ID A0A1B1Z5C0_9BACI Unreviewed; 486 AA.
AC A0A1B1Z5C0;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=Catalase {ECO:0000256|RuleBase:RU000498};
DE EC=1.11.1.6 {ECO:0000256|RuleBase:RU000498};
GN ORFNames=ABE41_011005 {ECO:0000313|EMBL:ANX12539.1};
OS Fictibacillus arsenicus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Fictibacillus.
OX NCBI_TaxID=255247 {ECO:0000313|EMBL:ANX12539.1, ECO:0000313|Proteomes:UP000077412};
RN [1] {ECO:0000313|EMBL:ANX12539.1, ECO:0000313|Proteomes:UP000077412}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G25-54 {ECO:0000313|EMBL:ANX12539.1,
RC ECO:0000313|Proteomes:UP000077412};
RA Zheng Z.;
RT "Complete genome sequence of Fictibacillus arsenicus G25-54, a strain with
RT toxicity to nematodes and a potential arsenic-resistance activity.";
RL Submitted (AUG-2016) 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}.
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DR EMBL; CP016761; ANX12539.1; -; Genomic_DNA.
DR RefSeq; WP_066290043.1; NZ_CP016761.1.
DR AlphaFoldDB; A0A1B1Z5C0; -.
DR STRING; 255247.ABE41_011005; -.
DR KEGG; far:ABE41_011005; -.
DR OrthoDB; 9760293at2; -.
DR Proteomes; UP000077412; Chromosome.
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:UP000077412}.
FT DOMAIN 9..393
FT /note="Catalase core"
FT /evidence="ECO:0000259|SMART:SM01060"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 56
FT /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT ACT_SITE 129
FT /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT BINDING 339
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 486 AA; 55037 MW; 1CCAFF1FA8EB08F3 CRC64;
MSNGNKHLTT SWGAPVGDNQ SSMTAGSRGP TLIQDVHLLE KLAHFNRERV PERVVHAKGA
GAHGYFEVTN DVRKYTKANF LSEAGKRTPL FVRFSTVAGE NGSADTVRDP RGFAVKFYTE
EGNYDLVGNN TPVFFIRDAI KFPDFIHTQK RHPQTHLKNP NAIWDFWSLS PESLHQVTIL
MSDRGIPATF RHMHGFGSHT FKWVNAEGDG VWVKYHFKTE QGVKNLSNEV AAKIAGENAD
YHTEDLFNAI ENGDFPAWKL YVQIMPLEDA NTYRFDPFDV TKVWSQKDYP LIEVGRMVLN
KNPENYFAEV EQATFSPGTL VPGIDVSPDK MLQGRLFAYH DAHRYRVGAN HQALPINRPR
YEVNNYQRDG QMRFDNNGGG SVYYEPNSFG GPKESTENKQ AAFPVTGIAD SVGYDHDDHY
TQPGDLYRLL SEEERSRLVE TIIGAMKPVE HDEIKLRQIH HFYKADPDYG MRIAKGLGLS
VPQEVK
//
