ID B7HVN6_BACC7 Unreviewed; 458 AA.
AC B7HVN6;
DT 10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT 10-FEB-2009, sequence version 1.
DT 24-JAN-2024, entry version 75.
DE SubName: Full=Catalase {ECO:0000313|EMBL:ACJ80715.1};
DE EC=1.11.1.6 {ECO:0000313|EMBL:ACJ80715.1};
GN OrderedLocusNames=BCAH187_A3057 {ECO:0000313|EMBL:ACJ80715.1};
OS Bacillus cereus (strain AH187).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=405534 {ECO:0000313|EMBL:ACJ80715.1, ECO:0000313|Proteomes:UP000002214};
RN [1] {ECO:0000313|EMBL:ACJ80715.1, ECO:0000313|Proteomes:UP000002214}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AH187 {ECO:0000313|EMBL:ACJ80715.1,
RC ECO:0000313|Proteomes:UP000002214};
RA Dodson R.J., Durkin A.S., Rosovitz M.J., Rasko D.A., Kolsto A.B.,
RA Okstad O.A., Ravel J., Sutton G.;
RT "Genome sequence of Bacillus cereus AH187.";
RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; CP001177; ACJ80715.1; -; Genomic_DNA.
DR AlphaFoldDB; B7HVN6; -.
DR KEGG; bcr:BCAH187_A3057; -.
DR HOGENOM; CLU_010645_2_0_9; -.
DR OMA; DTKIWDE; -.
DR Proteomes; UP000002214; Chromosome.
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 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; 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; 2.
DR PRINTS; PR00067; CATALASE.
DR SMART; SM01060; Catalase; 1.
DR SUPFAM; SSF56634; Heme-dependent catalase-like; 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 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:0000313|EMBL:ACJ80715.1};
KW Peroxidase {ECO:0000256|ARBA:ARBA00022559, ECO:0000313|EMBL:ACJ80715.1}.
FT DOMAIN 17..393
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 458 AA; 52737 MW; 055BC135DD321732 CRC64;
MNEHYDKQRQ SLLRKDFNDN GERNEQAILH SQTVGSRGPV LEQDSVLHEA LQQFIHEKIL
ERPVHVKGFG AFGYFQTIYP MPEHTKLNFL QNANEKVPVM VRFSLAVSTK GTPDTSRNVR
GFSTKFYTKE GIFDLLCNHI PVFSVRDPMR FPETIQALSP SPKNNLLDPN RFWSFVARAP
ESIHFVVRLY SDNGTVKSLR HIPGHSVNTY VWRNAEGNRK YVKYHWYPFE GVQFITSEEA
NKLAAENPDY SGKDLYDAIA NSKPVEYGLY VQLMDPKDEA HLSYDPLDDT KIWDEKAYPL
IPVGKMVLNK NPENYMEQVE KVAFSPSNLL DGAELSDDKM LQGRANIYSD SQRRRIGPEF
RKLTINQQQN WTPANQITSG DGRYVEGKIE RTSITKQDDF TQAGEFYTKL KPIEKEHLAE
NLAGDLKVIS DDIRKIVLEY FHNVSADLVK RIETKIEK
//