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P00431

- CCPR_YEAST

UniProt

P00431 - CCPR_YEAST

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Protein

Cytochrome c peroxidase, mitochondrial

Gene

CCP1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

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

Cofactori

heme bNote: Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei115 – 1151Transition state stabilizer
Active sitei119 – 1191Proton acceptor
Metal bindingi242 – 2421Iron (heme axial ligand)
Active sitei258 – 2581Tryptophan radical intermediate

GO - Molecular functioni

  1. cytochrome-c peroxidase activity Source: SGD
  2. heme binding Source: InterPro
  3. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. cellular response to oxidative stress Source: SGD
  2. hydrogen peroxide catabolic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase, Peroxidase

Keywords - Biological processi

Hydrogen peroxide

Keywords - Ligandi

Heme, Iron, Metal-binding

Enzyme and pathway databases

BioCyciYEAST:YKR066C-MONOMER.
SABIO-RKP00431.

Protein family/group databases

PeroxiBasei2361. SceCcP01.

Names & Taxonomyi

Protein namesi
Recommended name:
Cytochrome c peroxidase, mitochondrial (EC:1.11.1.5)
Short name:
CCP
Gene namesi
Name:CCP1
Synonyms:CCP, CPO
Ordered Locus Names:YKR066C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome XI

Organism-specific databases

CYGDiYKR066c.
SGDiS000001774. CCP1.

Subcellular locationi

GO - Cellular componenti

  1. mitochondrial intermembrane space Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi258 – 2581W → F: Substantially diminished activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 6767Mitochondrion1 PublicationAdd
BLAST
Chaini68 – 361294Cytochrome c peroxidase, mitochondrialPRO_0000023634Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei220 – 2201Phosphotyrosine1 Publication

Keywords - PTMi

Organic radical, Phosphoprotein

Proteomic databases

MaxQBiP00431.
PaxDbiP00431.
PeptideAtlasiP00431.

Miscellaneous databases

PMAP-CutDBP00431.

Expressioni

Gene expression databases

GenevestigatoriP00431.

Interactioni

Subunit structurei

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

Binary interactionsi

WithEntry#Exp.IntActNotes
CYC1P000443EBI-4389,EBI-5393

Protein-protein interaction databases

BioGridi34197. 22 interactions.
DIPiDIP-6251N.
IntActiP00431. 5 interactions.
MINTiMINT-598890.
STRINGi4932.YKR066C.

Structurei

Secondary structure

1
361
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi83 – 9917Combined sources
Turni100 – 1023Combined sources
Helixi103 – 1064Combined sources
Helixi110 – 12112Combined sources
Turni126 – 1283Combined sources
Beta strandi131 – 1333Combined sources
Helixi137 – 1393Combined sources
Helixi141 – 1444Combined sources
Helixi147 – 1493Combined sources
Turni150 – 1523Combined sources
Helixi153 – 16513Combined sources
Beta strandi167 – 1693Combined sources
Helixi171 – 18515Combined sources
Helixi202 – 2043Combined sources
Turni208 – 2103Combined sources
Helixi218 – 2269Combined sources
Turni227 – 2293Combined sources
Helixi232 – 2398Combined sources
Helixi240 – 2434Combined sources
Beta strandi244 – 2474Combined sources
Helixi249 – 2524Combined sources
Beta strandi256 – 2605Combined sources
Beta strandi262 – 2643Combined sources
Helixi268 – 2758Combined sources
Beta strandi278 – 2825Combined sources
Beta strandi284 – 2863Combined sources
Beta strandi288 – 2925Combined sources
Turni293 – 2953Combined sources
Beta strandi296 – 2983Combined sources
Helixi300 – 3078Combined sources
Helixi309 – 31911Combined sources
Helixi322 – 33817Combined sources
Beta strandi345 – 3473Combined sources
Helixi356 – 3594Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
4CVIOther2.10A70-361[»]
4CVJOther2.18A71-361[»]
4JB4X-ray2.39A/C68-361[»]
4NFGX-ray2.11A71-361[»]
5CCPX-ray2.20A68-361[»]
6CCPX-ray2.20A68-361[»]
7CCPX-ray2.20A68-361[»]
ProteinModelPortaliP00431.
SMRiP00431. Positions 43-361.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00431.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0376.
HOGENOMiHOG000189824.
InParanoidiP00431.
KOiK00428.
OMAiWRPGRID.
OrthoDBiEOG754J0N.

