CATA_SOLAP
ID CATA_SOLAP Reviewed; 492 AA.
AC O24339;
DT 13-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Catalase;
DE EC=1.11.1.6;
OS Soldanella alpina (Alpine snowbell).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; Ericales; Primulaceae; Soldanella.
OX NCBI_TaxID=66308;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Leaf;
RA Schmidt M.;
RL Submitted (SEP-1997) 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}.
CC -!- SIMILARITY: Belongs to the catalase family. {ECO:0000305}.
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DR EMBL; Z99633; CAB16749.1; -; mRNA.
DR AlphaFoldDB; O24339; -.
DR SMR; O24339; -.
DR PeroxiBase; 6267; SalpKat1.
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"
FT /id="PRO_0000084959"
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; 56921 MW; 0CC8A9B2597A9EEA CRC64;
MDPYKYRSSS AFNTPFWTTN SGAPVWNNNS SLTVGTRGPI LLEDYHLVEK LANFDRERIP
ERVVHARGAS AKGFFEVTHD ISHLTCADFL RAPGVQTPVI VRFSTVIHER GSPETLRDPR
GFAVKFYTRE GNFDLVGNNF PVFFVRDGMK FPDMVHALKP NPKSHIQENW RILDFFSHHP
ESLHMFTFLF DDLGVPQDYR HMEGSGVNTY TLINKAGKAQ YVKFHWKPTC GVKCLLEDEA
IKVGGANHSH ATKDLYDSIS AGNYPEWKLF IQIIEPDHED KFDFDPLDVT KTWPEDIIPL
MPVGRLVLNK NIDNFFAENE QLAFCPALIV PGVYYSDDKL LQTRIFSYAD TQRHRLGPNY
LQLPPNAPKC AHHNNHHEGL MNFMHRDEEV NYFPSRFDPV RHAERHPIPP PVLTGKRDRC
MIEKENNFKQ PGERYRTFAP DRQERFVCRW VDALSDPRVT HEIRSIWISY WTQADKSLGQ
KLASRLNVRP TM
