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Database: UniProt
Entry: A0A433XN62_9BACL
LinkDB: A0A433XN62_9BACL
Original site: A0A433XN62_9BACL 
ID   A0A433XN62_9BACL        Unreviewed;       484 AA.
AC   A0A433XN62;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   03-MAY-2023, entry version 13.
DE   RecName: Full=Catalase {ECO:0000256|RuleBase:RU000498};
DE            EC=1.11.1.6 {ECO:0000256|RuleBase:RU000498};
GN   ORFNames=EJP77_00605 {ECO:0000313|EMBL:RUT35557.1};
OS   Paenibacillus zeisoli.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=2496267 {ECO:0000313|EMBL:RUT35557.1, ECO:0000313|Proteomes:UP000272464};
RN   [1] {ECO:0000313|EMBL:RUT35557.1, ECO:0000313|Proteomes:UP000272464}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=3-5-3 {ECO:0000313|EMBL:RUT35557.1,
RC   ECO:0000313|Proteomes:UP000272464};
RA   Sun L., Chen Z.;
RL   Submitted (DEC-2018) 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:RUT35557.1}.
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DR   EMBL; RZNX01000001; RUT35557.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A433XN62; -.
DR   OrthoDB; 9760293at2; -.
DR   Proteomes; UP000272464; 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:UP000272464}.
FT   DOMAIN          8..392
FT                   /note="Catalase core"
FT                   /evidence="ECO:0000259|SMART:SM01060"
FT   REGION          1..25
FT                   /note="Disordered"
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   484 AA;  54200 MW;  470C6ADD0D9471CF CRC64;
     MDNQKPLTTS TGAPVGDNQN SMTAGHRGPT LIQDYHLLEK LAHFNRERVP ERVVHAKGAG
     AHGYFEVTKD ISQYTKAAFL SEVGKRTPIF IRFSTVAGEL GSADTVRDPR GFAVKFYTEE
     GNYDLVGNNT PVFFIRDAIK FPDFIHTQKR HPQTHLKNPN AVWDFWSLSP ESLHQVTILM
     SDRGIPASLR HMHGFGSHTF KWVNAEGEAV WVKYHFKTEQ GVKNMDVAVA ARLAGEHPDY
     HTEDLFTAID KGDFPAWKLY VQIMPVQDAE TYRFDPFDVT KVWSQKDYPL IEVGRMVLDR
     NPENYFAEVE QVTLSPGNFV PGIEASPDKM LQGRIFAYAD AHRYRVGANH NTLPINRPIA
     EVNNNQRDGA MRADGNGGSS IYYEPNSYGG ASESPSHKPA PFAVSGLADS VPYDHNDHYT
     QAGDLYRLLS EEERLRLVAN IVAAMTPVEK DEIKIRQIGH FYKADPEYGT RIAEGLGLPA
     PQGV
//
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