ID B4PIY6_DROYA Unreviewed; 506 AA. AC B4PIY6; DT 23-SEP-2008, integrated into UniProtKB/TrEMBL. DT 23-SEP-2008, sequence version 1. DT 02-SEP-2026, entry version 93. DE RecName: Full=Catalase {ECO:0000256|PROSITE-ProRule:PRU10013, ECO:0000256|RuleBase:RU000498}; DE EC=1.11.1.6 {ECO:0000256|PROSITE-ProRule:PRU10013, ECO:0000256|RuleBase:RU000498}; GN Name=Dyak\GE19975 {ECO:0000313|EMBL:EDW94577.1}; GN Synonyms=dyak_GLEANR_3827 {ECO:0000313|EMBL:EDW94577.1}, GE19975 GN {ECO:0000313|EMBL:EDW94577.1}; GN ORFNames=Dyak_GE19975 {ECO:0000313|EMBL:EDW94577.1}; OS Drosophila yakuba (Fruit fly). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Altocrustacea; Allotriocarida; OC Hexapoda; Insecta; Pterygota; Neoptera; Eumetabola; Endopterygota; OC Aparaglossata; Panorpida; Diptera; Brachycera; Muscomorpha; Ephydroidea; OC Drosophilidae; Drosophila; Sophophora. OX NCBI_TaxID=7245 {ECO:0000313|EMBL:EDW94577.1, ECO:0000313|Proteomes:UP000002282}; RN [1] {ECO:0000313|EMBL:EDW94577.1, ECO:0000313|Proteomes:UP000002282} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Tai18E2 / Tucson 14021-0261.01 RC {ECO:0000313|Proteomes:UP000002282}; RX PubMed=17994087; DOI=10.1038/nature06341; RG Drosophila 12 Genomes Consortium; RA Clark A.G., Eisen M.B., Smith D.R., Bergman C.M., Oliver B., Markow T.A., RA Kaufman T.C., Kellis M., Gelbart W., Iyer V.N., Pollard D.A., Sackton T.B., RA Larracuente A.M., Singh N.D., Abad J.P., Abt D.N., Adryan B., Aguade M., RA Akashi H., Anderson W.W., Aquadro C.F., Ardell D.H., Arguello R., RA Artieri C.G., Barbash D.A., Barker D., Barsanti P., Batterham P., RA Batzoglou S., Begun D., Bhutkar A., Blanco E., Bosak S.A., Bradley R.K., RA Brand A.D., Brent M.R., Brooks A.N., Brown R.H., Butlin R.K., Caggese C., RA Calvi B.R., Bernardo de Carvalho A., Caspi A., Castrezana S., RA Celniker S.E., Chang J.L., Chapple C., Chatterji S., Chinwalla A., RA Civetta A., Clifton S.W., Comeron J.M., Costello J.C., Coyne J.A., Daub J., RA David R.G., Delcher A.L., Delehaunty K., Do C.B., Ebling H., Edwards K., RA Eickbush T., Evans J.D., Filipski A., Findeiss S., Freyhult E., Fulton L., RA Fulton R., Garcia A.C., Gardiner A., Garfield D.A., Garvin B.E., Gibson G., RA Gilbert D., Gnerre S., Godfrey J., Good R., Gotea V., Gravely B., RA Greenberg A.J., Griffiths-Jones S., Gross S., Guigo R., Gustafson E.A., RA Haerty W., Hahn M.W., Halligan D.L., Halpern A.L., Halter G.M., Han M.V., RA Heger A., Hillier L., Hinrichs A.S., Holmes I., Hoskins R.A., Hubisz M.J., RA Hultmark D., Huntley M.A., Jaffe D.B., Jagadeeshan S., Jeck W.R., RA Johnson J., Jones C.D., Jordan W.C., Karpen G.H., Kataoka E., RA Keightley P.D., Kheradpour P., Kirkness E.F., Koerich L.B., Kristiansen K., RA Kudrna D., Kulathinal R.J., Kumar