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Identification
NameCytochrome c peroxidase, mitochondrial
Synonyms
  • CCP
Gene NameCCP1
Enzyme Class
Biological Properties
General FunctionInvolved in peroxidase activity
Specific FunctionDestroys radicals which are normally produced within the cells and which are toxic to biological systems
Cellular LocationMitochondrion matrix
SMPDB PathwaysNot Available
KEGG PathwaysNot Available
SMPDB ReactionsNot Available
KEGG ReactionsNot Available
Metabolites
YMDB IDNameView
YMDB00888Hydrogen peroxideShow
YMDB00890waterShow
GO Classification
Component
Not Available
Function
transition metal ion binding
iron ion binding
heme binding
antioxidant activity
peroxidase activity
binding
ion binding
cation binding
metal ion binding
Process
oxidation reduction
response to stimulus
response to stress
response to oxidative stress
metabolic process
Gene Properties
Chromosome Locationchromosome 11
LocusYKR066C
Gene Sequence>1086 bp ATGACTACTGCTGTTAGGCTTTTACCTTCACTGGGCAGAACCGCCCATAAGAGGTCTCTC TACCTGTTCTCCGCTGCTGCTGCTGCTGCTGCTGCTGCAACTTTTGCTTACTCGCAATCC CAAAAGAGATCATCGTCTTCTCCCGGGGGTGGTAGTAACCACGGATGGAACAACTGGGGG AAGGCAGCTGCTTTGGCTTCCACTACACCGCTCGTTCATGTCGCCTCTGTCGAAAAAGGG AGGTCATACGAGGACTTCCAAAAGGTGTACAATGCGATTGCACTCAAGCTGAGGGAAGAT GACGAATATGACAACTATATAGGCTATGGGCCCGTATTAGTCCGTCTTGCTTGGCACACT TCAGGGACCTGGGACAAGCACGACAATACAGGCGGGTCATACGGTGGTACATACAGATTC AAAAAGGAGTTTAACGATCCATCCAATGCGGGCTTGCAGAATGGCTTCAAGTTCCTGGAG CCCATTCACAAAGAGTTTCCCTGGATCTCCTCGGGTGATCTGTTCAGTCTAGGGGGTGTC ACTGCCGTGCAGGAAATGCAGGGTCCCAAGATTCCATGGAGATGTGGTAGAGTCGACACG CCAGAGGATACTACCCCTGACAACGGGAGACTGCCTGACGCTGATAAAGACGCTGACTAT GTCAGAACATTTTTTCAAAGACTTAATATGAATGACAGAGAAGTAGTTGCTCTTATGGGG GCTCACGCTCTGGGCAAGACCCACTTGAAGAACTCTGGATACGAAGGGCCATGGGGAGCC GCTAACAACGTCTTTACCAATGAGTTTTACTTGAACATGCTGAATGAAGACTGGAAATTG GAAAAGAACGACGCGAACAACGAACAGTGGGACTCTAAGAGCGGCTACATGATGCTGCCC ACTGATTATTCTTTGATTCAGGATCCCAAGTACTTAAGCATTGTGAAAGAATACGCTAAT GACCAGGACAAGTTCTTCAAGGATTTTTCCAAAGCTTTTGAAAAACTGTTGGAGAACGGT ATCACTTTCCCTAAAGACGCGCCCAGTCCATTTATTTTCAAGACTTTAGAGGAACAAGGT TTATAG
Protein Properties
Pfam Domain Function
Protein Residues361
Protein Molecular Weight40352.69922
Protein Theoretical pI6.32
PDB Fileshow
Signalling Regions
  • None
Transmembrane Regions
  • None
Protein Sequence>Cytochrome c peroxidase, mitochondrial MTTAVRLLPSLGRTAHKRSLYLFSAAAAAAAAATFAYSQSQKRSSSSPGGGSNHGWNNWG KAAALASTTPLVHVASVEKGRSYEDFQKVYNAIALKLREDDEYDNYIGYGPVLVRLAWHT SGTWDKHDNTGGSYGGTYRFKKEFNDPSNAGLQNGFKFLEPIHKEFPWISSGDLFSLGGV TAVQEMQGPKIPWRCGRVDTPEDTTPDNGRLPDADKDADYVRTFFQRLNMNDREVVALMG AHALGKTHLKNSGYEGPWGAANNVFTNEFYLNLLNEDWKLEKNDANNEQWDSKSGYMMLP TDYSLIQDPKYLSIVKEYANDQDKFFKDFSKAFEKLLENGITFPKDAPSPFIFKTLEEQG L
References
External Links
ResourceLink
Saccharomyces Genome Database CCP1
Uniprot IDP00431
Uniprot NameCCPR_YEAST
GenBank Gene IDAY557921
Genebank Protein ID45269733
PDB ID
1ZBZ
General Reference
