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Database: UniProt/TrEMBL
Entry: Q9KBE8_BACHD
LinkDB: Q9KBE8_BACHD
Original site: Q9KBE8_BACHD 
ID   Q9KBE8_BACHD            Unreviewed;       711 AA.
AC   Q9KBE8;
DT   01-OCT-2000, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2000, sequence version 1.
DT   20-JUN-2018, entry version 115.
DE   RecName: Full=Catalase {ECO:0000256|PIRNR:PIRNR038927, ECO:0000256|RuleBase:RU000498};
DE            EC=1.11.1.6 {ECO:0000256|PIRNR:PIRNR038927, ECO:0000256|RuleBase:RU000498};
GN   Name=katB {ECO:0000313|EMBL:BAB05699.1};
OS   Bacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM
OS   9153 / C-125).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=272558 {ECO:0000313|EMBL:BAB05699.1, ECO:0000313|Proteomes:UP000001258};
RN   [1] {ECO:0000313|EMBL:BAB05699.1, ECO:0000313|Proteomes:UP000001258}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125
RC   {ECO:0000313|Proteomes:UP000001258};
RX   PubMed=11058132; DOI=10.1093/nar/28.21.4317;
RA   Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N.,
RA   Fuji F., Hirama C., Nakamura Y., Ogasawara N., Kuhara S.,
RA   Horikoshi K.;
RT   "Complete genome sequence of the alkaliphilic bacterium Bacillus
RT   halodurans and genomic sequence comparison with Bacillus subtilis.";
RL   Nucleic Acids Res. 28:4317-4331(2000).
CC   -!- FUNCTION: Serves to protect cells from the toxic effects of
CC       hydrogen peroxide. {ECO:0000256|PIRNR:PIRNR038927}.
CC   -!- CATALYTIC ACTIVITY: 2 H(2)O(2) = O(2) + 2 H(2)O.
CC       {ECO:0000256|PIRNR:PIRNR038927, ECO:0000256|RuleBase:RU000498}.
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000256|PIRNR:PIRNR038927,
CC         ECO:0000256|PIRSR:PIRSR038927-2};
CC   -!- SIMILARITY: Belongs to the catalase family.
CC       {ECO:0000256|PIRNR:PIRNR038927, ECO:0000256|RuleBase:RU000498}.
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DR   EMBL; BA000004; BAB05699.1; -; Genomic_DNA.
DR   PIR; D83897; D83897.
DR   RefSeq; WP_010898138.1; NC_002570.2.
DR   ProteinModelPortal; Q9KBE8; -.
DR   STRING; 272558.BH1980; -.
DR   PeroxiBase; 3980; BhaKat01_C-125.
DR   EnsemblBacteria; BAB05699; BAB05699; BAB05699.
DR   KEGG; bha:BH1980; -.
DR   eggNOG; ENOG4105CH6; Bacteria.
DR   eggNOG; COG0753; LUCA.
DR   HOGENOM; HOG000087851; -.
DR   KO; K03781; -.
DR   OrthoDB; POG091H0424; -.
DR   Proteomes; UP000001258; Chromosome.
DR   GO; GO:0004096; F:catalase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0020037; F:heme binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR   Gene3D; 2.40.180.10; -; 1.
DR   Gene3D; 3.40.50.880; -; 1.
DR   InterPro; IPR018028; Catalase.
DR   InterPro; IPR024708; Catalase_AS.
DR   InterPro; IPR024712; Catalase_clade2.
DR   InterPro; IPR011614; Catalase_core.
DR   InterPro; IPR037060; Catalase_core_sf.
DR   InterPro; IPR002226; Catalase_haem_BS.
DR   InterPro; IPR010582; Catalase_immune_responsive.
DR   InterPro; IPR020835; Catalase_sf.
DR   InterPro; IPR029062; Class_I_gatase-like.
DR   InterPro; IPR002818; DJ-1/PfpI.
DR   PANTHER; PTHR42821; PTHR42821; 1.
DR   Pfam; PF00199; Catalase; 1.
DR   Pfam; PF06628; Catalase-rel; 1.
DR   Pfam; PF01965; DJ-1_PfpI; 1.
