB / EBI]
2IA8; X-ray; 1.48 A; A=71-361.[ExPASy / RCSB / EBI]
2ICV; X-ray; 1.60 A; A=71-361.[ExPASy / RCSB / EBI]
2PCB; X-ray; 2.80 A; A/C=68-361.[ExPASy / RCSB / EBI]
2PCC; X-ray; 2.30 A; A/C=68-361.[ExPASy / RCSB / EBI]
2RBT; X-ray; 1.24 A; X=71-361.[ExPASy / RCSB / EBI]
2RBU; X-ray; 1.80 A; X=71-361.[ExPASy / RCSB / EBI]
2RBV; X-ray; 1.39 A; X=71-361.[ExPASy / RCSB / EBI]
2RBW; X-ray; 1.50 A; X=71-361.[ExPASy / RCSB / EBI]
2RBX; X-ray; 1.50 A; X=71-361.[ExPASy / RCSB / EBI]
2RBY; X-ray; 1.50 A; X=71-361.[ExPASy / RCSB / EBI]
2RBZ; X-ray; 1.80 A; X=71-361.[ExPASy / RCSB / EBI]
2RC0; X-ray; 1.50 A; X=71-361.[ExPASy / RCSB / EBI]
2RC1; X-ray; 2.49 A; X=71-361.[ExPASy / RCSB / EBI]
2RC2; X-ray; 1.50 A; X=71-361.[ExPASy / RCSB / EBI]
2V23; X-ray; 1.80 A; A=68-361.[ExPASy / RCSB / EBI]
2V2E; X-ray; 1.68 A; A=71-361.[ExPASy / RCSB / EBI]
3CCP; X-ray; 2.20 A; A=68-361.[ExPASy / RCSB / EBI]
3CCX; X-ray; 2.30 A; A=71-361.[ExPASy / RCSB / EBI]
4CCP; X-ray; 2.20 A; A=68-361.[ExPASy / RCSB / EBI]
4CCX; X-ray; 1.90 A; A=71-361.[ExPASy / RCSB / EBI]
5CCP; X-ray; 2.20 A; A=68-361.[ExPASy / RCSB / EBI]
6CCP; X-ray; 2.20 A; A=68-361.[ExPASy / RCSB / EBI]
7CCP; X-ray; 2.20 A; A=68-361.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1A2F; -.
1A2G; -.
1AA4; -.
1AC4; -.
1AC8; -.
1AEB; -.
1AED; -.
1AEE; -.
1AEF; -.
1AEG; -.
1AEH; -.
1AEJ; -.
1AEK; -.
1AEM; -.
1AEN; -.
1AEO; -.
1AEQ; -.
1AES; -.
1AET; -.
1AEU; -.
1AEV; -.
1BEJ; -.
1BEK; -.
1BEM; -.
1BEP; -.
1BEQ; -.
1BES; -.
1BJ9; -.
1BVA; -.
1CCA; -.
1CCB; -.
1CCC; -.
1CCE; -.
1CCG; -.
1CCI; -.
1CCJ; -.
1CCK; -.
1CCL; -.
1CCP; -.
1CMP; -.
1CMQ; -.
1CMT; -.
1CMU; -.
1CPD; -.
1CPE; -.
1CPF; -.
1CPG; -.
1CYF; -.
1DCC; -.
1DJ1; -.
1DJ5; -.
1DS4; -.
1DSE; -.
1DSG; -.
1DSO; -.
1DSP; -.
1EBE; -.
1JCI; -.
1JDR; -.
1KOK; -.
1KRJ; -.
1KXM; -.
1KXN; -.
1MK8; -.
1MKQ; -.
1MKR; -.
1ML2; -.
1RYC; -.
1S6V; -.
1S73; -.
1SBM; -.
1SDQ; -.
1SOG; -.
1STQ; -.
1U74; -.
1U75; -.
1Z53; -.
1ZBY; -.
1ZBZ; -.
2ANZ; -.
2AQD; -.
2AS1; -.
2AS2; -.
2AS3; -.
2AS4; -.
2AS6; -.
2B0Z; -.
2B10; -.
2B11; -.
2B12; -.
2BCN; -.
2CCP; -.
2CEP; -.
2CYP; -.
2EUN; -.
2EUO; -.
2EUP; -.
2EUQ; -.
2EUR; -.
2EUS; -.
2EUT; -.
2EUU; -.
2GB8; -.
2IA8; -.
