ID A0A086W8F7_9BURK Unreviewed; 516 AA.
AC A0A086W8F7;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 54.
DE RecName: Full=Catalase {ECO:0000256|ARBA:ARBA00014132, ECO:0000256|RuleBase:RU000498};
DE EC=1.11.1.6 {ECO:0000256|RuleBase:RU000498};
GN ORFNames=JN27_18300 {ECO:0000313|EMBL:KFI06057.1};
OS Massilia sp. BSC265.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Telluria group; Massilia.
OX NCBI_TaxID=1549812 {ECO:0000313|EMBL:KFI06057.1, ECO:0000313|Proteomes:UP000028843};
RN [1] {ECO:0000313|EMBL:KFI06057.1, ECO:0000313|Proteomes:UP000028843}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BSC265 {ECO:0000313|EMBL:KFI06057.1,
RC ECO:0000313|Proteomes:UP000028843};
RA Kellom M., Bailey A., Poret-Peterson A., Noonan K., Raymond J.;
RT "Draft Genome of Massilia consociata BSC265, Isolated from Biological Soil
RT Crust of Moab, Utah.";
RL Submitted (AUG-2014) to the EMBL/GenBank/DDBJ databases.
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:KFI06057.1}.
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DR EMBL; JPXI01000037; KFI06057.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A086W8F7; -.
DR STRING; 1549812.JN27_18300; -.
DR Proteomes; UP000028843; 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:UP000028843};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..31
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 32..516
FT /note="Catalase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001816066"
FT DOMAIN 36..416
FT /note="Catalase core"
FT /evidence="ECO:0000259|SMART:SM01060"
FT REGION 35..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 391..428
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 35..56
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 83
FT /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT ACT_SITE 155
FT /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
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:PIRSR038928-2"
SQ SEQUENCE 516 AA; 56444 MW; A3306A27EADFD150 CRC64;
MNKLSLSYGR MALCALTVAT GLVAMANGAS ATPQLTKDNG APVGDNQHSQ TAGPNGPVLL
QDVHLVQKLQ RFDRERIPER VVHARGAGAH GSFTATEDLG ELTQAKLFTK GKVTPVFVRF
STVIGGSGST ETARDPRGFA TKFYTEEGNW DLVGNNLPVF FIRDAMKFPD MVHSLKPDPV
TNTGDPQRAF DFFSHIPEST HMLTRVYSNY GIPANYREMN GSSVHALKFV NAQGRYTYVK
FAWKSRQGER NLRPAEVAAQ QAKSTNHATA DLYEAIRKGQ FPAWDLTVQL IKPEDLGKFD
FDPLDPTKVW TGVPERKVGT MVLDRVPDNF FEASEQVALA PGNLVPGIEA SEDRLLQGRL
FSYIDTQHHR LGANFQSLPI NKPLVPVVNH QQDGAGNISG RKGSVNYEPS RLAPLPASPH
ARSSALPLSG ATQQQGIAKT LNFRQAGEFY RSLGKQDQDD LIANLSGDLK RVTDKDILHT
MLSHFWKADA GYGQRLAKAV GADAEAIAKL AATLKE
//
