ID A0A0R0GNE3_SOYBN Unreviewed; 492 AA. AC A0A0R0GNE3; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 15-MAR-2017, entry version 9. DE RecName: Full=Catalase {ECO:0000256|RuleBase:RU000498}; DE EC=1.11.1.6 {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; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; rosids; fabids; Fabales; Fabaceae; Papilionoideae; OC Phaseoleae; Glycine; Soja. OX NCBI_TaxID=3847 {ECO:0000313|EMBL:KRH17522.1}; RN [1] {ECO:0000313|EMBL:KRH17522.1} RP NUCLEOTIDE SEQUENCE. 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., RA May G.D., Yu Y., Sakurai T., Umezawa T., Bhattacharyya M.K., RA Sandhu D., Valliyodan B., Lindquist E., Peto M., Grant D., Shu S., RA Goodstein D., Barry K., Futrell-Griggs M., Abernathy B., Du J., RA Tian Z., Zhu L., Gill N., Joshi T., Libault M., Sethuraman A., RA Zhang X.-C., Shinozaki K., Nguyen H.T., Wing R.A., Cregan P., RA Specht J., Grimwood J., Rokhsar D., Stacey G., Shoemaker R.C., RA 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 Hoefler B.C., Straight P.D.; RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Occurs in almost all aerobically respiring organisms and CC serves to protect cells from the toxic effects of hydrogen CC peroxide. {ECO:0000256|RuleBase:RU004142}. CC -!- CATALYTIC ACTIVITY: 2 H(2)O(2) = O(2) + 2 H(2)O. CC {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|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 UniGene; Gma.587; -. DR ProteinModelPortal; A0A0R0GNE3; -. DR SMR; A0A0R0GNE3; -. DR GeneID; 100037447; -. DR KEGG; gmx:100037447; -. DR KO; K03781; -. DR OMA; ESTHMIT; -. 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 Gene3D; 2.40.180.10; -; 1. DR InterPro; IPR018028; Catalase. DR InterPro; IPR020835; Catalase-like_dom. 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 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 3: Inferred from homology; KW Heme {ECO:0000256|PIRSR:PIRSR038928-2, ECO:0000256|RuleBase:RU000498}; KW Hydrogen peroxide {ECO:0000256|RuleBase:RU000498}; KW Iron {ECO:0000256|PIRSR:PIRSR038928-2, ECO:0000256|RuleBase:RU000498}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR038928-2, KW ECO:0000256|RuleBase:RU000498}; KW Oxidoreductase {ECO:0000256|RuleBase:RU000498}; KW Peroxidase {ECO:0000256|RuleBase:RU000498}. FT DOMAIN 18 401 Catalase. {ECO:0000259|SMART:SM01060}. FT ACT_SITE 65 65 {ECO:0000256|PIRSR:PIRSR038928-1}. FT ACT_SITE 138 138 {ECO:0000256|PIRSR:PIRSR038928-1}. FT METAL 348 348 Iron (heme axial ligand). FT {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 //