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P00431

- CCPR_YEAST

UniProt

P00431 - CCPR_YEAST

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
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    • History
      Entry version 164 (01 Oct 2014)
      Sequence version 2 (01 Jun 1994)
      Previous versions | rss
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    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

    Binds 1 heme B (iron-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
    4. protein binding Source: IntAct

    GO - Biological processi

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

    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
    2. mitochondrial matrix Source: UniProtKB-SubCell

    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. 21 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 – 9917
    Turni100 – 1023
    Helixi103 – 1064
    Helixi110 – 12112
    Turni126 – 1283
    Beta strandi131 – 1333
    Helixi137 – 1393
    Helixi141 – 1444
    Helixi147 – 1493
    Turni150 – 1523
    Helixi153 – 16513
    Beta strandi167 – 1693
    Helixi171 – 18515
    Helixi202 – 2043
    Turni208 – 2103
    Helixi218 – 2269
    Turni227 – 2293
    Helixi232 – 2398
    Helixi240 – 2434
    Beta strandi244 – 2474
    Helixi249 – 2524
    Beta strandi256 – 2605
    Beta strandi262 – 2643
    Helixi268 – 2758
    Beta strandi278 – 2825
    Beta strandi284 – 2863
    Beta strandi288 – 2925
    Turni293 – 2953
    Beta strandi296 – 2983
    Helixi300 – 3078
    Helixi309 – 31911
    Helixi322 – 33817
    Beta strandi345 – 3473
    Helixi356 – 3594

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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[»]
    4JB4X-ray2.39A/C68-361[»]
    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.
    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

    MTTAVRLLPS LGRTAHKRSL YLFSAAAAAA AAATFAYSQS QKRSSSSPGG    50
    GSNHGWNNWG KAAALASTTP LVHVASVEKG RSYEDFQKVY NAIALKLRED 100
    DEYDNYIGYG PVLVRLAWHT SGTWDKHDNT GGSYGGTYRF KKEFNDPSNA 150
    GLQNGFKFLE PIHKEFPWIS SGDLFSLGGV TAVQEMQGPK IPWRCGRVDT 200
    PEDTTPDNGR LPDADKDADY VRTFFQRLNM NDREVVALMG AHALGKTHLK 250
    NSGYEGPWGA ANNVFTNEFY LNLLNEDWKL EKNDANNEQW DSKSGYMMLP 300
    TDYSLIQDPK YLSIVKEYAN DQDKFFKDFS KAFEKLLENG ITFPKDAPSP 350
    FIFKTLEEQG L 361
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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:
    PDBe
    RCSB PDB
    PDBj
    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 [» ]
    4JB4 X-ray 2.39 A/C 68-361 [» ]
    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. 21 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.
    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

    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: October 1, 2014
    This is version 164 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