ID CATA1_WHEAT Reviewed; 492 AA. AC Q43206; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 16-JUN-2009, entry version 57. DE RecName: Full=Catalase-1; DE EC=1.11.1.6; GN Name=CAT1; OS Triticum aestivum (Wheat). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; BEP clade; OC Pooideae; Triticeae; Triticum. OX NCBI_TaxID=4565; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RA Saruyama H., Matsumura T.; RL Submitted (JUL-1996) 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 (By similarity). 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; D86327; BAA13068.1; -; mRNA. DR PIR; T06478; T06478. DR UniGene; Ta.53948; -. DR HSSP; P46206; 1M7S. DR Gramene; Q43206; -. DR BRENDA; 1.11.1.6; 253. 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-1. FT /FTId=PRO_0000084967. 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; 56808 MW; 52899174D5BA2EAB CRC64; MDPYKYRPSS SFNAPMWSTN SGAPVWNNDN SLTVGSRGPI LLEDYHLVEK IADFDRERIP ERVVHARGAT AKGFFEVTHD VSHLTCADFL RAPGVQTPVI VRFSTVIHER GSPETLRDPR GFAIKFYTRE GNWDLVGNNF PVFFIRDGMK FPDMVHALKP NPKTHIQENW RILDFFSHHP ESLHMFTFLF DDIGVPADYR HMDGSGVNTY TLVNRAGKAH YVKFHWKPTC GVKSLLEEEA VTVGGTNHSH ATKDLTDSIA AGNYPEWTFY IQTIDPDYEE RFDFDPLDVT KTWPEDVVPL QPVGRLVLNR NIDNFFSENE QLAFCPGIIV PGVYYSDDKL LQTRIFSYSD TQRHRLGPNY LLLPANAPKC SHHNNHYDGL MNFMHRDEEV DYFPSRFDPA KHAPRYPIPS RTLNGRREKM VIEKENNFKQ PGERYRSMDP ARQERFINRW IDALSDPRLT HEIKAIWLSY WSQADKSLGQ KLASRLSSKP SM //