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Q96528 (CATA1_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 115. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Catalase-1

EC=1.11.1.6
Gene names
Name:CAT1
Ordered Locus Names:At1g20630
ORF Names:F2D10.11, F5M15.31
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

Cytoplasm Potential.

Induction

By hydrogen peroxide. By abscisic acid (ABA), drought, and salt stress through the MKK1-MPK6 mediation. Ref.6 Ref.7

Sequence similarities

Belongs to the catalase family.

Sequence caution

The sequence AAF79625.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence AAF80611.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
   Biological processHydrogen peroxide
   Cellular componentCytoplasm
   LigandHeme
Iron
Metal-binding
   Molecular functionOxidoreductase
Peroxidase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcellular 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 genetic interaction PubMed 21665322. Source: TAIR

response to abscisic acid

Inferred from expression pattern Ref.7. Source: TAIR

response to cadmium ion

Inferred from expression pattern PubMed 16502469. Source: TAIR

response to hydrogen peroxide

Inferred from expression pattern Ref.7. Source: TAIR

response to light stimulus

Inferred from expression pattern PubMed 15608336. Source: TAIR

   Cellular_componentcell wall

Inferred from direct assay PubMed 16287169. Source: TAIR

chloroplast envelope

Inferred from direct assay PubMed 12938931. Source: TAIR

cytosolic ribosome

Inferred from direct assay PubMed 15821981. Source: TAIR

mitochondrion

Inferred from direct assay PubMed 14671022. Source: TAIR

peroxisome

Inferred from direct assay PubMed 17951448. Source: TAIR

   Molecular_functioncatalase activity

Inferred from sequence or structural similarity PubMed 9214587. Source: TAIR

cobalt ion binding

Inferred from direct assay PubMed 20018591. Source: TAIR

heme binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 492492Catalase-1
PRO_0000084930

Sites

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

Experimental info

Sequence conflict1031F → L in AAB07026. Ref.1
Sequence conflict3321G → F in AAB07026. Ref.1
Sequence conflict339 – 3402KL → NV in AAB07026. Ref.1
Sequence conflict4231G → R in AAB07026. Ref.1
Sequence conflict4231G → R in AAC17731. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q96528 [UniParc].

Last modified July 11, 2002. Version 3.
Checksum: 271E55FF7D6910EB

FASTA49256,762
        10         20         30         40         50         60 
MDPYRVRPSS AHDSPFFTTN SGAPVWNNNS SLTVGTRGPI LLEDYHLLEK LANFDRERIP 

        70         80         90        100        110        120 
ERVVHARGAS AKGFFEVTHD ITQLTSADFL RGPGVQTPVI VRFSTVIHER GSPETLRDPR 

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

       190        200        210        220        230        240 
ESLHMFSFLF DDLGIPQDYR HMEGAGVNTY MLINKAGKAH YVKFHWKPTC GIKCLSDEEA 

       250        260        270        280        290        300 
IRVGGANHSH ATKDLYDSIA AGNYPQWNLF VQVMDPAHED KFDFDPLDVT KIWPEDILPL 

       310        320        330        340        350        360 
QPVGRLVLNK NIDNFFNENE QIAFCPALVV PGIHYSDDKL LQTRIFSYAD SQRHRLGPNY 

       370        380        390        400        410        420 
LQLPVNAPKC AHHNNHHDGF MNFMHRDEEV NYFPSRLDPV RHAEKYPTTP IVCSGNREKC 

       430        440        450        460        470        480 
FIGKENNFKQ PGERYRSWDS DRQERFVKRF VEALSEPRVT HEIRSIWISY WSQADKSLGQ 

       490 
KLATRLNVRP NF 

« Hide

References

« Hide 'large scale' references
[1]"Catalase is encoded by a multigene family in Arabidopsis thaliana (L.) Heynh."
Frugoli J.A., Zhong H.H., Nuccio M.L., McCourt P., McPeek M.A., Thomas T.L., McClung C.R.
Plant Physiol. 112:327-336(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: cv. Landsberg erecta.
[2]"Intron loss and gain during evolution of the catalase gene family in angiosperms."
Frugoli J.A., McPeek M.A., Thomas T.L., McClung C.R.
Genetics 149:355-365(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: cv. Columbia.
[3]"Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."
Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K. expand/collapse author list , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.
Nature 408:816-820(2000) [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.
[6]"AtMEK1 mediates stress-induced gene expression of CAT1 catalase by triggering H2O2 production in Arabidopsis."
Xing Y., Jia W., Zhang J.
J. Exp. Bot. 58:2969-2981(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION.
[7]"AtMKK1 mediates ABA-induced CAT1 expression and H2O2 production via AtMPK6-coupled signaling in Arabidopsis."
Xing Y., Jia W., Zhang J.
Plant J. 54:440-451(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U43340 mRNA. Translation: AAB07026.1.
AF021937 Genomic DNA. Translation: AAC17731.1.
AC027665 Genomic DNA. Translation: AAF79625.1. Sequence problems.
AC069251 Genomic DNA. Translation: AAF80611.1. Sequence problems.
CP002684 Genomic DNA. Translation: AEE29998.1.
AY136424 mRNA. Translation: AAM97090.1.
BT010373 mRNA. Translation: AAQ56816.1.
RefSeqNP_564121.1. NM_101914.3.
UniGeneAt.26213.

3D structure databases

ProteinModelPortalQ96528.
SMRQ96528. Positions 10-483.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid23891. 6 interactions.
IntActQ96528. 2 interactions.

Protein family/group databases

PeroxiBase5142. AtKat01.

Proteomic databases

PaxDbQ96528.
PRIDEQ96528.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT1G20630.1; AT1G20630.1; AT1G20630.
GeneID838652.
KEGGath:AT1G20630.

Organism-specific databases

TAIRAT1G20630.

Phylogenomic databases

eggNOGCOG0753.
HOGENOMHOG000087852.
InParanoidQ96528.
KOK03781.
OMAMLNEEAK.
PhylomeDBQ96528.
ProtClustDBPLN02609.

Gene expression databases

ArrayExpressQ96528.
GenevestigatorQ96528.

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 nameCATA1_ARATH
AccessionPrimary (citable) accession number: Q96528
Secondary accession number(s): O22529, Q9LDS9
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 11, 2002
Last modified: April 16, 2014
This is version 115 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