Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P25819

- CATA2_ARATH

UniProt

P25819 - CATA2_ARATH

Protein

Catalase-2

Gene

CAT2

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 141 (01 Oct 2014)
      Sequence version 3 (13 Dec 2001)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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: TAIR
    2. cobalt ion binding Source: TAIR
    3. heme binding Source: InterPro
    4. protein binding Source: UniProtKB

    GO - Biological processi

    1. cell death Source: TAIR
    2. cell redox homeostasis Source: TAIR
    3. cellular response to nitrogen starvation Source: TAIR
    4. cellular response to phosphate starvation Source: TAIR
    5. cellular response to sulfate starvation Source: TAIR
    6. hydrogen peroxide catabolic process Source: UniProtKB-KW
    7. photoperiodism Source: TAIR
    8. response to cold Source: TAIR
    9. response to light stimulus Source: TAIR
    10. response to oxidative stress Source: TAIR

    Keywords - Molecular functioni

    Oxidoreductase, Peroxidase

    Keywords - Biological processi

    Hydrogen peroxide

    Keywords - Ligandi

    Heme, Iron, Metal-binding

    Enzyme and pathway databases

    BioCyciARA:GQT-2443-MONOMER.
    MetaCyc:AT4G35090-MONOMER.

    Protein family/group databases

    PeroxiBasei5141. AtKat02.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Catalase-2 (EC:1.11.1.6)
    Gene namesi
    Name:CAT2
    Synonyms:CAT
    Ordered Locus Names:At4g35090
    ORF Names:M4E13.140
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    ProteomesiUP000006548: Chromosome 4

    Organism-specific databases

    TAIRiAT4G35090.

    Subcellular locationi

    GO - Cellular componenti

    1. chloroplast Source: TAIR
    2. cytosolic ribosome Source: TAIR
    3. glyoxysome Source: UniProtKB-SubCell
    4. mitochondrion Source: TAIR
    5. peroxisome Source: TAIR
    6. stromule Source: TAIR

    Keywords - Cellular componenti

    Glyoxysome, Peroxisome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 492492Catalase-2PRO_0000084931Add
    BLAST

    Proteomic databases

    PaxDbiP25819.
    PRIDEiP25819.

    Expressioni

    Gene expression databases

    ArrayExpressiP25819.
    GenevestigatoriP25819.

    Interactioni

    Subunit structurei

    Homotetramer and heterotetramer. At least six or seven isozymes are produced from a mixture of 3 gene products.

    Protein-protein interaction databases

    BioGridi14943. 3 interactions.
    IntActiP25819. 3 interactions.

    Structurei

    3D structure databases

    ProteinModelPortaliP25819.
    SMRiP25819. Positions 17-488.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the catalase family.Curated

    Phylogenomic databases

    eggNOGiCOG0753.
    HOGENOMiHOG000087852.
    InParanoidiP25819.
    KOiK03781.
    OMAiDPTKLWY.
    PhylomeDBiP25819.

    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.

    This entry describes 1 isoform i produced by alternative splicing. Align

    Note: A number of isoforms are produced. According to EST sequences.

