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Protein

Catalase

Gene

Cat

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein 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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei73 – 731PROSITE-ProRule annotation
Active sitei146 – 1461PROSITE-ProRule annotation
Metal bindingi356 – 3561Iron (heme axial ligand)By similarity

GO - Molecular functioni

  • antioxidant activity Source: FlyBase
  • catalase activity Source: FlyBase
  • heme binding Source: FlyBase
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

  • aging Source: FlyBase
  • calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules Source: FlyBase
  • cellular oxidant detoxification Source: GOC
  • determination of adult lifespan Source: FlyBase
  • heart morphogenesis Source: FlyBase
  • hydrogen peroxide catabolic process Source: UniProtKB-KW
  • paracrine signaling Source: FlyBase
  • reactive oxygen species metabolic process Source: FlyBase
  • regulation of hemocyte proliferation Source: FlyBase
  • response to ethanol Source: FlyBase
  • response to hydrogen peroxide Source: FlyBase
  • response to oxidative stress Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase, Peroxidase

Keywords - Biological processi

Hydrogen peroxide

Keywords - Ligandi

Heme, Iron, Metal-binding

Enzyme and pathway databases

ReactomeiR-DME-3299685. Detoxification of Reactive Oxygen Species.
R-DME-74259. Purine catabolism.

Protein family/group databases

PeroxiBasei8425. DmKat01.

Names & Taxonomyi

Protein namesi
Recommended name:
Catalase (EC:1.11.1.6)
Gene namesi
Name:Cat
ORF Names:CG6871
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 3L

Organism-specific databases

FlyBaseiFBgn0000261. Cat.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Peroxisome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 506506CatalasePRO_0000084912Add
BLAST

Proteomic databases

PaxDbiP17336.
PRIDEiP17336.

Expressioni

Gene expression databases

BgeeiP17336.
GenevisibleiP17336. DM.

Interactioni

Subunit structurei

Homotetramer.

Protein-protein interaction databases

BioGridi65329. 18 interactions.
DIPiDIP-18768N.
IntActiP17336. 30 interactions.
MINTiMINT-1601909.
STRINGi7227.FBpp0074825.

Structurei

3D structure databases

ProteinModelPortaliP17336.
SMRiP17336. Positions 25-491.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi504 – 5063Microbody targeting signalSequence analysis

Sequence similaritiesi

Belongs to the catalase family.Curated

Phylogenomic databases

eggNOGiKOG0047. Eukaryota.
COG0753. LUCA.
GeneTreeiENSGT00390000018100.
InParanoidiP17336.
KOiK03781.
OMAiQVHADFG.
OrthoDBiEOG7V7660.
PhylomeDBiP17336.

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]
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.

P17336-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAGRDAASNQ LIDYKNSQTV SPGAITTGNG APIGIKDASQ TVGPRGPILL
60 70 80 90 100
QDVNFLDEMS HFDRERIPER VVHAKGAGAF GYFEVTHDIT QYCAAKIFDK
110 120 130 140 150
VKKRTPLAVR FSTVGGESGS ADTARDPRGF AVKFYTEDGV WDLVGNNTPV
160 170 180 190 200
FFIRDPILFP SFIHTQKRNP QTHLKDPDMF WDFLTLRPES AHQVCILFSD
210 220 230 240 250
RGTPDGYCHM NGYGSHTFKL INAKGEPIYA KFHFKTDQGI KNLDVKTADQ
260 270 280 290 300
LASTDPDYSI RDLYNRIKTC KFPSWTMYIQ VMTYEQAKKF KYNPFDVTKV
310 320 330 340 350
WSQKEYPLIP VGKMVLDRNP KNYFAEVEQI AFSPAHLVPG VEPSPDKMLH
360 370 380 390 400
GRLFSYSDTH RHRLGPNYLQ IPVNCPYKVK IENFQRDGAM NVTDNQDGAP
410 420 430 440 450
NYFPNSFNGP QECPRARALS SCCPVTGDVY RYSSGDTEDN FGQVTDFWVH
460 470 480 490 500
VLDKCAKKRL VQNIAGHLSN ASQFLQERAV KNFTQVHADF GRMLTEELNL

