CATA3_NICPL
ID CATA3_NICPL Reviewed; 492 AA.
AC P49317;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Catalase isozyme 3;
DE EC=1.11.1.6;
GN Name=CAT3;
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=Flower;
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; Z36977; CAA85426.1; -; mRNA.
DR PIR; T16969; T16969.
DR AlphaFoldDB; P49317; -.
DR SMR; P49317; -.
DR PRIDE; P49317; -.
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 3"
FT /id="PRO_0000084951"
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; 57017 MW; 2A49AD89CC6FB4D5 CRC64;
MDPYKYRPSS ANNSPFWTTN SGAPVWNNNS SMTVGTRGPI LLEDYHLVEK LANFDRERIP
ERVVHARGAS AKGFFEVTHD ITHLTCADFL RAPGVQTPVI VRFSTVIHER GSPETLRDPR
GFAVKFYTRE GNFDLVGNNF PVFFVRDGMK FPDMVHALKP NPKSHIQENW RILDFFSHHP
ESLHMFSFLF DDLGVPQDYR HMEGSGVNTY MLINKAGKAH YVKFHWKPTC GVKCLLEEEA
IKVGGANHSH ATKDLYDSIA AGNYPEWKLF IQIIDPDHED RFDFDPLDVT KTWPEDILPL
QPVGRLVLNK NIDNFFAENE QLAFWPAIVV PGVYCSDDKL LQTRIFSYSD AQRHRLGPNY
LQLPVNAPKC AHHNNHHEGF MNFMHRDEEV NYFPSRFDPC RHAEQYPIPP CVLTGKRDKC
IIEKENNFKQ PGERYRSWAP DRQERFICRW VDALSDPRVT HEIRSIWFSY WSQADKTLGQ
KIASRLNVRP TM