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Protein

Catalase

Gene

cat

Organism
Danio rerio (Zebrafish) (Brachydanio rerio)
Status
Reviewed-Annotation score: 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.PROSITE-ProRule annotation

Cofactori

Protein has several cofactor binding sites:

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei75 – 751PROSITE-ProRule annotation
Active sitei148 – 1481PROSITE-ProRule annotation
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 – 526526CatalasePRO_0000084906Add
BLAST

Proteomic databases

PRIDEiQ9PT92.

Interactioni

Subunit structurei

Homotetramer.By similarity

Structurei

3D structure databases

ProteinModelPortaliQ9PT92.
SMRiQ9PT92. Positions 25-503.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the catalase family.Curated

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

« Hide

        10         20         30         40         50
MADDREKSTD QMKLWKEGRG SQRPDVLTTG AGVPIGDKLN AMTAGPRGPL
60 70 80 90 100
LVQDVVFTDE MAHFDRERIP ERVVHAKGAG AFGYFEVTHD ITRYSKAKVF
110 120 130 140 150
EHVGKTTPIV VRFSTVAGEA GSPDTVRDPR GFAVKFYTDE GNWDLTGNNT
160 170 180 190 200
PTFFIRDTLL SPSFIHSQKR NPQTHLKDPD MVWDFWSLRP ESLHQVSFLF
210 220 230 240 250
SDRGIPDGYR HMNGYGSHTF KLVNAQGQPV YCKFHYKTNQ GIKNIPVEEA
260 270 280 290 300
DRLAATDPDY SIRDLYNAIA NGNFPSWTFY IQVMTFEQAE NWKWNPFDLT
310 320 330 340 350
KVWSHKEFPL IPVGRFVLNR NPVNYFAEVE QLAFDPSNMP PGIEPSPDKM
360 370 380 390 400
LQGRLFSYPD THRHRLGANY LQLPVNCPYR TRVANYQRDG PMCMHDNQGG
410 420 430 440 450
APNYYPNSFS APDVQPRFLE SKCKVSPDVA RYNSADDDNV TQVRTFFTQV
460 470 480 490 500
LNEAERERLC QNMAGHLKGA QLFIQKRMVQ NLMAVHSDYG NRVQALLDKH
510 520
NAEGKKNTVH VYSRGGASAV AAASKM
Length:526
Mass (Da):59,654
Last modified:May 1, 2000 - v1
Checksum:iE1120D3796522785
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti110 – 1101V → A in AAF89686. (PubMed:11281262)Curated
Sequence conflicti123 – 1231P → S in AAF89686. (PubMed:11281262)Curated
Sequence conflicti152 – 1521T → I in AAF89686. (PubMed:11281262)Curated
Sequence conflicti161 – 1611S → F in AAF89686. (PubMed:11281262)Curated
Sequence conflicti350 – 3523MLQ → NAA in AAF89686. (PubMed:11281262)Curated
Sequence conflicti478 – 4781M → T in AAF89686. (PubMed:11281262)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ007505 mRNA. Translation: CAB64949.1.
AF170069 mRNA. Translation: AAF89686.1.
UniGeneiDr.1079.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ007505 mRNA. Translation: CAB64949.1.
AF170069 mRNA. Translation: AAF89686.1.
UniGeneiDr.1079.

3D structure databases

ProteinModelPortaliQ9PT92.
SMRiQ9PT92. Positions 25-503.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiQ9PT92.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

ZFINiZDB-GENE-000210-20. cat.

Phylogenomic databases

eggNOGiCOG0753.
HOGENOMiHOG000087852.
HOVERGENiHBG003986.
InParanoidiQ9PT92.
PhylomeDBiQ9PT92.

Miscellaneous databases

PROiQ9PT92.

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]
ProtoNetiSearch...

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: January 7, 2015
This is version 92 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.