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P00431 (CCPR_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 162. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cytochrome c peroxidase, mitochondrial

Short name=CCP
EC=1.11.1.5
Gene names
Name:CCP1
Synonyms:CCP, CPO
Ordered Locus Names:YKR066C
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length361 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Destroys radicals which are normally produced within the cells and which are toxic to biological systems.

Catalytic activity

2 ferrocytochrome c + H2O2 = 2 ferricytochrome c + 2 H2O.

Cofactor

Binds 1 heme B (iron-protoporphyrin IX) group per subunit.

Subunit structure

Forms a one-to-one complex with cytochrome c.

Subcellular location

Mitochondrion matrix.

Miscellaneous

Present with 6730 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the peroxidase family. Cytochrome c peroxidase subfamily.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

CYC1P000442EBI-4389,EBI-5393

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 6767Mitochondrion Ref.6
Chain68 – 361294Cytochrome c peroxidase, mitochondrial
PRO_0000023634

Sites

Active site1191Proton acceptor
Active site2581Tryptophan radical intermediate
Metal binding2421Iron (heme axial ligand)
Site1151Transition state stabilizer

Amino acid modifications

Modified residue2201Phosphotyrosine Ref.10

Natural variations

Natural variant331A → AA in allele 2.
Natural variant1201T → I in allele 2.
Natural variant2191D → G in allele 2.

Experimental info

Mutagenesis2581W → F: Substantially diminished activity. Ref.8
Sequence conflict411Q → H in AAA88709. Ref.3
Sequence conflict621A → P in AAA88709. Ref.3
Sequence conflict145 – 1462ND → DN AA sequence Ref.6
Sequence conflict2311Missing AA sequence Ref.6
Sequence conflict2731L → M in AAS56247. Ref.5

Secondary structure

............................................................ 361
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P00431 [UniParc].

Last modified June 1, 1994. Version 2.
Checksum: A5D26385DA6F0A0B

FASTA36140,353
        10         20         30         40         50         60 
MTTAVRLLPS LGRTAHKRSL YLFSAAAAAA AAATFAYSQS QKRSSSSPGG GSNHGWNNWG 

        70         80         90        100        110        120 
KAAALASTTP LVHVASVEKG RSYEDFQKVY NAIALKLRED DEYDNYIGYG PVLVRLAWHT 

       130        140        150        160        170        180 
SGTWDKHDNT GGSYGGTYRF KKEFNDPSNA GLQNGFKFLE PIHKEFPWIS SGDLFSLGGV 

       190        200        210        220        230        240 
TAVQEMQGPK IPWRCGRVDT PEDTTPDNGR LPDADKDADY VRTFFQRLNM NDREVVALMG 

       250        260        270        280        290        300 
AHALGKTHLK NSGYEGPWGA ANNVFTNEFY LNLLNEDWKL EKNDANNEQW DSKSGYMMLP 

       310        320        330        340        350        360 
TDYSLIQDPK YLSIVKEYAN DQDKFFKDFS KAFEKLLENG ITFPKDAPSP FIFKTLEEQG 