AKSSKF
Length:506
Mass (Da):57,150
Last modified:October 1, 1996 - v2
Checksum:i396377DC5F784ECE
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00145 Genomic DNA. Translation: AAC13738.1.
X52286 mRNA. Translation: CAA36529.1.
AE014296 Genomic DNA. Translation: AAF49228.1.
AY084154 mRNA. Translation: AAL89892.1.
PIRiS12725. CSFF.
RefSeqiNP_536731.1. NM_080483.3.
UniGeneiDm.6950.

Genome annotation databases

EnsemblMetazoaiFBtr0075058; FBpp0074825; FBgn0000261.
GeneIDi40048.
KEGGidme:Dmel_CG6871.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00145 Genomic DNA. Translation: AAC13738.1.
X52286 mRNA. Translation: CAA36529.1.
AE014296 Genomic DNA. Translation: AAF49228.1.
AY084154 mRNA. Translation: AAL89892.1.
PIRiS12725. CSFF.
RefSeqiNP_536731.1. NM_080483.3.
UniGeneiDm.6950.

3D structure databases

ProteinModelPortaliP17336.
SMRiP17336. Positions 25-491.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi65329. 18 interactions.
DIPiDIP-18768N.
IntActiP17336. 30 interactions.
MINTiMINT-1601909.
STRINGi7227.FBpp0074825.

Protein family/group databases

PeroxiBasei8425. DmKat01.

Proteomic databases

PaxDbiP17336.
PRIDEiP17336.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0075058; FBpp0074825; FBgn0000261.
GeneIDi40048.
KEGGidme:Dmel_CG6871.

Organism-specific databases

CTDi847.
FlyBaseiFBgn0000261. Cat.

Phylogenomic databases

eggNOGiKOG0047. Eukaryota.
COG0753. LUCA.
GeneTreeiENSGT00390000018100.
InParanoidiP17336.
KOiK03781.
OMAiQVHADFG.
OrthoDBiEOG7V7660.
PhylomeDBiP17336.

Enzyme and pathway databases

ReactomeiR-DME-3299685. Detoxification of Reactive Oxygen Species.
R-DME-74259. Purine catabolism.

Miscellaneous databases

ChiTaRSiCat. fly.
GenomeRNAii40048.
PROiP17336.

Gene expression databases

BgeeiP17336.
GenevisibleiP17336. DM.

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]
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

« Hide 'large scale' publications
  1. "Molecular analysis of the Drosophila catalase gene."
    Orr W.C., Orr E.C., Legan S.K., Sohal R.S.
    Arch. Biochem. Biophys. 330:251-258(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "cDNA and deduced amino acid sequence of Drosophila catalase."
    Orr E.C., Bewley G.C., Orr W.C.
    Nucleic Acids Res. 18:3663-3663(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "The genome sequence of Drosophila melanogaster."
    Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
    , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  4. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  5. "A Drosophila full-length cDNA resource."
    Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E.
    Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Embryo.
  6. "Identification of Drosophila wing imaginal disc proteins by two-dimensional gel analysis and microsequencing."
    Santaren J.F., van Damme J., Puype M., Vandekerckhove J., Garcia-Bellido A.
    Exp. Cell Res. 206:220-226(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 76-92.
    Strain: Vallecas.
    Tissue: Wing imaginal disk.

Entry informationi

Entry nameiCATA_DROME
AccessioniPrimary (citable) accession number: P17336
Secondary accession number(s): Q9VVT1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: October 1, 1996
Last modified: June 8, 2016
This is version 142 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. SIMILARITY comments
    Index of protein domains and families

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 one 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.