ID A0A0R0GNE3_SOYBN Unreviewed; 492 AA. AC A0A0R0GNE3; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 02-OCT-2024, entry version 38. DE RecName: Full=Catalase {ECO:0000256|ARBA:ARBA00012314, ECO:0000256|RuleBase:RU000498}; DE EC=1.11.1.6 {ECO:0000256|ARBA:ARBA00012314, ECO:0000256|RuleBase:RU000498}; GN ORFNames=GLYMA_14G223500 {ECO:0000313|EMBL:KRH17522.1}; OS Glycine max (Soybean) (Glycine hispida). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade; OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Glycine; OC Glycine subgen. Soja. OX NCBI_TaxID=3847 {ECO:0000313|EMBL:KRH17522.1}; RN [1] {ECO:0000313|EMBL:KRH17522.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC TISSUE=Callus {ECO:0000313|EMBL:KRH17522.1}; RX PubMed=20075913; DOI=10.1038/nature08670; RA Schmutz J., Cannon S.B., Schlueter J., Ma J., Mitros T., Nelson W., RA Hyten D.L., Song Q., Thelen J.J., Cheng J., Xu D., Hellsten U., May G.D., RA Yu Y., Sakurai T., Umezawa T., Bhattacharyya M.K., Sandhu D., RA Valliyodan B., Lindquist E., Peto M., Grant D., Shu S., Goodstein D., RA Barry K., Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N., RA Joshi T., Libault M., Sethuraman A., Zhang X.-C., Shinozaki K., RA Nguyen H.T., Wing R.A., Cregan P., Specht J., Grimwood J., Rokhsar D., RA Stacey G., Shoemaker R.C., Jackson S.A.; RT "Genome sequence of the palaeopolyploid soybean."; RL Nature 463:178-183(2010). RN [2] {ECO:0000313|EMBL:KRH17522.1} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Callus {ECO:0000313|EMBL:KRH17522.1}; RA Schmutz J., Cannon S., Schlueter J., Ma J., Mitros T., Nelson W., Hyten D., RA Song Q., Thelen J., Cheng J., Xu D., Hellsten U., May G., Yu Y., RA Sakurai T., Umezawa T., Bhattacharyya M., Sandhu D., Valliyodan B., RA Lindquist E., Peto M., Grant D., Shu S., Goodstein D., Barry K., RA Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N., Joshi T., RA Libault M., Sethuraman A., Zhang X., Shinozaki K., Nguyen H., Wing R., RA Cregan P., Specht J., Grimwood J., Rokhsar D., Stacey G., Shoemaker R., RA Jackson S.; RT "WGS assembly of Glycine max."; RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases. 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 = 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 -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}. 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; CM000847; KRH17522.1; -; Genomic_DNA. DR RefSeq; NP_001235974.1; NM_001249045.1. DR AlphaFoldDB; A0A0R0GNE3; -. DR SMR; A0A0R0GNE3; -. DR GeneID; 100037447; -. DR KEGG; gmx:100037447; -. DR OMA; PVFPIRD; -. DR OrthoDB; 3198922at2759; -. DR GO; GO:0005777; C:peroxisome; IEA:UniProtKB-KW. 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; cd08154; catalase_clade_1; 1. DR Gene3D; 2.40.180.10; Catalase core domain; 1. DR InterPro; IPR018028; Catalase. 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:SF23; CATALASE-2; 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 Peroxisome {ECO:0000256|ARBA:ARBA00023140}. FT DOMAIN 18..401 FT /note="Catalase core" FT /evidence="ECO:0000259|SMART:SM01060" FT ACT_SITE 65 FT /evidence="ECO:0000256|PIRSR:PIRSR038928-1" FT ACT_SITE 138 FT /evidence="ECO:0000256|PIRSR:PIRSR038928-1" FT BINDING 348 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 492 AA; 56911 MW; 36265068CF9F6CF1 CRC64; MDPYKNRPSS AFNSPFWTTN SGAPIWNNNS SLTVGSRGPI LLEDYHLVEK LANFDRERIP ERVVHARGAS AKGFFEVTHD ISHLTCADFL RAPGVQTPLI VRFSTVIHER GSPETLRDPR GFAVKFYTRE GNFDLVGNNF PVFFVRDGLK FPDMVHALKP NPKSHIQENW RILDFFSHHP ESLHMFSFLF DDVGIPQDYR HMDGFGVNTY TLINKAGKAV YVKFHWKTTC GEKCLLDDEA IRVGGSNHSH ATQDLYDSIA AGNYPEWKLY IQTLDPENED RLDFDPLDVT KTWPEDVLPL QPVGRMVLNK NIDNFFAENE QLAFCPAIIV PGVYYSDDKL LQTRIFSYAD TQRHRLGPNY LQLPANSPKC AHHNNHHDGF MNFMHRDEEV NYFPSRYDPV RHAERVPVPP RTLGGKREKC MIEKENNFKQ PGERYRSWPS DRQERFVRRW VDALSDPRVT HEIRSIWISY WSQADRSLGQ KIASHLNLKP SI //