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P15202

- CATA_YEAST

UniProt

P15202 - CATA_YEAST

Protein

Peroxisomal catalase A

Gene

CTA1

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 136 (01 Oct 2014)
      Sequence version 1 (01 Apr 1990)
      Previous versions | rss
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    Functioni

    Occurs in almost all aerobically respiring organisms and serves to protect cells from the toxic effects of hydrogen peroxide.

    Catalytic activityi

    2 H2O2 = O2 + 2 H2O.PROSITE-ProRule annotation

    Cofactori

    Heme group.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei70 – 701
    Active sitei143 – 1431
    Metal bindingi355 – 3551Iron (heme axial ligand)

    GO - Molecular functioni

    1. catalase activity Source: SGD
    2. heme binding Source: InterPro
    3. metal ion binding Source: UniProtKB-KW
    4. protein binding Source: IntAct

    GO - Biological processi

    1. age-dependent response to reactive oxygen species Source: SGD
    2. hydrogen peroxide catabolic process Source: SGD
    3. response to reactive oxygen species Source: SGD

    Keywords - Molecular functioni

    Oxidoreductase, Peroxidase

    Keywords - Biological processi

    Hydrogen peroxide

    Keywords - Ligandi

    Heme, Iron, Metal-binding

    Enzyme and pathway databases

    BioCyciYEAST:YDR256C-MONOMER.
    ReactomeiREACT_191152. Detoxification of Reactive Oxygen Species.

    Protein family/group databases

    PeroxiBasei5175. SceKat01.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Peroxisomal catalase A (EC:1.11.1.6)
    Gene namesi
    Name:CTA1
    Ordered Locus Names:YDR256C
    ORF Names:YD9320A.06C
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome IV

    Organism-specific databases

    CYGDiYDR256c.
    SGDiS000002664. CTA1.

    Subcellular locationi

    GO - Cellular componenti

    1. mitochondrial matrix Source: SGD
    2. peroxisomal matrix Source: SGD

    Keywords - Cellular componenti

    Peroxisome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 515514Peroxisomal catalase APRO_0000084928Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    PaxDbiP15202.
    PeptideAtlasiP15202.
    PRIDEiP15202.

    Expressioni

    Gene expression databases

    GenevestigatoriP15202.

    Interactioni

    Subunit structurei

    Homotetramer.

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    RSP5P399402EBI-4061,EBI-16219

    Protein-protein interaction databases

    BioGridi32306. 37 interactions.
    DIPiDIP-4320N.
    IntActiP15202. 7 interactions.
    MINTiMINT-545033.
    STRINGi4932.YDR256C.

    Structurei

    Secondary structure

    1
    515
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi31 – 344
    Beta strandi36 – 394
    Turni40 – 423
    Helixi50 – 5910
    Beta strandi72 – 8211
    Turni87 – 893
    Helixi93 – 953
    Beta strandi101 – 1099
    Beta strandi111 – 1133
    Beta strandi119 – 1235
    Beta strandi126 – 1338
    Beta strandi136 – 14712
    Helixi155 – 1639
    Turni167 – 1693
    Helixi174 – 1818
    Helixi184 – 1896
    Helixi190 – 1978
    Helixi199 – 2013
    Beta strandi202 – 2043
    Helixi206 – 2083
    Beta strandi217 – 2204
    Beta strandi226 – 23712
    Helixi244 – 25310
    Helixi257 – 26711
    Beta strandi273 – 2819
    Helixi283 – 2875
    Beta strandi289 – 2913
    Turni302 – 3043
    Beta strandi308 – 31710
    Helixi322 – 3254
    Turni326 – 3283
    Beta strandi340 – 3423
    Helixi346 – 36217
    Helixi367 – 3693
    Helixi371 – 3733
    Turni395 – 3984
    Beta strandi425 – 4273
    Beta strandi429 – 4324
    Beta strandi438 – 4403
    Helixi441 – 45414
    Helixi459 – 47113
    Helixi476 – 48712
    Helixi491 – 50111

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1A4EX-ray2.40A/B/C/D15-502[»]
    ProteinModelPortaliP15202.
    SMRiP15202. Positions 15-502.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP15202.

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi513 – 5153Microbody targeting signalSequence Analysis

    Sequence similaritiesi

    Belongs to the catalase family.Curated

    Phylogenomic databases

    eggNOGiCOG0753.
    GeneTreeiENSGT00390000018100.
    HOGENOMiHOG000087852.
    KOiK03781.
    OMAiEATTMIM.
    OrthoDBiEOG7K9KBN.

