ID   CATA_AVIMR              Reviewed;         492 AA.
AC   Q9AXH0;
DT   13-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   04-NOV-2026, entry version 88.
DE   RecName: Full=Catalase;
DE            EC=1.11.1.6 {ECO:0000255|PROSITE-ProRule:PRU10013};
OS   Avicennia marina (Grey mangrove) (Sceura marina).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Lamiales; Acanthaceae; Avicennioideae; Avicennia.
OX   NCBI_TaxID=82927;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Jithesh M.N., Parani M., Parida A.;
RT   "Characterization of a cDNA for catalase from the mangrove species
RT   Avicennia marina.";
RL   Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the degradation of hydrogen peroxide (H(2)O(2))
CC       generated by peroxisomal oxidases to water and oxygen, thereby
CC       protecting cells from the toxic effects of hydrogen peroxide.
CC       {ECO:0000250|UniProtKB:P04040}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 H2O2 = O2 + 2 H2O; 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         Evidence={ECO:0000250|UniProtKB:P04040};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC       {ECO:0000250|UniProtKB:P25819}. Peroxisome matrix
CC       {ECO:0000250|UniProtKB:P25819}.
CC   -!- SIMILARITY: Belongs to the catalase family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AF328861; AAK06839.1; -; mRNA.
DR   AlphaFoldDB; Q9AXH0; -.
DR   SMR; Q9AXH0; -.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0005782; C:peroxisomal matrix; ISS:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IEA:TreeGrafter.
DR   GO; GO:0004096; F:catalase activity; IEA:UniProtKB-EC.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:TreeGrafter.
DR   GO; GO:0042542; P:response to hydrogen peroxide; IEA:TreeGrafter.
DR   CDD; cd08154; catalase_clade_1; 1.
DR   FunFam; 2.40.180.10:FF:000002; Catalase; 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   2: Evidence at transcript level;
KW   Cytoplasm; Heme; Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase;
KW   Peroxidase; Peroxisome.
FT   CHAIN           1..492
FT                   /note="Catalase"
FT                   /id="PRO_0000084933"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        8..25
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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|UniProtKB:P04040"
SQ   SEQUENCE   492 AA;  57160 MW;  FCC681172808F925 CRC64;
     MDPYKYCPSS SFNTPHTTTN GGHPVYNDNS SLTVGTRGPV LLEDYQLIDK LAHFTRERIP
     ERVVHARGAT AKGFFEVTHD VSHLTCADFL RAPGVQTPLI VRFSTVIHER GSPETLRDPR
     GFAVKFYTRE GNFDIVGNNF PVFFIRDAIK FPDVIHAFKP NPKSHIQESW RILDFCSHFP
     ESLLTFAWFY DDVGIPQDYR HMEGFGVHSY TLINKAGKVN YVKFHWKPTC GVKCLMEDEA
     VRIGGTNHSH ATQDLYDSIA AGNYPEWKLY FQIMDPDQED RFDFDPLDTT KIWPEDIIPL
     IPVGRMVLNK NIDNFFAENE MLAFSPHMIV PGINFSNDKM LQTRIFAYGD TQRHRLGPNY
     LLLPVNAPKC AYHNNHYDGF MNFMHRDEEV DYFPSKYDPT RHAERHPIPN AVITGRRDRR
     VIEKEDNFKQ AGDRYRSWAP DRQERFLRRW VDALSDPRLT LEIRSIWVSY WSQADKSFGQ
     KLASRLNVRP TM
//