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P25819

- CATA2_ARATH

UniProt

P25819 - CATA2_ARATH

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Protein

Catalase-2

Gene

CAT2

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli

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

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
Complete GO annotation...

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-KW
  4. mitochondrion Source: TAIR
  5. peroxisome Source: TAIR
  6. stromule Source: TAIR
Complete GO annotation...

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

ExpressionAtlasiP25819. baseline and differential.
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.
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

        10         20         30         40         50
MDPYKYRPAS SYNSPFFTTN SGAPVWNNNS SMTVGPRGPI LLEDYHLVEK
60 70 80 90 100
LANFDRERIP ERVVHARGAS AKGFFEVTHD ISNLTCADFL RAPGVQTPVI
110 120 130 140 150
VRFSTVIHER GSPETLRDPR GFAVKFYTRE GNFDLVGNNF PVFFIRDGMK
160 170 180 190 200
FPDMVHALKP NPKSHIQENW RILDFFSHHP ESLNMFTFLF DDIGIPQDYR
210 220 230 240 250
HMDGSGVNTY MLINKAGKAH YVKFHWKPTC GVKSLLEEDA IRVGGTNHSH
260 270 280 290 300
ATQDLYDSIA AGNYPEWKLF IQIIDPADED KFDFDPLDVT KTWPEDILPL
310 320 330 340 350
QPVGRMVLNK NIDNFFAENE QLAFCPAIIV PGIHYSDDKL LQTRVFSYAD
360 370 380 390 400
TQRHRLGPNY LQLPVNAPKC AHHNNHHEGF MNFMHRDEEV NYFPSRYDQV
410 420 430 440 450
RHAEKYPTPP AVCSGKRERC IIEKENNFKE PGERYRTFTP ERQERFIQRW
460 470 480 490
IDALSDPRIT HEIRSIWISY WSQADKSLGQ KLASRLNVRP SI
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.
KOi K03781.
OMAi DPTKLWY.
PhylomeDBi P25819.

Enzyme and pathway databases

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

Gene expression databases

ExpressionAtlasi P25819. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 142 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