ID A0A395ML91_9HYPO Unreviewed; 589 AA.
AC A0A395ML91;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 22-FEB-2023, entry version 17.
DE SubName: Full=Catalase {ECO:0000313|EMBL:RFN48696.1};
GN ORFNames=FIE12Z_7015 {ECO:0000313|EMBL:RFN48696.1};
OS Fusarium flagelliforme.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium incarnatum-equiseti species complex.
OX NCBI_TaxID=2675880 {ECO:0000313|EMBL:RFN48696.1, ECO:0000313|Proteomes:UP000265631};
RN [1] {ECO:0000313|EMBL:RFN48696.1, ECO:0000313|Proteomes:UP000265631}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 13405 {ECO:0000313|EMBL:RFN48696.1,
RC ECO:0000313|Proteomes:UP000265631};
RX PubMed=29649280; DOI=10.1371/journal.ppat.1006946;
RA Proctor R.H., McCormick S.P., Kim H.S., Cardoza R.E., Stanley A.M.,
RA Lindo L., Kelly A., Brown D.W., Lee T., Vaughan M.M., Alexander N.J.,
RA Busman M., Gutierrez S.;
RT "Evolution of structural diversity of trichothecenes, a family of toxins
RT produced by plant pathogenic and entomopathogenic fungi.";
RL PLoS Pathog. 14:e1006946-e1006946(2018).
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}.
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:RFN48696.1}.
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DR EMBL; PXXK01000198; RFN48696.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A395ML91; -.
DR STRING; 2594813.A0A395ML91; -.
DR OrthoDB; 3198922at2759; -.
DR Proteomes; UP000265631; Unassembled WGS sequence.
DR GO; GO:0004096; F:catalase activity; IEA:InterPro.
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 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; IPR010582; Catalase_immune_responsive.
DR InterPro; IPR020835; Catalase_sf.
DR PANTHER; PTHR11465; CATALASE; 1.
DR PANTHER; PTHR11465:SF13; CATALASE (EUROFUNG); 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; 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 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 Peroxidase {ECO:0000256|ARBA:ARBA00022559};
KW Reference proteome {ECO:0000313|Proteomes:UP000265631}.
FT DOMAIN 68..454
FT /note="Catalase core"
FT /evidence="ECO:0000259|SMART:SM01060"
FT REGION 567..589
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 398
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 589 AA; 67165 MW; F65AB86DB956B092 CRC64;
MNNSNQLDPR QHPLQAIGNA ISAETQGERR APRMSHMMGA NEGPADVIAK VSGAVGGGKR
VDDGAYFTNN EGLPFPDPAH SKTVGGMPLV SDTFLLQKQQ HFNRSKNLER MVHPCGSGAF
GYFECTQDVT ELTKANFLSS VGEKTPVFVR FSTVTLGREF PDEARNPRGF AIKFYTMEGN
YDLVGLNFPV FFCRDPIQGP DVIRSQYRNP TNFLLDHDAL FDLLANTPEA NHAGLMFFSD
HGTPHGWRFN HGYGCHTFKW VNSNGEFVYI KYHFIAKHGQ KQFTDSEAMQ MCGEDPDYSK
RDLWEAIERG EEIEWTAHVQ VMDPRQADPD KLGFDPFDVT KVWPRSQFPM KEFGRLVLNK
NPENFHRDVE QAAFSPGSMV PGIEDSPDPL LQFRMFFYRD AQYHRIGVNL HQIPVNCPFM
AKSYASLNFD GPMRTDANHA GNKQYVPNSF AHKFRPDVAE APYQVNDNIV SRSSHYWHEG
KKNDYDQAKE LWTRVMSEQE KKNTCYNTAK GLRRVKYPEI QSKYLAQVYN ISEDYAQGIY
DLLEKPEFEF SKVKELAETA QEWYKEPKFR PGPGSKLTGY PPEAAVYQA
//
