ID CATA1_TOBAC Reviewed; 492 AA.
AC P49319;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 08-NOV-2023, entry version 110.
DE RecName: Full=Catalase isozyme 1;
DE EC=1.11.1.6;
DE AltName: Full=Salicylic acid-binding protein;
DE Short=SABP;
GN Name=CAT-1;
OS Nicotiana tabacum (Common tobacco).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC Nicotiana.
OX NCBI_TaxID=4097;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Petit Havana SR1; TISSUE=Leaf;
RX PubMed=7972525; DOI=10.1104/pp.106.1.399;
RA Schultes N.P., Zelitch I., McGonigle B., Nelson T.;
RT "The primary leaf catalase gene from Nicotiana tabacum and Nicotiana
RT sylvestris.";
RL Plant Physiol. 106:399-400(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 4-492, AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=cv. SR1, and cv. Xanthi NC; TISSUE=Leaf;
RX PubMed=8266079; DOI=10.1126/science.8266079;
RA Chen Z., Silva H., Klessig D.F.;
RT "Active oxygen species in the induction of plant systemic acquired
RT resistance by salicylic acid.";
RL Science 262:1883-1886(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 -!- ACTIVITY REGULATION: Inhibited by salicylic acid.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000250}. Glyoxysome
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the catalase family. {ECO:0000305}.
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DR EMBL; U07627; AAA57552.1; -; mRNA.
DR EMBL; U03473; AAC48918.1; -; mRNA.
DR PIR; A49388; A49388.
DR RefSeq; NP_001312341.1; NM_001325412.1.
DR AlphaFoldDB; P49319; -.
DR SMR; P49319; -.
DR STRING; 4097.P49319; -.
DR PaxDb; 4097-P49319; -.
DR GeneID; 107786140; -.
DR KEGG; nta:107786140; -.
DR OrthoDB; 3198922at2759; -.
DR Proteomes; UP000084051; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0009514; C:glyoxysome; IEA:UniProtKB-SubCell.
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; IBA:GO_Central.
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:0042542; P:response to hydrogen peroxide; IBA:GO_Central.
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:SF64; CATALASE ISOZYME 1; 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 1: Evidence at protein level;
KW Direct protein sequencing; Glyoxysome; Heme; Hydrogen peroxide; Iron;
KW Metal-binding; Oxidoreductase; Peroxidase; Peroxisome; Reference proteome.
FT CHAIN 1..492
FT /note="Catalase isozyme 1"
FT /id="PRO_0000084966"
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 CONFLICT 140
FT /note="V -> F (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 145
FT /note="N -> I (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 171
FT /note="K -> R (in Ref. 2; AAC48918)"
FT /evidence="ECO:0000305"
FT CONFLICT 438
FT /note="W -> F (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 439
FT /note="E -> T (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 453
FT /note="H -> A (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 469..470
FT /note="SY -> CS (in Ref. 2; AAC48918)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 492 AA; 56824 MW; 8AD3ED82F7CCE94E CRC64;
MDLSKFRPSS AYDSPFLTTN AGGPVYNNVS SLTVGPRGPV LLEDYHLIEK LATFDRERIP
ERVVHARGAS AKGFFEVTHD ISHLTCADFL RAPGVQTPVI CRFSTVVHER GSPESLRDIR
GFAVKFYTRE GNFDLVGNNV PVFFNRDAKS FPDTIRALKP NPKSHIQEYW KILDFFSFLP
ESLHTFAWFF DDVCLPTDYR HMEGYGVHAY QLINKAGKAH YVKFHWKPTC GVKCMSEEEA
IRVGGTNHSH ATKDLYDSIA AGNYPEWKLF IQIMDTEDVD KFDFDPLDVT KTWPEDILPL
MPVGRLVLNR NIDNFFAENE QLAFNPGHIV PGLYYSEDKL LQTRIFAYAD TQRHRIGPNY
MQLPVNAPKC AHHNNHRDGA MNFMHRDEEV DYLPSRFDPC RHAEQYPIPS RVLTGRREMC
VIEKENNFKQ AGERYRSWEP DRQDRYVSKW VEHLSDPRVT YEIRSIWISY LSQADKSCGQ
KVASRLTLKP TM
//
