ID A0A364NDL5_9PLEO Unreviewed; 575 AA.
AC A0A364NDL5;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 22-FEB-2023, entry version 18.
DE RecName: Full=Catalase {ECO:0000256|RuleBase:RU000498};
DE EC=1.11.1.6 {ECO:0000256|RuleBase:RU000498};
GN ORFNames=DDE83_001218 {ECO:0000313|EMBL:RAR15389.1};
OS Stemphylium lycopersici.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae;
OC Stemphylium.
OX NCBI_TaxID=183478 {ECO:0000313|EMBL:RAR15389.1, ECO:0000313|Proteomes:UP000249619};
RN [1] {ECO:0000313|Proteomes:UP000249619}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIDEFI 213 {ECO:0000313|Proteomes:UP000249619};
RA Medina R., Franco M.E.E., Lucentini C.G., Saparrat M.C.N., Balatti P.A.;
RT "Draft genome sequence of Stemphylium lycopersici strain CIDEFI 213.";
RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
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 -!- PATHWAY: Alkaloid biosynthesis. {ECO:0000256|ARBA:ARBA00004913}.
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:RAR15389.1}.
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DR EMBL; QGDH01000012; RAR15389.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A364NDL5; -.
DR STRING; 183478.A0A364NDL5; -.
DR Proteomes; UP000249619; 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:0009820; P:alkaloid metabolic process; 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 Alkaloid metabolism {ECO:0000256|ARBA:ARBA00022589};
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:UP000249619}.
FT DOMAIN 40..427
FT /note="Catalase core"
FT /evidence="ECO:0000259|SMART:SM01060"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 554..575
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 87
FT /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT ACT_SITE 159
FT /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT BINDING 373
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 575 AA; 64979 MW; B3500410E44E0820 CRC64;
MNGHTNGNGT QHAPTGGKNG DQFRSYADDR NATSEDIVYT TSNGVPYPHP YESQRAGENG
PLLLQDHHLV DLLSHFDRER IPERVVHAKG AGAHGTYTTT ESLEDLCMAD IFKQGKSCPV
TVRFSTVGGE SGSHDCARDP RGFSVKFRTE EGNWDVVANN TPTFFMRDPA KFPHFIHTQK
RHPATHLTHA DDATQFWDFA SQNPESAHQF MILFGDRGIP DGYRKMHGYH GHTHKLQNSK
GEFVYCQLHF KSRQGTGFIT QEDSANYSPD YSTKDLYQAI EKGDFPGWDV MFQTMTAQQA
EELWEKQKIN IFDMTHVWPQ GQFPLRKVGE FFLTENPKNY FAEVEQVAFN PAHLVPGIEP
SADPLLQSRL FSYPDTHRHR IGANYQQLPV NQPRVSYRMG NFQRDGNMAF YNQGSRPNYL
SSIQPISFKE RTVDLDKLHG AFTSEAVAFL SEIRPEDFNA PRALWEKVFD EDAKKRWINN
ISGHMSTVSD KEIIKRQIAI FREVSEDIAT RMEKATGVKG YPGIAELRFN GTHNGMAKSQ
DKKVANGMTG LSAKYEEKNK ANGAPVPGTH QQVKA
//
