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Database: UniProt
Entry: I0JT46_HALH3
LinkDB: I0JT46_HALH3
Original site: I0JT46_HALH3 
ID   I0JT46_HALH3            Unreviewed;       682 AA.
AC   I0JT46;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   24-JAN-2024, entry version 64.
DE   RecName: Full=Catalase {ECO:0000256|ARBA:ARBA00012314, ECO:0000256|PIRNR:PIRNR038927};
DE            EC=1.11.1.6 {ECO:0000256|ARBA:ARBA00012314, ECO:0000256|PIRNR:PIRNR038927};
GN   Name=katE {ECO:0000313|EMBL:CCG47318.1};
GN   OrderedLocusNames=HBHAL_4981 {ECO:0000313|EMBL:CCG47318.1};
OS   Halobacillus halophilus (strain ATCC 35676 / DSM 2266 / JCM 20832 / KCTC
OS   3685 / LMG 17431 / NBRC 102448 / NCIMB 2269) (Sporosarcina halophila).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Halobacillus.
OX   NCBI_TaxID=866895 {ECO:0000313|EMBL:CCG47318.1, ECO:0000313|Proteomes:UP000007397};
RN   [1] {ECO:0000313|EMBL:CCG47318.1, ECO:0000313|Proteomes:UP000007397}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35676 / DSM 2266 / JCM 20832 / KCTC 3685 / LMG 17431 /
RC   NBRC 102448 / NCIMB 2269 {ECO:0000313|Proteomes:UP000007397};
RX   PubMed=22583374; DOI=10.1111/j.1462-2920.2012.02770.x;
RA   Saum S.H., Pfeiffer F., Palm P., Rampp M., Schuster S.C., Muller V.,
RA   Oesterhelt D.;
RT   "Chloride and organic osmolytes: a hybrid strategy to cope with elevated
RT   salinities by the moderately halophilic, chloride-dependent bacterium
RT   Halobacillus halophilus.";
RL   Environ. Microbiol. 15:1619-1633(2013).
CC   -!- FUNCTION: Serves to protect cells from the toxic effects of hydrogen
CC       peroxide. {ECO:0000256|PIRNR:PIRNR038927}.
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|PIRNR:PIRNR038927,
CC         ECO:0000256|RuleBase:RU000498};
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000256|ARBA:ARBA00001971,
CC         ECO:0000256|PIRNR:PIRNR038927, ECO:0000256|PIRSR:PIRSR038927-2};
CC   -!- SIMILARITY: Belongs to the catalase family. HPII subfamily.
CC       {ECO:0000256|ARBA:ARBA00010660}.
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DR   EMBL; HE717023; CCG47318.1; -; Genomic_DNA.
DR   RefSeq; WP_014645202.1; NC_017668.1.
DR   AlphaFoldDB; I0JT46; -.
DR   STRING; 866895.HBHAL_4981; -.
DR   KEGG; hhd:HBHAL_4981; -.
DR   PATRIC; fig|866895.3.peg.4020; -.
DR   eggNOG; COG0693; Bacteria.
DR   eggNOG; COG0753; Bacteria.
DR   HOGENOM; CLU_010645_3_0_9; -.
DR   Proteomes; UP000007397; 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   CDD; cd08155; catalase_clade_2; 1.
DR   CDD; cd03132; GATase1_catalase; 1.
DR   Gene3D; 1.20.1370.20; -; 1.
DR   Gene3D; 3.40.50.880; -; 1.
DR   Gene3D; 2.40.180.10; Catalase core domain; 1.
DR   InterPro; IPR018028; Catalase.
DR   InterPro; IPR024708; Catalase_AS.
DR   InterPro; IPR024712; Catalase_clade2.
DR   InterPro; IPR043156; Catalase_clade2_helical.
DR   InterPro; IPR011614; Catalase_core.
DR   InterPro; IPR002226; Catalase_haem_BS.
DR   InterPro; IPR010582; Catalase_immune_responsive.
DR   InterPro; IPR041399; Catalase_large_C.
DR   InterPro; IPR020835; Catalase_sf.
DR   InterPro; IPR029062; Class_I_gatase-like.
DR   PANTHER; PTHR42821; CATALASE; 1.
DR   PANTHER; PTHR42821:SF1; CATALASE-B; 1.
DR   Pfam; PF00199; Catalase; 1.
DR   Pfam; PF06628; Catalase-rel; 1.
DR   Pfam; PF18011; Catalase_C; 1.
DR   PIRSF; PIRSF038927; Catalase_clade2; 1.
DR   PRINTS; PR00067; CATALASE.
DR   SMART; SM01060; Catalase; 1.
DR   SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 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|PIRNR:PIRNR038927};
KW   Hydrogen peroxide {ECO:0000256|ARBA:ARBA00023324,
KW   ECO:0000256|PIRNR:PIRNR038927};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRNR:PIRNR038927};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRNR:PIRNR038927};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|PIRNR:PIRNR038927};
KW   Peroxidase {ECO:0000256|ARBA:ARBA00022559, ECO:0000256|PIRNR:PIRNR038927};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007397}.
FT   DOMAIN          29..417
FT                   /note="Catalase core"
FT                   /evidence="ECO:0000259|SMART:SM01060"
FT   REGION          1..38
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..28
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        76
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038927-1"
FT   ACT_SITE        149
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038927-1"
FT   BINDING         73
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038927-3"
FT   BINDING         113
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038927-3"
FT   BINDING         162
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038927-3"
FT   BINDING         359
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038927-3"
FT   BINDING         363
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:PIRSR038927-2"
FT   BINDING         370
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038927-3"
SQ   SEQUENCE   682 AA;  76870 MW;  B2B8640BC9CFDF93 CRC64;
     MSDKKKVDKQ SKDEQLEHYR REDSGKHLTT NQGLKMSEDE FSLKAGERGP TLMEDFHFRE
     KMTHFDHERI PERVVHARGF AAHGEFELYK SLEKYTKADF LTDTSKKTPV FTRFSTVAGN
     RGSSETVRDA RGFATKFYTE EGNYDLVGNN IPVFFIQDAI KFPDLVHALK PEPHNEMPQA
     ASAHDTFWDF IANNQESAHM VMWAMSDRAI PRSFRMMEGF GVHTFRLVNA EGKSHFVKFH
     WKPVLGTHSL VWDEAQKISG KDADFHRGDL YSSIENGDYP EYELGIQVIP EEDEDKFEFD
     VLDPTKLWPE EDVPVEIVGK LTLNRNVDNV FAETEQVAFH PGHVVPGIDF TNDPLLQGRL
     FSYTDTQLIR LGGPNFHELP INRPVCPFFN NQRDGYGRQT INTGQVSYHK NSLAQNTPEP
     AAPEEGGYEH YHEKVEGRKI RARSVSFKDH FSQATLFWNS MSEPEKDHLI QAFSFELGKL
     ESDSVRKQVI EMFSNVSLDL VQGVAKNIGI TPPEHGGSDV TKSSPALSQQ NTVFKPDTRV
     VGVIVADNFA GSEVTNVLEG LADKGMSPVV ISTRQGTLKG ADGTELTVDH TFTTVDPVLL
     DAVYVAGGGE QSKAFRKKVS YYLNEAFTHF KPIGATHEGI QLLQDNELLE EPGVVAEENG
     VEFVSKFTEA VAAHRHWDRQ VI
//
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