ID A0A2I9DID3_9DEIO Unreviewed; 769 AA.
AC A0A2I9DID3;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, 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=DAERI_020078 {ECO:0000313|EMBL:GBF04481.1};
OS Deinococcus aerius.
OC Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=200253 {ECO:0000313|EMBL:GBF04481.1, ECO:0000313|Proteomes:UP000236569};
RN [1] {ECO:0000313|Proteomes:UP000236569}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TR0125 {ECO:0000313|Proteomes:UP000236569};
RA Satoh K., Arai H., Sanzen T., Kawaguchi Y., Hayashi H., Yokobori S.,
RA Yamagishi A., Oono Y., Narumi I.;
RT "Draft Genome Sequence of the Radioresistant Bacterium Deinococcus aerius
RT TR0125, Isolated from the Higher Atmosphere above Japan.";
RL Submitted (JAN-2018) 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}.
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:GBF04481.1}.
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DR EMBL; BFAG01000002; GBF04481.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2I9DID3; -.
DR OrthoDB; 9760293at2; -.
DR Proteomes; UP000236569; 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}.
FT DOMAIN 41..429
FT /note="Catalase core"
FT /evidence="ECO:0000259|SMART:SM01060"
FT REGION 23..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..39
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 88
FT /evidence="ECO:0000256|PIRSR:PIRSR038927-1"
FT ACT_SITE 161
FT /evidence="ECO:0000256|PIRSR:PIRSR038927-1"
FT BINDING 85
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000256|PIRSR:PIRSR038927-3"
FT BINDING 125
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000256|PIRSR:PIRSR038927-3"
FT BINDING 174
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000256|PIRSR:PIRSR038927-3"
FT BINDING 371
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000256|PIRSR:PIRSR038927-3"
FT BINDING 375
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 382
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000256|PIRSR:PIRSR038927-3"
SQ SEQUENCE 769 AA; 83236 MW; AD99C8309C9FC8A2 CRC64;
MAQNRKLSTP LSLDDTASKL DEQTKAQDLS ANTASPGARL TDNMGHAVSD DQNSLRAGVR
GPTLMEDFLF REKLHHFDHE RIPERVVHAR GAGAHGYFQL DKSLSAYTTA KVLTEVGVQT
PVFARFSTVA GSRGSADTAR DVRGFAVRFY TQEGNWDLVG NNIPVFFIQD AIKFPDLIHS
VKPEPHNEIP QAASAHDTFY DFISLTPESM HMLMWVHSDR AIPRSFAMME GFGVHTFRLV
NAQGHAHLVK FHWKPLLGVH SLVWDEAQKI AGKDPDFHRR TMWESIEAGQ PFEWELGVQV
FTEAQAEGWD FDVLDATKIV PEDLVPVQRV GRMVLNRNPD NYFAETEQVA FMTTNIVPGI
DFSDDPLLQG RNFSYLDTQL SRLGSPNWPE LPINRPVNRV ANNQRDGHMR QTVNRGRVSY
EPNTLGGNKP AEVPQARGGY VSYPERVSGP KVRARAESFG DHYGQARLFW NSMTPVEKEH
ITRSLQFELS KVETRDIRLR MLGHLERINE VLAAQVARAL GERPRVGGTA RPGGTADSAA
ETAVLAAATT PTSASGRLHR AKGLSQEEGQ PRLARGRKVA ILAAEGVNAA QVAAVSKALT
DAGAMADIVG PHLGALAEGV VANKTLANTD PVLYDAVLVP GGAASIQTLI GLGDAHNFVA
QAYKHAKPIG ALGEGTELLT ASEIGRLLRA IAGPAAGAVQ APAGRPDAVQ NLSEVGGMRL
ASGAGAQKLA EYGIVVGQNG GTPAALTAFV TALGHHRYWG RPNVGQVPA
//
