ID Q2M0D6_DROPS Unreviewed; 506 AA.
AC Q2M0D6; A0A6I8UD32;
DT 21-FEB-2006, integrated into UniProtKB/TrEMBL.
DT 21-FEB-2006, sequence version 1.
DT 27-MAR-2024, entry version 106.
DE RecName: Full=Catalase {ECO:0000256|RuleBase:RU000498};
DE EC=1.11.1.6 {ECO:0000256|RuleBase:RU000498};
GN Name=LOC4813007 {ECO:0000313|RefSeq:XP_001353487.1};
OS Drosophila pseudoobscura pseudoobscura (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=46245 {ECO:0000313|Proteomes:UP000001819, ECO:0000313|RefSeq:XP_001353487.1};
RN [1] {ECO:0000313|RefSeq:XP_001353487.1}
RP IDENTIFICATION.
RC STRAIN=MV2-25 {ECO:0000313|RefSeq:XP_001353487.1};
RC TISSUE=Whole body {ECO:0000313|RefSeq:XP_001353487.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Occurs in almost all aerobically respiring organisms and
CC serves to protect cells from the toxic effects of hydrogen peroxide.
CC {ECO:0000256|RuleBase:RU004142}.
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:0000256|ARBA:ARBA00000720,
CC ECO:0000256|RuleBase:RU000498};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000256|ARBA:ARBA00001971,
CC ECO:0000256|PIRSR:PIRSR038928-2};
CC -!- SIMILARITY: Belongs to the catalase family.
CC {ECO:0000256|ARBA:ARBA00005329, ECO:0000256|RuleBase:RU000498}.
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DR RefSeq; XP_001353487.1; XM_001353451.4.
DR AlphaFoldDB; Q2M0D6; -.
DR SMR; Q2M0D6; -.
DR STRING; 46245.Q2M0D6; -.
DR PeroxiBase; 5273; DpKat01.
DR EnsemblMetazoa; FBtr0276067; FBpp0274505; FBgn0079916.
DR GeneID; 4813007; -.
DR KEGG; dpo:4813007; -.
DR eggNOG; KOG0047; Eukaryota.
DR HOGENOM; CLU_010645_2_0_1; -.
DR InParanoid; Q2M0D6; -.
DR OMA; KFRWNVF; -.
DR Proteomes; UP000001819; Chromosome X.
DR Bgee; FBgn0079916; Expressed in adult organism and 3 other cell types or tissues.
DR GO; GO:0004096; F:catalase activity; IEA:UniProtKB-EC.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003007; P:heart morphogenesis; IEA:EnsemblMetazoa.
DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:UniProtKB-KW.
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 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:UP000001819}.
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 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; 57174 MW; 1B0DA57C5CC92E56 CRC64;
MAARDAASNQ LIDYKNTQTV SPGSITTGHG SPIGIKDATQ TVGPRGPVLL QDVNFLDEMA
HFDRERIPER VVHAKGAGAF GYFEVTHDIS KYCAAKMFDK VKKRTPLAIR FSTVGGESGS
ADTARDPRGF AVKFYTEDGV WDLVGNNTPI FFIRDPILFP SFIHTQKRNP QTHLKDPDMF
WDFLTLRPES THQVCFLFGD RGTPDGYCHM NGYGSHTFKL VNAKGEPIYA KFHMKTDQGI
KNLDVKAADE LASSDPDYSI RDLYNRIKTC KFPSWTMYIQ VMTFEEAKKF KYNPFDVTKV
WSHKEFPLIP VGKLVLDRNP KNYFAEVEQI AFSPAHLVPG IEPSPDKMLQ GRLFSYSDTH
RHRLGPNYLQ IPVNCPYRVK VNNFQRDGLM NVTDNQDGAP NYFPNSFNGP QECPRARALS
TCCPVTGDVY RYSSGDTEDN YGQVTDFWVH TLDNCARKRL VANIAGHLNN ASQFLQERAV
KNFTQVHADF GRMLTEALNL AKSSKF
//
