ID A0A1H6YDN7_9DEIO Unreviewed; 726 AA.
AC A0A1H6YDN7;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 29.
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=SAMN04488058_106118 {ECO:0000313|EMBL:SEJ34845.1};
OS Deinococcus reticulitermitis.
OC Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=856736 {ECO:0000313|EMBL:SEJ34845.1, ECO:0000313|Proteomes:UP000199223};
RN [1] {ECO:0000313|Proteomes:UP000199223}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.10218 {ECO:0000313|Proteomes:UP000199223};
RA Varghese N., Submissions S.;
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; FNZA01000006; SEJ34845.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H6YDN7; -.
DR STRING; 856736.SAMN04488058_106118; -.
DR OrthoDB; 9760293at2; -.
DR Proteomes; UP000199223; 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; 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 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 526..570
FT /note="Disordered"
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 726 AA; 80009 MW; EAF6F2DCA59695B9 CRC64;
MDSHRKRPTP HALSDQSVTL DEHSKIEDLS TNTANPGEAL TDNMGHVVSD DQNTLKAGER
GPGLLEDFFF REKMHHFDHE RIPERVVHAR GTGAHGYFEL TESLEDYTHA RVLTQVGKRT
PVFVRFSTVV GFRGSPDTPR DVRGFAVKLY TEEGNWDLVG NNIPVFFIQD AIKFPDLVHA
IKPEPHNEIP QAASAHDTFF DFISLTPESM HMMMWLLSDR TLPRAFDNME GFGVHTFRLI
NAAGESHFVK FHWKPVLGVK SLLWDESQKI AGKDPDFQRR KLWETLDEGG TLEWEFGVQI
FSAEQAGTWD FDILDATKIV PEDLVPVRRV GRLVLNRNVD NFFAETEQVA FMPTNIVPGI
DFTNDPLLQG RTFSYLDTQL LRLGGPNWQE LPINRPLAPV HNNQRDGHMR QTINRGRVSY
FPNRLGGNKP THMGDAGFVS YPEEVRGTKR RARAESFGDH YGQARLFWNS MTPVEKEHMV
KAWSFELAMC EEREVRVRML EHLARVNEIL AEQVAYAIGE LPQTEGVAEP GGAQDSADEV
ARLAGAESPT SASGGLHKAS ALSMEEGQPQ SAKGRKVAVL VAPGVDAEQV AQAQQALKAA
GAQAVVIGPR LGEIAPGVHA EKSLINSDPV LFDALLIPGG EASVRVLAQR PEALHFVADT
YRHAKPLAAI AEGHALLSAS PVASGLNVLG DTGPAFGILK GSGADATLTA LVAALAQHRF
WGRPQA
//