    Isoform 1 (identifier: P25819-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MDPYKYRPAS SYNSPFFTTN SGAPVWNNNS SMTVGPRGPI LLEDYHLVEK    50
    LANFDRERIP ERVVHARGAS AKGFFEVTHD ISNLTCADFL RAPGVQTPVI 100
    VRFSTVIHER GSPETLRDPR GFAVKFYTRE GNFDLVGNNF PVFFIRDGMK 150
    FPDMVHALKP NPKSHIQENW RILDFFSHHP ESLNMFTFLF DDIGIPQDYR 200
    HMDGSGVNTY MLINKAGKAH YVKFHWKPTC GVKSLLEEDA IRVGGTNHSH 250
    ATQDLYDSIA AGNYPEWKLF IQIIDPADED KFDFDPLDVT KTWPEDILPL 300
    QPVGRMVLNK NIDNFFAENE QLAFCPAIIV PGIHYSDDKL LQTRVFSYAD 350
    TQRHRLGPNY LQLPVNAPKC AHHNNHHEGF MNFMHRDEEV NYFPSRYDQV 400
    RHAEKYPTPP AVCSGKRERC IIEKENNFKE PGERYRTFTP ERQERFIQRW 450
    IDALSDPRIT HEIRSIWISY WSQADKSLGQ KLASRLNVRP SI 492
    Length:492
    Mass (Da):56,931
    Last modified:December 13, 2001 - v3
    Checksum:iAB622230561FD79B
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti39 – 391P → L in CAA45564. (PubMed:16669103)Curated
    Sequence conflicti109 – 1091E → A in CAA45564. (PubMed:16669103)Curated
    Sequence conflicti154 – 1541M → I in CAA45564. (PubMed:16669103)Curated
    Sequence conflicti243 – 2431V → L in CAA45564. (PubMed:16669103)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti421 – 4211I → V in strain: cv. Landsberg erecta.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X64271 mRNA. Translation: CAA45564.1.
    X94447 Genomic DNA. Translation: CAA64220.1.
    AL022023 Genomic DNA. Translation: CAA17773.1.
    AL161586 Genomic DNA. Translation: CAB80226.1.
    CP002687 Genomic DNA. Translation: AEE86462.1.
    AY074301 mRNA. Translation: AAL66998.1.
    AY113854 mRNA. Translation: AAM44902.1.
    PIRiT05779.
    RefSeqiNP_195235.1. NM_119675.3. [P25819-1]
    UniGeneiAt.24350.
    At.64718.

    Genome annotation databases

    EnsemblPlantsiAT4G35090.1; AT4G35090.1; AT4G35090. [P25819-1]
    GeneIDi829661.
    KEGGiath:AT4G35090.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X64271 mRNA. Translation: CAA45564.1 .
    X94447 Genomic DNA. Translation: CAA64220.1 .
    AL022023 Genomic DNA. Translation: CAA17773.1 .
    AL161586 Genomic DNA. Translation: CAB80226.1 .
    CP002687 Genomic DNA. Translation: AEE86462.1 .
    AY074301 mRNA. Translation: AAL66998.1 .
    AY113854 mRNA. Translation: AAM44902.1 .
    PIRi T05779.
    RefSeqi NP_195235.1. NM_119675.3. [P25819-1 ]
    UniGenei At.24350.
    At.64718.

    3D structure databases

    ProteinModelPortali P25819.
    SMRi P25819. Positions 17-488.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 14943. 3 interactions.
    IntActi P25819. 3 interactions.

    Protein family/group databases

    PeroxiBasei 5141. AtKat02.

    Proteomic databases

    PaxDbi P25819.
    PRIDEi P25819.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi AT4G35090.1 ; AT4G35090.1 ; AT4G35090 . [P25819-1 ]
    GeneIDi 829661.
    KEGGi ath:AT4G35090.

    Organism-specific databases

    TAIRi AT4G35090.

    Phylogenomic databases

    eggNOGi COG0753.
    HOGENOMi HOG000087852.
    InParanoidi P25819.
    KOi K03781.
    OMAi DPTKLWY.
    PhylomeDBi P25819.

    Enzyme and pathway databases

    BioCyci ARA:GQT-2443-MONOMER.
    MetaCyc:AT4G35090-MONOMER.

    Gene expression databases

    ArrayExpressi P25819.
    Genevestigatori P25819.

    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. "Nucleotide sequence of a cDNA for catalase from Arabidopsis thaliana."
      Chevalier C., Yamaguchi J., McCourt P.
      Plant Physiol. 99:1726-1728(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: cv. Columbia.
    2. "A gene encoding a catalase isoform from Arabidopsis thaliana."
      Zentgraf U., Zinkernagel I.
      Plant Gene Register PGR96-005
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: cv. Landsberg erecta.
    3. "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana."
      Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B.
      , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R.
      Nature 402:769-777(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: cv. Columbia.
    4. The Arabidopsis Information Resource (TAIR)
      Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
      Cited for: GENOME REANNOTATION.
      Strain: cv. Columbia.
    5. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
      Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
      , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
      Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: cv. Columbia.

    Entry informationi

    Entry nameiCATA2_ARATH
    AccessioniPrimary (citable) accession number: P25819
    Secondary accession number(s): O49615
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 1, 1992
    Last sequence update: December 13, 2001
    Last modified: October 1, 2014
    This is version 141 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Arabidopsis thaliana
      Arabidopsis thaliana: entries and gene names
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3