Skip Header

 
Contribute Send feedback

Reviewed, UniProtKB/Swiss-Prot P48351 (CATA2_CUCPE)

Last modified November 25, 2008. Version 45. 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 2
    EC=1.11.1.6
Gene names
Name: CAT2
OrganismCucurbita pepo (Vegetable marrow) (Summer squash)
Taxonomic identifier3663 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsrosidseurosids ICucurbitalesCucurbitaceaeCucurbita

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 H(2)O(2) = O(2) + 2 H(2)O.

Cofactor

Heme group By similarity.

Subunit structure

Homotetramer By similarity.

Subcellular location

PeroxisomeProbable.

Tissue specificity

High levels in green cotyledons, mature leaf, stem and green hypocotyl.

Sequence similarities

Belongs to the catalase family.

Ontologies

Keywords

   Biological processHydrogen peroxide
   Cellular componentPeroxisome
   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 componentperoxisome

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functioncatalase activity

Inferred from electronic annotation. Source: InterPro

iron 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 2
PRO_0000084936

Sites

Active site651 By similarity
Active site1381 By similarity
Metal binding3471Iron (heme axial ligand) By similarity

Sequences

Sequence LengthMass (Da)Tools
P48351-1 [UniParc].

Last modified February 1, 1996. Version 1.
Checksum: 1D3C97F8E026D600

FASTA49256,953
        10         20         30         40         50         60 
MDPYKYRPSS AYNTPFCTTN SGAPIWNNTA VMSVGERGPI LLEDYQLIEK IATFTRERIP 

        70         80         90        100        110        120 
ERVVHARGAS AKGFFEVTHD VSDLSCADFL RAPGVQTPVI VRFSTVIHER VSPETVRDPR 

       130        140        150        160        170        180 
GFAVKFYTRE GNFDLVGNNF PVFFVRDAMQ FPDVIRAFKP NPKSHLQESW RFLDFCSYHP 

       190        200        210        220        230        240 
ESLLSFAWFY DDVGIPINYR HMEGFGVQAY SLINKAGKAR LVKFHWKPTC GVKSMLEEEA 

       250        260        270        280        290        300 
IRVGGSNHSH ATQDLYESIA AGNFPEWRLY IQTIDYEDQN NYDFEPLDTT IAWPEDVVPL 

       310        320        330        340        350        360 
RPVGRLVLNK NIDNFFAENE MLAFSMSLVP GIHYSDDKML QARSFAYADT QRHRLGPNYL 

       370        380        390        400        410        420 
QLPVNAPKCP HHNNHHEGFM NFMHRDEEVN YFPSRYDACR HAEKYPMPPN VLSGKRERCV 

       430        440        450        460        470        480 
IPKENHNFKQ AGDRYRSWAP DRQERFVNRF VEALSDSKVT HEVRNIWISY WTQADRSLGQ 

       490 
KIASRMNARP NM 

« Hide

References

[1]"cDNA cloning and differential gene expression of three catalases in pumpkin."
Esaka M., Yamada N., Kitabayashi M., Setoguchi Y., Tsugeki R., Kondo M., Nishimura M.
Plant Mol. Biol. 33:141-155(1997) [PubMed: 9037166] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Cotyledon.

Cross-references

Sequence databases

D55646 mRNA. Translation: BAA09507.1.
PIRT09754.

3D structure databases

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

Family and domain databases

InterProIPR002226. Catalase.
IPR011614. Catalase_N.
[Graphical view]
Gene3DG3DSA:2.40.180.10. Catalase_N. 1 hit.
PANTHERPTHR11465. Catalase. 1 hit.
PfamPF00199. Catalase. 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 nameCATA2_CUCPE
AccessionPrimary (citable) accession number: P48351
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: November 25, 2008
This is version 45 of the entry and version 1 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