Reviewed, UniProtKB/Swiss-Prot P00431 (CCPR_YEAST)

Names and origin

Protein names

Recommended name:
    Cytochrome c peroxidase, mitochondrial
      Short name=CCP
    EC=1.11.1.5

Gene names

Name:	CCP1
Synonyms:	CCP, CPO
Ordered Locus Names:	YKR066C

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	361 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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. Ref.8
Sequence similarities	Belongs to the peroxidase family. Cytochrome c peroxidase subfamily.

Ontologies

Keywords
Biological process	Hydrogen peroxide
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	Heme Iron Metal-binding
Molecular function	Oxidoreductase Peroxidase
PTM	Organic radical Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	hydrogen peroxide catabolic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	mitochondrial intermembrane space Inferred from direct assay. Source: SGD mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	cytochrome-c peroxidase activity Inferred from direct assay. Source: SGD heme binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – 67

67

Mitochondrion Ref.5

Chain

68 – 361

294

Cytochrome c peroxidase, mitochondrial

PRO_0000023634

Sites

Active site

119

1

Proton acceptor

Active site

258

1

Tryptophan radical intermediate

Metal binding

242

1

Iron (heme axial ligand)

Site

115

1

Transition state stabilizer

Amino acid modifications

Modified residue

220

1

Phosphotyrosine Ref.9

Natural variations

Natural variant

33

1

A → AA in allele 2.

Natural variant

120

1

T → I in allele 2.

Natural variant

219

1

D → G in allele 2.

Experimental info

Mutagenesis

258

1

W → F: Substantially diminished activity. Ref.7

Sequence conflict

41

1

Q → H in AAA88709. Ref.3

Sequence conflict

62

1

A → P in AAA88709. Ref.3

Sequence conflict

145 – 146

2

ND → DN AA sequence Ref.5

Sequence conflict

231

1

Missing AA sequence Ref.5

Sequence conflict

273

1

L → M in AAS56247. Ref.4

Secondary structure

1

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361

Helix Strand Turn

Details...

Helix

83 – 99

17

Helix

103 – 106

4

Helix

110 – 121

12

Turn

126 – 128

3

Beta 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

Beta strand

244 – 247

4

Helix

249 – 252

4

Beta strand

256 – 260

5

Helix

268 – 275

8

Beta strand

278 – 282

5

Beta strand

288 – 292

5

Helix

300 – 307

8

Helix

309 – 319

11

Helix

322 – 338

17

Helix

356 – 359

4

Sequences

	Sequence		Length	Mass (Da)
	P00431-1 [UniParc]. Last modified June 1, 1994. Version 2. Checksum: A5D26385DA6F0A0B	FASTA	361	40,353
	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

References

	« Hide 'large scale' referencesShow '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: 6294090] [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. , 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: 8196765] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[4]	"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. , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J. Genome Res. 17:536-543(2007) [PubMed: 17322287] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[5]	"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: 6257176] [Abstract] Cited for: PROTEIN SEQUENCE OF 68-361.
[6]	"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: 6286684] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 253-332.
[7]	"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: 2851317] [Abstract] Cited for: MUTAGENESIS OF TRP-258.
[8]	"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: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[9]	"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: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-220, MASS SPECTROMETRY.
[10]	"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: 6092361] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
[11]	"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: 2169873] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF MUTANTS.
[12]	"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: 8384877] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
[13]	"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: 8673607] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
[14]	"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: 10722697] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.93 ANGSTROMS).
[15]	"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: 11170452] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.56 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

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.

PIR

OPBYC. S19064.

RefSeq

NP_012992.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1A2F	X-ray	2.10	A	71-361	[»]
1A2G	X-ray	2.10	A	71-361	[»]
1AA4	X-ray	2.10	A	71-361	[»]
1AC4	X-ray	2.10	A	71-361	[»]
1AC8	X-ray	2.10	A	71-361	[»]
1AEB	X-ray	2.10	A	71-361	[»]
1AED	X-ray	2.10	A	71-361	[»]
1AEE	X-ray	2.10	A	71-361	[»]
1AEF	X-ray	2.10	A	71-361	[»]
1AEG	X-ray	2.10	A	71-361	[»]
1AEH	X-ray	2.10	A	71-361	[»]
1AEJ	X-ray	2.10	A	71-361	[»]
1AEK	X-ray	2.10	A	71-361	[»]
1AEM	X-ray	2.10	A	71-361	[»]
1AEN	X-ray	2.10	A	71-361	[»]
1AEO	X-ray	2.10	A	71-361	[»]
1AEQ	X-ray	2.10	A	71-361	[»]
1AES	X-ray	2.10	A	71-361	[»]
1AET	X-ray	2.10	A	71-361	[»]
1AEU	X-ray	2.10	A	71-361	[»]
1AEV	X-ray	2.10	A	71-361	[»]
1BEJ	X-ray	2.40	A	71-361	[»]
1BEK	X-ray	2.20	A	71-361	[»]
1BEM	X-ray	2.20	A	71-361	[»]
1BEP	X-ray	2.20	A	71-361	[»]
1BEQ	X-ray	2.16	A	71-361	[»]
1BES	X-ray	2.00	A	71-361	[»]
1BJ9	X-ray	2.20	A	71-361	[»]
1BVA	X-ray	1.89	A	71-361	[»]
1CCA	X-ray	1.80	A	68-361	[»]
1CCB	X-ray	2.10	A	68-361	[»]
1CCC	X-ray	2.00	A	68-361	[»]
1CCE	X-ray	2.30	A	71-361	[»]
1CCG	X-ray	2.10	A	71-361	[»]
1CCI	X-ray	2.40	A	71-361	[»]
1CCJ	X-ray	2.10	A	71-361	[»]
1CCK	X-ray	2.10	A	71-361	[»]
1CCL	X-ray	2.00	A	71-361	[»]
1CCP	X-ray	2.20	A	68-361	[»]
1CMP	X-ray	1.90	A	71-361	[»]
1CMQ	X-ray	2.30	A	71-361	[»]
1CMT	X-ray	2.10	A	71-361	[»]
1CMU	X-ray	2.10	A	71-361	[»]
1CPD	X-ray	2.20	A	68-361	[»]
1CPE	X-ray	2.20	A	68-361	[»]
1CPF	X-ray	2.20	A	68-361	[»]
1CPG	X-ray	2.20	A	71-361	[»]
1CYF	X-ray	2.35	A	68-361	[»]
1DCC	X-ray	2.20	A	68-361	[»]
1DJ1	X-ray	1.93	A	71-361	[»]
1DJ5	X-ray	1.93	A	71-361	[»]
1DS4	X-ray	2.02	A	71-361	[»]
1DSE	X-ray	2.00	A	71-361	[»]
1DSG	X-ray	2.56	A	71-361	[»]
1DSO	X-ray	2.03	A	71-361	[»]
1DSP	X-ray	2.03	A	71-361	[»]
1EBE	X-ray	2.20	A	68-361	[»]
1JCI	X-ray	1.90	A	68-361	[»]
1JDR	X-ray	1.50	A	68-361	[»]
1KOK	X-ray	1.70	A	68-361	[»]
1KRJ	X-ray	2.00	A	68-361	[»]
1KXM	X-ray	1.74	A	71-361	[»]
1KXN	X-ray	1.80	A	71-361	[»]
1MK8	X-ray	1.65	A	68-361	[»]
1MKQ	X-ray	1.64	A	68-361	[»]
1MKR	X-ray	1.58	A	68-361	[»]
1ML2	X-ray	1.65	A	68-361	[»]
1RYC	X-ray	1.80	A	71-361	[»]
1S6V	X-ray	1.88	A/C	68-361	[»]
1S73	X-ray	1.53	A	68-361	[»]
1SBM	X-ray	1.69	A	68-361	[»]
1SDQ	X-ray	1.69	A	68-361	[»]
1SOG	X-ray	1.85	A	68-361	[»]
1STQ	X-ray	1.82	A	68-361	[»]
1U74	X-ray	2.40	A/C	68-361	[»]
1U75	X-ray	2.55	A/C	68-361	[»]
1Z53	X-ray	1.13	A	68-361	[»]
1ZBY	X-ray	1.20	A	68-361	[»]
1ZBZ	X-ray	1.29	A	68-361	[»]
2ANZ	X-ray	1.75	A	71-361	[»]
2AQD	X-ray	1.35	A	71-361	[»]
2AS1	X-ray	1.55	A	71-361	[»]
2AS2	X-ray	1.45	A	71-361	[»]
2AS3	X-ray	1.40	A	71-361	[»]
2AS4	X-ray	1.30	A	71-361	[»]
2AS6	X-ray	1.45	A	71-361	[»]
2B0Z	X-ray	2.70	A	68-361	[»]
2B10	X-ray	2.80	A/C	68-361	[»]
2B11	X-ray	2.30	A/C	68-361	[»]
2B12	X-ray	3.02	A	68-361	[»]
2BCN	X-ray	1.70	A/C	68-361	[»]
2CCP	X-ray	2.20	A	68-361	[»]
2CEP	X-ray	2.20	A	68-361	[»]
2CYP	X-ray	1.70	A	68-361	[»]
2EUN	X-ray	1.70	A	71-361	[»]
2EUO	X-ray	1.45	A	71-361	[»]
2EUP	X-ray	1.40	A	71-361	[»]
2EUQ	X-ray	1.30	A	71-361	[»]
2EUR	X-ray	1.39	A	71-361	[»]
2EUS	X-ray	1.55	A	71-361	[»]
2EUT	X-ray	1.12	A	71-361	[»]
2EUU	X-ray	1.45	A	71-361	[»]
2GB8	NMR	-	A	68-361	[»]
2IA8	X-ray	1.48	A	71-361	[»]
2ICV	X-ray	1.60	A	71-361	[»]
2JTI	NMR	-	A	68-361	[»]
2PCB	X-ray	2.80	A/C	68-361	[»]
2PCC	X-ray	2.30	A/C	68-361	[»]
2RBT	X-ray	1.24	X	71-361	[»]
2RBU	X-ray	1.80	X	71-361	[»]
2RBV	X-ray	1.39	X	71-361	[»]
2RBW	X-ray	1.50	X	71-361	[»]
2RBX	X-ray	1.50	X	71-361	[»]
2RBY	X-ray	1.50	X	71-361	[»]
2RBZ	X-ray	1.80	X	71-361	[»]
2RC0	X-ray	1.50	X	71-361	[»]
2RC1	X-ray	2.49	X	71-361	[»]
2RC2	X-ray	1.50	X	71-361	[»]
2V23	X-ray	1.80	A	68-361	[»]
2V2E	X-ray	1.68	A	71-361	[»]
3CCP	X-ray	2.20	A	68-361	[»]
3CCX	X-ray	2.30	A	71-361	[»]
3E2N	X-ray	1.30	A	68-361	[»]
3E2O	X-ray	1.06	A	68-361	[»]
3EXB	X-ray	1.60	A	68-361	[»]
4CCP	X-ray	2.20	A	68-361	[»]
4CCX	X-ray	1.90	A	71-361	[»]
5CCP	X-ray	2.20	A	68-361	[»]
6CCP	X-ray	2.20	A	68-361	[»]
7CCP	X-ray	2.20	A	68-361	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:6251N.

