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Q9PT92

- CATA_DANRE

UniProt

Q9PT92 - CATA_DANRE

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Protein
Catalase
Gene
cat
Organism
Danio rerio (Zebrafish) (Brachydanio rerio)
Status
Reviewed - Annotation score: 3 out of 5 - Experimental evidence at transcript leveli

Functioni

Occurs in almost all aerobically respiring organisms and serves to protect cells from the toxic effects of hydrogen peroxide.

Catalytic activityi

2 H2O2 = O2 + 2 H2O.

Cofactori

Heme group By similarity.
NADP By similarity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei75 – 751 By similarity
Active sitei148 – 1481 By similarity
Metal bindingi358 – 3581Iron (heme axial ligand) By similarity

GO - Molecular functioni

  1. catalase activity Source: UniProtKB-EC
  2. heme binding Source: InterPro
  3. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. hydrogen peroxide catabolic process Source: UniProtKB-KW
  2. response to copper ion Source: ZFIN
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase, Peroxidase

Keywords - Biological processi

Hydrogen peroxide

Keywords - Ligandi

Heme, Iron, Metal-binding, NADP

Names & Taxonomyi

Protein namesi
Recommended name:
Catalase (EC:1.11.1.6)
Gene namesi
Name:cat
OrganismiDanio rerio (Zebrafish) (Brachydanio rerio)
Taxonomic identifieri7955 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiOstariophysiCypriniformesCyprinidaeDanio
ProteomesiUP000000437: Unplaced

Organism-specific databases

ZFINiZDB-GENE-000210-20. cat.

Subcellular locationi

Peroxisome By similarity

GO - Cellular componenti

  1. peroxisome Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Peroxisome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 526526Catalase
PRO_0000084906Add
BLAST

Proteomic databases

PRIDEiQ9PT92.

Interactioni

Subunit structurei

Homotetramer By similarity.

Structurei

3D structure databases

ProteinModelPortaliQ9PT92.
SMRiQ9PT92. Positions 25-503.

Family & Domainsi

Sequence similaritiesi

Belongs to the catalase family.

Phylogenomic databases

eggNOGiCOG0753.
HOGENOMiHOG000087852.
HOVERGENiHBG003986.
InParanoidiQ9PT92.
PhylomeDBiQ9PT92.

Family and domain databases

Gene3Di2.40.180.10. 1 hit.
InterProiIPR018028. 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]
PANTHERiPTHR11465. PTHR11465. 1 hit.
PfamiPF00199. Catalase. 1 hit.
PF06628. Catalase-rel. 1 hit.
[Graphical view]
PIRSFiPIRSF038928. Catalase_clade1-3. 1 hit.
PRINTSiPR00067. CATALASE.
SMARTiSM01060. Catalase. 1 hit.
[Graphical view]
SUPFAMiSSF56634. SSF56634. 1 hit.
PROSITEiPS00437. CATALASE_1. 1 hit.
PS00438. CATALASE_2. 1 hit.
PS51402. CATALASE_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9PT92-1 [UniParc]FASTAAdd to Basket

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MADDREKSTD QMKLWKEGRG SQRPDVLTTG AGVPIGDKLN AMTAGPRGPL    50
LVQDVVFTDE MAHFDRERIP ERVVHAKGAG AFGYFEVTHD ITRYSKAKVF 100
EHVGKTTPIV VRFSTVAGEA GSPDTVRDPR GFAVKFYTDE GNWDLTGNNT 150
PTFFIRDTLL SPSFIHSQKR NPQTHLKDPD MVWDFWSLRP ESLHQVSFLF 200
SDRGIPDGYR HMNGYGSHTF KLVNAQGQPV YCKFHYKTNQ GIKNIPVEEA 250
DRLAATDPDY SIRDLYNAIA NGNFPSWTFY IQVMTFEQAE NWKWNPFDLT 300
KVWSHKEFPL IPVGRFVLNR NPVNYFAEVE QLAFDPSNMP PGIEPSPDKM 350
LQGRLFSYPD THRHRLGANY LQLPVNCPYR TRVANYQRDG PMCMHDNQGG 400
APNYYPNSFS APDVQPRFLE SKCKVSPDVA RYNSADDDNV TQVRTFFTQV 450
LNEAERERLC QNMAGHLKGA QLFIQKRMVQ NLMAVHSDYG NRVQALLDKH 500
NAEGKKNTVH VYSRGGASAV AAASKM 526
Length:526
Mass (Da):59,654
Last modified:May 1, 2000 - v1
Checksum:iE1120D3796522785
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti110 – 1101V → A in AAF89686. 1 Publication
Sequence conflicti123 – 1231P → S in AAF89686. 1 Publication
Sequence conflicti152 – 1521T → I in AAF89686. 1 Publication
Sequence conflicti161 – 1611S → F in AAF89686. 1 Publication
Sequence conflicti350 – 3523MLQ → NAA in AAF89686. 1 Publication
Sequence conflicti478 – 4781M → T in AAF89686. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ007505 mRNA. Translation: CAB64949.1.
AF170069 mRNA. Translation: AAF89686.1.
UniGeneiDr.1079.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ007505 mRNA. Translation: CAB64949.1 .
AF170069 mRNA. Translation: AAF89686.1 .
UniGenei Dr.1079.

3D structure databases

ProteinModelPortali Q9PT92.
SMRi Q9PT92. Positions 25-503.
ModBasei Search...
MobiDBi Search...

Proteomic databases

PRIDEi Q9PT92.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Organism-specific databases

ZFINi ZDB-GENE-000210-20. cat.

Phylogenomic databases

eggNOGi COG0753.
HOGENOMi HOG000087852.
HOVERGENi HBG003986.
InParanoidi Q9PT92.
PhylomeDBi Q9PT92.

Miscellaneous databases

PROi Q9PT92.

Family and domain databases

Gene3Di 2.40.180.10. 1 hit.
InterProi IPR018028. 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 ]
PANTHERi PTHR11465. PTHR11465. 1 hit.
Pfami PF00199. Catalase. 1 hit.
PF06628. Catalase-rel. 1 hit.
[Graphical view ]
PIRSFi PIRSF038928. Catalase_clade1-3. 1 hit.
PRINTSi PR00067. CATALASE.
SMARTi SM01060. Catalase. 1 hit.
[Graphical view ]
SUPFAMi SSF56634. SSF56634. 1 hit.
PROSITEi PS00437. CATALASE_1. 1 hit.
PS00438. CATALASE_2. 1 hit.
PS51402. CATALASE_3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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].

Entry informationi

Entry nameiCATA_DANRE
AccessioniPrimary (citable) accession number: Q9PT92
Secondary accession number(s): Q9I8V5
Entry historyi
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 statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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