CATA_SOLME
ID CATA_SOLME Reviewed; 492 AA.
AC P55311;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Catalase;
DE EC=1.11.1.6;
OS Solanum melongena (Eggplant) (Aubergine).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum.
OX NCBI_TaxID=4111;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Sinsadoharanasu; TISSUE=Hypocotyl;
RA Toguri T.;
RL Submitted (JAN-1994) to the EMBL/GenBank/DDBJ databases.
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:0000250}. Glyoxysome
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the catalase family. {ECO:0000305}.
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DR EMBL; X71653; CAA50644.1; -; mRNA.
DR AlphaFoldDB; P55311; -.
DR SMR; P55311; -.
DR PRIDE; P55311; -.
DR GO; GO:0009514; C:glyoxysome; 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 Glyoxysome; Heme; Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase;
KW Peroxidase; Peroxisome.
FT CHAIN 1..492
FT /note="Catalase"
FT /id="PRO_0000084960"
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; 56620 MW; DFC40D8CA714FB1A CRC64;
MDLSKYRPSS AYDTPFLTTN AGGPVYNNVS SLTVGPRGPV LLEDYHLIEK LATFDRERIP
ERVVHARGAS AKGFFEVTHD VSHLTCADFL RAPGVQTPVI CRFSTVVHER GSPESIRDIR
GFAVKFYTRE GNFDLVGNNV PVFFNRDAKS FPDTIRALKP NPKSHIQENW RILDFFSFLP
ESLHTFAFFY DDVCLPINYR HMEGFGVHAY QLINKAGKAH YVKFHWKPTC GVKSMTEEEA
IRVGGTNHSH ATKDLYDSIA AGNYPEWKLF IQIMDPEDVD KFDFDPLDVT KTWPEDILPL
MPVGRLVLNR NIDNFFAENE QLAFNPGHIV PGVYYSEDKL LQTRIFAYAD TQRHRIGPNY
MQLPVNAPKC AHHNNHRDGA MNFMHRDEEV DYLPSRFDPC RPAEQYPIPS CVLTGRREKC
VIPKENNFKQ AGERYRTWEP DRQDRYINKW VESLSDPRVT HEIRSIWISY LSQADKSCGQ
KVASRLLVKP TM
