CATA_DROME
ID CATA_DROME Reviewed; 506 AA.
AC P17336; Q9VVT1;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Catalase;
DE EC=1.11.1.6;
GN Name=Cat; ORFNames=CG6871;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8660653; DOI=10.1006/abbi.1996.0250;
RA Orr W.C., Orr E.C., Legan S.K., Sohal R.S.;
RT "Molecular analysis of the Drosophila catalase gene.";
RL Arch. Biochem. Biophys. 330:251-258(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2362827; DOI=10.1093/nar/18.12.3663;
RA Orr E.C., Bewley G.C., Orr W.C.;
RT "cDNA and deduced amino acid sequence of Drosophila catalase.";
RL Nucleic Acids Res. 18:3663-3663(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [6]
RP PROTEIN SEQUENCE OF 76-92.
RC STRAIN=Vallecas; TISSUE=Wing imaginal disk;
RX PubMed=8500545; DOI=10.1006/excr.1993.1141;
RA Santaren J.F., van Damme J., Puype M., Vandekerckhove J.,
RA Garcia-Bellido A.;
RT "Identification of Drosophila wing imaginal disc proteins by two-
RT dimensional gel analysis and microsequencing.";
RL Exp. Cell Res. 206:220-226(1993).
CC -!- FUNCTION: Occurs in almost all aerobically respiring organisms and
CC serves to protect cells from the toxic effects of hydrogen peroxide.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 H2O2 = 2 H2O + O2; Xref=Rhea:RHEA:20309, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16240; EC=1.11.1.6;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10013};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC -!- SUBUNIT: Homotetramer.
CC -!- SUBCELLULAR LOCATION: Peroxisome.
CC -!- SIMILARITY: Belongs to the catalase family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U00145; AAC13738.1; -; Genomic_DNA.
DR EMBL; X52286; CAA36529.1; -; mRNA.
DR EMBL; AE014296; AAF49228.1; -; Genomic_DNA.
DR EMBL; AY084154; AAL89892.1; -; mRNA.
DR PIR; S12725; CSFF.
DR RefSeq; NP_536731.1; NM_080483.3.
DR AlphaFoldDB; P17336; -.
DR SMR; P17336; -.
DR BioGRID; 65329; 28.
DR DIP; DIP-18768N; -.
DR IntAct; P17336; 31.
DR STRING; 7227.FBpp0074825; -.
DR PeroxiBase; 8425; DmKat01.
DR PaxDb; P17336; -.
DR PRIDE; P17336; -.
DR DNASU; 40048; -.
DR EnsemblMetazoa; FBtr0075058; FBpp0074825; FBgn0000261.
DR GeneID; 40048; -.
DR KEGG; dme:Dmel_CG6871; -.
DR CTD; 847; -.
DR FlyBase; FBgn0000261; Cat.
DR VEuPathDB; VectorBase:FBgn0000261; -.
DR eggNOG; KOG0047; Eukaryota.
DR GeneTree; ENSGT00390000018100; -.
DR HOGENOM; CLU_010645_2_0_1; -.
DR InParanoid; P17336; -.
DR OMA; WTCYVQV; -.
DR OrthoDB; 507937at2759; -.
DR PhylomeDB; P17336; -.
DR Reactome; R-DME-3299685; Detoxification of Reactive Oxygen Species.
DR Reactome; R-DME-6798695; Neutrophil degranulation.
DR Reactome; R-DME-9033241; Peroxisomal protein import.
DR SignaLink; P17336; -.
DR BioGRID-ORCS; 40048; 0 hits in 3 CRISPR screens.
DR ChiTaRS; Cat; fly.
DR GenomeRNAi; 40048; -.
DR PRO; PR:P17336; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0000261; Expressed in adult Malpighian tubule (Drosophila) and 62 other tissues.
DR Genevisible; P17336; DM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0005777; C:peroxisome; ISS:FlyBase.
DR GO; GO:0004096; F:catalase activity; IDA:FlyBase.
DR GO; GO:0020037; F:heme binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0007568; P:aging; TAS:FlyBase.
DR GO; GO:0008340; P:determination of adult lifespan; TAS:FlyBase.
DR GO; GO:0003007; P:heart morphogenesis; IMP:FlyBase.
DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IGI:FlyBase.
DR GO; GO:0036335; P:intestinal stem cell homeostasis; IMP:FlyBase.
DR GO; GO:0038001; P:paracrine signaling; IMP:FlyBase.
DR GO; GO:0072593; P:reactive oxygen species metabolic process; IMP:FlyBase.
DR GO; GO:0035206; P:regulation of hemocyte proliferation; IMP:FlyBase.
DR GO; GO:0048167; P:regulation of synaptic plasticity; IMP:UniProtKB.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; IMP:FlyBase.
DR GO; GO:0042542; P:response to hydrogen peroxide; IMP:FlyBase.
DR CDD; cd08156; catalase_clade_3; 1.
DR InterPro; IPR018028; Catalase.
DR InterPro; IPR040333; Catalase_3.
DR InterPro; IPR024708; Catalase_AS.
DR InterPro; IPR024711; Catalase_clade1/3.
DR InterPro; IPR011614; Catalase_core.
DR InterPro; IPR002226; Catalase_haem_BS.
DR InterPro; IPR010582; Catalase_immune_responsive.
DR InterPro; IPR020835; Catalase_sf.
DR PANTHER; PTHR11465; PTHR11465; 1.
DR Pfam; PF00199; Catalase; 1.
DR Pfam; PF06628; Catalase-rel; 1.
DR PIRSF; PIRSF038928; Catalase_clade1-3; 1.
DR PRINTS; PR00067; CATALASE.
DR SMART; SM01060; Catalase; 1.
DR SUPFAM; SSF56634; SSF56634; 1.
DR PROSITE; PS00437; CATALASE_1; 1.
DR PROSITE; PS00438; CATALASE_2; 1.
DR PROSITE; PS51402; CATALASE_3; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Heme; Hydrogen peroxide; Iron; Metal-binding;
KW Oxidoreductase; Peroxidase; Peroxisome; Reference proteome.
FT CHAIN 1..506
FT /note="Catalase"
FT /id="PRO_0000084912"
FT MOTIF 504..506
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000255"
FT ACT_SITE 73
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10013"
FT ACT_SITE 146
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10013"
FT BINDING 356
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250"
SQ 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