L 

« Hide

References

« Hide 'large scale' references
[1]"Nucleotide sequence of the yeast nuclear gene for cytochrome c peroxidase precursor. Functional implications of the pre sequence for protein transport into mitochondria."
Kaput J., Goltz S., Blobel G.
J. Biol. Chem. 257:15054-15058(1982) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Isolation and sequence analysis of a second allele of the yeast nuclear gene cytochrome C peroxidase."
Piattoni M., Miyazaki W., Jayaraman K., Kaput J.
Submitted (OCT-1991) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: DBY939.
[3]"Complete DNA sequence of yeast chromosome XI."
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. expand/collapse author list , 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.
Nature 369:371-378(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[4]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[5]"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae."
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. expand/collapse author list , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J.
Genome Res. 17:536-543(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[6]"Primary structure of yeast cytochrome c peroxidase. II. The complete amino acid sequence."
Takio K., Titani K., Ericsson L.H., Yonetani T.
Arch. Biochem. Biophys. 203:615-629(1980) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 68-361.
[7]"Isolation of the yeast nuclear gene encoding the mitochondrial protein, cytochrome c peroxidase."
Goltz S., Kaput J., Blobel G.
J. Biol. Chem. 257:11186-11190(1982) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 253-332.
[8]"Tryptophan-191-->phenylalanine, a proximal-side mutation in yeast cytochrome c peroxidase that strongly affects the kinetics of ferrocytochrome c oxidation."
Mauro J.M., Fishel L.A., Hazzard J.T., Meyer T.E., Tollin G., Cusanovich M.A., Kraut J.
Biochemistry 27:6243-6256(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF TRP-258.
[9]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[10]"A multidimensional chromatography technology for in-depth phosphoproteome analysis."
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-220, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"Crystal structure of yeast cytochrome c peroxidase refined at 1.7-A resolution."
Finzel B.C., Poulos T.L., Kraut J.
J. Biol. Chem. 259:13027-13036(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
[12]"X-ray structures of recombinant yeast cytochrome c peroxidase and three heme-cleft mutants prepared by site-directed mutagenesis."
Wang J.M., Mauro M., Edwards S.L., Oatley S.J., Fishel L.A., Ashford V.A., Xuong N.-H., Kraut J.
Biochemistry 29:7160-7173(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF MUTANTS.
[13]"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."
Goodin D.B., McRee D.E.
Biochemistry 32:3313-3324(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
[14]"A ligand-gated, hinged loop rearrangement opens a channel to a buried artificial protein cavity."
Fitzgerald M.M., Musah R.A., McRee D.E., Goodin D.B.
Nat. Struct. Biol. 3:626-631(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
[15]"Unusual oxidative chemistry of N(omega)-hydroxyarginine and N-hydroxyguanidine catalyzed at an engineered cavity in a heme peroxidase."
Hirst J., Goodin D.B.
J. Biol. Chem. 275:8582-8591(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.93 ANGSTROMS).
[16]"Replacement of the axial histidine ligand with imidazole in cytochrome c peroxidase. 1. Effects on structure."
Hirst J., Wilcox S.K., Williams P.A., Blankenship J., McRee D.E., Goodin D.B.
Biochemistry 40:1265-1273(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.56 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J01468 Genomic DNA. Translation: AAA88709.1.
X62422 Genomic DNA. Translation: CAA44288.1.
Z28291 Genomic DNA. Translation: CAA82145.1.
AY557921 Genomic DNA. Translation: AAS56247.1.
J01321 Genomic DNA. Translation: AAA88710.1.
BK006944 Genomic DNA. Translation: DAA09217.1.
PIROPBYC. S19064.
