CATA_AVIMR
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 03-AUG-2022, entry version 80.
DE RecName: Full=Catalase;
DE EC=1.11.1.6;
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: 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 -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000250}.
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: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 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; Oxidoreductase; Peroxidase;
KW 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 7..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"
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