ID A0A069DK77_9BACL Unreviewed; 549 AA.
AC A0A069DK77;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=Catalase {ECO:0000256|RuleBase:RU000498};
DE EC=1.11.1.6 {ECO:0000256|RuleBase:RU000498};
GN ORFNames=TCA2_5323 {ECO:0000313|EMBL:GAK42830.1};
OS Paenibacillus sp. TCA20.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1499968 {ECO:0000313|EMBL:GAK42830.1, ECO:0000313|Proteomes:UP000028160};
RN [1] {ECO:0000313|EMBL:GAK42830.1, ECO:0000313|Proteomes:UP000028160}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TCA20 {ECO:0000313|EMBL:GAK42830.1,
RC ECO:0000313|Proteomes:UP000028160};
RA Fujinami S., Takeda-Yano K., Onodera T., Satoh K., Sano M., Takahashi Y.,
RA Narumi I., Ito M.;
RT "Draft Genome Sequence of Calcium-Dependent Paenibacillus sp. Strain TCA20,
RT Isolated from a Hot Spring Containing a High Concentration of Calcium
RT Ions.";
RL Genome Announc. 2:e00866-14(2014).
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}.
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:GAK42830.1}.
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DR EMBL; BBIW01000015; GAK42830.1; -; Genomic_DNA.
DR RefSeq; WP_047913856.1; NZ_BBIW01000015.1.
DR AlphaFoldDB; A0A069DK77; -.
DR eggNOG; COG0753; Bacteria.
DR OrthoDB; 9760293at2; -.
DR Proteomes; UP000028160; 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:UP000028160}.
FT DOMAIN 21..414
FT /note="Catalase core"
FT /evidence="ECO:0000259|SMART:SM01060"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 379..401
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 504..549
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..40
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 383..400
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 522..536
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 68
FT /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT ACT_SITE 146
FT /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT BINDING 356
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 549 AA; 62618 MW; 39D6D12CCF00F2C8 CRC64;
MAENKDKNAS SEQDVQRETL TTRQGHPVRD NQNIRTIGNR GPATLENYHF IEKISHFDRE
EVPERVVHAR GTGAFGYFET YGKVGDEPVE KYTRAKVFSG AGKKTPLMVR FSTVAGAKDS
PETARDPRGF AVKMYTEDGN WDLVGNNLKI FFIRDAMKFP DMIHAFKADP ASNVSHPQRM
FDFVSRSPEA THMITFLFSP WGIPATYRHM QGSGVNTYKW VNDKGEAVLV KYHWEPKQGI
RNLTQEEADS IQAKNVGHAT QDLYEAIERG DYPEWELFVQ IMEDDYHPEL DFDPLDDTKL
WPEDKFPWLP VGRMVLDRNP VDFHAEIEQA AFGTGVLVDG MDFSDDKMLQ GRTFSYSDTQ
RYRVGANYLK LPVNAPKTEV RTNQHRGQMD IRDPKESGDN PHINYEPSMI GGYQEASREG
HPQHRPTYNA AAMSEPIDRP NNYGQAGETY RSFEDWERDE LIKNLSEALA VCDPRIQTAM
VEHFTQADED YGRRVREGIE KKVKELREME QEGKLPGRES GSSKYGQGSL AANQATKDAV
KKSHEADPY
//
