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Database: UniProt
Entry: W4RTM1_9BACI
LinkDB: W4RTM1_9BACI
Original site: W4RTM1_9BACI 
ID   W4RTM1_9BACI            Unreviewed;       444 AA.
AC   W4RTM1;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   RecName: Full=Catalase {ECO:0000256|RuleBase:RU000498};
DE            EC=1.11.1.6 {ECO:0000256|RuleBase:RU000498};
GN   ORFNames=JCM21738_3915 {ECO:0000313|EMBL:GAE46979.1};
OS   Mesobacillus boroniphilus JCM 21738.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Mesobacillus.
OX   NCBI_TaxID=1294265 {ECO:0000313|EMBL:GAE46979.1, ECO:0000313|Proteomes:UP000018949};
RN   [1] {ECO:0000313|EMBL:GAE46979.1, ECO:0000313|Proteomes:UP000018949}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 21738 {ECO:0000313|EMBL:GAE46979.1,
RC   ECO:0000313|Proteomes:UP000018949};
RA   Hattori M., Oshima K., Inaba H., Suda W., Sakamoto M., Iino T.,
RA   Kitahara M., Oshida Y., Iida T., Kudo T., Itoh T., Ahmed I., Ohkuma M.;
RT   "NBRP : Genome information of microbial organism related human and
RT   environment.";
RL   Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
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|ARBA:ARBA00000720,
CC         ECO:0000256|RuleBase:RU000498};
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000256|PIRSR:PIRSR038928-2};
CC   -!- SIMILARITY: Belongs to the catalase family.
CC       {ECO:0000256|ARBA:ARBA00005329, ECO:0000256|RuleBase:RU000498}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:GAE46979.1}.
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DR   EMBL; BAUW01000059; GAE46979.1; -; Genomic_DNA.
DR   AlphaFoldDB; W4RTM1; -.
DR   eggNOG; COG0753; Bacteria.
DR   Proteomes; UP000018949; Unassembled WGS sequence.
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; cd08156; catalase_clade_3; 1.
DR   Gene3D; 2.40.180.10; Catalase core domain; 1.
DR   InterPro; IPR018028; Catalase.
DR   InterPro; IPR040333; Catalase_3.
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:SF9; CATALASE; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018949}.
FT   DOMAIN          1..352
FT                   /note="Catalase core"
FT                   /evidence="ECO:0000259|SMART:SM01060"
FT   ACT_SITE        15
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT   ACT_SITE        88
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT   BINDING         298
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   444 AA;  50215 MW;  AE1D091DACF278B9 CRC64;
     MAHFNRERVP ERVVHAKGAG AHGYFEVTND VSKYTKAAFL SEVGKKTPLF IRFSTVAGEL
     GSADTVRDPR GFAVKFYTEE GNYDIVGNNT PVFFIRDAIK FPDFIHTQKR NPQTHLKDPN
     AIWDFWSLSP ESLHQVTILM SDRGIPATFR HMHGFGSHTF KWTNAEGDGV WIKYHFKTEQ
     GVKNLAADVA AKIAGENPDY HTEDLFNAIE AGDFPAWKLY VQIMPLEDAN TYRFDPFDVT
     KVWSQKDYPL IEVGRMVLDR NPENYFAEVE QATFSPGNLV PGVDVSPDKM LQGRLFAYAD
     AHRYRVGANH NHLPINRAKS EVNSYQRDGQ MRFDGNGGKS VNYEPNSFGG PSELNEHKQA
     AFPVSGVAEN VGYDHNDHYT QAGDLYRLMS EEERERLVAN IVAAMKPVQR DDIKLRQIGH
     FYKADPEYGT RIAQGLGLQV PHEV
//
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