CATA2_MAIZE
ID CATA2_MAIZE Reviewed; 491 AA.
AC P12365;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 3.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Catalase isozyme 2;
DE EC=1.11.1.6;
GN Name=CAT2;
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. Wisconsin 64A;
RX PubMed=16668346; DOI=10.1104/pp.96.4.1379;
RA Guan L., Ruzsa S., Skadsen R.W., Scandalios J.G.;
RT "Comparison of the cat2 complementary DNA sequences of a normal catalase
RT activity line (W64A) and a high catalase activity line (R6-67) of maize.";
RL Plant Physiol. 96:1379-1381(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Wisconsin 64A; TISSUE=Leaf;
RX PubMed=8639750; DOI=10.1007/bf00020803;
RA Guan L., Polidoros A.N., Scandalios J.G.;
RT "Isolation, characterization and expression of the maize Cat2 catalase
RT gene.";
RL Plant Mol. Biol. 30:913-924(1996).
RN [3]
RP PRELIMINARY NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. R6-67;
RX PubMed=2821546; DOI=10.1073/pnas.84.19.6830;
RA Bethards L.A., Skadsen R.W., Scandalios J.G.;
RT "Isolation and characterization of a cDNA clone for the Cat2 gene in maize
RT and its homology with other catalases.";
RL Proc. Natl. Acad. Sci. U.S.A. 84:6830-6834(1987).
RN [4]
RP SEQUENCE REVISION TO C-TERMINUS.
RX PubMed=2395887; DOI=10.1073/pnas.87.17.6927;
RA Bethards L.A., Skadsen R.W., Scandalios J.G.;
RT "Isolation and characterization of a cDNA clone for the Cat2 gene in maize
RT and its homology with other catalases.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:6927-6927(1990).
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. Cytoplasm.
CC -!- SIMILARITY: Belongs to the catalase family. {ECO:0000305}.
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DR EMBL; X54819; CAA38588.1; -; mRNA.
DR EMBL; Z54358; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; J02976; AAA33440.1; -; mRNA.
DR PIR; S71455; S71455.
DR AlphaFoldDB; P12365; -.
DR SMR; P12365; -.
DR STRING; 4577.GRMZM2G090568_P01; -.
DR PeroxiBase; 6438; ZmKat2.
DR PaxDb; P12365; -.
DR MaizeGDB; 13855; -.
DR eggNOG; KOG0047; Eukaryota.
DR Proteomes; UP000007305; Unplaced.
DR ExpressionAtlas; P12365; 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:0042744; P:hydrogen peroxide catabolic process; IBA:GO_Central.
DR GO; GO:0009733; P:response to auxin; IEP:AgBase.
DR GO; GO:0042542; P:response to hydrogen peroxide; IBA:GO_Central.
DR GO; GO:0009416; P:response to light stimulus; TAS:AgBase.
DR GO; GO:0000302; P:response to reactive oxygen species; IEP:AgBase.
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 Cytoplasm; Heme; Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase;
KW Peroxidase; Peroxisome; Reference proteome.
FT CHAIN 1..491
FT /note="Catalase isozyme 2"
FT /id="PRO_0000084947"
FT ACT_SITE 64
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10013"
FT ACT_SITE 137
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10013"
FT BINDING 347
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 296
FT /note="T -> R"
FT CONFLICT 14
FT /note="A -> P (in Ref. 3; AAA33440)"
FT /evidence="ECO:0000305"
FT CONFLICT 124
FT /note="K -> N (in Ref. 3; AAA33440)"
FT /evidence="ECO:0000305"
FT CONFLICT 241..242
FT /note="RC -> AVG (in Ref. 2; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 296
FT /note="T -> A (in Ref. 2; no nucleotide entry)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 491 AA; 56466 MW; 6B686B6A94EA8598 CRC64;
MDPYKHRPSS AFNAPYWTTN SGAPVWNNDS SLTVGARGPI LLEDYHCEKL ANFDRERIPE
RVVHARGASA KGFFEVTHDI THLTCADFLR APGVQTPVIV RFSTVIHERG SPETLRDPRG
FAVKFYTREG NWDLVGNNFP VFFIRDGIKF PDMVHALKPN PRTHIQDNWR ILDFFSHHPE
SLHMFSFLFD DVGIPADYRH MDGSGVHTYT LVSRAGTVTY VKFHWRPTCG VRSLMDDEAV
RCGANHSHAT KDLTDAIAAG NFPEWTLYIQ TMDPEMEDRL DDLDPLDVTK TWPEDTFPLQ
PVGRLVLNRN IDNFFAENEQ LAFCPGLIVP GIYYSDDKLL QTRIFSYSDT QRHRLGPNYL
LLPANAPKCA HHNNHYDGSM NFMHRHEEVD YFPSRYDAVR NAPRYPIPTA HIAGRREKTV
ISKENNFKQP GERYRAMDPA RQERFITRWV DALSDPRLTH EIRTIWLSNW SQADRSLGQK
LASRLSAKPS M
