ID A0A401GR27_9APHY Unreviewed; 509 AA.
AC A0A401GR27;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 28-JUN-2023, entry version 13.
DE RecName: Full=Catalase {ECO:0000256|RuleBase:RU000498};
DE EC=1.11.1.6 {ECO:0000256|RuleBase:RU000498};
GN ORFNames=SCP_0606440 {ECO:0000313|EMBL:GBE84665.1};
OS Sparassis crispa.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Sparassidaceae; Sparassis.
OX NCBI_TaxID=139825 {ECO:0000313|EMBL:GBE84665.1, ECO:0000313|Proteomes:UP000287166};
RN [1] {ECO:0000313|EMBL:GBE84665.1, ECO:0000313|Proteomes:UP000287166}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=30375506; DOI=10.1038/s41598-018-34415-6;
RA Kiyama R., Furutani Y., Kawaguchi K., Nakanishi T.;
RT "Genome sequence of the cauliflower mushroom Sparassis crispa
RT (Hanabiratake) and its association with beneficial usage.";
RL Sci. Rep. 8:16053-16053(2018).
CC -!- FUNCTION: Occurs in almost all aerobically respiring organisms and
CC serves to protect cells from the toxic effects of hydrogen peroxide.
CC {ECO:0000256|RuleBase:RU004142}.
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:GBE84665.1}.
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DR EMBL; BFAD01000006; GBE84665.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A401GR27; -.
DR STRING; 139825.A0A401GR27; -.
DR InParanoid; A0A401GR27; -.
DR OrthoDB; 3198922at2759; -.
DR Proteomes; UP000287166; 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; cd08157; catalase_fungal; 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:SF62; CATALASE T; 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:UP000287166}.
FT DOMAIN 16..398
FT /note="Catalase core"
FT /evidence="ECO:0000259|SMART:SM01060"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 63
FT /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT ACT_SITE 136
FT /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT BINDING 346
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 509 AA; 56482 MW; 2943943769242C89 CRC64;
MPSQQVFNSR DGAVYTTSTG APVGEPYAAE RIGGLGPLLL QDFHHIDLLA HFDRERIPER
VVHAKGAGAH GYFEVTHDIT DLTCASIFKK VGNKARATVR FSTVGGESGS ADTARDPRGF
AIKIKTDEGN LDWVFNNTPV FFIRDPAKFP HFIHTQKRDP QTHLKDADMF WDYLSLNPES
IHQVMILFSD RGTPDGFHRM HGYSGHTFKF VKENGEFVYV QIHLIKDGGA KSLAEPVAGK
LGGDNPDYGI QGLFEDIEAG NFPSWTVYVQ TMTTQQAESF RYNILDLTKI WSHKDYPLRP
VGKLVLNDNP QNYFAEIEQA AFSPSHLVPG IEASADPVLQ SRLFSYPDTH RHRLGTNYNQ
LPVNAPIAPV ANFQRAGAMA FVSQGARPNY QSSLVPLTYK PKPYATVKHE TWLGAANADL
SFITELDFEQ PRALWQKVFN DTDREHFVHN VAVHLGNAKS AAVKARQLSV FAAVDQEIAD
RIAKAIGVPT VPPLKVASAS EAIRFKAFA
//
