ID E0VNL6_PEDHC Unreviewed; 491 AA. AC E0VNL6; DT 02-NOV-2010, integrated into UniProtKB/TrEMBL. DT 02-NOV-2010, sequence version 1. DT 27-MAR-2024, entry version 69. DE RecName: Full=Catalase {ECO:0000256|RuleBase:RU000498}; DE EC=1.11.1.6 {ECO:0000256|RuleBase:RU000498}; GN Name=8231793 {ECO:0000313|EnsemblMetazoa:PHUM336860-PA}; GN ORFNames=Phum_PHUM336860 {ECO:0000313|EMBL:EEB14972.1}; OS Pediculus humanus subsp. corporis (Body louse). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Paraneoptera; Psocodea; Phthiraptera; Anoplura; Pediculidae; OC Pediculus. OX NCBI_TaxID=121224; RN [1] {ECO:0000313|EMBL:EEB14972.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=USDA {ECO:0000313|EMBL:EEB14972.1}; RA Kirkness E., Hannick L., Hass B., Bruggner R., Lawson D., Bidwell S., RA Joardar V., Caler E., Walenz B., Inman J., Schobel S., Galinsky K., RA Amedeo P., Strausberg R.; RT "Annotation of Pediculus humanus corporis strain USDA."; RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:EEB14972.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=USDA {ECO:0000313|EMBL:EEB14972.1}; RG The Human Body Louse Genome Consortium; RA Kirkness E., Walenz B., Hass B., Bruggner R., Strausberg R.; RT "The genome of the human body louse."; RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|EnsemblMetazoa:PHUM336860-PA} RP IDENTIFICATION. RC STRAIN=USDA {ECO:0000313|EnsemblMetazoa:PHUM336860-PA}; RG EnsemblMetazoa; RL Submitted (FEB-2021) 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}. 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; AAZO01003917; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; DS235340; EEB14972.1; -; Genomic_DNA. DR RefSeq; XP_002427710.1; XM_002427665.1. DR AlphaFoldDB; E0VNL6; -. DR STRING; 121224.E0VNL6; -. DR EnsemblMetazoa; PHUM336860-RA; PHUM336860-PA; PHUM336860. DR GeneID; 8231793; -. DR KEGG; phu:Phum_PHUM336860; -. DR CTD; 8231793; -. DR VEuPathDB; VectorBase:PHUM336860; -. DR eggNOG; KOG0047; Eukaryota. DR HOGENOM; CLU_010645_2_0_1; -. DR InParanoid; E0VNL6; -. DR OMA; KFRWNVF; -. DR OrthoDB; 3198922at2759; -. DR Proteomes; UP000009046; Unassembled WGS sequence. 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:0042744; P:hydrogen peroxide catabolic process; IEA:UniProtKB-KW. DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro. 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:UP000009046}. FT DOMAIN 25..410 FT /note="Catalase core" FT /evidence="ECO:0000259|SMART:SM01060" FT REGION 1..27 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 72 FT /evidence="ECO:0000256|PIRSR:PIRSR038928-1" FT ACT_SITE 145 FT /evidence="ECO:0000256|PIRSR:PIRSR038928-1" FT BINDING 355 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 491 AA; 55924 MW; 6FB3B51CD89C4D95 CRC64; MALRDPATEQ LSNYKKNHPK PEVLVTGHGA PIDDKLNSLS IGPRGPLLLQ DVTYIDEIAH FDRERIPERV VHAKGAGAFG YFEVTHDIRK YCRASVFSEI GKKTPVAVRF STVGGESGSA DTVRDPRGFA VKFYTDEGNW DLVGNNTPIF FIRDPLLFPS FIHTQKRNPA THLKDPDMFW DFITLRPETT HQVMILFSDR GIPDGYRHMN GYGSHTFKLV NDKYEAVYCK FHLKTDQGIK NCLPSKANQL SADDPDYAIR DLYNAIENGQ YPSWSFYIQV MTFEQAERFK YNPFDLTKIW PHSEYPLIPV GKLVLNRNPK NYFAEVEQIA FSPSHLVPGI EPSPDKMLQG RLFSYADTHR HRLGANYLQL PVNCPYRTTV ANYQRDGPQN YGNNQDGAPN YFPNSFNGPM DDKKQVQHVF KATGDVARYN SSNEDNFSQA NDLWSKVLND EERERLVSNI ADHLKSASGF IQDRAIKNFS SVNAAMGHHF K //