S., Kwok R., Lander E., Langley C.H., RA Lapoint R., Lazzaro B.P., Lee S.J., Levesque L., Li R., Lin C.F., Lin M.F., RA Lindblad-Toh K., Llopart A., Long M., Low L., Lozovsky E., Lu J., Luo M., RA Machado C.A., Makalowski W., Marzo M., Matsuda M., Matzkin L., RA McAllister B., McBride C.S., McKernan B., McKernan K., Mendez-Lago M., RA Minx P., Mollenhauer M.U., Montooth K., Mount S.M., Mu X., Myers E., RA Negre B., Newfeld S., Nielsen R., Noor M.A., O'Grady P., Pachter L., RA Papaceit M., Parisi M.J., Parisi M., Parts L., Pedersen J.S., Pesole G., RA Phillippy A.M., Ponting C.P., Pop M., Porcelli D., Powell J.R., RA Prohaska S., Pruitt K., Puig M., Quesneville H., Ram K.R., Rand D., RA Rasmussen M.D., Reed L.K., Reenan R., Reily A., Remington K.A., RA Rieger T.T., Ritchie M.G., Robin C., Rogers Y.H., Rohde C., Rozas J., RA Rubenfield M.J., Ruiz A., Russo S., Salzberg S.L., Sanchez-Gracia A., RA Saranga D.J., Sato H., Schaeffer S.W., Schatz M.C., Schlenke T., RA Schwartz R., Segarra C., Singh R.S., Sirot L., Sirota M., Sisneros N.B., RA Smith C.D., Smith T.F., Spieth J., Stage D.E., Stark A., Stephan W., RA Strausberg R.L., Strempel S., Sturgill D., Sutton G., Sutton G.G., Tao W., RA Teichmann S., Tobari Y.N., Tomimura Y., Tsolas J.M., Valente V.L., RA Venter E., Venter J.C., Vicario S., Vieira F.G., Vilella A.J., RA Villasante A., Walenz B., Wang J., Wasserman M., Watts T., Wilson D., RA Wilson R.K., Wing R.A., Wolfner M.F., Wong A., Wong G.K., Wu C.I., Wu G., RA Yamamoto D., Yang H.P., Yang S.P., Yorke J.A., Yoshida K., Zdobnov E., RA Zhang P., Zhang Y., Zimin A.V., Baldwin J., Abdouelleil A., Abdulkadir J., RA Abebe A., Abera B., Abreu J., Acer S.C., Aftuck L., Alexander A., An P., RA Anderson E., Anderson S., Arachi H., Azer M., Bachantsang P., Barry A., RA Bayul T., Berlin A., Bessette D., Bloom T., Blye J., Boguslavskiy L., RA Bonnet C., Boukhgalter B., Bourzgui I., Brown A., Cahill P., Channer S., RA Cheshatsang Y., Chuda L., Citroen M., Collymore A., Cooke P., Costello M., RA D'Aco K., Daza R., De Haan G., DeGray S., DeMaso C., Dhargay N., Dooley K., RA Dooley E., Doricent M., Dorje P., Dorjee K., Dupes A., Elong R., Falk J., RA Farina A., Faro S., Ferguson D., Fisher S., Foley C.D., Franke A., RA Friedrich D., Gadbois L., Gearin G., Gearin C.R., Giannoukos G., Goode T., RA Graham J., Grandbois E., Grewal S., Gyaltsen K., Hafez N., Hagos B., RA Hall J., Henson C., Hollinger A., Honan T., Huard M.D., Hughes L., RA Hurhula B., Husby M.E., Kamat A., Kanga B., Kashin S., Khazanovich D., RA Kisner P., Lance K., Lara M., Lee W., Lennon N., Letendre F., LeVine R., RA Lipovsky A., Liu X., Liu J., Liu S., Lokyitsang T., Lokyitsang Y., RA Lubonja R., Lui A., MacDonald P., Magnisalis V., Maru K., Matthews