RefSeqNP_012992.1. NM_001179856.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1A2FX-ray2.10A71-361[»]
1A2GX-ray2.10A71-361[»]
1AA4X-ray2.10A71-361[»]
1AC4X-ray2.10A71-361[»]
1AC8X-ray2.10A71-361[»]
1AEBX-ray2.10A71-361[»]
1AEDX-ray2.10A71-361[»]
1AEEX-ray2.10A71-361[»]
1AEFX-ray2.10A71-361[»]
1AEGX-ray2.10A71-361[»]
1AEHX-ray2.10A71-361[»]
1AEJX-ray2.10A71-361[»]
1AEKX-ray2.10A71-361[»]
1AEMX-ray2.10A71-361[»]
1AENX-ray2.10A71-361[»]
1AEOX-ray2.10A71-361[»]
1AEQX-ray2.10A71-361[»]
1AESX-ray2.10A71-361[»]
1AETX-ray2.10A71-361[»]
1AEUX-ray2.10A71-361[»]
1AEVX-ray2.10A71-361[»]
1BEJX-ray2.40A71-361[»]
1BEKX-ray2.20A71-361[»]
1BEMX-ray2.20A71-361[»]
1BEPX-ray2.20A71-361[»]
1BEQX-ray2.16A71-361[»]
1BESX-ray2.00A71-361[»]
1BJ9X-ray2.20A71-361[»]
1BVAX-ray1.89A71-361[»]
1CCAX-ray1.80A68-361[»]
1CCBX-ray2.10A68-361[»]
1CCCX-ray2.00A68-361[»]
1CCEX-ray2.30A71-361[»]
1CCGX-ray2.10A71-361[»]
1CCIX-ray2.40A71-361[»]
1CCJX-ray2.10A71-361[»]
1CCKX-ray2.10A71-361[»]
1CCLX-ray2.00A71-361[»]
1CCPX-ray2.20A68-361[»]
1CMPX-ray1.90A71-361[»]
1CMQX-ray2.30A71-361[»]
1CMTX-ray2.10A71-361[»]
1CMUX-ray2.10A71-361[»]
1CPDX-ray2.20A68-361[»]
1CPEX-ray2.20A68-361[»]
1CPFX-ray2.20A68-361[»]
1CPGX-ray2.20A71-361[»]
1CYFX-ray2.35A68-361[»]
1DCCX-ray2.20A68-361[»]
1DJ1X-ray1.93A71-361[»]
1DJ5X-ray1.93A71-361[»]
1DS4X-ray2.02A71-361[»]
1DSEX-ray2.00A71-361[»]
1DSGX-ray2.56A71-361[»]
1DSOX-ray2.03A71-361[»]
1DSPX-ray2.03A71-361[»]
1EBEX-ray2.20A68-361[»]
1JCIX-ray1.90A68-361[»]
1JDRX-ray1.50A68-361[»]
1KOKX-ray1.70A68-361[»]
1KRJX-ray2.00A68-361[»]
1KXMX-ray1.74A71-361[»]
1KXNX-ray1.80A71-361[»]
1MK8X-ray1.65A68-361[»]
1MKQX-ray1.64A68-361[»]
1MKRX-ray1.58A68-361[»]
1ML2X-ray1.65A68-361[»]
1RYCX-ray1.80A71-361[»]
1S6VX-ray1.88A/C68-361[»]
1S73X-ray1.53A68-361[»]
1SBMX-ray1.69A68-361[»]
1SDQX-ray1.69A68-361[»]
1SOGX-ray1.85A68-361[»]
1STQX-ray1.82A68-361[»]
1U74X-ray2.40A/C68-361[»]
1U75X-ray2.55A/C68-361[»]
1Z53X-ray1.13A68-361[»]
1ZBYX-ray1.20A68-361[»]
1ZBZX-ray1.29A68-361[»]
2ANZX-ray1.75A71-361[»]
2AQDX-ray1.35A71-361[»]
2AS1X-ray1.55A71-361[»]
2AS2X-ray1.45A71-361[»]
2AS3X-ray1.40A71-361[»]
2AS4X-ray1.30A71-361[»]
2AS6X-ray1.45A71-361[»]
2B0ZX-ray2.70A68-361[»]
2B10X-ray2.80A/C68-361[»]
2B11X-ray2.30A/C68-361[»]
2B12X-ray3.02A68-361[»]
2BCNX-ray1.70A/C68-361[»]
2CCPX-ray2.20A68-361[»]
2CEPX-ray2.20A68-361[»]
2CYPX-ray1.70A68-361[»]
2EUNX-ray1.70A71-361[»]
2EUOX-ray1.45A71-361[»]
2EUPX-ray1.40A71-361[»]
2EUQX-ray1.30A71-361[»]
2EURX-ray1.39A71-361[»]
2EUSX-ray1.55A71-361[»]
2EUTX-ray1.12A71-361[»]
2EUUX-ray1.45A71-361[»]
2GB8NMR-A68-361[»]
2IA8X-ray1.48A71-361[»]
2ICVX-ray1.60A71-361[»]
2JTINMR-A68-361[»]
2PCBX-ray2.80A/C68-361[»]
2PCCX-ray2.30A/C68-361[»]
2RBTX-ray1.24X71-361[»]
2RBUX-ray1.80X71-361[»]
2RBVX-ray1.39X71-361[»]
2RBWX-ray1.50X71-361[»]
2RBXX-ray1.50X71-361[»]
2RBYX-ray1.50X71-361[»]
2RBZX-ray1.80X71-361[»]
2RC0X-ray1.50X71-361[»]
2RC1X-ray2.49X71-361[»]
2RC2X-ray1.50X71-361[»]
2V23X-ray1.80A68-361[»]
2V2EX-ray1.68A71-361[»]
2X07X-ray1.86A69-361[»]
2X08X-ray2.01A69-361[»]
2XILX-ray1.68A71-361[»]
2XJ5X-ray1.69A71-361[»]
2XJ8X-ray1.69A71-361[»]
2Y5AX-ray1.25A71-361[»]
2YCGX-ray1.81A68-361[»]
3CCPX-ray2.20A68-361[»]
3CCXX-ray2.30A71-361[»]
3E2NX-ray1.30A68-96[»]
A110-361[»]
3E2OX-ray1.06A68-361[»]
3EXBX-ray1.60A68-361[»]
3M23X-ray1.40A71-361[»]
3M25X-ray1.40A71-361[»]
3M26X-ray1.40A71-361[»]
3M27X-ray1.40A71-361[»]
3M28X-ray1.40A71-361[»]
3M29X-ray1.40A71-361[»]
3M2AX-ray1.40A71-361[»]
3M2BX-ray1.40A71-361[»]
3M2CX-ray1.40A71-361[»]
3M2DX-ray1.40A71-361[»]
3M2EX-ray1.40A71-361[»]
3M2FX-ray1.40A71-361[»]
3M2GX-ray1.40A71-361[»]
3M2HX-ray1.40A71-361[»]
3M2IX-ray1.40A71-361[»]
3R98Other2.40A69-361[»]
3R99Other2.40A69-361[»]
4A6ZX-ray1.61A68-361[»]
4A71X-ray1.61A68-361[»]
4A78X-ray2.01A68-361[»]
4A7MX-ray1.71A68-361[»]
4CCPX-ray2.20A68-361[»]
4CCXX-ray1.90A71-361[»]
4JB4X-ray2.39A/C68-361[»]
5CCPX-ray2.20A68-361[»]
6CCPX-ray2.20A68-361[»]
7CCPX-ray2.20A68-361[»]
ProteinModelPortalP00431.
SMRP00431. Positions 43-361.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid34197. 21 interactions.
DIPDIP-6251N.
IntActP00431. 5 interactions.
MINTMINT-598890.
STRING4932.YKR066C.

