ID CATA_CAPAN Reviewed; 492 AA. AC Q9M5L6; DT 13-DEC-2001, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 25-NOV-2008, entry version 40. DE RecName: Full=Catalase; DE EC=1.11.1.6; DE AltName: Full=CaCat1; GN Name=CAT; OS Capsicum annuum (Bell pepper). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Capsiceae; OC Capsicum. OX NCBI_TaxID=4072; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=11297793; DOI=10.1016/S0168-9452(01)00332-6; RA Kwon S.-I., An C.-S.; RT "Molecular cloning, characterization and expression analysis of a RT catalase cDNA from hot pepper (Capsicum annuum L.)."; RL Plant Sci. 160:961-969(2001). 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). CC -!- TISSUE SPECIFICITY: In stems, leaves, roots and developing fruits. CC -!- INDUCTION: In roots, by aluminum and salt. Expressed with a CC circadian rhythm reaching a maximum at late in the dark period or CC early in the light period. 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; AF227952; AAF34718.1; -; mRNA. DR PIR; JE0126; JE0126. DR HSSP; P46206; 1M7S. DR GO; GO:0005777; C:peroxisome; IEA:UniProtKB-KW. DR GO; GO:0004096; F:catalase activity; IEA:InterPro. DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-KW. 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; IPR011614; Catalase_N. DR Gene3D; G3DSA:2.40.180.10; Catalase_N; 1. DR PANTHER; PTHR11465; Catalase; 1. DR Pfam; PF00199; Catalase; 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 Heme; Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase; KW Peroxidase; Peroxisome. FT CHAIN 1 492 Catalase. FT /FTId=PRO_0000084934. 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; 56480 MW; 5D987B637FCDD4E7 CRC64; MDLSKYRPSS AYDSPFLTTN AGGPVYNNVS SLTVGPRGPV LLEDYHLIEK LATFVRERIP ERVVHARGAS AKGFFEVTHD ISHLTCADFL RAPGVQTPVI CRFSTVVHER GSPESIRDIR GFAVKFYTRE GNFDLVGNNV PVFFNRDAKS FPDTIRALKP NPKSHIQENW RILDFFSFLP ESLHTFAFFY DDVCLPTDYR HMEGFGVHAY QLINKAGKAH YVKFHWKPTC GVKSMTEEEA IRVGGTNHSH ATKDLYDSIA AGNYPEWKLF IQIMNPEDVD KFDFDPLDVT KTWPEDILPL MPVGRLVLNR NIDNFFAENE QLAFNPGHIV PGVYYSEDKL LQTRIFAYAD TQRHRIGPNY MQLPVNAPKC AHHNNHRDGA MNFMHRDEEV DYLPSRFDPC RPAEQYPIPS CVLTGRREKC VIPKENNFKQ AGERYRSWAP DRQDRYINKW VESLSDPRAT HEIRSIWISY LSQADKSCGQ KVASRLTVKP TM //