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CATA1_TOBAC
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   03-AUG-2022, entry version 107.
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; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
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   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   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 peroxide.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 H2O2 = 2 H2O + O2; Xref=Rhea:RHEA:20309, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:16240; EC=1.11.1.6;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU10013};
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC   -!- ACTIVITY REGULATION: Inhibited by salicylic acid.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000250}. Glyoxysome
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the catalase family. {ECO:0000305}.
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DR   EMBL; U07627; AAA57552.1; -; mRNA.
DR   EMBL; U03473; AAC48918.1; -; mRNA.
DR   PIR; A49388; A49388.
DR   RefSeq; NP_001312341.1; NM_001325412.1.
DR   AlphaFoldDB; P49319; -.
DR   SMR; P49319; -.
DR   STRING; 4097.P49319; -.
DR   PRIDE; P49319; -.
DR   GeneID; 107786140; -.
DR   KEGG; nta:107786140; -.
DR   Proteomes; UP000084051; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0009514; C:glyoxysome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005777; C:peroxisome; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0004096; F:catalase activity; IBA:GO_Central.
DR   GO; GO:0020037; F:heme binding; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0042744; P:hydrogen peroxide catabolic process; IBA:GO_Central.
DR   GO; GO:0042542; P:response to hydrogen peroxide; IBA:GO_Central.
DR   InterPro; IPR018028; Catalase.
DR   InterPro; IPR024708; Catalase_AS.
DR   InterPro; IPR024711; Catalase_clade1/3.
DR   InterPro; IPR011614; Catalase_core.
DR   InterPro; IPR002226; Catalase_haem_BS.
DR   InterPro; IPR010582; Catalase_immune_responsive.
DR   InterPro; IPR020835; Catalase_sf.
DR   PANTHER; PTHR11465; PTHR11465; 1.
DR   Pfam; PF00199; Catalase; 1.
DR   Pfam; PF06628; Catalase-rel; 1.
DR   PIRSF; PIRSF038928; Catalase_clade1-3; 1.
DR   PRINTS; PR00067; CATALASE.
DR   SMART; SM01060; Catalase; 1.
DR   SUPFAM; SSF56634; SSF56634; 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; Reference proteome.
FT   CHAIN           1..492
FT                   /note="Catalase isozyme 1"
FT                   /id="PRO_0000084966"
FT   ACT_SITE        65
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10013"
FT   ACT_SITE        138
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10013"
FT   BINDING         348
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        140
FT                   /note="V -> F (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        145
FT                   /note="N -> I (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        171
FT                   /note="K -> R (in Ref. 2; AAC48918)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        438
FT                   /note="W -> F (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        439
FT                   /note="E -> T (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        453
FT                   /note="H -> A (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        469..470
FT                   /note="SY -> CS (in Ref. 2; AAC48918)"
FT                   /evidence="ECO:0000305"
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
 
 
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