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P25819 (CATA2_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 137. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Catalase-2

EC=1.11.1.6
Gene names
Name:CAT2
Synonyms:CAT
Ordered Locus Names:At4g35090
ORF Names:M4E13.140
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length492 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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

Catalytic activity

2 H2O2 = O2 + 2 H2O.

Cofactor

Heme group.

Subunit structure

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

Subcellular location

Peroxisome. Glyoxysome.

Sequence similarities

Belongs to the catalase family.

Ontologies

Keywords
   Biological processHydrogen peroxide
   Cellular componentGlyoxysome
Peroxisome
   Coding sequence diversityAlternative splicing
   LigandHeme
Iron
Metal-binding
   Molecular functionOxidoreductase
Peroxidase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcell death

Inferred from mutant phenotype PubMed 17877712. Source: TAIR

cell redox homeostasis

Inferred from mutant phenotype PubMed 17877712. Source: TAIR

cellular response to nitrogen starvation

Inferred from expression pattern PubMed 15032878. Source: TAIR

cellular response to phosphate starvation

Inferred from expression pattern PubMed 15032878. Source: TAIR

cellular response to sulfate starvation

Inferred from expression pattern PubMed 15032878. Source: TAIR

hydrogen peroxide catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

photoperiodism

Inferred from mutant phenotype PubMed 17877712. Source: TAIR

response to cold

Inferred from expression pattern PubMed 16923014PubMed 18230142. Source: TAIR

response to light stimulus

Inferred from expression pattern PubMed 18230142. Source: TAIR

response to oxidative stress

Inferred from mutant phenotype PubMed 17877712. Source: TAIR

   Cellular_componentchloroplast

Inferred from direct assay PubMed 15028209. Source: TAIR

cytosolic ribosome

Inferred from direct assay PubMed 15821981. Source: TAIR

glyoxysome

Inferred from electronic annotation. Source: UniProtKB-SubCell

mitochondrion

Inferred from direct assay PubMed 14671022. Source: TAIR

peroxisome

Inferred from direct assay PubMed 17951448. Source: TAIR

stromule

Inferred from direct assay PubMed 16923014. Source: TAIR

   Molecular_functioncatalase activity

Inferred from mutant phenotype PubMed 15200641PubMed 20452979. Source: TAIR

cobalt ion binding

Inferred from direct assay PubMed 20018591. Source: TAIR

heme binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Alternative products

This entry describes 1 isoform produced by alternative splicing. [Select]

Note: A number of isoforms are produced. According to EST sequences.
Isoform 1 (identifier: P25819-1)

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 492492Catalase-2
PRO_0000084931

Sites

Active site651 By similarity
Active site1381 By similarity
Metal binding3481Iron (heme axial ligand) By similarity

Natural variations

Natural variant4211I → V in strain: cv. Landsberg erecta.

Experimental info

Sequence conflict391P → L in CAA45564. Ref.1
Sequence conflict1091E → A in CAA45564. Ref.1
Sequence conflict1541M → I in CAA45564. Ref.1
Sequence conflict2431V → L in CAA45564. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified December 13, 2001. Version 3.
Checksum: AB622230561FD79B

FASTA49256,931
        10         20         30         40         50         60 
MDPYKYRPAS SYNSPFFTTN SGAPVWNNNS SMTVGPRGPI LLEDYHLVEK LANFDRERIP 

        70         80         90        100        110        120 
ERVVHARGAS AKGFFEVTHD ISNLTCADFL RAPGVQTPVI VRFSTVIHER GSPETLRDPR 

       130        140        150        160        170        180 
GFAVKFYTRE GNFDLVGNNF PVFFIRDGMK FPDMVHALKP NPKSHIQENW RILDFFSHHP 

       190        200        210        220        230        240 
ESLNMFTFLF DDIGIPQDYR HMDGSGVNTY MLINKAGKAH YVKFHWKPTC GVKSLLEEDA 

       250        260        270        280        290        300 
IRVGGTNHSH ATQDLYDSIA AGNYPEWKLF IQIIDPADED KFDFDPLDVT KTWPEDILPL 

       310        320        330        340        350        360 
QPVGRMVLNK NIDNFFAENE QLAFCPAIIV PGIHYSDDKL LQTRVFSYAD TQRHRLGPNY 

       370        380        390        400        410        420 
LQLPVNAPKC AHHNNHHEGF MNFMHRDEEV NYFPSRYDQV RHAEKYPTPP AVCSGKRERC 

       430        440        450        460        470        480 
IIEKENNFKE PGERYRTFTP ERQERFIQRW IDALSDPRIT HEIRSIWISY WSQADKSLGQ 

       490 
KLASRLNVRP SI 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRT05779.
RefSeqNP_195235.1. NM_119675.3.
UniGeneAt.24350.
At.64718.

3D structure databases

ProteinModelPortalP25819.
SMRP25819. Positions 15-490.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid14943. 3 interactions.
IntActP25819. 3 interactions.

Protein family/group databases

PeroxiBase5141. AtKat02.

Proteomic databases

PaxDbP25819.
PRIDEP25819.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT4G35090.1; AT4G35090.1; AT4G35090. [P25819-1]
GeneID829661.
KEGGath:AT4G35090.

Organism-specific databases

TAIRAT4G35090.

Phylogenomic databases

eggNOGCOG0753.
HOGENOMHOG000087852.
InParanoidP25819.
KOK03781.
OMADPTKLWY.
PhylomeDBP25819.
ProtClustDBPLN02609.

Enzyme and pathway databases

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

Gene expression databases

ArrayExpressP25819.
GenevestigatorP25819.

Family and domain databases

Gene3D2.40.180.10. 1 hit.
InterProIPR018028. 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]
PANTHERPTHR11465. PTHR11465. 1 hit.
PfamPF00199. Catalase. 1 hit.
PF06628. Catalase-rel. 1 hit.
[Graphical view]
PIRSFPIRSF038928. Catalase_clade1-3. 1 hit.
PRINTSPR00067. CATALASE.
SMARTSM01060. Catalase. 1 hit.
[Graphical view]
SUPFAMSSF56634. SSF56634. 1 hit.
PROSITEPS00437. CATALASE_1. 1 hit.
PS00438. CATALASE_2. 1 hit.
PS51402. CATALASE_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCATA2_ARATH
AccessionPrimary (citable) accession number: P25819
Secondary accession number(s): O49615
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: December 13, 2001
Last modified: April 16, 2014
This is version 137 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names