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Database: UniProt
Entry: A0A0C9TZM8_PAXIN
LinkDB: A0A0C9TZM8_PAXIN
Original site: A0A0C9TZM8_PAXIN 
ID   A0A0C9TZM8_PAXIN        Unreviewed;       497 AA.
AC   A0A0C9TZM8;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   22-FEB-2023, entry version 24.
DE   RecName: Full=Catalase core domain-containing protein {ECO:0000259|SMART:SM01060};
GN   ORFNames=PAXINDRAFT_163859 {ECO:0000313|EMBL:KIJ12721.1};
OS   Paxillus involutus ATCC 200175.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Boletales; Paxilineae; Paxillaceae; Paxillus.
OX   NCBI_TaxID=664439 {ECO:0000313|EMBL:KIJ12721.1, ECO:0000313|Proteomes:UP000053647};
RN   [1] {ECO:0000313|EMBL:KIJ12721.1, ECO:0000313|Proteomes:UP000053647}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 200175 {ECO:0000313|EMBL:KIJ12721.1,
RC   ECO:0000313|Proteomes:UP000053647};
RG   DOE Joint Genome Institute;
RA   Kuo A., Kohler A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA   Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA   Lundell T., Morin E., Murat C., Sun H., Tunlid A., Henrissat B.,
RA   Grigoriev I.V., Hibbett D.S., Martin F., Nordberg H.P., Cantor M.N.,
RA   Hua S.X.;
RL   Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000053647}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 200175 {ECO:0000313|Proteomes:UP000053647};
RG   DOE Joint Genome Institute;
RG   Mycorrhizal Genomics Consortium;
RA   Kohler A., Kuo A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA   Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA   Lundell T., Morin E., Murat C., Riley R., Ohm R., Sun H., Tunlid A.,
RA   Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.;
RT   "Evolutionary Origins and Diversification of the Mycorrhizal Mutualists.";
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; KN819360; KIJ12721.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0C9TZM8; -.
DR   HOGENOM; CLU_010645_2_0_1; -.
DR   OrthoDB; 3198922at2759; -.
DR   Proteomes; UP000053647; 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; 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; 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:UP000053647}.
FT   DOMAIN          27..370
FT                   /note="Catalase core"
FT                   /evidence="ECO:0000259|SMART:SM01060"
FT   ACT_SITE        54
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT   ACT_SITE        127
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT   BINDING         337
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   497 AA;  55796 MW;  3C9BF22FFCBC203D CRC64;
     MSILVNTSTP CHGLKFILFG IVWLIYNALH HDLNKAGPTQ TLYREKRIPE RVVHAKGAGA
     HGYFESTHDL SDITSCKLFT SVGKKARATV RFSTVGGESG SADTARDPRG FAIKLRTEDG
     NLDWVFNNTP VFFLRDPAKF PHFIHTQKRD PQTHLKDADM FWDYLSQNPE SAHQILILFS
     DRGTPDGYHN MHGYSGHTYK LVKDDGNWVY TQIHLIADGG FKTFDAATAG KLAGENPDYG
     IQSLFETIEA RKYPSWTVYV QTMTPEQAES FRYNVLDLTK VWPHKDYPMR PVGKLVLDEN
     VQNYFAEIEQ AAFSPSHTIP YLEPSADPVL QSRLFSYPDT HRHRLGRDGL MAINNQGARP
     GYQSTIAPLT YLKYKGAING SPRDYERAAK HETWIGGAFW DLSEVTELDF EQPRALYQNV
     MNDTDRDHLV SNIAGHLGNV KSPVIKARTL SYFASVDQSL SNHIAEAIGA PNAKPLPVKP
     VSEAISFRAN VNKAVKL
//
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