C., RA McCusker W., McDonough S., Mehta T., Meldrim J., Meneus L., Mihai O., RA Mihalev A., Mihova T., Mittelman R., Mlenga V., Montmayeur A., Mulrain L., RA Navidi A., Naylor J., Negash T., Nguyen T., Nguyen N., Nicol R., Norbu C., RA Norbu N., Novod N., O'Neill B., Osman S., Markiewicz E., Oyono O.L., RA Patti C., Phunkhang P., Pierre F., Priest M., Raghuraman S., Rege F., RA Reyes R., Rise C., Rogov P., Ross K., Ryan E., Settipalli S., Shea T., RA Sherpa N., Shi L., Shih D., Sparrow T., Spaulding J., Stalker J., RA Stange-Thomann N., Stavropoulos S., Stone C., Strader C., Tesfaye S., RA Thomson T., Thoulutsang Y., Thoulutsang D., Topham K., Topping I., RA Tsamla T., Vassiliev H., Vo A., Wangchuk T., Wangdi T., Weiand M., RA Wilkinson J., Wilson A., Yadav S., Young G., Yu Q., Zembek L., Zhong D., RA Zimmer A., Zwirko Z., Jaffe D.B., Alvarez P., Brockman W., Butler J., RA Chin C., Gnerre S., Grabherr M., Kleber M., Mauceli E., MacCallum I.; RT "Evolution of genes and genomes on the Drosophila phylogeny."; RL Nature 450:203-218(2007). RN [2] {ECO:0000313|EMBL:EDW94577.1, ECO:0000313|Proteomes:UP000002282} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Tai18E2 / Tucson 14021-0261.01 RC {ECO:0000313|Proteomes:UP000002282}; RX PubMed=17550304; DOI=10.1371/journal.pbio.0050152; RA Ranz J.M., Maurin D., Chan Y.S., von Grotthuss M., Hillier L.W., Roote J., RA Ashburner M., Bergman C.M.; RT "Principles of genome evolution in the Drosophila melanogaster species RT group."; RL PLoS Biol. 5:E152-E152(2007). CC -!- FUNCTION: Catalyzes the degradation of hydrogen peroxide (H(2)O(2)) CC generated by peroxisomal oxidases to water and oxygen, thereby CC protecting cells from the toxic effects of hydrogen peroxide. CC {ECO:0000256|RuleBase:RU004142}. CC -!- CATALYTIC ACTIVITY: CC Reaction=2 H2O2 = O2 + 2 H2O; Xref=Rhea:RHEA:20309, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16240; EC=1.11.1.6; CC Evidence={ECO:0000256|ARBA:ARBA00049254, ECO:0000256|PROSITE- CC ProRule:PRU10013, ECO:0000256|RuleBase:RU000498}; CC -!- COFACTOR: CC Name=heme; Xref=ChEBI:CHEBI:30413; CC Evidence={ECO:0000256|PIRSR:PIRSR038928-2}; CC -!- SIMILARITY: Belongs to the catalase family. CC {ECO:0000256|ARBA:ARBA00005329, ECO:0000256|RuleBase:RU000498}. 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; CM000159; EDW94577.1; -; Genomic_DNA. DR AlphaFoldDB; B4PIY6; -. DR SMR; B4PIY6; -. DR GeneID; 6534182; -. DR KEGG; dya:Dyak_GE19975; -. DR eggNOG; KOG0047; Eukaryota. DR HOGENOM; CLU_010645_2_0_1; -. DR OMA; KFRWNVF; -. DR OrthoDB; 6880011at2759; -. DR PhylomeDB; B4PIY6; -. DR Proteomes; UP000002282; Chromosome 3L. DR GO; GO:0005829; C:cytosol; IEA:EnsemblMetazoa. DR GO; GO:0016008; C:major mitochondrial derivative; IEA:EnsemblMetazoa. DR GO; GO:0005739; C:mitochondrion; IEA:TreeGrafter. DR GO; GO:0005777; C:peroxisome; IEA:TreeGrafter. DR GO; GO:0004096; F:catalase activity; IEA:UniProtKB-EC. