ID   CATA1_TOBAC             Reviewed;         492 AA.
AC   P49319;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 2.
DT   16-JUN-2009, entry version 63.
DE   RecName: Full=Catalase isozyme 1;
DE            EC=1.11.1.6;
DE   AltName: Full=Salicylic acid-binding protein;
DE            Short=SABP;
GN   Name=CAT-1;
OS   Nicotiana tabacum (Common tobacco).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC   asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC   Nicotiana.
OX   NCBI_TaxID=4097;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Petit Havana SR1; TISSUE=Leaf;
RX   MEDLINE=95062747; PubMed=7972525; DOI=10.1104/pp.106.1.399;
RA   Schultes N.P., Zelitch I., McGonigle B., Nelson T.;
RT   "The primary leaf catalase gene from Nicotiana tabacum and Nicotiana
RT   sylvestris.";
RL   Plant Physiol. 106:399-400(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 4-492, AND PARTIAL PROTEIN SEQUENCE.
RC   STRAIN=cv. SR1, and cv. Xanthi NC; TISSUE=Leaf;
RX   MEDLINE=94090318; PubMed=8266079; DOI=10.1126/science.8266079;
RA   Chen Z., Silva H., Klessig D.F.;
RT   "Active oxygen species in the induction of plant systemic acquired
RT   resistance by salicylic acid.";
RL   Science 262:1883-1886(1993).
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   -!- ENZYME REGULATION: Inhibited by salicylic acid.
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; U07627; AAA57552.1; -; mRNA.
DR   EMBL; U03473; AAC48918.1; -; mRNA.
DR   PIR; A49388; A49388.
DR   HSSP; P46206; 1M7S.
DR   BRENDA; 1.11.1.6; 298.
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   1: Evidence at protein level;
KW   Direct protein sequencing; Glyoxysome; Heme; Hydrogen peroxide; Iron;
KW   Metal-binding; Oxidoreductase; Peroxidase; Peroxisome.
FT   CHAIN         1    492       Catalase isozyme 1.
FT                                /FTId=PRO_0000084966.
FT   ACT_SITE     65     65       By similarity.
FT   ACT_SITE    138    138       By similarity.
FT   METAL       348    348       Iron (heme axial ligand) (By similarity).
FT   CONFLICT    140    140       V -> F (in Ref. 2; AA sequence).
FT   CONFLICT    145    145       N -> I (in Ref. 2; AA sequence).
FT   CONFLICT    171    171       K -> R (in Ref. 2; AAC48918).
FT   CONFLICT    438    438       W -> F (in Ref. 2; AA sequence).
FT   CONFLICT    439    439       E -> T (in Ref. 2; AA sequence).
FT   CONFLICT    453    453       H -> A (in Ref. 2; AA sequence).
FT   CONFLICT    469    470       SY -> CS (in Ref. 2; AAC48918).
SQ   SEQUENCE   492 AA;  56824 MW;  8AD3ED82F7CCE94E CRC64;
     MDLSKFRPSS AYDSPFLTTN AGGPVYNNVS SLTVGPRGPV LLEDYHLIEK LATFDRERIP
     ERVVHARGAS AKGFFEVTHD ISHLTCADFL RAPGVQTPVI CRFSTVVHER GSPESLRDIR
     GFAVKFYTRE GNFDLVGNNV PVFFNRDAKS FPDTIRALKP NPKSHIQEYW KILDFFSFLP
     ESLHTFAWFF DDVCLPTDYR HMEGYGVHAY QLINKAGKAH YVKFHWKPTC GVKCMSEEEA
     IRVGGTNHSH ATKDLYDSIA AGNYPEWKLF IQIMDTEDVD KFDFDPLDVT KTWPEDILPL
     MPVGRLVLNR NIDNFFAENE QLAFNPGHIV PGLYYSEDKL LQTRIFAYAD TQRHRIGPNY
     MQLPVNAPKC AHHNNHRDGA MNFMHRDEEV DYLPSRFDPC RHAEQYPIPS RVLTGRREMC
     VIEKENNFKQ AGERYRSWEP DRQDRYVSKW VEHLSDPRVT YEIRSIWISY LSQADKSCGQ
     KVASRLTLKP TM
//