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Q9AXH0 (CATA_AVIMR) Reviewed, UniProtKB/Swiss-Prot

Last modified March 6, 2013. Version 61. 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
OrganismAvicennia marina (Grey mangrove) (Sceura marina)
Taxonomic identifier82927 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › asterids › lamiids › Lamiales › Acanthaceae › Avicennioideae › Avicennia

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 By similarity.

Subcellular location

Peroxisome By similarity.

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

   Cellular_componentperoxisome

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functioncatalase activity

Inferred from electronic annotation. Source: 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
PRO_0000084933

Sites

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

Sequences

Sequence LengthMass (Da)Tools
Q9AXH0 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: FCC681172808F925

FASTA49257,160
        10         20         30         40         50         60 
MDPYKYCPSS SFNTPHTTTN GGHPVYNDNS SLTVGTRGPV LLEDYQLIDK LAHFTRERIP 

        70         80         90        100        110        120 
ERVVHARGAT AKGFFEVTHD VSHLTCADFL RAPGVQTPLI VRFSTVIHER GSPETLRDPR 

       130        140        150        160        170        180 
GFAVKFYTRE GNFDIVGNNF PVFFIRDAIK FPDVIHAFKP NPKSHIQESW RILDFCSHFP 

       190        200        210        220        230        240 
ESLLTFAWFY DDVGIPQDYR HMEGFGVHSY TLINKAGKVN YVKFHWKPTC GVKCLMEDEA 

       250        260        270        280        290        300 
VRIGGTNHSH ATQDLYDSIA AGNYPEWKLY FQIMDPDQED RFDFDPLDTT KIWPEDIIPL 

       310        320        330        340        350        360 
IPVGRMVLNK NIDNFFAENE MLAFSPHMIV PGINFSNDKM LQTRIFAYGD TQRHRLGPNY 

       370        380        390        400        410        420 
LLLPVNAPKC AYHNNHYDGF MNFMHRDEEV DYFPSKYDPT RHAERHPIPN AVITGRRDRR 

       430        440        450        460        470        480 
VIEKEDNFKQ AGDRYRSWAP DRQERFLRRW VDALSDPRLT LEIRSIWVSY WSQADKSFGQ 

       490 
KLASRLNVRP TM

« Hide

References

[1]"Characterization of a cDNA for catalase from the mangrove species Avicennia marina."
Jithesh M.N., Parani M., Parida A.
Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF328861 mRNA. Translation: AAK06839.1.

3D structure databases

ProteinModelPortalQ9AXH0.
ModBaseSearch...

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. 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_AVIMR
AccessionPrimary (citable) accession number: Q9AXH0
Entry history
Integrated into UniProtKB/Swiss-Prot: December 13, 2001
Last sequence update: June 1, 2001
Last modified: March 6, 2013
This is version 61 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

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