ID CATA3_SOYBN Reviewed; 492 AA. AC O48560; DT 13-DEC-2001, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1998, sequence version 1. DT 16-JUN-2009, entry version 53. DE RecName: Full=Catalase-3; DE EC=1.11.1.6; GN Name=CAT3; OS Glycine max (Soybean). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC rosids; eurosids I; Fabales; Fabaceae; Papilionoideae; Phaseoleae; OC Glycine. OX NCBI_TaxID=3847; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=cv. Corsoy 79; RA Su H., Hardy K.A., Hermsmeier D., Baum T.J.; RL Submitted (NOV-1997) 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. CC -!- CATALYTIC ACTIVITY: 2 H(2)O(2) = O(2) + 2 H(2)O. CC -!- COFACTOR: Heme group. CC -!- SUBUNIT: Homotetramer (By similarity). CC -!- SUBCELLULAR LOCATION: Peroxisome (By similarity). Glyoxysome (By CC similarity). CC -!- SIMILARITY: Belongs to the catalase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF035254; AAB88171.1; -; mRNA. DR UniGene; Gma.587; -. DR HSSP; P46206; 1M7S. DR PeroxiBase; 6261; GmKat03. DR BRENDA; 1.11.1.6; 299. DR GO; GO:0009514; C:glyoxysome; IEA:UniProtKB-SubCell. DR GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell. DR GO; GO:0004096; F:catalase activity; IEA:EC. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:UniProtKB-KW. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR InterPro; IPR002226; Catalase. DR InterPro; IPR010582; Catalase-rel_immune_responsive. DR InterPro; IPR011614; Catalase_N. DR InterPro; IPR018028; Catalase_rel_subgroup. DR Gene3D; G3DSA:2.40.180.10; Catalase_N; 1. DR PANTHER; PTHR11465; Catalase; 1. DR Pfam; PF00199; Catalase; 1. DR Pfam; PF06628; Catalase-rel; 1. DR PRINTS; PR00067; CATALASE. DR ProDom; PD000510; Catalase; 1. DR PROSITE; PS00437; CATALASE_1; 1. DR PROSITE; PS00438; CATALASE_2; 1. DR PROSITE; PS51402; CATALASE_3; 1. PE 2: Evidence at transcript level; KW Glyoxysome; Heme; Hydrogen peroxide; Iron; Metal-binding; KW Oxidoreductase; Peroxidase; Peroxisome. FT CHAIN 1 492 Catalase-3. FT /FTId=PRO_0000084964. FT ACT_SITE 65 65 By similarity. FT ACT_SITE 138 138 By similarity. FT METAL 348 348 Iron (heme axial ligand) (By similarity). 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 //