ID Q9AXE7_ZANAE Unreviewed; 492 AA.
AC Q9AXE7;
DT 01-JUN-2001, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2004, sequence version 2.
DT 03-MAY-2023, entry version 87.
DE RecName: Full=Catalase {ECO:0000256|ARBA:ARBA00012314, ECO:0000256|RuleBase:RU000498};
DE EC=1.11.1.6 {ECO:0000256|ARBA:ARBA00012314, ECO:0000256|RuleBase:RU000498};
GN Name=Cat2 {ECO:0000313|EMBL:AAG61140.2};
OS Zantedeschia aethiopica (White calla lily) (Calla aethiopica).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Araceae; Philodendroideae;
OC Zantedeschieae; Zantedeschia.
OX NCBI_TaxID=69721 {ECO:0000313|EMBL:AAG61140.2};
RN [1] {ECO:0000313|EMBL:AAG61140.2}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Spathe {ECO:0000313|EMBL:AAG61140.2};
RX AGRICOLA=IND43645536;
RA Lino-Neto T., Piques M.C., Barbeta C., Sousa M.F., Tavares R.M., Pais M.S.;
RT "Identification of Zantedeschia aethiopica Cat1 and Cat2 catalase genes and
RT their expression analysis during spathe senescence and regreening.";
RL Plant Sci. 167:889-898(2004).
CC -!- FUNCTION: Occurs in almost all aerobically respiring organisms and
CC serves to protect cells from the toxic effects of hydrogen peroxide.
CC {ECO:0000256|RuleBase:RU004142}.
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:0000256|ARBA:ARBA00000720,
CC ECO:0000256|RuleBase:RU000498};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000256|ARBA:ARBA00001971,
CC ECO:0000256|PIRSR:PIRSR038928-2};
CC -!- SIMILARITY: Belongs to the catalase family.
CC {ECO:0000256|ARBA:ARBA00005329, ECO:0000256|RuleBase:RU000498}.
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DR EMBL; AF332973; AAG61140.2; -; mRNA.
DR AlphaFoldDB; Q9AXE7; -.
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:0009628; P:response to abiotic stimulus; IEA:UniProt.
DR GO; GO:0000302; P:response to reactive oxygen species; IEA:UniProt.
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:SF45; CATALASE ISOZYME A; 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 {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PIRSR:PIRSR038928-2};
KW Hydrogen peroxide {ECO:0000256|ARBA:ARBA00023324,
KW ECO:0000256|RuleBase:RU000498};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR038928-2};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR038928-2};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU000498};
KW Peroxidase {ECO:0000256|ARBA:ARBA00022559, ECO:0000256|RuleBase:RU000498}.
FT DOMAIN 18..401
FT /note="Catalase core"
FT /evidence="ECO:0000259|SMART:SM01060"
FT ACT_SITE 65
FT /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT ACT_SITE 138
FT /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
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:0000256|PIRSR:PIRSR038928-2"
SQ SEQUENCE 492 AA; 56983 MW; A8BCEE08EB2A9D01 CRC64;
MDPCKYRPSS SYDASFTTTN AGGPVWNDDV ALTVGSRGPI LLEDYHLIEK VAHFARERIP
ERVVHARGAS AKGFFECTHD VTHLTFADFL RAPGVQTPVI VRFSTVIHER GSPETIRDPR
GFAVKFYTRE GNWDLLGNNF PVFFIRDGIK FPDVIHAFKP NPKSNVQEYW RVLDFLSHLP
ESLHTFCFLY DDVGVPLNYR HMEGFGVNTY TFINKAGKTN YVKFHWKPTC GVKCMLEDEA
VVVGGKNHSH ATQDLYDSIA AGNYPEWKLF VQVMDPDEED KYDFDPLDDT KTWPEDLLPL
QPVGRLVLNR NIDNFFNENE QLAFSPGIIV PGIYYSDDKM LQCRTFAYGD TQRYRLGPNY
LMLPVNAPKC AHKNSHYDGL MNFMHRDEEV NYYPSRHDRL RNAERFPINN RPIIGKREKC
TIEKQNDFKQ PGERYRSWAP DRQERFVRRW VEALAHPKVT FEIRTIWVSY LSKCDASLGQ
KVANRLNMKP SM
//