    Family and domain databases

    Gene3Di2.40.180.10. 1 hit.
    InterProiIPR018028. Catalase.
    IPR020835. Catalase-like_dom.
    IPR024708. Catalase_AS.
    IPR024711. Catalase_clade1/3.
    IPR011614. Catalase_core.
    IPR002226. Catalase_haem_BS.
    IPR010582. Catalase_immune_responsive.
    [Graphical view]
    PANTHERiPTHR11465. PTHR11465. 1 hit.
    PfamiPF00199. Catalase. 1 hit.
    PF06628. Catalase-rel. 1 hit.
    [Graphical view]
    PIRSFiPIRSF038928. Catalase_clade1-3. 1 hit.
    PRINTSiPR00067. CATALASE.
    SMARTiSM01060. Catalase. 1 hit.
    [Graphical view]
    SUPFAMiSSF56634. SSF56634. 1 hit.
    PROSITEiPS00437. CATALASE_1. 1 hit.
    PS00438. CATALASE_2. 1 hit.
    PS51402. CATALASE_3. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P15202-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSKLGQEKNE VNYSDVREDR VVTNSTGNPI NEPFVTQRIG EHGPLLLQDY    50
    NLIDSLAHFN RENIPQRNPH AHGSGAFGYF EVTDDITDIC GSAMFSKIGK 100
    RTKCLTRFST VGGDKGSADT VRDPRGFATK FYTEEGNLDW VYNNTPVFFI 150
    RDPSKFPHFI HTQKRNPQTN LRDADMFWDF LTTPENQVAI HQVMILFSDR 200
    GTPANYRSMH GYSGHTYKWS NKNGDWHYVQ VHIKTDQGIK NLTIEEATKI 250
    AGSNPDYCQQ DLFEAIQNGN YPSWTVYIQT MTERDAKKLP FSVFDLTKVW 300
    PQGQFPLRRV GKIVLNENPL NFFAQVEQAA FAPSTTVPYQ EASADPVLQA 350
    RLFSYADAHR YRLGPNFHQI PVNCPYASKF FNPAIRDGPM NVNGNFGSEP 400
    TYLANDKSYT YIQQDRPIQQ HQEVWNGPAI PYHWATSPGD VDFVQARNLY 450
    RVLGKQPGQQ KNLAYNIGIH VEGACPQIQQ RVYDMFARVD KGLSEAIKKV 500
    AEAKHASELS SNSKF 515
    Length:515
    Mass (Da):58,555
    Last modified:April 1, 1990 - v1
    Checksum:i22DFCC599D79801F
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti131 – 1311F → L in AAU09703. (PubMed:17322287)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X13028 Genomic DNA. Translation: CAA31443.1.
    Z68329 Genomic DNA. Translation: CAA92713.1.
    Z70202 Genomic DNA. Translation: CAA94095.1.
    AY723786 Genomic DNA. Translation: AAU09703.1.
    BK006938 Genomic DNA. Translation: DAA12096.1.
    PIRiS07868. CSBYP.
    RefSeqiNP_010542.1. NM_001180564.1.

    Genome annotation databases

    EnsemblFungiiYDR256C; YDR256C; YDR256C.
    GeneIDi851843.
    KEGGisce:YDR256C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X13028 Genomic DNA. Translation: CAA31443.1 .
    Z68329 Genomic DNA. Translation: CAA92713.1 .
    Z70202 Genomic DNA. Translation: CAA94095.1 .
    AY723786 Genomic DNA. Translation: AAU09703.1 .
    BK006938 Genomic DNA. Translation: DAA12096.1 .
    PIRi S07868. CSBYP.
    RefSeqi NP_010542.1. NM_001180564.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1A4E X-ray 2.40 A/B/C/D 15-502 [» ]
    ProteinModelPortali P15202.
    SMRi P15202. Positions 15-502.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 32306. 37 interactions.
    DIPi DIP-4320N.
    IntActi P15202. 7 interactions.
    MINTi MINT-545033.
    STRINGi 4932.YDR256C.

    Protein family/group databases

    PeroxiBasei 5175. SceKat01.

    Proteomic databases

    PaxDbi P15202.
    PeptideAtlasi P15202.
    PRIDEi P15202.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YDR256C ; YDR256C ; YDR256C .
    GeneIDi 851843.
    KEGGi sce:YDR256C.

    Organism-specific databases

    CYGDi YDR256c.
    SGDi S000002664. CTA1.

    Phylogenomic databases

    eggNOGi COG0753.
    GeneTreei ENSGT00390000018100.
    HOGENOMi HOG000087852.
    KOi K03781.
    OMAi EATTMIM.
    OrthoDBi EOG7K9KBN.

    Enzyme and pathway databases

    BioCyci YEAST:YDR256C-MONOMER.
    Reactomei REACT_191152. Detoxification of Reactive Oxygen Species.

    Miscellaneous databases

    EvolutionaryTracei P15202.
    NextBioi 969751.
    PROi P15202.

    Gene expression databases

    Genevestigatori P15202.

    Family and domain databases

    Gene3Di 2.40.180.10. 1 hit.
    InterProi IPR018028. Catalase.
    IPR020835. Catalase-like_dom.
    IPR024708. Catalase_AS.
    IPR024711. Catalase_clade1/3.
    IPR011614. Catalase_core.
    IPR002226. Catalase_haem_BS.
    IPR010582. Catalase_immune_responsive.
    [Graphical view ]
    PANTHERi PTHR11465. PTHR11465. 1 hit.
    Pfami PF00199. Catalase. 1 hit.
    PF06628. Catalase-rel. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF038928. Catalase_clade1-3. 1 hit.
    PRINTSi PR00067. CATALASE.
    SMARTi SM01060. Catalase. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56634. SSF56634. 1 hit.
    PROSITEi PS00437. CATALASE_1. 1 hit.
    PS00438. CATALASE_2. 1 hit.
    PS51402. CATALASE_3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Sequence of the Saccharomyces cerevisiae CTA1 gene and amino acid sequence of catalase A derived from it."
      Cohen G., Rapatz W., Ruis H.
      Eur. J. Biochem. 176:159-163(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
      Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T.
      , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
      Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    3. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    4. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    5. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    6. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    7. Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).

    Entry informationi

    Entry nameiCATA_YEAST
    AccessioniPrimary (citable) accession number: P15202
    Secondary accession number(s): D6VSN6, E9P947
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1990
    Last sequence update: April 1, 1990
    Last modified: October 1, 2014
    This is version 136 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    This is one of two catalases in S.cerevisiae; the other is catalase T, which is the cytoplasmic form.
    Present with 623 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    3D-structure, Complete proteome, 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 IV
      Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

    External Data

    Dasty 3