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Database: UniProt/TrEMBL
Entry: A0A1C3SKP8_9BACI
LinkDB: A0A1C3SKP8_9BACI
Original site: A0A1C3SKP8_9BACI 
ID   A0A1C3SKP8_9BACI        Unreviewed;       691 AA.
AC   A0A1C3SKP8;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   20-JUN-2018, entry version 13.
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   ORFNames=BGLY_4588 {ECO:0000313|EMBL:SCA88411.1};
OS   Bacillus glycinifermentans.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1664069 {ECO:0000313|EMBL:SCA88411.1, ECO:0000313|Proteomes:UP000093092};
RN   [1] {ECO:0000313|EMBL:SCA88411.1, ECO:0000313|Proteomes:UP000093092}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGLY {ECO:0000313|EMBL:SCA88411.1};
RA   Florea S., Webb J.S., Jaromczyk J., Schardl C.L.;
RL   Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
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; LT603683; SCA88411.1; -; Genomic_DNA.
DR   RefSeq; WP_046130494.1; NZ_LT603683.1.
DR   EnsemblBacteria; SCA88411; SCA88411; BGLY_4588.
DR   GeneID; 34775810; -.
DR   KEGG; bgy:BGLY_4588; -.
DR   PATRIC; fig|1664069.6.peg.4927; -.
DR   KO; K03781; -.
DR   Proteomes; UP000093092; Chromosome 1.
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:UP000093092};
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}.
FT   DOMAIN       31    419       Catalase. {ECO:0000259|SMART:SM01060}.
FT   ACT_SITE     78     78       {ECO:0000256|PIRSR:PIRSR038927-1}.
FT   ACT_SITE    151    151       {ECO:0000256|PIRSR:PIRSR038927-1}.
FT   METAL       365    365       Iron (heme axial ligand).
FT                                {ECO:0000256|PIRSR:PIRSR038927-2}.
FT   BINDING      75     75       Heme. {ECO:0000256|PIRSR:PIRSR038927-3}.
FT   BINDING     115    115       Heme. {ECO:0000256|PIRSR:PIRSR038927-3}.
FT   BINDING     164    164       Heme. {ECO:0000256|PIRSR:PIRSR038927-3}.
FT   BINDING     361    361       Heme. {ECO:0000256|PIRSR:PIRSR038927-3}.
FT   BINDING     372    372       Heme. {ECO:0000256|PIRSR:PIRSR038927-3}.
SQ   SEQUENCE   691 AA;  77997 MW;  92EFF58CE3D02ADE CRC64;
     MNKNERRKAD KNSKDEQLEY YRTDNRGKKM TTNQGVRISE DEHSLKAGTR GPTLMEDFHF
     REKITHFDHE RIPERVVHAR GFGAHGHFQV YEPMTKYTKA KFLQDPSVKT PVFVRFSTVA
     GSRGSGDTVR DVRGFAVKFY TEEGNYDLVG NNIPVFFIQD AIKFPDLVHA FKPEPHNEIP
     QASTAHDTFW DFVANNQETA HMIMWAMSDR AIPRSYRMME GFGVHTFRFV NDKGKARFVK
     FHWKPLLGVH SLVWDEAQKI AGKDPDFHRR DLWEAIERGA DVEYELGVQM IDEEDEFKFD
     FDILDPTKLW PEEMIPVRII GKMTLNRNQD NVFAETEQAA FHPGNVVPGI DFTNDPLLQG
     RLFSYTDTQL IRLGGPNFHE IPINRPVCPF HNNQYDGYHR MTINTGPVAY HKNSLQQNDP
     APASEEEGGY IHYQEKVEGR KIRRRSDSFK DHFSQAKLFW NSMSPVEKEH IVSAFRFEVG
     KVKSKDVRKQ VVEMFNKVDG ELAKQIAAGV GVKPPEKDEG SKVMLKSPAL SQENTRKSPL
     TRTVAILAED GFSHSEVIRV ITALIKAGLV PDVISSHLGA VKGDNGKEIE AGNTLQTADS
     VLYDAVYIPG GKDSIERLKK QKAALDFINE AFSHFKAIGA ASEGVDLLAS AAGTRALSES
     GIVTAAGGAP DAFSKKLIEA VGQHRHWERT V
//
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