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Reviewed, UniProtKB/Swiss-Prot Q01297 (CATA1_RICCO)

Last modified June 16, 2009. Version 61. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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 lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsrosidseurosids IMalpighialesEuphorbiaceaeAcalyphoideaeAcalypheaeRicinus

Protein attributes

Sequence length492 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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

oxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentglyoxysome

Inferred from electronic annotation. Source: UniProtKB-SubCell

peroxisome

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functioncatalase activity

Inferred from electronic annotation. Source: EC

heme binding

Inferred from electronic annotation. Source: InterPro

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
Q01297-1 [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: 8049373] [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: 1712298] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 404-492.
Strain: cv. Hale.

Cross-references

Sequence databases

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

3D structure databases

HSSPHSSP built from PDB template 1M7S based on UniProtKB P46206.
ModBaseSearch...

Enzyme and pathway databases

BRENDA1.11.1.6. 816.

Family and domain databases

InterProIPR002226. Catalase.
IPR010582. Catalase-rel_immune_responsive.
IPR011614. Catalase_N.
IPR018028. Catalase_rel_subgroup.
[Graphical view]
Gene3DG3DSA:2.40.180.10. Catalase_N. 1 hit.
PANTHERPTHR11465. Catalase. 1 hit.
PfamPF00199. Catalase. 1 hit.
PF06628. Catalase-rel. 1 hit.
[Graphical view]
PRINTSPR00067. CATALASE.
ProDomPD000510. Catalase. 1 hit.
[Graphical view] [Entries sharing at least one domain]
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: June 16, 2009
This is version 61 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents