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Database: UniProt
Entry: A0A175WDK1_9PEZI
LinkDB: A0A175WDK1_9PEZI
Original site: A0A175WDK1_9PEZI 
ID   A0A175WDK1_9PEZI        Unreviewed;       588 AA.
AC   A0A175WDK1;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   SubName: Full=Catalase {ECO:0000313|EMBL:KXX81756.1};
GN   ORFNames=MMYC01_200698 {ECO:0000313|EMBL:KXX81756.1};
OS   Madurella mycetomatis.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariales incertae sedis; Madurella.
OX   NCBI_TaxID=100816 {ECO:0000313|EMBL:KXX81756.1, ECO:0000313|Proteomes:UP000078237};
RN   [1] {ECO:0000313|Proteomes:UP000078237}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=mm55 {ECO:0000313|Proteomes:UP000078237};
RA   van de Sande W.W.J.;
RL   Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KXX81756.1, ECO:0000313|Proteomes:UP000078237}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=mm55 {ECO:0000313|Proteomes:UP000078237};
RA   Van De Sande W.;
RT   "Madurella mycetomatis genome sequencing.";
RL   Submitted (JAN-2016) 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}.
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:KXX81756.1}.
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DR   EMBL; LCTW02000028; KXX81756.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A175WDK1; -.
DR   STRING; 100816.A0A175WDK1; -.
DR   VEuPathDB; FungiDB:MMYC01_200698; -.
DR   OrthoDB; 3198922at2759; -.
DR   Proteomes; UP000078237; 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:UP000078237}.
FT   DOMAIN          67..453
FT                   /note="Catalase core"
FT                   /evidence="ECO:0000259|SMART:SM01060"
FT   BINDING         397
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   588 AA;  66632 MW;  D3A2E5842115EEAD CRC64;
     MNSNQLDPRQ HPLKATAAAI GAGLQGESRG PRVSHMQSAN EGPADIMKKV AGVVPGGKRE
     DDGPYFTNNE GIPFPDPAHS KTVGGIPVAS DVFLFQKQQH FNRSKPLERM VHPCGSGAFG
     YFECTQDVTG LTKANFLSSV GEKTPVFVRF STVTFGREFP DEGRNPRGFA IKFYTMEGNY
     DIVGLNFPVF FCRDPIQGPD VIRSQYRNPQ NFLLDYDALF DLLANTPEGN HAGLMFFSDH
     GTPQGWRFNH GYGCHTFKWV NQEGQFVYIK YHFVAKHGQK QFTDAEAVRM CGEDPDYSKR
     DLWSAIERGE HLEWTAHVQV MQPEQADPDK LGFDPFDVTK VWPRDQFPMQ EFGRLVLNKN
     PENFTRDVEQ AAFSPGSMVP GIEDSPDPLL QFRMFFYRDA QYHRLGINLH QIPVNCPFMA
     QSFASLNFDG PLRTDANHAG NKQYAPNSFK NKFRPDTAEA PYVVSDNIVS RKSHYWHEGK
     KNDYAQATQL WAKVMTPQQR ANTCHNTAKY LGYVAYPEIQ KKYLAQLHNI SPDYSEGVYR
     RLKDPQFSLD EVKELAKDAH TWGKERKFMP STGQKLSGFA PAGPVYNF
//
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