  • Kaput, J., Goltz, S., Blobel, G. (1982). "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 257:15054-15058.6294090
  • Dujon, B., Alexandraki, D., Andre, B., Ansorge, W., Baladron, V., Ballesta, J. P., Banrevi, A., Bolle, P. A., Bolotin-Fukuhara, M., Bossier, P., et, a. l. .. (1994). "Complete DNA sequence of yeast chromosome XI." Nature 369:371-378.8196765
  • Hu, Y., Rolfs, A., Bhullar, B., Murthy, T. V., 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., Bulyk, M. L., Harlow, E., Marsischky, G., Kolodner, R. D., LaBaer, J. (2007). "Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae." Genome Res 17:536-543.17322287
  • Takio, K., Titani, K., Ericsson, L. H., Yonetani, T. (1980). "Primary structure of yeast cytochrome c peroxidase. II. The complete amino acid sequence." Arch Biochem Biophys 203:615-629.6257176
  • Goltz, S., Kaput, J., Blobel, G. (1982). "Isolation of the yeast nuclear gene encoding the mitochondrial protein, cytochrome c peroxidase." J Biol Chem 257:11186-11190.6286684
  • Mauro, J. M., Fishel, L. A., Hazzard, J. T., Meyer, T. E., Tollin, G., Cusanovich, M. A., Kraut, J. (1988). "Tryptophan-191----phenylalanine, a proximal-side mutation in yeast cytochrome c peroxidase that strongly affects the kinetics of ferrocytochrome c oxidation." Biochemistry 27:6243-6256.2851317
  • Ghaemmaghami, S., Huh, W. K., Bower, K., Howson, R. W., Belle, A., Dephoure, N., O'Shea, E. K., Weissman, J. S. (2003). "Global analysis of protein expression in yeast." Nature 425:737-741.14562106
  • Albuquerque, C. P., Smolka, M. B., Payne, S. H., Bafna, V., Eng, J., Zhou, H. (2008). "A multidimensional chromatography technology for in-depth phosphoproteome analysis." Mol Cell Proteomics 7:1389-1396.18407956
  • Finzel, B. C., Poulos, T. L., Kraut, J. (1984). "Crystal structure of yeast cytochrome c peroxidase refined at 1.7-A resolution." J Biol Chem 259:13027-13036.6092361
  • Wang, J. M., Mauro, M., Edwards, S. L., Oatley, S. J., Fishel, L. A., Ashford, V. A., Xuong, N. H., Kraut, J. (1990). "X-ray structures of recombinant yeast cytochrome c peroxidase and three heme-cleft mutants prepared by site-directed mutagenesis." Biochemistry 29:7160-7173.2169873
  • Goodin, D. B., McRee, D. E. (1993). "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 32:3313-3324.8384877
  • Fitzgerald, M. M., Musah, R. A., McRee, D. E., Goodin, D. B. (1996). "A ligand-gated, hinged loop rearrangement opens a channel to a buried artificial protein cavity." Nat Struct Biol 3:626-631.8673607
  • Hirst, J., Goodin, D. B. (2000). "Unusual oxidative chemistry of N(omega)-hydroxyarginine and N-hydroxyguanidine catalyzed at an engineered cavity in a heme peroxidase." J Biol Chem 275:8582-8591.10722697
  • Hirst, J., Wilcox, S. K., Williams, P. A., Blankenship, J., McRee, D. E., Goodin, D. B. (2001). "Replacement of the axial histidine ligand with imidazole in cytochrome c peroxidase. 1. Effects on structure." Biochemistry 40:1265-1273.11170452