CATA2_NICPL
ID CATA2_NICPL Reviewed; 492 AA.
AC P49316;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Catalase isozyme 2;
DE EC=1.11.1.6;
GN Name=CAT2;
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 3-aminotriazole.
CC -!- SIMILARITY: Belongs to the catalase family. {ECO:0000305}.
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DR EMBL; Z36976; CAA85425.1; -; mRNA.
DR AlphaFoldDB; P49316; -.
DR SMR; P49316; -.
DR PRIDE; P49316; -.
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 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 2: Evidence at transcript level;
KW Heme; Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase; Peroxidase;
KW Peroxisome.
FT CHAIN 1..492
FT /note="Catalase isozyme 2"
FT /id="PRO_0000084950"
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"
SQ SEQUENCE 492 AA; 56897 MW; 4AD3FC90E24CA662 CRC64;
MDPSKFRPSS AYDSPFLTTN AGGPVYNNVS SLTVGPRGPV LLEDYHLIEK LATFDRERIP
ERVVHARGAS AKGFFEVTHD ISHLTCADFL RAPGVQTPVI VRFSTVVHER GSPESLRDIR
GFAVKFYTRE GNFDLVGNNV PVFFNRDAKS FPDTIRALKP NPKSHIQEYW RILDFFSFLP
ESLHTFAWFF DDVCLPINYR HMEGYGVHAY QLINKAGKAH YVKFHWKPTC GVKCMTEEEA
IRVGGTNHSH ATKDLYDSIA VGNYPEWKLS IHIMDPEDVE RFDFDPLDVT KIWPEDILPL
MPVGRLVLNR NIDNFFAENE QLAFNPGHIV PGLYYSEDKL LQTRIFAYAD TQRHRIGPNY
MQLPVNAPKC AHHNNHRDGA MNFMHRDEEV DYLPSRFDPC RHAEQYPIPS RVLNGRREMC
VIEKENNFKQ AGERYRSWEP DRQDRYVSKW VEHLSDPRVT YEIRSIWISY LSQADKSCGQ
KVASRLTLKP TM