Family and domain databases

InterProiIPR002207. Asc_peroxidase.
IPR010255. Haem_peroxidase.
IPR002016. Haem_peroxidase_pln/fun/bac.
IPR019794. Peroxidases_AS.
IPR019793. Peroxidases_heam-ligand_BS.
[Graphical view]
PfamiPF00141. peroxidase. 1 hit.
[Graphical view]
PRINTSiPR00459. ASPEROXIDASE.
PR00458. PEROXIDASE.
SUPFAMiSSF48113. SSF48113. 1 hit.
PROSITEiPS00435. PEROXIDASE_1. 1 hit.
PS00436. PEROXIDASE_2. 1 hit.
PS50873. PEROXIDASE_4. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P00431-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MTTAVRLLPS LGRTAHKRSL YLFSAAAAAA AAATFAYSQS QKRSSSSPGG
60 70 80 90 100
GSNHGWNNWG KAAALASTTP LVHVASVEKG RSYEDFQKVY NAIALKLRED
110 120 130 140 150
DEYDNYIGYG PVLVRLAWHT SGTWDKHDNT GGSYGGTYRF KKEFNDPSNA
160 170 180 190 200
GLQNGFKFLE PIHKEFPWIS SGDLFSLGGV TAVQEMQGPK IPWRCGRVDT
210 220 230 240 250
PEDTTPDNGR LPDADKDADY VRTFFQRLNM NDREVVALMG AHALGKTHLK
260 270 280 290 300
NSGYEGPWGA ANNVFTNEFY LNLLNEDWKL EKNDANNEQW DSKSGYMMLP
310 320 330 340 350
TDYSLIQDPK YLSIVKEYAN DQDKFFKDFS KAFEKLLENG ITFPKDAPSP
360
FIFKTLEEQG L
Length:361
Mass (Da):40,353
Last modified:June 1, 1994 - v2
Checksum:iA5D26385DA6F0A0B
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti41 – 411Q → H in AAA88709. (PubMed:8196765)Curated
Sequence conflicti62 – 621A → P in AAA88709. (PubMed:8196765)Curated
Sequence conflicti145 – 1462ND → DN AA sequence (PubMed:6257176)Curated
Sequence conflicti231 – 2311Missing AA sequence (PubMed:6257176)Curated
Sequence conflicti273 – 2731L → M in AAS56247. (PubMed:17322287)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti33 – 331A → AA in allele 2.
Natural varianti120 – 1201T → I in allele 2.
Natural varianti219 – 2191D → G in allele 2.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiS19064. OPBYC.
RefSeqiNP_012992.1. NM_001179856.1.

