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Q01297 (CATA1_RICCO) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 84. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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 isozyme 1

EC=1.11.1.6
Gene names
Name:CAT1
OrganismRicinus communis (Castor bean)
Taxonomic identifier3988 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsMalpighialesEuphorbiaceaeAcalyphoideaeAcalypheaeRicinus

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.

Subcellular location

Peroxisome Potential. Glyoxysome Potential.

Tissue specificity

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

Sequence similarities

Belongs to the catalase family.

Ontologies

Keywords
   Biological processHydrogen peroxide
   Cellular componentGlyoxysome
Peroxisome
   LigandHeme
Iron
Metal-binding
   Molecular functionOxidoreductase
Peroxidase
Gene Ontology (GO)
   Biological_processhydrogen peroxide catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentglyoxysome

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functioncatalase activity

Inferred from electronic annotation. Source: UniProtKB-EC

heme binding

Inferred from electronic annotation. Source: InterPro

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 492492Catalase isozyme 1
PRO_0000084956

Sites

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

Experimental info

Sequence conflict4391A → P in CAA42215. Ref.2
Sequence conflict4461F → S in CAA42215. Ref.2
Sequence conflict4541L → F Ref.2
Sequence conflict4561D → E Ref.2
Sequence conflict4611H → Q in CAA42215. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q01297 [UniParc].

Last modified February 1, 1996. Version 2.
Checksum: B5E28A425088BF63

FASTA49256,464
        10         20         30         40         50         60 
MDPYRNRPSS GFNTPFWTTN SGAPVWNNNS SLTVGSRGPI LLEDYHLIEK LANFDRERIP 

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

       130        140        150        160        170        180 
GFAVKFYTRE GNFDLVGNNF PVFFIRDGMK FPDVVHAFKP NPKSHLQENW RIFDFLSHVP 

       190        200        210        220        230        240 
ESLHMLTFLL DDLGIPQDYR HMEGSGVNTY TLINKAGKVH YVKFHWKPTC GVKCLLENEA 

       250        260        270        280        290        300 
IKVGGSNHSH ATQDLYDSIS AGNYPEWKLY IQIMDPAHED KFDFDPLDVT KTWPEDILPL 

       310        320        330        340        350        360 
QPVGRLVLNK NIDNFFAENE QLAFCPGIVV PGVSYSEDKL LQTRIFSYSD TQRHRLGPNY 

       370        380        390        400        410        420 
LQLPVNAPKC AHHNNHHEGF MNFMHRDEEV NYFPSRCDPA RNAESFPVPS AICSGKREKC 

       430        440        450        460        470        480 
VIEKENNFKQ PGERYRSWAP DRQERFLNRL VGGLSDPRIT HELRTIWISY WIQCDKSLGQ 

       490 
KLATRLNVKP SI 

« Hide

References

[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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D21161 Genomic DNA. Translation: BAA04697.1.
X59694 mRNA. Translation: CAA42215.1.
PIRS46297.

3D structure databases

ProteinModelPortalQ01297.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEQ01297.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

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_RICCO
AccessionPrimary (citable) accession number: Q01297
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: February 1, 1996
Last modified: February 19, 2014
This is version 84 of the entry and version 2 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