IntAct

P00431. 5 interactions.

Protein family/group databases

PeroxiBase

2361. SceCcP01.

Proteomic databases

PeptideAtlas

P00431.

Genome annotation databases

Ensembl

YKR066C. Saccharomyces cerevisiae. [Contig view]

GeneID

853940.

GenomeReviews

Gene locus YKR066C in contig Y13137_GR.

KEGG

sce:YKR066C.

NMPDR

fig|4932.3.peg.3978.

Organism-specific databases

CYGD

YKR066c.

SGD

S000001774. CCP1.

Yeast-GFP

Search...

Phylogenomic databases

HOGENOM

P00431.

OMA

P00431. HALGKTH.

Enzyme and pathway databases

BRENDA

1.11.1.5. 250.

Gene expression databases

ArrayExpress

P00431.

GermOnline

YKR066C. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR002207. Asc_perxdse.
IPR002016. Haem_peroxidase_pln/fun/bac.
IPR019794. Peroxidases_AS.
IPR019793. Peroxidases_heam-ligand_BS.
[Graphical view]

Pfam

PF00141. peroxidase. 1 hit.
[Graphical view]

PRINTS

PR00459. ASPEROXIDASE.
PR00458. PEROXIDASE.

PROSITE

PS00435. PEROXIDASE_1. 1 hit.
PS00436. PEROXIDASE_2. 1 hit.
PS50873. PEROXIDASE_4. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

975327.

PMAP-CutDB

P00431.

Entry information

Entry name

CCPR_YEAST

Accession

Primary (citable) accession number: P00431
Secondary accession number(s): Q6Q5M9

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	June 1, 1994
Last modified:	June 16, 2009
This is version 115 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)