ID   Q6HM27_BACHK            Unreviewed;       488 AA.
AC   Q6HM27;
DT   19-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   19-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 118.
DE   RecName: Full=Catalase {ECO:0000256|RuleBase:RU000498};
DE            EC=1.11.1.6 {ECO:0000256|RuleBase:RU000498};
GN   Name=katB {ECO:0000313|EMBL:AAT61340.1};
GN   OrderedLocusNames=BT9727_1057 {ECO:0000313|EMBL:AAT61340.1};
OS   Bacillus thuringiensis subsp. konkukian (strain 97-27).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=281309 {ECO:0000313|EMBL:AAT61340.1, ECO:0000313|Proteomes:UP000001301};
RN   [1] {ECO:0000313|EMBL:AAT61340.1, ECO:0000313|Proteomes:UP000001301}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=97-27 {ECO:0000313|EMBL:AAT61340.1,
RC   ECO:0000313|Proteomes:UP000001301};
RX   PubMed=16621833; DOI=10.1128/JB.188.9.3382-3390.2006;
RA   Han C.S., Xie G., Challacombe J.F., Altherr M.R., Bhotika S.S., Brown N.,
RA   Bruce D., Campbell C.S., Campbell M.L., Chen J., Chertkov O., Cleland C.,
RA   Dimitrijevic M., Doggett N.A., Fawcett J.J., Glavina T., Goodwin L.A.,
RA   Green L.D., Hill K.K., Hitchcock P., Jackson P.J., Keim P.,
RA   Kewalramani A.R., Longmire J., Lucas S., Malfatti S., McMurry K.,
RA   Meincke L.J., Misra M., Moseman B.L., Mundt M., Munk A.C., Okinaka R.T.,
RA   Parson-Quintana B., Reilly L.P., Richardson P., Robinson D.L., Rubin E.,
RA   Saunders E., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA   Ticknor L.O., Wills P.L., Brettin T.S., Gilna P.;
RT   "Pathogenomic sequence analysis of Bacillus cereus and Bacillus
RT   thuringiensis isolates closely related to Bacillus anthracis.";
RL   J. Bacteriol. 188:3382-3390(2006).
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   -!- 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|RuleBase:RU000498};
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, ECO:0000256|RuleBase:RU000498}.
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DR   EMBL; AE017355; AAT61340.1; -; Genomic_DNA.
DR   RefSeq; WP_001069157.1; NC_005957.1.
DR   RefSeq; YP_035394.1; NC_005957.1.
DR   AlphaFoldDB; Q6HM27; -.
DR   SMR; Q6HM27; -.
DR   GeneID; 45021173; -.
DR   KEGG; btk:BT9727_1057; -.
DR   PATRIC; fig|281309.8.peg.1111; -.
DR   HOGENOM; CLU_010645_2_0_9; -.
DR   Proteomes; UP000001301; 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   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: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; 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}.
FT   DOMAIN          8..391
FT                   /note="Catalase core"
FT                   /evidence="ECO:0000259|SMART:SM01060"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..25
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        55
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT   ACT_SITE        128
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT   BINDING         338
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   488 AA;  55833 MW;  3BDA51F4E7B914E2 CRC64;
     MNPNNRLTTN QGAPVGDNQN SRTAGRRGPV LLEDYHLVEK LAHFDRERIP ERVVHARGAG
     AHGVFVTKNS MKKYTKAAFL QNEGTETPVF VRFSTVIHGQ GSPETARDPR GFAVKFYTEE
     GNYDIVGNHL PVFFIRDAIK FPDMVHSLKP APDTNIQTPD RYWDFMTLSP ESTHMMTWVF
     SDYGTPASYR EMEGFGVHSF KWINAEGKIV YIKYHWKPQQ GVRNLSAKEV QEVQGKDFNH
     ATRDLFDAIE KGNYPKWDLH VQVMQLEETD SLDFDPLDPT KVWPEDRFPL MEVGTMTLNR
     NPKNFFAEVE QVAFSPSATV NGIEPSEDKL LQGRLFSYPD TQRYRLGANY LQIPVNCPYA
     AVHNQQRDGA MQINQNPSTI NYEPSRHAEN PVEDPAYRDS TMKVEGYVSR EKIDKPNDFK
     QAGERYRSFS KEEQDNLIAN LTSDLKDVNE RTKLLAVCNF FRADQEYGMR LAQALNVDIT
     QYVGNAPK
//