CATA3_MAIZE
ID CATA3_MAIZE Reviewed; 496 AA.
AC P18123;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Catalase isozyme 3;
DE EC=1.11.1.6;
GN Name=CAT3;
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 [GENOMIC DNA].
RC STRAIN=cv. Wisconsin 64A; TISSUE=Seedling leaf;
RX PubMed=8400123; DOI=10.1007/bf00028975;
RA Abler M.L., Scandalios J.G.;
RT "Isolation and characterization of a genomic sequence encoding the maize
RT Cat3 catalase gene.";
RL Plant Mol. Biol. 22:1031-1038(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Wisconsin 64A; TISSUE=Epicotyl;
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).
CC -!- FUNCTION: Occurs in almost all aerobically respiring organisms and
CC serves to protect cells from the toxic effects of hydrogen peroxide.
CC Its levels are highest in the light period and are lowest in the dark
CC period, hence it may be important for scavenging hydrogen peroxide at
CC night, rather than during the day.
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: Mitochondrion.
CC -!- TISSUE SPECIFICITY: Leaf mesophyll cells, pericarp, seedling roots and
CC the coleoptile.
CC -!- SIMILARITY: Belongs to the catalase family. {ECO:0000305}.
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DR EMBL; L05934; AAC37357.1; -; Genomic_DNA.
DR EMBL; M33103; AAA33441.1; -; mRNA.
DR EMBL; X12539; CAA31057.1; -; mRNA.
DR PIR; S37379; S37379.
DR RefSeq; NP_001105416.1; NM_001111946.1.
DR AlphaFoldDB; P18123; -.
DR SMR; P18123; -.
DR STRING; 4577.GRMZM2G079348_P01; -.
DR PeroxiBase; 6439; ZmKat3.
DR PaxDb; P18123; -.
DR PRIDE; P18123; -.
DR MaizeGDB; 13855; -.
DR eggNOG; KOG0047; Eukaryota.
DR Proteomes; UP000007305; Unplaced.
DR ExpressionAtlas; P18123; differential.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IDA:AgBase.
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; TAS:AgBase.
DR GO; GO:0009631; P:cold acclimation; IMP:AgBase.
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:0006979; P:response to oxidative stress; IDA: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 Heme; Hydrogen peroxide; Iron; Metal-binding; Mitochondrion;
KW Oxidoreductase; Peroxidase; Reference proteome.
FT CHAIN 1..496
FT /note="Catalase isozyme 3"
FT /id="PRO_0000084948"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 402..422
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 67
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10013"
FT ACT_SITE 140
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10013"
FT BINDING 351
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 CONFLICT 57
FT /note="A -> D (in Ref. 2; AAA33441/CAA31057)"
FT /evidence="ECO:0000305"
FT CONFLICT 79
FT /note="C -> S (in Ref. 2; AAA33441/CAA31057)"
FT /evidence="ECO:0000305"
FT CONFLICT 107
FT /note="T -> Q (in Ref. 2; AAA33441/CAA31057)"
FT /evidence="ECO:0000305"
FT CONFLICT 110..116
FT /note="HERGSPE -> PEPGSGR (in Ref. 2; AAA33441/CAA31057)"
FT /evidence="ECO:0000305"
FT CONFLICT 121
FT /note="P -> A (in Ref. 2; AAA33441/CAA31057)"
FT /evidence="ECO:0000305"
FT CONFLICT 194
FT /note="D -> H (in Ref. 2; AAA33441)"
FT /evidence="ECO:0000305"
FT CONFLICT 234
FT /note="V -> E (in Ref. 2; AAA33441/CAA31057)"
FT /evidence="ECO:0000305"
FT CONFLICT 236
FT /note="C -> S (in Ref. 2; AAA33441)"
FT /evidence="ECO:0000305"
FT CONFLICT 244..245
FT /note="AL -> R (in Ref. 2; AAA33441/CAA31057)"
FT /evidence="ECO:0000305"
FT CONFLICT 254
FT /note="Missing (in Ref. 2; AAA33441/CAA31057)"
FT /evidence="ECO:0000305"
FT CONFLICT 264
FT /note="A -> AE (in Ref. 2; AAA33441/CAA31057)"
FT /evidence="ECO:0000305"
FT CONFLICT 280..281
FT /note="DT -> AQ (in Ref. 2; AAA33441/CAA31057)"
FT /evidence="ECO:0000305"
FT CONFLICT 282
FT /note="E -> Q (in Ref. 2; AAA33441)"
FT /evidence="ECO:0000305"
FT CONFLICT 319
FT /note="F -> L (in Ref. 2; AAA33441/CAA31057)"
FT /evidence="ECO:0000305"
FT CONFLICT 374..375
FT /note="AH -> GT (in Ref. 2; AAA33441/CAA31057)"
FT /evidence="ECO:0000305"
FT CONFLICT 386
FT /note="F -> L (in Ref. 2; AAA33441/CAA31057)"
FT /evidence="ECO:0000305"
FT CONFLICT 402..408
FT /note="PLRQAAP -> RRCGRAA (in Ref. 2; AAA33441/CAA31057)"
FT /evidence="ECO:0000305"
FT CONFLICT 452..460
FT /note="RRFADSLGH -> KAIRRLART (in Ref. 2; AAA33441/
FT CAA31057)"
FT /evidence="ECO:0000305"
FT CONFLICT 463
FT /note="V -> G (in Ref. 2; CAA31057)"
FT /evidence="ECO:0000305"
FT CONFLICT 463
FT /note="V -> R (in Ref. 2; AAA33441)"
FT /evidence="ECO:0000305"
FT CONFLICT 478
FT /note="C -> V (in Ref. 2; AAA33441/CAA31057)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 496 AA; 56796 MW; 566FFD05B3795B49 CRC64;
MTMDPTKFRP SSSHDTTVTT TNAGAPVWND NEALTVGPRG PILLEDYHLI EKVAHFARER
IPERVVHARG ASAKGFFECT HDVTSLTCAD FLRAPGVRTP VIVRFSTVIH ERGSPETIRD
PRGFAVKFYT REGNWDLLGN NFPVFFIRDG IKFPDVIHAF KPNPRSHVQE YWRVFDFLSH
LPESLHTFFF LFDDVGVPSD YRHMEGFGVN TYTFVSAAGK AQYVKFHWKP TCGVRCILTD
EEAALVGGRN HSHATQDLYD SIAAGSFPEW TLYVQVMDPD TEEQYDFDPL DDTKTWPEDL
LPLRPVGRLV LDRNVDNFFN ENEQLAFGPG LVVPGIYYSD DKMLQCRVFA YADTQRYRLG
PNYLMLPVNA PRCAHHNNHY DGAMNFMHRD EEVDYYPSRH APLRQAAPPT PLPPRPVAGR
REKATIRKPN DFKQPGERYR SWDADRQDRF VRRFADSLGH PKVSQELRSI WIDLLAKCDA
SLGMKIATRL NMKANM
