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
//