Protein family/group databases

PeroxiBase2361. SceCcP01.

Proteomic databases

MaxQBP00431.
PaxDbP00431.
PeptideAtlasP00431.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYKR066C; YKR066C; YKR066C.
GeneID853940.
KEGGsce:YKR066C.

Organism-specific databases

CYGDYKR066c.
SGDS000001774. CCP1.

Phylogenomic databases

eggNOGCOG0376.
HOGENOMHOG000189824.
KOK00428.
OMAWRPGRID.
OrthoDBEOG754J0N.

Enzyme and pathway databases

BioCycYEAST:YKR066C-MONOMER.
SABIO-RKP00431.

Gene expression databases

GenevestigatorP00431.

Family and domain databases

InterProIPR002207. Asc_peroxidase.
IPR010255. Haem_peroxidase.
IPR002016. Haem_peroxidase_pln/fun/bac.
IPR019794. Peroxidases_AS.
IPR019793. Peroxidases_heam-ligand_BS.
[Graphical view]
PfamPF00141. peroxidase. 1 hit.
[Graphical view]
PRINTSPR00459. ASPEROXIDASE.
PR00458. PEROXIDASE.
SUPFAMSSF48113. SSF48113. 1 hit.
PROSITEPS00435. PEROXIDASE_1. 1 hit.
PS00436. PEROXIDASE_2. 1 hit.
PS50873. PEROXIDASE_4. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP00431.
NextBio975327.
PMAP-CutDBP00431.

Entry information

Entry nameCCPR_YEAST
AccessionPrimary (citable) accession number: P00431
Secondary accession number(s): D6VXC7, Q6Q5M9
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: June 1, 1994
Last modified: July 9, 2014
This is version 162 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome XI

Yeast (Saccharomyces cerevisiae) chromosome XI: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references