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   04-NOV-2008, entry version 74.
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; Magnoliophyta; Liliopsida; Poales; Poaceae;
OC   PACCAD clade; Panicoideae; Andropogoneae; Zea.
OX   NCBI_TaxID=4577;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=cv. Wisconsin 64A;
RX   PubMed=16668346;
RA   Guan L., Ruzsa S., Skadsen R.W., Scandalios J.G.;
RT   "Comparison of the cat2 complementary DNA sequences of a normal
RT   catalase activity line (W64A) and a high catalase activity line (R6-
RT   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   MEDLINE=96270370; 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   MEDLINE=88016183; PubMed=2821546;
RA   Bethards L.A., Skadsen R.W., Scandalios J.G.;
RT   "Isolation and characterization of a cDNA clone for the Cat2 gene in
RT   maize 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   MEDLINE=90370897; PubMed=2395887;
RA   Bethards L.A., Skadsen R.W., Scandalios J.G.;
RT   "Isolation and characterization of a cDNA clone for the Cat2 gene in
RT   maize 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
CC       peroxide.
CC   -!- CATALYTIC ACTIVITY: 2 H(2)O(2) = O(2) + 2 H(2)O.
CC   -!- COFACTOR: Heme group.
CC   -!- SUBUNIT: Homotetramer.
CC   -!- SUBCELLULAR LOCATION: Peroxisome. Cytoplasm.
CC   -!- SIMILARITY: Belongs to the catalase family.
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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   RefSeq; NP_001105310.1; -.
DR   UniGene; Zm.157; -.
DR   HSSP; P46206; 1M7S.
DR   GeneID; 542230; -.
DR   Gramene; P12365; -.
DR   MaizeGDB; 13855; -.
DR   GO; GO:0005777; C:peroxisome; IEA:UniProtKB-KW.
DR   GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR002226; Catalase.
DR   InterPro; IPR011614; Catalase_N.
DR   Gene3D; G3DSA:2.40.180.10; Catalase_N; 1.
DR   PANTHER; PTHR11465; Catalase; 1.
DR   Pfam; PF00199; Catalase; 1.
DR   PRINTS; PR00067; CATALASE.
DR   ProDom; PD000510; Catalase; 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;
KW   Oxidoreductase; Peroxidase; Peroxisome; Polymorphism.
FT   CHAIN         1    491       Catalase isozyme 2.
FT                                /FTId=PRO_0000084947.
FT   ACT_SITE     64     64       By similarity.
FT   ACT_SITE    137    137       By similarity.
FT   METAL       347    347       Iron (heme axial ligand) (By similarity).
FT   VARIANT     296    296       T -> R.
FT   CONFLICT     14     14       A -> P (in Ref. 3; AAA33440).
FT   CONFLICT    124    124       K -> N (in Ref. 3; AAA33440).
FT   CONFLICT    241    242       RC -> AVG (in Ref. 2).
FT   CONFLICT    296    296       T -> A (in Ref. 2).
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
//