ID   CATA1_NICPL             Reviewed;         485 AA.
AC   P49315;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   22-FEB-2023, entry version 94.
DE   RecName: Full=Catalase isozyme 1;
DE            EC=1.11.1.6;
DE   Flags: Fragment;
GN   Name=CAT1;
OS   Nicotiana plumbaginifolia (Leadwort-leaved tobacco) (Tex-Mex 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=4092;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Leaf;
RX   PubMed=7925949; DOI=10.1016/0014-5793(94)00923-6;
RA   Willekens H., Villarroel R., van Montagu M., Inze D., van Camp W.;
RT   "Molecular identification of catalases from Nicotiana plumbaginifolia
RT   (L.).";
RL   FEBS Lett. 352:79-83(1994).
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   -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000305}.
CC   -!- INDUCTION: By paraquat and 3-aminotriazole.
CC   -!- SIMILARITY: Belongs to the catalase family. {ECO:0000305}.
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DR   EMBL; Z36975; CAA85424.1; -; mRNA.
DR   PIR; S48650; S48650.
DR   AlphaFoldDB; P49315; -.
DR   SMR; P49315; -.
DR   GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
DR   GO; GO:0004096; F:catalase activity; IEA:UniProtKB-EC.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR   CDD; cd08154; catalase_clade_1; 1.
DR   Gene3D; 2.40.180.10; Catalase core domain; 1.
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; CATALASE; 1.
DR   PANTHER; PTHR11465:SF41; CATALASE ISOZYME 2; 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; Heme-dependent catalase-like; 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; Peroxidase;
KW   Peroxisome.
FT   CHAIN           <1..485
FT                   /note="Catalase isozyme 1"
FT                   /id="PRO_0000084949"
FT   ACT_SITE        58
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10013"
FT   ACT_SITE        131
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10013"
FT   BINDING         341
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   NON_TER         1
SQ   SEQUENCE   485 AA;  55850 MW;  00BA53BEF7699A13 CRC64;
     PSSAFNSPFC TTNSGAPVFN NNSSLTVGAR GPVLLEDYHL VEKLANFDRE RVPERVVHAR
     GASAKGFFEV THDITHLTCA DFLRAPGVQT PVIVRFSTVI HERGSPETLR DPRGFAVKFY
     TREGNFDLVG NNFPVFFIRD GMKFPDMVHA LKPNPKSHIQ ENWRVLDFFS HVPESLHMFT
     FLFDDIGIPQ DYRHMDGSGV HTFTLINKAG KSTYVKFHWK PTCGVKSLLE DEAARVGGAN
     HSHATQDLYD SIAAGNYPEW KLFIQTMDPD HEDRFDFDPL DVTKTWPEDI LPLQPVGRLV
     LNKNIDNFSN ENEQLAFCPS IVVPGVYYSD DKMLQTRIFS YSDTQRYRLG PNYLQLPANA
     PKCAHHNNHY DGSMNFMHRD EEIDYFPSRY DPVRHAEKYP IPSTMCTGKR EKCVIQKENN
     FKQPGERYRS FTPDRQERFI RRWVETLSDP RITYEIRSIW ISYWSQADKS LGQKLASRLN
     VRPSI
//