DR   PIRSF; PIRSF038927; Catalase_clade2; 1.
DR   PRINTS; PR00067; CATALASE.
DR   SMART; SM01060; Catalase; 1.
DR   SUPFAM; SSF52317; SSF52317; 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   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000001258};
KW   Heme {ECO:0000256|PIRNR:PIRNR038927, ECO:0000256|PIRSR:PIRSR038927-3,
KW   ECO:0000256|RuleBase:RU000498};
KW   Hydrogen peroxide {ECO:0000256|PIRNR:PIRNR038927,
KW   ECO:0000256|RuleBase:RU000498};
KW   Iron {ECO:0000256|PIRNR:PIRNR038927, ECO:0000256|PIRSR:PIRSR038927-2,
KW   ECO:0000256|RuleBase:RU000498};
KW   Metal-binding {ECO:0000256|PIRNR:PIRNR038927,
KW   ECO:0000256|PIRSR:PIRSR038927-2, ECO:0000256|RuleBase:RU000498};
KW   Oxidoreductase {ECO:0000256|PIRNR:PIRNR038927,
KW   ECO:0000256|RuleBase:RU000498};
KW   Peroxidase {ECO:0000256|PIRNR:PIRNR038927,
KW   ECO:0000256|RuleBase:RU000498};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001258}.
FT   DOMAIN       32    420       Catalase. {ECO:0000259|SMART:SM01060}.
FT   ACT_SITE     79     79       {ECO:0000256|PIRSR:PIRSR038927-1}.
FT   ACT_SITE    152    152       {ECO:0000256|PIRSR:PIRSR038927-1}.
FT   METAL       366    366       Iron (heme axial ligand).
FT                                {ECO:0000256|PIRSR:PIRSR038927-2}.
FT   BINDING      76     76       Heme. {ECO:0000256|PIRSR:PIRSR038927-3}.
FT   BINDING     116    116       Heme. {ECO:0000256|PIRSR:PIRSR038927-3}.
FT   BINDING     165    165       Heme. {ECO:0000256|PIRSR:PIRSR038927-3}.
FT   BINDING     362    362       Heme. {ECO:0000256|PIRSR:PIRSR038927-3}.
FT   BINDING     373    373       Heme. {ECO:0000256|PIRSR:PIRSR038927-3}.
SQ   SEQUENCE   711 AA;  79981 MW;  022125B4E016683A CRC64;
     MDKDQQGTES SENKKNEQLE PFKVDHKNTK LTTNQGVRVS DTDDSLKAGD RGPTLMEDFH
     FREKMTHFDH ERIPERVVHA RGFGAHGYFQ VYEPMTEYTK ASFLQDPNVK TPVFVRFSTV
     VGSRGSADTV RDVRGFATKF YTEDGNYDLV ANNIPIFFIQ DAIKFPDVVH ALKPEPHNEI
     PQASAAHDTF WDFVVSNTET AHMIMWLLSD RAIPRSFRMM EGFGVNTFRF VNEQGKARFV
     KFHWKPKLGV HSLVWDEAQK LAGKDPDFHR RDLWEAINMG EYPEYELGVQ MIEEEDEFSF
     DFDILDPTKF WPEEMVPVKL IGKMTLNRNQ DNFFAETEQV AFHAGNVVPG IDFSNDPLLQ
     GRLFSYLDTQ LLRLSGPNFH EIPINRPIAP VNNNQRDGFH RMTIDKGAVS YSPNTLRNNS
     PEPASDQEHG YVHYMEKVEG QKIRRRSESF NDHFSQATLF WNSLSTAEKQ HLIKAFHFEV
     GSVKDKNLKQ RVVEMFNQVD GKLAAEIAKG IGVNPPTTPG GTGVTASSPA VSQENTIKLA
     RTRKVAVLID HGFAFDEVSQ VVTALQSAGL GVDLVSKQLG MISSAEGEQL EANKSFATTG
     AIMYDALYIG GGAQSISSLN LYSESKTFVD EAFKHAKTIG ATNEGIELLI AAQVQGITFA
     GPDSNDHVVN DLGIITIQTD KDFKAFTDEM IHAIAQHRHW MREFKDGKLS G
//
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