ID A0A1I6C074_9BACI Unreviewed; 690 AA.
AC A0A1I6C074;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=Catalase {ECO:0000256|ARBA:ARBA00012314, ECO:0000256|PIRNR:PIRNR038927};
DE EC=1.11.1.6 {ECO:0000256|ARBA:ARBA00012314, ECO:0000256|PIRNR:PIRNR038927};
GN ORFNames=SAMN04488577_2827 {ECO:0000313|EMBL:SFQ86559.1};
OS Bacillus sp. cl95.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1761761 {ECO:0000313|EMBL:SFQ86559.1, ECO:0000313|Proteomes:UP000199578};
RN [1] {ECO:0000313|EMBL:SFQ86559.1, ECO:0000313|Proteomes:UP000199578}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CL95 {ECO:0000313|EMBL:SFQ86559.1,
RC ECO:0000313|Proteomes:UP000199578};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Serves to protect cells from the toxic effects of hydrogen
CC peroxide. {ECO:0000256|PIRNR:PIRNR038927}.
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|PIRNR:PIRNR038927,
CC ECO:0000256|RuleBase:RU000498};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000256|ARBA:ARBA00001971,
CC ECO:0000256|PIRNR:PIRNR038927, ECO:0000256|PIRSR:PIRSR038927-2};
CC -!- SIMILARITY: Belongs to the catalase family. HPII subfamily.
CC {ECO:0000256|ARBA:ARBA00010660}.
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DR EMBL; FOYF01000004; SFQ86559.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I6C074; -.
DR STRING; 1761761.SAMN04488577_2827; -.
DR OrthoDB; 9760293at2; -.
DR Proteomes; UP000199578; Unassembled WGS sequence.
DR GO; GO:0004096; F:catalase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0020037; F:heme binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR CDD; cd08155; catalase_clade_2; 1.
DR CDD; cd03132; GATase1_catalase; 1.
DR Gene3D; 1.20.1370.20; -; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR Gene3D; 2.40.180.10; Catalase core domain; 1.
DR InterPro; IPR018028; Catalase.
DR InterPro; IPR024708; Catalase_AS.
DR InterPro; IPR024712; Catalase_clade2.
DR InterPro; IPR043156; Catalase_clade2_helical.
DR InterPro; IPR011614; Catalase_core.
DR InterPro; IPR002226; Catalase_haem_BS.
DR InterPro; IPR010582; Catalase_immune_responsive.
DR InterPro; IPR041399; Catalase_large_C.
DR InterPro; IPR020835; Catalase_sf.
DR InterPro; IPR029062; Class_I_gatase-like.
DR PANTHER; PTHR42821; CATALASE; 1.
DR PANTHER; PTHR42821:SF1; CATALASE-B; 1.
DR Pfam; PF00199; Catalase; 1.
DR Pfam; PF06628; Catalase-rel; 1.
DR Pfam; PF18011; Catalase_C; 1.
DR PIRSF; PIRSF038927; Catalase_clade2; 1.
DR PRINTS; PR00067; CATALASE.
DR SMART; SM01060; Catalase; 1.
DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 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|PIRNR:PIRNR038927};
KW Hydrogen peroxide {ECO:0000256|ARBA:ARBA00023324,
KW ECO:0000256|PIRNR:PIRNR038927};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRNR:PIRNR038927};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRNR:PIRNR038927};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|PIRNR:PIRNR038927};
KW Peroxidase {ECO:0000256|ARBA:ARBA00022559, ECO:0000256|PIRNR:PIRNR038927};
KW Reference proteome {ECO:0000313|Proteomes:UP000199578}.
FT DOMAIN 29..417
FT /note="Catalase core"
FT /evidence="ECO:0000259|SMART:SM01060"
FT REGION 509..528
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 76
FT /evidence="ECO:0000256|PIRSR:PIRSR038927-1"
FT ACT_SITE 149
FT /evidence="ECO:0000256|PIRSR:PIRSR038927-1"
FT BINDING 73
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000256|PIRSR:PIRSR038927-3"
FT BINDING 113
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000256|PIRSR:PIRSR038927-3"
FT BINDING 162
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000256|PIRSR:PIRSR038927-3"
FT BINDING 359
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000256|PIRSR:PIRSR038927-3"
FT BINDING 363
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:PIRSR038927-2"
FT BINDING 370
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000256|PIRSR:PIRSR038927-3"
SQ SEQUENCE 690 AA; 77583 MW; 33EFCDBEBF888D88 CRC64;
MTKNDDINEQ NKEKQLEVYT VDNNGQRLTT NQGLRVSDDE HSLKAGVRGP TLMEDFHFRE
KMTHFDHERI PERVVHARGY AAHGFFQVYE SMADYTKAKF LQDPNTKTPV FVRFSTVAGS
RGSGDTVRDV RGFATKFYTE EGNYDLVGNN IPVFFIQDAI KFPDLVHSFK PEPHNEMPQA
STAHDTFWDF VANNTESAHM VMWAMSDRAI PRSFRMMEGF GVHTFRFVND EGKARFVKFH
WKPVLGVHSL VWDEAQKIAG KDPDFHRRDL YESIEMGNFP EYELGVQMID EADEFNFDFD
ILDPTKLWPE EIVPVKIVGK MTLNRNVNNV FAETEQVAFH PGHVVPGIDF SNDPLLQGRL
FSYTDTQLTR LGGPNFHEIP INRPVCPFHN NQLDGMHRMT INKGPVAYHK NSLQGNDPQT
SSAAEGGYEH YQEKIDGKKV RQRSESFKDH YSQAKMFFNS MSQVEKQHIT QAFLFEVGKV
RSKDVQQQVV DMLNNIDLNL AQQVAEGVGA LPPNGGESSA SSQASPALSQ ENTVKLPYTR
KVALLAANGF NGKEVETVIE SLRASGIMTE VISKNLGMIT SDEGQPLKVD KTLLTSDSVF
YDAVYVPGGS QSVGALKTQK EALQFVDDAF SHFKAIALGR SADELFAAAG LNKGEETQPG
VVSLPQEGTQ SFGENFINAI VQHRHWNRIV
//
