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Q01297

- CATA1_RICCO

UniProt

Q01297 - CATA1_RICCO

Protein

Catalase isozyme 1

Gene

CAT1

Organism
Ricinus communis (Castor bean)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 85 (01 Oct 2014)
      Sequence version 2 (01 Feb 1996)
      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 sitei65 – 651PROSITE-ProRule annotation
    Active sitei138 – 1381PROSITE-ProRule annotation
    Metal bindingi348 – 3481Iron (heme axial ligand)By similarity

    GO - Molecular functioni

    1. catalase activity Source: UniProtKB-EC
    2. heme binding Source: InterPro
    3. metal ion binding Source: UniProtKB-KW

    GO - Biological processi

    1. hydrogen peroxide catabolic process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Oxidoreductase, Peroxidase

    Keywords - Biological processi

    Hydrogen peroxide

    Keywords - Ligandi

    Heme, Iron, Metal-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Catalase isozyme 1 (EC:1.11.1.6)
    Gene namesi
    Name:CAT1
    OrganismiRicinus communis (Castor bean)
    Taxonomic identifieri3988 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsMalpighialesEuphorbiaceaeAcalyphoideaeAcalypheaeRicinus

    Subcellular locationi

    Peroxisome Curated. Glyoxysome Curated

    GO - Cellular componenti

    1. glyoxysome Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Glyoxysome, Peroxisome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 492492Catalase isozyme 1PRO_0000084956Add
    BLAST

    Proteomic databases

    PRIDEiQ01297.

    Expressioni

    Tissue specificityi

    Abundant in endosperms and cotyledons. Only in small amount in root.

    Interactioni

    Subunit structurei

    Homotetramer.

    Structurei

    3D structure databases

    ProteinModelPortaliQ01297.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the catalase family.Curated

    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.

    Q01297-1 [UniParc]FASTAAdd to Basket

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    MDPYRNRPSS GFNTPFWTTN SGAPVWNNNS SLTVGSRGPI LLEDYHLIEK    50
    LANFDRERIP ERVVHARGAS AKGFFEVTHD VSHLTCADFL RAPGVQTPVI 100
    VRFSTVIHER GSPETLRDPR GFAVKFYTRE GNFDLVGNNF PVFFIRDGMK 150
    FPDVVHAFKP NPKSHLQENW RIFDFLSHVP ESLHMLTFLL DDLGIPQDYR 200
    HMEGSGVNTY TLINKAGKVH YVKFHWKPTC GVKCLLENEA IKVGGSNHSH 250
    ATQDLYDSIS AGNYPEWKLY IQIMDPAHED KFDFDPLDVT KTWPEDILPL 300
    QPVGRLVLNK NIDNFFAENE QLAFCPGIVV PGVSYSEDKL LQTRIFSYSD 350
    TQRHRLGPNY LQLPVNAPKC AHHNNHHEGF MNFMHRDEEV NYFPSRCDPA 400
    RNAESFPVPS AICSGKREKC VIEKENNFKQ PGERYRSWAP DRQERFLNRL 450
    VGGLSDPRIT HELRTIWISY WIQCDKSLGQ KLATRLNVKP SI 492
    Length:492
    Mass (Da):56,464
    Last modified:February 1, 1996 - v2
    Checksum:iB5E28A425088BF63
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti439 – 4391A → P in CAA42215. (PubMed:1712298)Curated
    Sequence conflicti446 – 4461F → S in CAA42215. (PubMed:1712298)Curated
    Sequence conflicti454 – 4541L → F(PubMed:1712298)Curated
    Sequence conflicti456 – 4561D → E(PubMed:1712298)Curated
    Sequence conflicti461 – 4611H → Q in CAA42215. (PubMed:1712298)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D21161 Genomic DNA. Translation: BAA04697.1.
    X59694 mRNA. Translation: CAA42215.1.
    PIRiS46297.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D21161 Genomic DNA. Translation: BAA04697.1 .
    X59694 mRNA. Translation: CAA42215.1 .
    PIRi S46297.

    3D structure databases

    ProteinModelPortali Q01297.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PRIDEi Q01297.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    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. "Isolation and characterization of two tightly linked catalase genes from castor bean that are differentially regulated."
      Suzuki M., Ario T., Hattori T., Nakamura K., Asahi T.
      Plant Mol. Biol. 25:507-516(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Tissue: Hypocotyl.
    2. "The C-terminal domain of plant catalases. Implications for a glyoxysomal targeting sequence."
      Gonzalez E.
      Eur. J. Biochem. 199:211-215(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 404-492.
      Strain: cv. Hale.

    Entry informationi

    Entry nameiCATA1_RICCO
    AccessioniPrimary (citable) accession number: Q01297
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1993
    Last sequence update: February 1, 1996
    Last modified: October 1, 2014
    This is version 85 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3