ID A0A285CS72_9BACI Unreviewed; 531 AA.
AC A0A285CS72;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=Catalase {ECO:0000256|RuleBase:RU000498};
DE EC=1.11.1.6 {ECO:0000256|RuleBase:RU000498};
GN ORFNames=SAMN05877753_104119 {ECO:0000313|EMBL:SNX70439.1};
OS Bacillus oleivorans.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1448271 {ECO:0000313|EMBL:SNX70439.1, ECO:0000313|Proteomes:UP000219546};
RN [1] {ECO:0000313|EMBL:SNX70439.1, ECO:0000313|Proteomes:UP000219546}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JC228 {ECO:0000313|EMBL:SNX70439.1,
RC ECO:0000313|Proteomes:UP000219546};
RA de Groot N.N.;
RL Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Decomposes hydrogen peroxide into water and oxygen; serves to
CC protect cells from the toxic effects of hydrogen peroxide.
CC {ECO:0000256|ARBA:ARBA00002974}.
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|RuleBase:RU000498};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000256|ARBA:ARBA00001971,
CC ECO:0000256|PIRSR:PIRSR038928-2};
CC -!- SIMILARITY: Belongs to the catalase family.
CC {ECO:0000256|ARBA:ARBA00005329, ECO:0000256|RuleBase:RU000498}.
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DR EMBL; OAOP01000004; SNX70439.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A285CS72; -.
DR OrthoDB; 9760293at2; -.
DR Proteomes; UP000219546; 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; cd08154; catalase_clade_1; 1.
DR Gene3D; 2.40.180.10; Catalase core domain; 1.
DR InterPro; IPR018028; Catalase.
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:SF23; CATALASE-2; 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:UP000219546}.
FT DOMAIN 18..411
FT /note="Catalase core"
FT /evidence="ECO:0000259|SMART:SM01060"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 498..531
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 65
FT /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT ACT_SITE 143
FT /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT BINDING 353
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 531 AA; 60773 MW; 03A2CE619609CC85 CRC64;
MTNDQNQPNN IENDDTLTNR QGHPITNNQN IRTVGNRGPA TLENYDFIEK ISHFDREKVP
ERIVHARGAG AHGYFEAYGM CGDEPISKYT RAKLFQEKGK RTPVFVRFST VVHGLHSPET
LRDPRGFAVK FYTEDGNWDL VGNNLKIFFI RDAMKFPDMI HAFRPDPVTN YQDPERFFDF
CANSPESFHM VTFVYSPWGI PANYRMMQGS GVNTYKWINK EGKAVLVKYH WEPKQGIKNL
TQKEAEEIQG KNFNHATQDL YEAIERGDYP EWELFVQIME DGPHPELDFD PLDDTKLWPN
DQFPWRAVGR MVLNKNPENF FNEVELSAFG TGVLVDGLDF SDDKMLQGRT FSYSDTQRYR
VGANYLQLPI NAAKKRVATN QEGGQMRYYN DKAPGQNPHI NYEPSILGGL QEAEQTGVEH
TPHVEGNLVR QSIDRNDNTK QAGQTYREFE QWEKDELINN LVNDLSKCDK RIQDKMIALA
EDADEEYGRR LREGLAMAAK DGSSGKHALG NKGGENAPQQ AVEKGHEADP Y
//
