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Database: UniProt
Entry: A0A1U7Y628_NICSY
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ID   A0A1U7Y628_NICSY        Unreviewed;       492 AA.
AC   A0A1U7Y628;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   RecName: Full=Catalase {ECO:0000256|ARBA:ARBA00012314, ECO:0000256|RuleBase:RU000498};
DE            EC=1.11.1.6 {ECO:0000256|ARBA:ARBA00012314, ECO:0000256|RuleBase:RU000498};
GN   Name=LOC104241039 {ECO:0000313|RefSeq:XP_009794245.1};
OS   Nicotiana sylvestris (Wood tobacco) (South American 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=4096 {ECO:0000313|Proteomes:UP000189701, ECO:0000313|RefSeq:XP_009794245.1};
RN   [1] {ECO:0000313|Proteomes:UP000189701}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23773524; DOI=10.1186/gb-2013-14-6-r60;
RA   Sierro N., Battey J.N., Ouadi S., Bovet L., Goepfert S., Bakaher N.,
RA   Peitsch M.C., Ivanov N.V.;
RT   "Reference genomes and transcriptomes of Nicotiana sylvestris and Nicotiana
RT   tomentosiformis.";
RL   Genome Biol. 14:R60.1-R60.17(2013).
RN   [2] {ECO:0000313|RefSeq:XP_009794245.1}
RP   IDENTIFICATION.
RC   TISSUE=Leaf {ECO:0000313|RefSeq:XP_009794245.1};
RG   RefSeq;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- FUNCTION: Occurs in almost all aerobically respiring organisms and
CC       serves to protect cells from the toxic effects of hydrogen peroxide.
CC       {ECO:0000256|ARBA:ARBA00003918, ECO:0000256|RuleBase:RU004142}.
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:0000256|ARBA:ARBA00000720,
CC         ECO:0000256|RuleBase:RU000498};
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000256|ARBA:ARBA00001971,
CC         ECO:0000256|PIRSR:PIRSR038928-2};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
CC   -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000256|ARBA:ARBA00004275}.
CC   -!- SIMILARITY: Belongs to the catalase family.
CC       {ECO:0000256|ARBA:ARBA00005329, ECO:0000256|RuleBase:RU000498}.
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DR   RefSeq; XP_009794245.1; XM_009795943.1.
DR   AlphaFoldDB; A0A1U7Y628; -.
DR   SMR; A0A1U7Y628; -.
DR   STRING; 4096.A0A1U7Y628; -.
DR   GeneID; 104241039; -.
DR   KEGG; nsy:104241039; -.
DR   eggNOG; KOG0047; Eukaryota.
DR   OrthoDB; 3198922at2759; -.
DR   Proteomes; UP000189701; Unplaced.
DR   GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
DR   GO; GO:0004096; F:catalase activity; IEA:UniProtKB-EC.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
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:SF41; CATALASE ISOZYME 2; 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   3: Inferred from homology;
KW   Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PIRSR:PIRSR038928-2};
KW   Hydrogen peroxide {ECO:0000256|ARBA:ARBA00023324,
KW   ECO:0000256|RuleBase:RU000498};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR038928-2};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR038928-2};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU000498};
KW   Peroxidase {ECO:0000256|ARBA:ARBA00022559, ECO:0000256|RuleBase:RU000498};
KW   Peroxisome {ECO:0000256|ARBA:ARBA00023140};
KW   Reference proteome {ECO:0000313|Proteomes:UP000189701}.
FT   DOMAIN          18..401
FT                   /note="Catalase core"
FT                   /evidence="ECO:0000259|SMART:SM01060"
FT   ACT_SITE        65
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT   ACT_SITE        138
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
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:0000256|PIRSR:PIRSR038928-2"
SQ   SEQUENCE   492 AA;  56822 MW;  F9E604006CF65A5A CRC64;
     MDPYKYRPSS AFNSPFCTTN SGAPVFNNNS SLTVGARGPV LLEDYHLVEK LANFDRERVP
     ERVVHARGAS AKGFFEVTHD ITHLTCADFL RAPGVQTPVI VRFSTVIHER GSPETLRDPR
     GFAVKFYTRE GNFDLVGNNF PVFFIRDGMK FPDMVHALKP NPKSHIQENW RVLDFFSHVP
     ESLHMFTFLF DDIGIPQDYR HMDGSGVHTF TLINKAGKST YVKFHWKPTC GVKSLLEEEA
     ARIGGANHSH ATQDLYDSIA AGNYPEWKLF IQTMDPDHED RFDFDPLDVT KTWPEDILPL
     QPVGRLVLNK NIDNFFNENE QLAFCPSIVV PGVYYSDDKM LQTRIFSYSD TQRYRLGPNY
     LQLPANAPKC AHHNNHYDGS MNFMHRDEEI DYFPSRYDPV RHAEKYPIPS TMCTGKREKC
     VIQKENNFKQ AGDRYRSFTP DRQERFIRRW VEALSDPRIT YEIRSIWISY WSQADKSLGQ
     KLASRLNVRP SI
//
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