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Entry: A0A099W9Q1_9LIST
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ID   A0A099W9Q1_9LIST        Unreviewed;       486 AA.
AC   A0A099W9Q1;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   SubName: Full=Catalase {ECO:0000313|EMBL:KGL41168.1};
GN   ORFNames=EP56_11225 {ECO:0000313|EMBL:KGL41168.1};
OS   Listeriaceae bacterium FSL A5-0209.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Listeriaceae.
OX   NCBI_TaxID=1497679 {ECO:0000313|EMBL:KGL41168.1, ECO:0000313|Proteomes:UP000029855};
RN   [1] {ECO:0000313|EMBL:KGL41168.1, ECO:0000313|Proteomes:UP000029855}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FSL A5-0209 {ECO:0000313|EMBL:KGL41168.1,
RC   ECO:0000313|Proteomes:UP000029855};
RA   den Bakker H.C.;
RT   "Novel Listeriaceae from food processing plants.";
RL   Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Decomposes hydrogen peroxide into water and oxygen; serves to
CC       protect cells from the toxic effects of hydrogen peroxide.
CC       {ECO:0000256|ARBA:ARBA00002974}.
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000256|ARBA:ARBA00001971,
CC         ECO:0000256|PIRSR:PIRSR038928-2};
CC   -!- SIMILARITY: Belongs to the catalase family.
CC       {ECO:0000256|ARBA:ARBA00005329}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KGL41168.1}.
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DR   EMBL; JNEZ01000034; KGL41168.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A099W9Q1; -.
DR   STRING; 1497679.EP56_11225; -.
DR   eggNOG; COG0753; Bacteria.
DR   Proteomes; UP000029855; Unassembled WGS sequence.
DR   GO; GO:0004096; F:catalase activity; IEA:InterPro.
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; 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:SF23; CATALASE-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; 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   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   Peroxidase {ECO:0000256|ARBA:ARBA00022559}.
FT   DOMAIN          6..389
FT                   /note="Catalase core"
FT                   /evidence="ECO:0000259|SMART:SM01060"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        53
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT   ACT_SITE        126
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT   BINDING         336
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   486 AA;  55596 MW;  3303C0CBE09E0949 CRC64;
     MSKKLTTNQG VPIGDNQNSM TAGHRGPTLL EDYVLIEKLA HFDRERVPER VVHARGIGAH
     GVFTVKNSMK KYTKAAFLQE EGQQTEVFAR FSTVIHGLHS PETLRDPRGF AVKFYTEEGN
     YDFVGNNLPV FFIRDAIKFP DVIHSLKPDP STNMQDANRY WDFFSLTPEA TTMITYLFSD
     EGIPASFRQI RGSSVHAFKW TNEEGKTVYI KMRWVPKEGI VNLSTDQAAQ IQAKEFSHAT
     RDLYEAIENG DFPEWELYIQ VLDPADIDNY DFNPLDATKD WFEDVFPYEH VGTMVLNRNP
     ENIFAETESV GFNPGVLVPG ILPSEDRMLQ GRLFSYSDTQ RHRVGPNYLQ LPINSPKVDV
     NNNQRDGAMP FKQQTSSINY EPNSYDTTPK ETPRYVEDEQ DLVAGKLGRI EQQKPNNFGH
     AREVWNRYSD GERDALVNNI VGDWEGVRED IKIRNLRNFY QVEPVFAERV AKGTGVDLEK
     HIADLK
//
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