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Q9PT92 (CATA_DANRE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 88. 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 attributes

Sequence length526 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 By similarity.

NADP By similarity.

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
NADP
   Molecular functionOxidoreductase
Peroxidase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processhydrogen peroxide catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

response to copper ion

Inferred from direct assay PubMed 17855494. Source: ZFIN

   Cellular_componentperoxisome

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 – 526526Catalase
PRO_0000084906

Sites

Active site751 By similarity
Active site1481 By similarity
Metal binding3581Iron (heme axial ligand) By similarity

Experimental info

Sequence conflict1101V → A in AAF89686. Ref.2
Sequence conflict1231P → S in AAF89686. Ref.2
Sequence conflict1521T → I in AAF89686. Ref.2
Sequence conflict1611S → F in AAF89686. Ref.2
Sequence conflict350 – 3523MLQ → NAA in AAF89686. Ref.2
Sequence conflict4781M → T in AAF89686. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q9PT92 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: E1120D3796522785

FASTA52659,654
        10         20         30         40         50         60 
MADDREKSTD QMKLWKEGRG SQRPDVLTTG AGVPIGDKLN AMTAGPRGPL LVQDVVFTDE 

        70         80         90        100        110        120 
MAHFDRERIP ERVVHAKGAG AFGYFEVTHD ITRYSKAKVF EHVGKTTPIV VRFSTVAGEA 

       130        140        150        160        170        180 
GSPDTVRDPR GFAVKFYTDE GNWDLTGNNT PTFFIRDTLL SPSFIHSQKR NPQTHLKDPD 

       190        200        210        220        230        240 
MVWDFWSLRP ESLHQVSFLF SDRGIPDGYR HMNGYGSHTF KLVNAQGQPV YCKFHYKTNQ 

       250        260        270        280        290        300 
GIKNIPVEEA DRLAATDPDY SIRDLYNAIA NGNFPSWTFY IQVMTFEQAE NWKWNPFDLT 

       310        320        330        340        350        360 
KVWSHKEFPL IPVGRFVLNR NPVNYFAEVE QLAFDPSNMP PGIEPSPDKM LQGRLFSYPD 

       370        380        390        400        410        420 
THRHRLGANY LQLPVNCPYR TRVANYQRDG PMCMHDNQGG APNYYPNSFS APDVQPRFLE 

       430        440        450        460        470        480 
SKCKVSPDVA RYNSADDDNV TQVRTFFTQV LNEAERERLC QNMAGHLKGA QLFIQKRMVQ 

       490        500        510        520 
NLMAVHSDYG NRVQALLDKH NAEGKKNTVH VYSRGGASAV AAASKM 

« Hide

References

[1]"Cloning and expression of a cDNA coding for catalase from zebrafish (Danio rerio)."
Ken C.F., Lin C.T., Wu J.L., Shaw J.F.
J. Agric. Food Chem. 48:2092-2096(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Molecular cloning and sequence analysis of the Danio rerio catalase gene."
Gerhard G.S., Kauffman E.J., Grundy M.A.
Comp. Biochem. Physiol. 127B:447-457(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ007505 mRNA. Translation: CAB64949.1.
AF170069 mRNA. Translation: AAF89686.1.
UniGeneDr.1079.

3D structure databases

ProteinModelPortalQ9PT92.
SMRQ9PT92. Positions 25-503.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEQ9PT92.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Organism-specific databases

ZFINZDB-GENE-000210-20. cat.

Phylogenomic databases

eggNOGCOG0753.
HOGENOMHOG000087852.
HOVERGENHBG003986.
InParanoidQ9PT92.
PhylomeDBQ9PT92.

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...

Other

PROQ9PT92.

Entry information

Entry nameCATA_DANRE
AccessionPrimary (citable) accession number: Q9PT92
Secondary accession number(s): Q9I8V5
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: May 1, 2000
Last modified: April 16, 2014
This is version 88 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families