Genome annotation databases

EnsemblFungiiYKR066C; YKR066C; YKR066C.
GeneIDi853940.
KEGGisce:YKR066C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 .
PIRi S19064. OPBYC.
RefSeqi NP_012992.1. NM_001179856.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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 [» ]
2X07 X-ray 1.86 A 69-361 [» ]
2X08 X-ray 2.01 A 69-361 [» ]
2XIL X-ray 1.68 A 71-361 [» ]
2XJ5 X-ray 1.69 A 71-361 [» ]
2XJ8 X-ray 1.69 A 71-361 [» ]
2Y5A X-ray 1.25 A 71-361 [» ]
2YCG X-ray 1.81 A 68-361 [» ]
3CCP X-ray 2.20 A 68-361 [» ]
3CCX X-ray 2.30 A 71-361 [» ]
3E2N X-ray 1.30 A 68-96 [» ]
A 110-361 [» ]
3E2O X-ray 1.06 A 68-361 [» ]
3EXB X-ray 1.60 A 68-361 [» ]
3M23 X-ray 1.40 A 71-361 [» ]
3M25 X-ray 1.40 A 71-361 [» ]
3M26 X-ray 1.40 A 71-361 [» ]
3M27 X-ray 1.40 A 71-361 [» ]
3M28 X-ray 1.40 A 71-361 [» ]
3M29 X-ray 1.40 A 71-361 [» ]
3M2A X-ray 1.40 A 71-361 [» ]
3M2B X-ray 1.40 A 71-361 [» ]
3M2C X-ray 1.40 A 71-361 [» ]
3M2D X-ray 1.40 A 71-361 [» ]
3M2E X-ray 1.40 A 71-361 [» ]
3M2F X-ray 1.40 A 71-361 [» ]
3M2G X-ray 1.40 A 71-361 [» ]
3M2H X-ray 1.40 A 71-361 [» ]
3M2I X-ray 1.40 A 71-361 [» ]
3R98 Other 2.40 A 69-361 [» ]
3R99 Other 2.40 A 69-361 [» ]
4A6Z X-ray 1.61 A 68-361 [» ]
4A71 X-ray 1.61 A 68-361 [» ]
4A78 X-ray 2.01 A 68-361 [» ]
4A7M X-ray 1.71 A 68-361 [» ]
4CCP X-ray 2.20 A 68-361 [» ]
4CCX X-ray 1.90 A 71-361 [» ]
4CVI Other 2.10 A 70-361 [» ]
4CVJ Other 2.18 A 71-361 [» ]
4JB4 X-ray 2.39 A/C 68-361 [» ]
4NFG X-ray 2.11 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 [» ]
ProteinModelPortali P00431.
SMRi P00431. Positions 43-361.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 34197. 22 interactions.
DIPi DIP-6251N.
IntActi P00431. 5 interactions.
MINTi MINT-598890.
STRINGi 4932.YKR066C.

Protein family/group databases

PeroxiBasei 2361. SceCcP01.

Proteomic databases

MaxQBi P00431.
PaxDbi P00431.
PeptideAtlasi P00431.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YKR066C ; YKR066C ; YKR066C .
GeneIDi 853940.
KEGGi sce:YKR066C.

Organism-specific databases

CYGDi YKR066c.
SGDi S000001774. CCP1.

Phylogenomic databases

eggNOGi COG0376.
HOGENOMi HOG000189824.
InParanoidi P00431.
KOi K00428.
OMAi WRPGRID.
OrthoDBi EOG754J0N.

Enzyme and pathway databases

BioCyci YEAST:YKR066C-MONOMER.
SABIO-RK P00431.

Miscellaneous databases

EvolutionaryTracei P00431.
NextBioi 975327.
PMAP-CutDB P00431.

Gene expression databases

Genevestigatori P00431.

Family and domain databases

InterProi IPR002207. Asc_peroxidase.
IPR010255. Haem_peroxidase.
IPR002016. Haem_peroxidase_pln/fun/bac.
IPR019794. Peroxidases_AS.
IPR019793. Peroxidases_heam-ligand_BS.
[Graphical view ]
Pfami PF00141. peroxidase. 1 hit.
[Graphical view ]
PRINTSi PR00459. ASPEROXIDASE.
PR00458. PEROXIDASE.
SUPFAMi SSF48113. SSF48113. 1 hit.
PROSITEi PS00435. PEROXIDASE_1. 1 hit.
PS00436. PEROXIDASE_2. 1 hit.
PS50873. PEROXIDASE_4. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  5. 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. 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).

Entry informationi

Entry nameiCCPR_YEAST
AccessioniPrimary (citable) accession number: P00431
Secondary accession number(s): D6VXC7, Q6Q5M9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: June 1, 1994
Last modified: November 26, 2014
This is version 166 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 6730 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome XI
    Yeast (Saccharomyces cerevisiae) chromosome XI: entries and gene names

External Data

Dasty 3