2ICV; -.
2PCB; -.
2PCC; -.
2RBT; -.
2RBU; -.
2RBV; -.
2RBW; -.
2RBX; -.
2RBY; -.
2RBZ; -.
2RC0; -.
2RC1; -.
2RC2; -.
2V23; -.
2V2E; -.
3CCP; -.
3CCX; -.
4CCP; -.
4CCX; -.
5CCP; -.
6CCP; -.
7CCP; -.
ModBase P00431.
Protein-protein interaction databases
DIP DIP:6251N; -.
IntAct P00431; -.
Protein family/group databases
PeroxiBase 2361; SceCcP01.
Organism-specific databases
CYGD YKR066c; -.
SGD S000001774; CCP1.
Yeast-GFP YKR066C.
Gene expression databases
ArrayExpress P00431; -.
GermOnline YKR066C; Saccharomyces cerevisiae.
Ontologies
GO
GO:0005758; Cellular component: mitochondrial intermembrane space (inferred from direct assay from SGD).
GO:0004130; Molecular function: cytochrome-c peroxidase activity (inferred from direct assay from SGD).
GO:0006979; Biological process: response to oxidative stress (inferred from mutant phenotype from SGD).
QuickGo view.
Family and domain databases
InterPro IPR002207; Asc_perxdse.
IPR002016; Haem_peroxidase_pln/fun/bac.
Graphical view of domain structure.
Pfam PF00141; peroxidase; 1.
Pfam graphical view of domain structure.
PRINTS PR00459; ASPEROXIDASE.
PR00458; PEROXIDASE.
PROSITE PS00435; PEROXIDASE_1; 1.
PS00436; PEROXIDASE_2; 1.
PS50873; PEROXIDASE_4; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS P00431.
Other
SWISS-3DIMAGE P00431.
Proteomic databases
PeptideAtlas P00431; -.
Genome annotation databases
Ensembl YKR066C; Saccharomyces cerevisiae. [Contig view]
GeneID 853940; -.
GenomeReviews Y13137_GR; YKR066C.
KEGG sce:YKR066C; -.
NMPDR fig|4932.3.peg.3978; -.
Phylogenomic databases
HOGENOM P00431; -.
Other
LinkHub P00431; -.
ProtoNet P00431.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Complete proteome; Direct protein sequencing; Heme; Hydrogen peroxide; Iron; Metal-binding; Mitochondrion; Organic radical; Oxidoreductase; Peroxidase; Phosphoprotein; Transit peptide.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
TRANSIT   1    67  67     Mitochondrion. 
CHAIN   68   361  294     Cytochrome c peroxidase, mitochondrial. PRO_0000023634
ACT_SITE   119   119        Proton acceptor. 
ACT_SITE   258   258        Tryptophan radical intermediate. 
METAL   242   242        Iron (heme axial ligand). 
SITE   115   115  1     Transition state stabilizer. 
MOD_RES   220   220        Phosphotyrosine. 
VARIANT   33    33  1     A -> AA (in allele 2). 
VARIANT   120   120  1     T -> I (in allele 2). 
VARIANT   219   219  1     D -> G (in allele 2). 
MUTAGEN   258   258        W->F: Substantially diminished activity. 
CONFLICT   41    41        Q -> H (in Ref. 3; AAA88709). 
CONFLICT   62    62        A -> P (in Ref. 3; AAA88709). 
CONFLICT   145   146        ND -> DN (in Ref. 5; AA sequence). 
CONFLICT   231   231        Missing (in Ref. 5; AA sequence). 
CONFLICT   273   273        L -> M (in Ref. 4; AAS56247). 
HELIX   83    99  17      
HELIX   103   106  4      
HELIX   110   121  12      
TURN   126   128  3      
STRAND   131   133  3      
HELIX   137   139  3      
HELIX   141   144  4      
HELIX   147   149  3      
TURN   150   152  3      
HELIX   153   165  13      
HELIX   171   185  15      
HELIX   202   204  3      
HELIX   218   226  9      
TURN   227   229  3      
HELIX   232   239  8      
HELIX   240   243  4      
STRAND   244   247  4      
HELIX   249   252  4      
STRAND   256   260  5      
HELIX   268   275  8      
STRAND   278   282  5      
STRAND   288   292  5      
HELIX   300   307  8      
HELIX   309   319  11      
HELIX   322   338  17      
HELIX   356   359  4      
Sequence information
Length