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0003007; P:heart morphogenesis; IEA:EnsemblMetazoa. DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:EnsemblMetazoa. DR GO; GO:0036335; P:intestinal stem cell homeostasis; IEA:EnsemblMetazoa. DR GO; GO:0038001; P:paracrine signaling; IEA:EnsemblMetazoa. DR GO; GO:0035206; P:regulation of hemocyte proliferation; IEA:EnsemblMetazoa. DR GO; GO:0048167; P:regulation of synaptic plasticity; IEA:EnsemblMetazoa. DR GO; GO:0034976; P:response to endoplasmic reticulum stress; IEA:EnsemblMetazoa. DR GO; GO:0042542; P:response to hydrogen peroxide; IEA:EnsemblMetazoa. DR CDD; cd08156; catalase_clade_3; 1. DR FunFam; 2.40.180.10:FF:000001; Catalase; 1. DR Gene3D; 2.40.180.10; Catalase core domain; 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; CATALASE; 1. DR PANTHER; PTHR11465:SF9; CATALASE; 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; Heme-dependent catalase-like; 1. DR PROSITE; PS00437; CATALASE_1; 1. DR PROSITE; PS00438; CATALASE_2; 1. DR PROSITE; PS51402; CATALASE_3; 1. PE 3: Inferred from homology; KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PIRSR:PIRSR038928-2}; KW Hydrogen peroxide {ECO:0000256|ARBA:ARBA00023324, KW ECO:0000256|RuleBase:RU000498}; KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR038928-2}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, KW ECO:0000256|PIRSR:PIRSR038928-2}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, KW ECO:0000256|RuleBase:RU000498}; KW Peroxidase {ECO:0000256|ARBA:ARBA00022559, ECO:0000256|RuleBase:RU000498}; KW Reference proteome {ECO:0000313|Proteomes:UP000002282}. FT DOMAIN 26..411 FT /note="Catalase core" FT /evidence="ECO:0000259|SMART:SM01060" FT ACT_SITE 73 FT /evidence="ECO:0000256|PIRSR:PIRSR038928-1, FT ECO:0000256|PROSITE-ProRule:PRU10013" FT ACT_SITE 146 FT /evidence="ECO:0000256|PIRSR:PIRSR038928-1" 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:0000256|PIRSR:PIRSR038928-2" SQ SEQUENCE 506 AA; 57101 MW; CBEAA41E5D17DE82 CRC64; MAGRDAASNQ LIDYKNSQTV SPGAITTGNG APIGIKDATQ TVGPRGPILL QDVNFLDEMS HFDRERIPER VVHAKGAGAF GYFEVTHDIT QYCAAKVFDK VKKRTPLAVR FSTVGGESGS ADTARDPRGF AVKFYTEDGV WDLVGNNTPI FFIRDPILFP SFIHTQKRNP QTHLKDPDMF WDFLTLRPES AHQVCFLFGD RGTPDGYCHM NGYGSHTFKL INAKGEPIYA KFHLKTDQGI KNLDVKTADQ LASSDPDYSI RDLYNRIKTC KFPSWTMYIQ VMTFEQAKKF KYNPFDITKV WSHKEYPLIP VGKMVLDRNP KNYFAEVEQI AFSPAHLVPG IEPSPDKMLQ GRLFSYSDTH RHRLGPNYLQ IPVNCPYKVK IENFQRDGPM NVTDNQDGAP NYFPNSFNGP QECPRARALS SCCPVTGDVY RYSSGDTEDN FGQVTDFWVH VLDKCAKKRL VQNIAGHLSG ASQFLQERAV KNFTQVHADF GRMLTEELNL AKSSKF //