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Database: UniProt
Entry: A0A1I1BYY3_9BACL
LinkDB: A0A1I1BYY3_9BACL
Original site: A0A1I1BYY3_9BACL 
ID   A0A1I1BYY3_9BACL        Unreviewed;       323 AA.
AC   A0A1I1BYY3;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 12.
DE   RecName: Full=Catalase-related peroxidase {ECO:0000256|PIRNR:PIRNR000296};
DE            EC=1.11.1.- {ECO:0000256|PIRNR:PIRNR000296};
GN   ORFNames=SAMN05216312_1126 {ECO:0000313|EMBL:SFB53513.1};
OS   Cohnella sp. OV330.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Cohnella.
OX   NCBI_TaxID=1855288 {ECO:0000313|EMBL:SFB53513.1, ECO:0000313|Proteomes:UP000198686};
RN   [1] {ECO:0000313|EMBL:SFB53513.1, ECO:0000313|Proteomes:UP000198686}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OV330 {ECO:0000313|EMBL:SFB53513.1,
RC   ECO:0000313|Proteomes:UP000198686};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Has an organic peroxide-dependent peroxidase activity.
CC       {ECO:0000256|PIRNR:PIRNR000296}.
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000256|PIRNR:PIRNR000296};
CC   -!- SIMILARITY: Belongs to the catalase family.
CC       {ECO:0000256|PIRNR:PIRNR000296}.
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DR   EMBL; FOKE01000012; SFB53513.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I1BYY3; -.
DR   Proteomes; UP000198686; Unassembled WGS sequence.
DR   GO; GO:0004096; F:catalase activity; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR   Gene3D; 1.20.1280.120; -; 1.
DR   Gene3D; 2.40.180.10; Catalase core domain; 1.
DR   InterPro; IPR018028; Catalase.
DR   InterPro; IPR011614; Catalase_core.
DR   InterPro; IPR020835; Catalase_sf.
DR   InterPro; IPR024168; Catalase_SrpA-type_pred.
DR   PANTHER; PTHR11465; CATALASE; 1.
DR   PANTHER; PTHR11465:SF9; CATALASE; 1.
DR   Pfam; PF00199; Catalase; 1.
DR   PIRSF; PIRSF000296; SrpA; 1.
DR   SMART; SM01060; Catalase; 1.
DR   SUPFAM; SSF56634; Heme-dependent catalase-like; 1.
DR   PROSITE; PS51402; CATALASE_3; 1.
PE   3: Inferred from homology;
KW   Heme {ECO:0000256|PIRNR:PIRNR000296, ECO:0000256|PIRSR:PIRSR000296-2};
KW   Iron {ECO:0000256|PIRNR:PIRNR000296, ECO:0000256|PIRSR:PIRSR000296-2};
KW   Metal-binding {ECO:0000256|PIRNR:PIRNR000296,
KW   ECO:0000256|PIRSR:PIRSR000296-2};
KW   Oxidoreductase {ECO:0000256|PIRNR:PIRNR000296};
KW   Peroxidase {ECO:0000256|PIRNR:PIRNR000296};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198686}.
FT   DOMAIN          13..321
FT                   /note="Catalase core"
FT                   /evidence="ECO:0000259|SMART:SM01060"
FT   ACT_SITE        44
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000296-1"
FT   BINDING         312
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:PIRSR000296-2"
SQ   SEQUENCE   323 AA;  35067 MW;  4879FB274195510B CRC64;
     MEKTFADQSL AADKHLGDPI QLPHRTVDAL EGLSGVHPGK RRVHAKGLCC RAVFKPSGLA
     AGLTTAAHLR DKDGEIDAIV RFSGSSSDPS LADLLSPGKG LAVRFMPAGG DVSVLAAVTV
     PVFFAKTPAS FLDLIKEANR LKGGGIEAIA AAAELAAHFP EARHAMAHVG KLRPPASYGT
     CRYYAIHAFM LVDEEGIRRP AKFEWMPELG VETLSIGELK SLPEDYLERD AAERIHKAPL
     RFRLNIVLGR EEDPTDDPTL PWPDDRERIE AGILDVTDVI AEPDGLVMDP TITGAGIEPS
     DDPILRFRSP VYEESMRRRS RGE
//
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