CATA1_MAIZE
ID CATA1_MAIZE Reviewed; 492 AA.
AC P18122;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Catalase isozyme 1;
DE EC=1.11.1.6;
GN Name=CAT1;
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. R6-67; TISSUE=Scutellum;
RX PubMed=2461221; DOI=10.1016/0167-4781(88)90030-9;
RA Redinbaugh M.G., Wadsworth G.J., Scandalios J.G.;
RT "Characterization of catalase transcripts and their differential expression
RT in maize.";
RL Biochim. Biophys. Acta 951:104-116(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Wisconsin 64A; TISSUE=Leaf;
RX PubMed=8220459; DOI=10.1046/j.1365-313x.1993.03040527.x;
RA Guan L., Scandalios J.G.;
RT "Characterization of the catalase antioxidant defense gene Cat1 of maize,
RT and its developmentally regulated expression in transgenic tobacco.";
RL Plant J. 3:527-536(1993).
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.
CC -!- SUBCELLULAR LOCATION: Peroxisome.
CC -!- TISSUE SPECIFICITY: Scutella, milky endosperm of immature kernels,
CC leaves and epicotyls.
CC -!- SIMILARITY: Belongs to the catalase family. {ECO:0000305}.
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DR EMBL; X12538; CAA31056.1; -; mRNA.
DR EMBL; X60135; CAA42720.1; -; Genomic_DNA.
DR PIR; S48124; S48124.
DR RefSeq; NP_001105415.1; NM_001111945.1.
DR AlphaFoldDB; P18122; -.
DR SMR; P18122; -.
DR STRING; 4577.GRMZM2G088212_P01; -.
DR PeroxiBase; 6437; ZmKat1.
DR PaxDb; P18122; -.
DR PRIDE; P18122; -.
DR MaizeGDB; 13855; -.
DR eggNOG; KOG0047; Eukaryota.
DR Proteomes; UP000007305; Unplaced.
DR ExpressionAtlas; P18122; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005777; C:peroxisome; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0004096; F:catalase activity; IDA:AgBase.
DR GO; GO:0020037; F:heme binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0007623; P:circadian rhythm; IEA:EnsemblPlants.
DR GO; GO:0009631; P:cold acclimation; IMP:AgBase.
DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IBA:GO_Central.
DR GO; GO:1900034; P:regulation of cellular response to heat; IEA:EnsemblPlants.
DR GO; GO:0009737; P:response to abscisic acid; TAS:AgBase.
DR GO; GO:0009646; P:response to absence of light; IEA:EnsemblPlants.
DR GO; GO:0009733; P:response to auxin; IEP:AgBase.
DR GO; GO:0046686; P:response to cadmium ion; IEA:EnsemblPlants.
DR GO; GO:0009408; P:response to heat; IEA:EnsemblPlants.
DR GO; GO:0042542; P:response to hydrogen peroxide; IBA:GO_Central.
DR GO; GO:0006979; P:response to oxidative stress; IDA:AgBase.
DR GO; GO:0000302; P:response to reactive oxygen species; IEP:AgBase.
DR GO; GO:0009751; P:response to salicylic acid; IEA:EnsemblPlants.
DR GO; GO:1902074; P:response to salt; IEA:EnsemblPlants.
DR GO; GO:0009414; P:response to water deprivation; IEA:EnsemblPlants.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:AgBase.
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; Reference proteome.
FT CHAIN 1..492
FT /note="Catalase isozyme 1"
FT /id="PRO_0000084946"
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"
FT VARIANT 157
FT /note="A -> V (in strain: cv. W64A)"
FT VARIANT 211
FT /note="S -> T (in strain: cv. W64A)"
FT VARIANT 329
FT /note="S -> I (in strain: cv. W64A)"
FT VARIANT 483
FT /note="P -> A (in strain: cv. W64A)"
FT CONFLICT 332
FT /note="A -> G (in Ref. 1; CAA31056/CAA42720)"
FT /evidence="ECO:0000305"
FT CONFLICT 415
FT /note="R -> G (in Ref. 1; CAA31056/CAA42720)"
FT /evidence="ECO:0000305"
FT CONFLICT 456
FT /note="H -> D (in Ref. 1; CAA31056/CAA42720)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 492 AA; 56877 MW; CE10C93BEC1D9529 CRC64;
MDPYKHRPSS GSNSSFWTTN SGAPVWNNNS ALTVGQRGPI LLEDYHLIEK LAQFDRERIP
ERVVHARGAS AKGFFEVTHD VSHLTCADFL RAPGVQTPVI VRFSTVVHER GSPETLRDPR
GFAVKFYTRE GNFDLVGNNM PVFFIRDGMK FPDMVHAFKP NPKTNLQENW RIVDFFSHHP
ESLHMFTFLF DDVGIPLNYR HMEGFGVNTY SLINRDGKPH LVKFHWKPTC GVKCLLDNEA
VTVGGTCHSH ATKDLYDSIA AGNYPEWKLY IQTIDLDHED KFDFDPLDVT KTWPEDIIPL
QPVGRMVLNK NVDNFFAENE QIAFCPAISV PAIHYSDDKL LQTRIFSYAD TQRHRLGPNY
LMLPVNAPKC AHHNNHHDGF MNFMHRDEEV NYFPSRFDPA RHAEKVPIPP RVLTRCREKC
IIQKENNFKQ AGERYRSFDP ARQDRFIQRW VDALTHPRVT HEHRTIWISY WSQCDAALGQ
KLPSRLNLKP SM
