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Catalase (EC 1.11.1.6)

 CATA_DROME              Reviewed;         506 AA.
P17336; Q9VVT1;
01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 2.
12-SEP-2018, entry version 160.
RecName: Full=Catalase;
EC=1.11.1.6;
Name=Cat; ORFNames=CG6871;
Drosophila melanogaster (Fruit fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
Ephydroidea; Drosophilidae; Drosophila; Sophophora.
NCBI_TaxID=7227;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=8660653; DOI=10.1006/abbi.1996.0250;
Orr W.C., Orr E.C., Legan S.K., Sohal R.S.;
"Molecular analysis of the Drosophila catalase gene.";
Arch. Biochem. Biophys. 330:251-258(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2362827; DOI=10.1093/nar/18.12.3663;
Orr E.C., Bewley G.C., Orr W.C.;
"cDNA and deduced amino acid sequence of Drosophila catalase.";
Nucleic Acids Res. 18:3663-3663(1990).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley;
PubMed=10731132; DOI=10.1126/science.287.5461.2185;
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.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[4]
GENOME REANNOTATION.
STRAIN=Berkeley;
PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
Lewis S.E.;
"Annotation of the Drosophila melanogaster euchromatic genome: a
systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Berkeley; TISSUE=Embryo;
PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
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.;
"A Drosophila full-length cDNA resource.";
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
[6]
PROTEIN SEQUENCE OF 76-92.
STRAIN=Vallecas; TISSUE=Wing imaginal disk;
PubMed=8500545; DOI=10.1006/excr.1993.1141;
Santaren J.F., van Damme J., Puype M., Vandekerckhove J.,
Garcia-Bellido A.;
"Identification of Drosophila wing imaginal disc proteins by two-
dimensional gel analysis and microsequencing.";
Exp. Cell Res. 206:220-226(1993).
-!- FUNCTION: Occurs in almost all aerobically respiring organisms and
serves to protect cells from the toxic effects of hydrogen
peroxide.
-!- CATALYTIC ACTIVITY: 2 H(2)O(2) = O(2) + 2 H(2)O.
{ECO:0000255|PROSITE-ProRule:PRU10013}.
-!- COFACTOR:
Name=heme; Xref=ChEBI:CHEBI:30413;
-!- SUBUNIT: Homotetramer.
-!- SUBCELLULAR LOCATION: Peroxisome.
-!- SIMILARITY: Belongs to the catalase family. {ECO:0000305}.
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EMBL; U00145; AAC13738.1; -; Genomic_DNA.
EMBL; X52286; CAA36529.1; -; mRNA.
EMBL; AE014296; AAF49228.1; -; Genomic_DNA.
EMBL; AY084154; AAL89892.1; -; mRNA.
PIR; S12725; CSFF.
RefSeq; NP_536731.1; NM_080483.3.
UniGene; Dm.6950; -.
ProteinModelPortal; P17336; -.
SMR; P17336; -.
BioGrid; 65329; 27.
DIP; DIP-18768N; -.
IntAct; P17336; 31.
STRING; 7227.FBpp0074825; -.
PeroxiBase; 8425; DmKat01.
PaxDb; P17336; -.
PRIDE; P17336; -.
EnsemblMetazoa; FBtr0075058; FBpp0074825; FBgn0000261.
GeneID; 40048; -.
KEGG; dme:Dmel_CG6871; -.
CTD; 847; -.
FlyBase; FBgn0000261; Cat.
eggNOG; KOG0047; Eukaryota.
eggNOG; COG0753; LUCA.
GeneTree; ENSGT00390000018100; -.
InParanoid; P17336; -.
KO; K03781; -.
OMA; HADFGRM; -.
OrthoDB; EOG091G04V5; -.
PhylomeDB; P17336; -.
Reactome; R-DME-3299685; Detoxification of Reactive Oxygen Species.
Reactome; R-DME-6798695; Neutrophil degranulation.
Reactome; R-DME-9033241; Peroxisomal protein import.
ChiTaRS; Cat; fly.
GenomeRNAi; 40048; -.
PRO; PR:P17336; -.
Proteomes; UP000000803; Chromosome 3L.
Bgee; FBgn0000261; Expressed in 58 organ(s), highest expression level in Malpighian tubule.
Genevisible; P17336; DM.
GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
GO; GO:0005777; C:peroxisome; ISS:FlyBase.
GO; GO:0016209; F:antioxidant activity; NAS:FlyBase.
GO; GO:0004096; F:catalase activity; IDA:FlyBase.
GO; GO:0020037; F:heme binding; IBA:GO_Central.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0007568; P:aging; TAS:FlyBase.
GO; GO:0008340; P:determination of adult lifespan; TAS:FlyBase.
GO; GO:0003007; P:heart morphogenesis; IMP:FlyBase.
GO; GO:0042744; P:hydrogen peroxide catabolic process; IBA:GO_Central.
GO; GO:0036335; P:intestinal stem cell homeostasis; IMP:FlyBase.
GO; GO:0038001; P:paracrine signaling; IMP:FlyBase.
GO; GO:0072593; P:reactive oxygen species metabolic process; IMP:FlyBase.
GO; GO:0035206; P:regulation of hemocyte proliferation; IMP:FlyBase.
GO; GO:0034976; P:response to endoplasmic reticulum stress; IMP:FlyBase.
GO; GO:0045471; P:response to ethanol; IMP:FlyBase.
GO; GO:0042542; P:response to hydrogen peroxide; IMP:FlyBase.
Gene3D; 2.40.180.10; -; 1.
InterPro; IPR018028; Catalase.
InterPro; IPR024708; Catalase_AS.
InterPro; IPR024711; Catalase_clade1/3.
InterPro; IPR011614; Catalase_core.
InterPro; IPR037060; Catalase_core_sf.
InterPro; IPR002226; Catalase_haem_BS.
InterPro; IPR010582; Catalase_immune_responsive.
InterPro; IPR020835; Catalase_sf.
PANTHER; PTHR11465; PTHR11465; 1.
Pfam; PF00199; Catalase; 1.
Pfam; PF06628; Catalase-rel; 1.
PIRSF; PIRSF038928; Catalase_clade1-3; 1.
PRINTS; PR00067; CATALASE.
SMART; SM01060; Catalase; 1.
SUPFAM; SSF56634; SSF56634; 1.
PROSITE; PS00437; CATALASE_1; 1.
PROSITE; PS00438; CATALASE_2; 1.
PROSITE; PS51402; CATALASE_3; 1.
1: Evidence at protein level;
Complete proteome; Direct protein sequencing; Heme; Hydrogen peroxide;
Iron; Metal-binding; Oxidoreductase; Peroxidase; Peroxisome;
Reference proteome.
CHAIN 1 506 Catalase.
/FTId=PRO_0000084912.
MOTIF 504 506 Microbody targeting signal.
{ECO:0000255}.
ACT_SITE 73 73 {ECO:0000255|PROSITE-ProRule:PRU10013}.
ACT_SITE 146 146 {ECO:0000255|PROSITE-ProRule:PRU10013}.
METAL 356 356 Iron (heme axial ligand). {ECO:0000250}.
SEQUENCE 506 AA; 57150 MW; 396377DC5F784ECE CRC64;
MAGRDAASNQ LIDYKNSQTV SPGAITTGNG APIGIKDASQ TVGPRGPILL QDVNFLDEMS
HFDRERIPER VVHAKGAGAF GYFEVTHDIT QYCAAKIFDK VKKRTPLAVR FSTVGGESGS
ADTARDPRGF AVKFYTEDGV WDLVGNNTPV FFIRDPILFP SFIHTQKRNP QTHLKDPDMF
WDFLTLRPES AHQVCILFSD RGTPDGYCHM NGYGSHTFKL INAKGEPIYA KFHFKTDQGI
KNLDVKTADQ LASTDPDYSI RDLYNRIKTC KFPSWTMYIQ VMTYEQAKKF KYNPFDVTKV
WSQKEYPLIP VGKMVLDRNP KNYFAEVEQI AFSPAHLVPG VEPSPDKMLH GRLFSYSDTH
RHRLGPNYLQ IPVNCPYKVK IENFQRDGAM NVTDNQDGAP NYFPNSFNGP QECPRARALS
SCCPVTGDVY RYSSGDTEDN FGQVTDFWVH VLDKCAKKRL VQNIAGHLSN ASQFLQERAV
KNFTQVHADF GRMLTEELNL AKSSKF


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