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P32290 (CATA_VIGRR) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 69. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Catalase

EC=1.11.1.6
OrganismVigna radiata var. radiata (Mung bean) (Phaseolus aureus)
Taxonomic identifier3916 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsrosidsfabidsFabalesFabaceaePapilionoideaePhaseoleaeVigna

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 By similarity. Glyoxysome By similarity.

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: 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
PRO_0000084955

Sites

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

Sequences

Sequence LengthMass (Da)Tools
P32290 [UniParc].

Last modified October 1, 1993. Version 1.
Checksum: 933E604D2611CE85

FASTA49256,844
        10         20         30         40         50         60 
MDPYKYRPSS AFNSPFWTTN SGAPVWNNNN SLTVGTRGPI LLEDYHLVEK LANFDRERIP 

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

       130        140        150        160        170        180 
GFAVKFYTRE GNFDLVGNNL PVFFVRDGMK FPDMVHALKP NPKNHIQENW RILDFFSHFP 

       190        200        210        220        230        240 
ESLHMFSFLF DDLGVPQDYR HMDGFGVNTY TLINKAGKAV YVKFHWKTTS GVKCLLEEEA 

       250        260        270        280        290        300 
IKVGGANHSH ATQDLHDSIA AGNYPEWKLF IQTIDPEHED KFDFDPLDVT KTWPEDIIPL 

       310        320        330        340        350        360 
QPVGRLVLNK NIDNFFAENE QLAFCPAIIV PGVYYSDDKM LQTRIFSYAD SQRHRLGPNY 

       370        380        390        400        410        420 
LLLPANAPKS AHHNNHHEGF MNFIHRDEEV NYFPSRYDPV RHAEKFPIPP AVFSGRREKI 

       430        440        450        460        470        480 
AIEKENNFKQ AGERFRSWAP DRQDRFIRRW VDALSDPRVT HEIRSVWISY WSQADRSLGQ 

       490 
KIASHLNMRP NI 

« Hide

References

[1]"cDNA for catalase from etiolated mung bean (Vigna radiata) hypocotyls."
Mori H., Imaseki H.
Plant Physiol. 102:691-692(1993) [PubMed: 8108520] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D13557 mRNA. Translation: BAA02755.1.
PIRT10902.

3D structure databases

ProteinModelPortalP32290.
ModBaseSearch...

Protein family/group databases

PeroxiBase6264. PauKat01.

Proteomic databases

PRIDEP32290.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

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]
Gene3DG3DSA:2.40.180.10. Catalase_N. 1 hit.
PANTHERPTHR11465. Catalase. 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. Catalase_N. 1 hit.
PROSITEPS00437. CATALASE_1. 1 hit.
PS00438. CATALASE_2. 1 hit.
PS51402. CATALASE_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCATA_VIGRR
AccessionPrimary (citable) accession number: P32290
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: January 25, 2012
This is version 69 of the entry and version 1 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