ID CATA4_SOYBN Reviewed; 492 AA. AC O48561; DT 13-DEC-2001, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1998, sequence version 1. DT 16-JUN-2009, entry version 58. DE RecName: Full=Catalase-4; DE EC=1.11.1.6; GN Name=CAT4; 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; AF035255; AAB88172.1; -; mRNA. DR UniGene; Gma.29859; -. DR HSSP; P46206; 1M7S. DR PeroxiBase; 6266; GmKat04. 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-4. FT /FTId=PRO_0000084965. 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; 56737 MW; FEF3B4706A4FD669 CRC64; MDPYKHRPSS AFNSPFWTTN SGAPIWNNNS SLTVGARGPI LLEDYHLVEK LANFDRERIP ERVVHARGAS AKGFFEVTHD ISHLTCADFL RAPGVQTPVI VRFSTVIHER GSPETLRDPR GFAVKFYTRE GNFDLVGNNL PVFFVRDGMK FPDMVHALKP NPKNHIQENW RILDFFSHFP ESLHMFTFLF DDLGVPQDYR HMDGFGVNTY TLINKAGKAV YVKFHWKTTS GIKCLLEEEA IKVGGANHSH ATQDLHDSIA AGNYPEWKLF VQTIDPEHED KFDFDPLDVT KTWPEDIIPL QPVGRLVLNK NIDNFFAENE QLAFCPAIVV PGVYYSDDKM LQTRIFSYAD SQRHRLGPNY LQLPANAPKC AHHNNHHEGF MNFIHRDEEV NYFPSRYDPV RHAERFPIPP AICSGRREKC GIEKENNFKQ PGERYRSWAP DRQDRFARRW VDALSDPRVT HEIRSVWISY WSQADRSLGQ KIASHLSTRP NI //