ID N1RYY6_FUSC4 Unreviewed; 509 AA.
AC N1RYY6;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 22-FEB-2023, entry version 38.
DE SubName: Full=Peroxisomal catalase {ECO:0000313|EMBL:EMT69477.1};
GN ORFNames=FOC4_g10003201 {ECO:0000313|EMBL:EMT69477.1};
OS Fusarium oxysporum f. sp. cubense (strain race 4) (Panama disease fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=2502994 {ECO:0000313|EMBL:EMT69477.1, ECO:0000313|Proteomes:UP000016929};
RN [1] {ECO:0000313|Proteomes:UP000016929}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=race 4 {ECO:0000313|Proteomes:UP000016929};
RA Fang X., Huang J.;
RT "Genome sequencing and comparative transcriptomics of race 1 and race 4 of
RT banana pathogen: Fusarium oxysporum f. sp. cubense.";
RL Submitted (SEP-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000016929}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=race 4 {ECO:0000313|Proteomes:UP000016929};
RX PubMed=24743270;
RA Guo L., Han L., Yang L., Zeng H., Fan D., Zhu Y., Feng Y., Wang G.,
RA Peng C., Jiang X., Zhou D., Ni P., Liang C., Liu L., Wang J., Mao C.,
RA Fang X., Peng M., Huang J.;
RT "Genome and Transcriptome Analysis of the Fungal Pathogen Fusarium
RT oxysporum f. sp. cubense Causing Banana Vascular Wilt Disease.";
RL PLoS ONE 9:E95543-E95543(2014).
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}.
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DR EMBL; KB726365; EMT69477.1; -; Genomic_DNA.
DR AlphaFoldDB; N1RYY6; -.
DR STRING; 1229665.N1RYY6; -.
DR HOGENOM; CLU_010645_2_0_1; -.
DR Proteomes; UP000016929; 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 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; IPR010582; Catalase_immune_responsive.
DR InterPro; IPR020835; Catalase_sf.
DR PANTHER; PTHR11465; CATALASE; 1.
DR PANTHER; PTHR11465:SF26; 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; 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:UP000016929}.
FT DOMAIN 11..401
FT /note="Catalase core"
FT /evidence="ECO:0000259|SMART:SM01060"
FT REGION 490..509
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 494..509
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 347
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; 57529 MW; 5D4316350AB07142 CRC64;
MSDSNEAPVY TLAEGKPVED PTSSVVLRGP KVRGGGLALL ADTQLIETLA HFPRERIPER
VVHAKAAGAW GYFECTHDIT DWCSAAPFRR IGKQTQVLAR LSTVAGEKGS SDTLRDIRGF
ALKMKTEEGN WDFVGNDLPV FFIRDPAKFP SLNRSHKRHP QTAVADASMF WDFHNNNQEG
AHCLMQLFGP RGVPESLKNV NGFGNHTFKF GKPEDGSFKY VKIHFKPDAG IKNLSQEDAV
RLAGEEPDYH VKDMYNSIER GDYPTWTMYL QVMDPREAET YKWNIFDITK IWPHKDYPLI
PVGKLVLNKN PENHFHDIEQ AAFSPSTLIP GIAPSADIML HARMFSYPDA ARYRVGPNYQ
QLPCNRPLDA YSPYQRDGPM RLDGNYGSDP DYVRSSFRKV KSGPADVAHS EWVGRVQAYS
SDVEEEDWEQ PRHLWKIFKD NGEDEVFLNN LSGHVNKALP EVQEATVGMW ANVDEEISKR
LGEKLKKLTG NFDHSKAPPS QTVLASRRK
//
