ID A0A0D2EWL8_9EURO Unreviewed; 509 AA.
AC A0A0D2EWL8;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 22-FEB-2023, entry version 25.
DE RecName: Full=Catalase core domain-containing protein {ECO:0000259|SMART:SM01060};
GN ORFNames=PV05_03633 {ECO:0000313|EMBL:KIW59160.1};
OS Exophiala xenobiotica.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=348802 {ECO:0000313|EMBL:KIW59160.1, ECO:0000313|Proteomes:UP000054342};
RN [1] {ECO:0000313|EMBL:KIW59160.1, ECO:0000313|Proteomes:UP000054342}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 118157 {ECO:0000313|EMBL:KIW59160.1,
RC ECO:0000313|Proteomes:UP000054342};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Exophiala xenobiotica CBS118157.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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; KN847318; KIW59160.1; -; Genomic_DNA.
DR RefSeq; XP_013319744.1; XM_013464290.1.
DR AlphaFoldDB; A0A0D2EWL8; -.
DR STRING; 348802.A0A0D2EWL8; -.
DR GeneID; 25325541; -.
DR HOGENOM; CLU_010645_2_0_1; -.
DR OrthoDB; 3198922at2759; -.
DR Proteomes; UP000054342; 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:UP000054342}.
FT DOMAIN 11..401
FT /note="Catalase core"
FT /evidence="ECO:0000259|SMART:SM01060"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 485..509
FT /note="Disordered"
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; 57467 MW; 513338334AEA9AB4 CRC64;
MSDSTEPPVY TLAEGRPVND PTSSVVLRGP KVRGGGLALL EDTQLIETLA HFPRERIPER
VVHAKAAGAW GEFECTHDVT DWCSAAFLST VGKKTEVLAR LSTVAGEKGS SDTARDIRGF
ALKFKTEEGN WDFVGNDLPV FFIRDPIKFP SLNRSHKRHP QTGVADASMF WDFHNHNQEG
VHCLMQLFGG RGVPASLRNV NGFGNHTFKF GKPKDGSFKY VKIHFKPDAG IQTLSQEDAV
RLAGEEPDYH VKDMFNAIER GNFPTWTMSL QVMDPKDAET YRWNIFDITK VWPHEDYPLI
PVGKLTLNRN PENHFQEIEQ AAFSPSNLVP GIGPSADTML HARMFSYPDA ARYRVGPNYQ
QLPPNRALRV YSPYQRDGPM RLDGNYGSDP DYVRSSFRKI RSGPADVAHD EWVGRVQAYS
SDVTEEDFEQ PRMLWKIFKD TGEDKEFLHN LSGHVGKALP EVQKDTIEMW RRVDEEIAQR
LADALQKGNQ RADHDKAPPT QVALAAHRR
//
